Unnamed: 0
int64 0
562k
| Entry
stringlengths 6
10
| Sequence
stringlengths 2
35.2k
| Protein names
stringlengths 1
2.59k
| Organism
stringlengths 8
196
| Organism (ID)
int64 14
3.4M
| Length
int64 2
35.2k
| Mass
int64 260
3.91M
| Keywords
stringlengths 3
1.61k
⌀ | Gene Ontology IDs
stringlengths 10
3.48k
⌀ | Protein existence
stringclasses 5
values | Annotation
float64 1
5
| Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Signal peptide
stringlengths 11
302
⌀ | Transmembrane
stringlengths 31
5.51k
⌀ | Pfam
stringlengths 8
232
⌀ | InterPro
stringlengths 10
820
⌀ | PDB
stringlengths 5
11.6k
⌀ | Taxonomic lineage
stringlengths 49
843
| Gene Names
stringlengths 1
583
⌀ | Toxin
bool 2
classes |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
500 |
A0A5F8MPU3
|
MELPPPGNRRVSINNPQETSGRVPTTSAGFPTQSSKISLKRSTYAYRPSMMSNRSSGGQSLLPSSILQKTSLNPPGSLQSKPSNLSSVHYADEEGKPLTDKNKDKDKGRGKGKGTGTRLLTMLRKTLQGSQSDEMAIANQTPNLIPFGDVVGCLAIHIKSCRQFSQRFLGQQRFNLFMRVSINNIVKCTKIRHLKAVNNEKNLVLRFGEMKYFSVQVPRRQDDERNFIYLELMHDGGDPESPPIPLGGAESHLYEVIQKGCFTEVMHLMHKNSSICRVEVEFMFSYGNFGYGFSHQLKPLQKAIEPSMFMNIAPPPERTDPVTNVITPQRVEYPAFLSPEFNVSIGVPEASHATVVQLEKLREKPRERLERMKEEYKNMSTWIEKADYLRNLINPKMTKRDNKGSSIPSESNSSALEELERTTYDIHHRKYEAISNEYGDKEGRVIPVLKVLDQNYSEVFLPKSSDSTPLEDVLLPPIHSLQIVEENEMPHLPKTSEPEDRPHEERKSIVFSSDEELMPKHPSILKISSSQQENRRKMEKSPHFSDVLIIPDKPFEDLNTNKKGRPPIELRKSWERHPTDVACSLRKVAFAQKDYTIPVCKAETTEFKPKHQFQKLSKSGLDPFLRNINSKMSFRKKKDHDDGYRNLSTSSAEILEHEDQDPPYPGHSGSAGSDATWAENPSPVTVQMVNRDSLPPDLITATIVISDRKNKLSLDSVFNSANSLNTKSIFASDNPVVSLTKLSDSDNKLITDSSFNTTKPSNRRLSKDSNFNTTKPSDRKLSSDPSSNTTKPSDTKLFSDPSSNKLSQGPSSNASQLSGSNRLSHNPSINGNKSSYTSDLNKVSRDPSIVSTISSDPNKLSRDPSFVLAKSSDPNKLSHYPSIISAKSSDPNKLSHDPSFVSARSSDPNKLSHDPSIISARSSDPIKLSRDPSFVSARSSDPNKLSHDPSIISARSSDPNKLSRDPSINSTKLSDPSKLSRDPSIFSTKSSDPNKLYRVPSIISGMSSNPKLSRDPSIISGMSSDPKLSRDPSIISAKSSDPNKLSHDPSIISGMSSNPNKLSHDPSIISMKLSDMSKLSRESSINASKSSDTNQLSYDPNIISAKSLDSNNSSASSSPTVNSDTTTNAAEPSGTKNMLDPVVSTIDSSDKQSKLEWLPNVQGASSVTENINTHRSSNSVNFTSDIDILKQSIVLKSILSKNLQDLSDELFSKSELYTNDEGYSPPPSVHSRPSDSTDDRVLGKVQDLNSWRSSKDLLNSQVLLSPVVKNSPQDLLPEGEPGKSSDIEDYVSEKLLEAAGRNFPMNRKSSFKKKHLVSEESSSEHVLSGSIYEYVIKQIFTAPIFSQLGIGIKSSSEARMDSQNQLLTPWERSVTSHIINYEEKDSDVNLSQSKSIISQIIQSFPVNTLLESGVIKVIELDKEHQNSLLDSQTTSSTEQYSDSRSQIKLLSRQNTSSINPLDSSVSGAEYTEDCQSISTQESKYPVRDTKSDSPNDTEEMELDSNLESSSSSLDKVKDTDTAKLKNILKNIFSIFFKYNQSERRQQPEKDSESLIKHSSSSGSEHLEKTQENFNKADKKVDRKPILNPKLRMFLEKLSETEVKNLKSELSKHIQHYLVERLTESGHITKEDLPTIYHKLYLMNEKVELKEQTPFQEKYSETVKEIMSFVNNFNHHFIDKHLETKLRGFLSEILQNYFLKNLSVSNLFNETDAMALHASMSPVRSKSELGQDIADGNFGSSLKINMQYPVTKSLQHYLQDLSENELLSLKTDLSKYLQVLFIEKLYKSGLVSERQLKGISQEIISLHSPSIPLKHIKTNLPFRNESYFMREDSEEQMKYLKNGQNAALHVLLKDKCGETELSRKKERESSFSQILKENLPAIWEQKNIYTREEETLNLIQMQSFLNKNNQANPLTRSPERPSDISLKKQKKDHGFMQFTQVEGSVYKTEIQDPYSWDSRSKTIQSKPCLEKTLKMKLLDKRENNNFYKLTAQEKLDTEFSSYLKLPNCKIPKEKEPISRLSFPTWKTNTFIHVKPEIGEQSKLDHYYQRLKGNNNNNKKHLVTFAQFKNEMETLYRNPYEACNEKRAKISESQSFKYKEKEKSSRPFFFPEVLKRENTKSKRKERDHATKPKKSFHKIVRLLPATLPTTRPHLRKSAPRNLLHWTARRTIHDCLDRFDDLHAPTVKCPKKSKSGARLLGKSPEDSHNQAKHCARPYTAPEPNKRRESAAWKFASPRMVSAGLLHLYVTPAYGIRKVRSKRKLKEDIEKRPLISEIIQMLDNAE
|
Cation channel sperm-associated targeting subunit tau (CatSper-tau) (C2 calcium-dependent domain-containing 6)
|
Mus musculus (Mouse)
| 10,090 | 2,282 | 257,620 |
Alternative splicing;Cell membrane;Cell projection;Cilium;Coiled coil;Flagellum;Membrane;Reference proteome
|
GO:0007283; GO:0007338; GO:0030317; GO:0036126; GO:0036128; GO:0048240; GO:0065003; GO:0070588; GO:0097228; GO:0098876
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:34998468}. Note=Specifically located in the principal piece of the sperm tail. {ECO:0000269|PubMed:34998468}.
| null | null |
PF15729;
|
IPR031462;IPR048363;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Mus (genus), Mus (subgenus)
|
C2cd6 Als2cr11 CATSPERT
| false |
501 |
A0A5J5T2N2
|
MAVMKFTWRSIIPRCSKGIEEPEAEAEAEPETKKQDSKQGSFSRLAMIDLSYPSSRFTEDLSTSLAGSNLYVFTLEELKVITQCFSSANFLGEGGFGPVHKGFIDDNLRPGLEAQPVAVKLLDLEGLQGHREWLTEVVFLAQLSHPHLVKLIGYCCEDEHRLLVYEYMPRGSLENQLFAKYSVPLPWSTRMKIALGAAKGLAYLHEAEKPVIYRDFKASNILLDSDYSAKLSDFGLAKDGPEGDKTHVSTRVMGTRGYAAPEYIMTGHLTAMSDVYSFGVVLLELLTGRRSLDKSRSPREQNLAEWARPMLNESRRLARIMDPKLEGQYSETGARKAAALAYQCLSHRAKQRPKMSDVVNILEPLLDYEETSVGTFVYTVPTHQNGGSPPKDDTDTKECEAKTELKKENGDHHNRHHHRRSHKSRDGHRHRNKSSSQSSVHSENYTSKQTLENGSNEECNID
|
EPD1-interacting receptor-like cytoplasmic serine/threonine-protein kinase 5A (GbEIR5A) (EC 2.7.11.1)
|
Gossypium barbadense (Sea Island cotton) (Hibiscus barbadensis)
| 3,634 | 462 | 51,936 |
ATP-binding;Cell membrane;Hypersensitive response elicitation;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Plant defense;Serine/threonine-protein kinase;Transferase
|
GO:0004672; GO:0005524; GO:0005886
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ZUF4}.
| null | null |
PF07714;
|
IPR011009;IPR050823;IPR000719;IPR001245;IPR008271;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), malvids (clade), Malvales (order), Malvaceae (family), Malvoideae (subfamily), Gossypium (genus)
|
EIR5A ES319_A13G211700v1
| false |
502 |
A0A5K1K8H0
|
MKETEVEDMDTNRKDGKIKKKEKIVNMKNEEVKSTTKSTLADSDEDYSIITLCTKCLSKKLEDNKNRIILDSKAFKDNRLKGRCSVSSNEDPLDNKLNLSPYFDRSQIIQEIILMNNDELSDVYEIDRYKLGKGSYGNVVKAVSKRTGQQRAIKIIEKKKIHNIERLKREILIMKQMDHPNIIKLYEVYEDNEKLYLVLELCDGGELFDKIVKYGSFSEYEAYKIMKQIFSALYYCHSKNIMHRDLKPENILYVDNTEDSPIQIIDWGFASKCMNNHNLKSVVGTPYYIAPEILRGKYDKRCDIWSSGVIMYILLCGYPPFNGKNNDEILKKVEKGEFVFDSNYWARVSDDAKDLICQCLNYNYKERIDVEQVLKHRWFKKFKSNNLIINKTLNKTLIEKFKEFHKLCKIKKLAVTCIAYQLNEKDIGKLKKTFEAFDHNGDGVLTISEIFQCLKVNDNEFDRELYFLLKQLDTDGNGLIDYTEFLAACLDHSIFQQDVICRNAFNVFDLDGDGVITKDELFKILSFSAVQVSFSKEIIENLIKEVDSNNDGFIDYDEFYKMMTGVKE
|
Calcium-dependent protein kinase 5 (EC 2.7.11.1) (PfCDPK5)
|
Plasmodium falciparum (isolate 3D7)
| 36,329 | 568 | 66,248 |
ATP-binding;Calcium;Cell membrane;Cytoplasm;Cytoplasmic vesicle;Kinase;Lipoprotein;Membrane;Metal-binding;Nucleotide-binding;Palmitate;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase
|
GO:0004683; GO:0005509; GO:0005516; GO:0005524; GO:0005634; GO:0005737; GO:0005886; GO:0006468; GO:0009931; GO:0019898; GO:0031234; GO:0031410; GO:0033163; GO:0035556; GO:0106310; GO:1903307
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29487234}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:29487234}; Peripheral membrane protein {ECO:0000269|PubMed:29487234}; Cytoplasmic side {ECO:0000269|PubMed:29487234}. Cell membrane {ECO:0000269|PubMed:20466936, ECO:0000269|PubMed:29487234, ECO:0000269|PubMed:31915223}; Peripheral membrane protein {ECO:0000303|PubMed:20466936}; Cytoplasmic side {ECO:0000305}. Note=During the late stages of schizogony, localizes to the cytoplasm in immature daughter merozoites, co-localizes with AMA1 to a subset of micronemes and to the apical region in maturing daughter merozoites, and near the plasma membrane in mature daughter and free merozoites. {ECO:0000269|PubMed:29487234}.
| null | null |
PF13499;PF00069;
|
IPR050205;IPR011992;IPR018247;IPR002048;IPR011009;IPR000719;IPR017441;IPR008271;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Laverania) (subgenus), Plasmodium falciparum (species)
|
CDPK5 PF3D7_1337800
| false |
503 |
A0A5K6CNB8
|
MNQFVTNTKNVIRGKYHPEFLQNEVLADIFAHTAQTLPDKTALIEADKTLSYGELYQQALIMAQHLALKGVKPGHIVGLWLPRGIELLKAQLAICLSGAAWLPFDMDTPADRIAVCLEDAEAVGMITTDEWYEHLAEVPQTKWTNTELQKPLSESVSLAKTTPDQPAYIIYTSGSTGKPKGIVITQKNICHFLRSENSILGIQEQDKVYQGFSVAFDMSFEEIWLSYLVGATLWIAPKSLVSDPERLCQTLKQEQITVLHAVPTLLALFPEDVPNLRIINLGGEMCPDSLVDRWALPHHQMFNTYGPTETTVSASLELLERGKPVTIGKPLPNYGMLVINSERELLEQGETGELCIFGPSVAQGYLGRPDLTADKFIENPWAMSVEEELLYRTGDLAKIDEFGQVHCLGRADDQVKIRGFRVELGEIEAALCDIDGIGTAAVILRPEDGIDQLIAFIAPEIDAKQAIEIKELRHNLSQRLPPYMVPNRFEIIEEVPRLLSGKIDRKALKARPLTSVVDRSESDQPQNPAEEILFEILNRLFPNMPIKLDSDFFDDLGGHSLLAAVLISNLREHAEYSHLTIQNLYQARRVGAIAALMLEQPEPTLFDSQIGQDNPRNQTYKWLCGIAQLVTIPVLISINILQWLAPFFTYHYFTGGTRDSIPYAIALSLLVYVSVIMSSFVLSITVKRLLMLGIGAGRYPLWGLTYFRWWLADRISNISPVYLLSGSTLLNLYLKALGAKIGHDVTISSVHIRMPSLLTIEDGVSIGSQVNLENAKVEHGHLVLGSIHLKQDSYVGSYAVLEENTVLEKQAHVNALTSIEYDTVVPEGEIWDGTPAQKIGHIDEQAKLPERPKLSFIRKIAEYGYYGVSALIIACLFFIPIFPSFLLVDWLDVNVFNINPNNHLQIALYYFILAIPASAMMMMITAVISSGLRKIALPRLEIGTYAVHGSTYYRKWFAAQILETSLQTLHGLFATIYAPTWFRMLGAKVGKNTEISTATGVIPEMLTLGEESFIADAVMLGDEEIKGGWMSLKATKIGNRSFVGNSAYIADGTVLPDNVLIGVQSKTPDNREMYDGQTWFGSPALLLPAREAAEKYPDHLTFKPSIKRRLMRGFIEGLRIVLPAALAIGVGYMIVLDVIDVINNYNIETGLVALTLAGLLYGVGCFLIVALLKWILIGRYQPRSAPMWTMFVWLSEGITSLYESVAIPNFLNYLRGTPMLPFFLRILGVRIGKDVYMDTADITEFDCVSIGDRAEFNSFSGPQTHLFEDRIMKIGQVNVGNDVVVNTRSIILYNANVSNHAVLGPLTLVMKGENIPAKSAWIGSPAVPWVHK
|
Delta-poly-L-ornithine synthetase (Delta-POs) (EC 6.3.-.-)
|
Acinetobacter baumannii (strain AB307-0294)
| 557,600 | 1,332 | 148,074 |
3D-structure;Cell membrane;Ligase;Membrane;Phosphopantetheine;Phosphoprotein;Transmembrane;Transmembrane helix
|
GO:0005737; GO:0005886; GO:0016874; GO:0031177; GO:0043041; GO:0044550
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 629..649; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 664..684; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 868..888; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 908..928; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1120..1140; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1151..1171; /note="Helical"; /evidence="ECO:0000255"
|
PF00501;PF13193;PF00550;
|
IPR010071;IPR036736;IPR025110;IPR045851;IPR020845;IPR000873;IPR042099;IPR012728;IPR009081;IPR011004;
|
8G95;8G96;8G97;8G98;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Moraxellales (order), Moraxellaceae (family), Acinetobacter (genus), Acinetobacter calcoaceticus/baumannii complex (no rank), Acinetobacter baumannii (species)
|
posA dhbF_1 ABBFA_00818
| false |
504 |
A0A5K7RLP0
|
MLGSDKFSCFSDQHRARSPSPTDRKDKKNHTNKLRELALLIPVTMKTRDKKYTKKEILLRVLHYIQYLQRNIDMTKALLKLHSSNGKGRFVGPGLNPSAGQTQQQHSTPSSSQKPSLWSTSSKPRKKKFTRVSEHPSWPYNPRRSLALDQAENPNTIHPGLKEENEECATYPGVLSPSTYPTTEPSVSEGDGQGAQLVFLDMAQNIFAYDILSDHAVEVQGGEPNADIKVQRSFFLTRAQPCVSSCRQKLFLCTSSEADKEAPDSDPWLPVWTSEDSPNGSPLALGSSQINTWHVADYLNEILGVSSSLFSSPSKILPDHVLEDGTYFLTEGLLESSPATCEVESPQEKEVSSEGPTGPPNFQSSVSLDHCYLSLSENVKVLSNCGSSSESTDTESLWGQEEVRGVATYPRRTGVFSLAQPSVLQQANPEGLQTSSDEDRDYTWTPTGQSSGLPVASKKIKKVQASQGPVKPKDSRKACPGQVKKKCVNGFIMFCRMNRKQYIRACPGTASTAATKDLAQLWRGMTLEEKKPYCTKARRFSRQNNRIVKQENSSSEDDDGETPKPFYQLLAEKAQVSLGLTSLPTPNCQ
|
Meiosis initiator protein
|
Mus musculus (Mouse)
| 10,090 | 589 | 65,090 |
Alternative splicing;DNA-binding;Meiosis;Nucleus;Reference proteome;Transcription;Transcription regulation
|
GO:0003677; GO:0005634; GO:0006357; GO:0007283; GO:0046983; GO:0048477; GO:0051321; GO:0071300; GO:0090427
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32032549}.
| null | null |
PF00505;
|
IPR011598;IPR036638;IPR009071;IPR036910;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Mus (genus), Mus (subgenus)
|
Meiosin Bhmg1
| false |
505 |
A0A5R8T042
|
MVKKSLRQFTLMATATVTLLLGSVPLYAQTADVQQKLAELERQSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAAAAVLKKSESEPNLLNQRVEIKKSDLVNYNPIAEKHVNGTMSLAELSAAALQYSDNVAMNKLIAHVGGPASVTAFARQLGDETFRLDRTEPTLNTAIPGDPRDTTSPRAMAQTLRNLTLGKALGDSQRAQLVTWMKGNTTGAASIQAGLPASWVVGDKTGSGGYGTTNDIAVIWPKDRAPLILVTYFTQPQPKAESRRDVLASAAKIVTDGL
|
Beta-lactamase CTX-M-15 (EC 3.5.2.6) (Cefotaximase 15)
|
Escherichia coli O25b:H4
| 941,280 | 291 | 31,144 |
3D-structure;Antibiotic resistance;Hydrolase;Secreted;Signal
|
GO:0005576; GO:0008800; GO:0030655; GO:0046677
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34310213}. Note=Type I secretion system (T1SS) probably involved in secretion process. {ECO:0000269|PubMed:34310213}.
|
SIGNAL 1..28; /evidence="ECO:0000255"
| null |
PF13354;
|
IPR012338;IPR045155;IPR000871;IPR023650;
|
4HBT;4HBU;5FA7;5FAO;5FAP;7U48;7U49;7U4B;7U57;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
|
bla blaCTX-M-15 EWT59_27045
| false |
506 |
A0A5S9I252
|
MGQPTTTSLFMRDVMFHRMTGTSQAVNDVATLSGERREIIRRALNKKILVPNILELMPAWPSEFQPNIDEVNVEIDEWLKTVNVAKEKKLKHRARGNYTLLAGIYYPHCRKEKMLALSQFLYWIFFWDDEIDTGGELTEDREGTILCCAETNKCINDCLGPEPNYTPPPGSRGTVEMLYPILRDLRAGLSPVSTMRLKQELHDYVNGVKNQQKVRQEDHLPNPWDHFQMRVDDVGVIPSITQNEYAMDFTLPDWIRRHEAMEEIVLQCTKLTILLNEILSLQKEFRVSQLENLCLLFMNTYDMSIEQSIHKVLGLLKDHYKICIEAEARLPWSTTDEKLNNNIREYIRGCQRLATGTACWSYNCERYFKLSQLNDQQELLLDLSRT
|
Terpene cyclase 6 (EC 4.2.3.-) (EC 4.2.3.104) (EC 4.2.3.137) (EC 4.2.3.157) (EC 4.2.3.182) (EC 4.2.3.57) (Sesquiterpene synthase 6)
|
Hypocrea atroviridis (Trichoderma atroviride)
| 63,577 | 386 | 44,939 |
3D-structure;Lyase;Magnesium;Metal-binding
|
GO:0008299; GO:0046872; GO:0080016; GO:0080017
|
Evidence at protein level
| 5 | null | null | null |
PF19086;
|
IPR008949;IPR034686;
|
7W5F;7W5G;7W5H;7W5I;7W5J;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), sordariomyceta (clade), Sordariomycetes (class), Hypocreomycetidae (subclass), Hypocreales (order), Hypocreaceae (family), Trichoderma (genus)
|
tatc6
| false |
507 |
A0A5S9MMK5
|
MMTTTVQKNCWRLDQTMLGLEKPGSSDISSSSTDTSAISPISVSSMPLSPDKEKKKISFVRYNPDIPQIVTSFKGYQKLMYQGYRYNIYQIAPERNFKSWRCVCAKKMHDGQWCKCRAETTMDNKNACTKGSHNHPPRHHVAEIEFIKSQLYSAALENPDHDAGDLVNQASMYLSDGVMFDNKESIKKSLVVARNKDGKPKKPRSKRMMKFEVDDDDENEYKMPKLETDISCFLPFINNMVKVEPPFSHTPTIQIPQPIPTPIQHQQQEQSNLLQPATLNGMNNPWMGMEDHLAMIWAANAMLNPGLDVLSTIAALSKHQQHVQGPSPQQAATAPTTASLSSNLSVSSFTPQMPKEASIAIPAPLQVLNLKDLKPLPPLANIQTSPVIQAANLLLPVAALKKDSSTQTTEEIKVSQCLTSGCGCRVIRICCCDEGVCRRTAAC
|
FLYWCH-type zinc finger-containing protein peb-1 (Pharyngeal enhancer binding protein peb-1)
|
Caenorhabditis elegans
| 6,239 | 443 | 49,148 |
Alternative splicing;Developmental protein;DNA-binding;Metal-binding;Nucleus;Reference proteome;Transcription;Transcription regulation;Zinc;Zinc-finger
|
GO:0000122; GO:0000978; GO:0005634; GO:0008270; GO:0045944
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11203704, ECO:0000269|PubMed:15165844}. Note=Localization to nucleus dependent, in part, on FLYWCH-type domain. {ECO:0000269|PubMed:15165844}.
| null | null |
PF04500;
|
IPR007588;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Nematoda (phylum), Chromadorea (class), Rhabditida (order), Rhabditina (suborder), Rhabditomorpha (infraorder), Rhabditoidea (superfamily), Rhabditidae (family), Peloderinae (subfamily), Caenorhabditis (genus)
|
peb-1 T14F9.4
| false |
508 |
A0A644F0Y1
|
MPREVITIQCGQCGNQIGEVFWNRLCTEHGINPDGTLRPEAYTFNDRKDVFFYQSDDEHYVPRAILLDTEPGVISHIRNGPIKELINPENVYIDSTGGGAGNIWTKGFQCGEAGFEKIVEIIDREADGADSLAGFSLTHSIAGGTGSGMGSFLLDRLSDRYPKALLQTYSVFPNTTADIIVQPYNSILTLQRLALCADAVVVLDNTALDRIITNHIPNELLTNPFEHVNSLVSTVMAASTSTLRLPGFMSNDLLSLVSSLVPTPRLHFLMSSYTPITSSSLNVKEHTKDQEAGSGAVAGAAAGATRRQVHTDSIVQLVKRLLHPTNGMVSCGRDGKYISLLNIVQGEAESNQLYKSLQQIKEGRDVKFIDWGPSNMQMALSKRSPFTNEAHKVSGLMLANHTAIRKIFDNINNTFTQLFSKRAYLQNYIDSMVTGGEPEILEQFTDAQAVCTSLSKEYEAAESKDYLEYIGM
|
Tubulin gamma chain (Gamma-tubulin) (Glgamma-tubulin)
|
Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)
| 184,922 | 472 | 51,870 |
Cell projection;Cilium;Cytoplasm;Cytoskeleton;Flagellum;GTP-binding;Microtubule;Nucleotide-binding;Reference proteome
|
GO:0000070; GO:0000212; GO:0000278; GO:0000931; GO:0005525; GO:0005634; GO:0005737; GO:0005813; GO:0005815; GO:0005819; GO:0005874; GO:0005930; GO:0007020; GO:0007052; GO:0008275; GO:0031122; GO:0035082; GO:0036064; GO:0044458; GO:0072686; GO:0097556; GO:0097557; GO:0097558; GO:0097559; GO:0097568; GO:0097729; GO:0140490; GO:1902410; GO:1903673
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:10928459, ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10928459, ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:30318753}. Note=Localizes mainly to basal bodies of trophozoites during interface (PubMed:30318753). Localizes as four dots at the basis of posterolateral and ventral flagellar pairs in interphase (PubMed:10928459). Also localizes to axonemes and median body in over half of the interphase cells (PubMed:30318753). Colocalizes with microtubules in the median bodies of the interphase cells (PubMed:30318753). Localizes to basal bodies and median bodies in dividing stages of the trophozoites (PubMed:30318753). The four dots are absent in late prophase and early metaphase, but reappear as tiny dots at the perikinetosomal areas of the separated parent flagella in anaphase (PubMed:10928459). Localizes transiently to the centers of the mitotic spindles in anaphase (PubMed:30318753). The four dots localize at the basal body regions of each daughter karyomastigont in telophase (PubMed:10928459). Colocalizes with centrin outside the two nuclei in telophase (PubMed:30318753). Localizes to basal bodies and axonemes of the two daughter cells during cytokinesis (PubMed:30318753). Does not localize at the spindle poles of the dividing nuclei (PubMed:10928459). {ECO:0000269|PubMed:10928459, ECO:0000269|PubMed:30318753}.
| null | null |
PF00091;PF03953;
|
IPR002454;IPR008280;IPR000217;IPR037103;IPR018316;IPR036525;IPR023123;IPR017975;IPR003008;
| null |
cellular organisms (no rank), Eukaryota (domain), Metamonada (clade), Fornicata (phylum), Diplomonadida (order), Hexamitidae (family), Giardiinae (subfamily), Giardia (genus), Giardia intestinalis (species)
|
GL50803_00114218 GL50803_114218
| false |
509 |
A0A644F649
|
MTQNWRPQSRLQTMTFAGTARPMTSMTAAGFTKNPLATAGVASIFDKLPPEPPKDSPEQKADQMEINIFKLLRDGMSAASCKDYVTALGRIREAIKLEQKVSQHRTMNGLADSINLDLRTCIWMHWAQIQALGGQPEMALSTYEKIVKTAEGATLAQIRFNMGNINHNLGKYNEALKNFRMAIDQASPSLPRFRQKIASHMAQSCIKLHRWQDAVDRIEEYLIKQYTLASSVGTDVERQNFYAMTTRFDPLYTVLIGYYALGVPEKMIDAYSRLIDSSILISDHPDSLEIDDHHNGISSKQIAMADAELCNMSNDDELDDLSRYNATLRHEHTNKLLISARLLAPAIAWEESQGYAKLSDILREKGHHGISLQVQMSMALTLLKRNEFEKATDIMLRIDREGLESALALGINVPLSILQKTRNLSLTAAATAVTNQESDLHLLGIDPSVLANQQSVVDRDAVASRGAPEVDMLKTDDDNGTKKQPYAAFVPRGVHTNIAFIYYLKGDYEASARHAQIALEIDPYDSFAHINLGCTYSKTNQWELSLREFLKAQEINMESVQATYNAGLVYFKQQEYKTAYSCFQKVASKLPSYGDAIYMSADCLARMSQIDEAIQMLSNLVTMFSAVKAYDPSIYIRLGELYSIAGDEGQAAHYFKEAHRLVPFSLAVINWLGSHYIKNELYEQARVCFEKASRVDTTTPKWSLAVAACLRKSKQYRDAIYEYKHILKRFPTNTTAMTHLISSLNNIGQHKEADEWAEKLTKLTNNKVPEVTEDRELDEFVKQERRNSVAAVGPGSRAGQDRFEASNNRVSSNTGDLFGDVDIAEELLTEN
|
Intraflagellar transport protein 88 (IFT88) (Intraflagellar transport particle protein IFT88) (Intraflagellar transport protein IFT88)
|
Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)
| 184,922 | 831 | 93,307 |
Cell projection;Cilium;Cilium biogenesis/degradation;Cytoplasm;Cytoskeleton;Flagellum;Reference proteome;Repeat;TPR repeat
|
GO:0005814; GO:0005930; GO:0019894; GO:0030992; GO:0035735; GO:0036064; GO:0060271; GO:0097542; GO:0097546; GO:0097729; GO:0097730; GO:1990900
|
Predicted
| 5 |
SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:31855176}. Note=Localizes to the cytoplasmic and membrane-bound portions of each of the eight axonemes, localizing particularly at the flagellar pores and at the distal flagellar tips. Localizes to the basal bodies. {ECO:0000269|PubMed:31855176}.
| null | null |
PF13174;PF13181;
|
IPR011990;IPR019734;
| null |
cellular organisms (no rank), Eukaryota (domain), Metamonada (clade), Fornicata (phylum), Diplomonadida (order), Hexamitidae (family), Giardiinae (subfamily), Giardia (genus), Giardia intestinalis (species)
|
GL50803_0016660 GL50803_16660
| false |
510 |
A0A644F7M7
|
MSSVFADPRVKELLNLHRSPKLATEGKTPPSQVQDLVNKYSRLGSNVVSHPTRSSPEKTTDKPADSKPSIPPLKSESVMTRLTALSSNNTTQNVASLVTAIASHPATAALPKQEASQQPVIPTSVEKRAVTQPLSQQNMNKLMNAIDPQAAPLIEDQVAGKHTGTKPLLTLQQQQAISSLPTKSERESALNEIALNTAIQSAQHANMELSKAGITFPMWFFGVQNQSDLVSRSFISLAHIQQPMVMNDSLLQEHLLVSDCIAVLQGCMQTTYLQVSEQNKEYVVTIRKEVATELPATLVAMTQRVLVHAHARFQIVNTIYTHQVPEYGRIANAFSQALRCIIKEYDFYLADLSKKHYGKMQSSAERGSLSLQTLEVKTKQIHIILENVADLCSRLGVVRGCALLQQLETAVLQSSGLSVKEVFQYLLSESLKPLGRIMDRYINEAVIPDSDAADFFIRKSHSTELAEEQGKTTINTWMQMFKVDDAQVPLFLNNIKTHLCDIGRSTVLLKWKKKQYIDKGPNASGQELLLLSAEASGETTQGFRHGEETVASLVCGDGSTGDLELAHIRLYKQLIDINARVQTKVLDFFINPEYLDFRGHLQNIYAFYLVMAGDFLSCFVESAISELVLSRSVANILRIRSKFKMVIKTSSLANLPYNERMNVIVCPELFKHHLNSVLYPQTYVPDRATDSPDPKVLNLLGLQYDVTYPLNLVLTTPVMERLNLVFRHILRAKVSEIELQKAWTTLQRLRKLERVPHDKIEVYANALRSDKSPIIIFFGVAYKMLITMLDFIHSLQFQYVTILTECIAKFQDTLVNAKSLDDLVSGMSAFANGLIMSLGLVSNNVVNILDTLFNDCIVYSHHIVKTFCIISNEDDEFIRKIVTINEESREGKSGPRGVKGSERMTSLLKKREAIEMTRLIAIANSVYSLIVDNRGLIATLMTKFNKGVASYEQVIRNFDDR
|
Gamma-tubulin small complex component GCP2 (Gamma-TuSC component GCP2) (Gamma-tubulin complex protein 2) (GCP2) (GlGCP2)
|
Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)
| 184,922 | 961 | 107,504 |
Cell projection;Cilium;Cytoplasm;Cytoskeleton;Flagellum;Microtubule;Reference proteome
|
GO:0000278; GO:0000922; GO:0000930; GO:0005874; GO:0005930; GO:0007020; GO:0008275; GO:0031122; GO:0036064; GO:0043015; GO:0044458; GO:0051225; GO:0051321; GO:0097568; GO:0097729; GO:1902410; GO:1903673
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:30318753}. Note=Localizes to basal bodies, axonemes and median bodies of the trophozoites during interface. Colocalizes with tubulin gamma chain. {ECO:0000269|PubMed:30318753}.
| null | null |
PF04130;PF17681;
|
IPR007259;IPR040457;IPR042241;IPR041470;
| null |
cellular organisms (no rank), Eukaryota (domain), Metamonada (clade), Fornicata (phylum), Diplomonadida (order), Hexamitidae (family), Giardiinae (subfamily), Giardia (genus), Giardia intestinalis (species)
|
GL50803_0017429
| false |
511 |
A0A649V088
|
MVTKRVQRMMFAAAACIPLLLGSAPLYAQTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMAAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAAALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDPRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTSWTVGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDVLASAARIIAEGL
|
Beta-lactamase CTX-M-14 (EC 3.5.2.6) (Cefotaximase 14)
|
Escherichia coli
| 562 | 291 | 30,979 |
3D-structure;Antibiotic resistance;Hydrolase;Secreted;Signal
|
GO:0005576; GO:0008800; GO:0030655; GO:0046677
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A5R8T042}.
|
SIGNAL 1..28; /evidence="ECO:0000255"
| null |
PF13354;
|
IPR012338;IPR045155;IPR000871;IPR023650;
|
8SJ3;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus)
|
bla blaCTX-M blaCTX-M-14
| false |
512 |
A0A6B9HEI0
|
MSAELASRGRKVYFVGLNEYPFLPLVAGLLRTYAEQDERIAAAYDFQEPVFLVAPVQEMADGIVEPDVLALSCYVWNFRRQMKVAKLVKERYPNVLVVAGGPHVPDRPGNFFEKHPYVDVLAHGEGEVAFRELLATRLSDHPDYTAVPGVSVRRGTEAVVGPKAKRLPRLIDTPSPYLLGVMDGAVATCRERGLRFYALWETNRGCPYSCSFCDWGSATMSTLRKFEDERLQDEIEWFARHDVEDLFICDANFGIMPRDLEIAHALAEARGELGAPRQVRVNFAKNSNDRVFDISKTWHDADLLMGTTLSMQSTDMDVLEAIDRKNIGLDNYRKLQQRYAAENIHTYTELILGLPMETARSFRDGIGSLLEAGNHEDLRVYELGILPNAPLNTPEKIEQYGLRTVPKRMYVERPGTPDDEAETFEMVMETNAMPRDAWVESFSFIQAVQFLHNGCYTRYLSIFLRQEHGIGYTRFYEGLQDYFTGRPDTVLGALYLRMRSLYHDYIDMPALPLANLVASQPDMAADLAPYGRRRGWTIDNWGWLRIATDFDRFHTELREYLATLGLDPAGDARLEDVLRFQQDVMLRPDYSPELGKSAEYAHDWPGYFAGGLLRPRRVRVAYGDQSFGANGRYRPVPGDLKAFTMAAIGTSYPVSRMGHFCHRFESAEVTSLAEPVVSEQW
|
Cobalamin-dependent radical SAM methyltransferase TokK (EC 2.1.1.-) (B12-dependent SAM enzyme TokK)
|
Streptomyces tokunonensis
| 2,689,386 | 681 | 77,368 |
3D-structure;4Fe-4S;Antibiotic biosynthesis;Cobalamin;Cobalt;Iron;Iron-sulfur;Metal-binding;Methyltransferase;S-adenosyl-L-methionine;Transferase
|
GO:0005829; GO:0008168; GO:0017000; GO:0031419; GO:0032259; GO:0046872; GO:0051539
|
Evidence at protein level
| 5 | null | null | null |
PF02310;
|
IPR006158;IPR036724;IPR006638;IPR007197;IPR023404;IPR051198;IPR034514;
|
7KDX;7KDY;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Kitasatosporales (order), Streptomycetaceae (family), Streptomyces (genus)
|
tokK
| false |
513 |
A0A6B9HER0
|
MEKSGYGNDGIYRSLRPPVLFPNDPNLSVTSYLFQRSDAYPDRLALADANSGETLNFAQFKAMVQRVSHGLSRLGIKKGDVVLIFSPNSIYFPVCFLAIVALGAVVTTGNPQYTSAEITKQANDSKPKLVITVPQLWDKVNHLGLPAVFLGSKISGDGTIAPSNRNINGTVTYFSNLVELGGHVSEFPPVSIKRSDIAALLYSSGTSGTSKGVILTHRNLISTACMTTSDQEFDGEDPNVFLCFLPMSHVFGLVIICYSQLMRGNSVVSVEKFDLEMVLRSVGKYRVTYLCVVPPVMIALAKQNWGKIYDLSSLKRIICGSAPLGKEVIEECAKNYPHVPIIQGYGLTESCGIASLEIPEGVREYGSSGILFPAVEAKIVHVENLTPLPPNQLGEIWIRGPNMMQGYLNNPQATKLTIDEQGWVHTGDLGYFNGEGRLSVVDRIKELIKCKGFQVAPAELEGLLLSHQEILDAVVIPYPDAEAGEVPIAYVVRALSSTLDEEAVKKFIAEQVAPFKRLRKVTFVNSVPKSASGKILRRELIAKVRSKI
|
Piperic acid--CoA ligase (PipCoA ligase) (EC 6.2.1.-)
|
Piper nigrum (Black pepper)
| 13,216 | 548 | 59,821 |
ATP-binding;Ligase;Nucleotide-binding;Peroxisome
|
GO:0004467; GO:0005524; GO:0005777; GO:0016405
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q9M0X9}.
| null | null |
PF00501;PF13193;
|
IPR025110;IPR045851;IPR020845;IPR000873;IPR042099;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), Magnoliidae (clade), Piperales (order), Piperaceae (family), Piper (genus)
| null | false |
514 |
A0A6C0PI29
|
MKAFATRALAFSVAAGQALAAVTQGVSDNTYNRLVEMATISQAAYANLCNIPATIQTVEKIYNAQTDINGWVLRDDSRQEIITVFRGTGSDTNLQLDTNYTLAPFDTLPQCVGCAVHGGYYLGWLSVQDQVQSLVQQQASQYRGYAVTVTGHSLGASMAAITAAQLSATYDNVNLYTFGEPRTGNQAYASYMNEAFDSASPETTRYFRVTHADDGIPNVPPAEQGYVHSGVEYWSVEPHSPQNTYICTGDEIQCCEAQGGQGVNAAHVTYFGMTSGACSW
|
Feruloyl esterase 1 (EC 3.1.1.73) (Ferulic acid esterase 1)
|
Penicillium parvum (Eupenicillium parvum)
| 70,113 | 280 | 30,201 |
Carbohydrate metabolism;Disulfide bond;Glycoprotein;Hydrolase;Polysaccharide degradation;Secreted;Serine esterase;Signal;Xylan degradation
|
GO:0005576; GO:0006629; GO:0017000; GO:0030600; GO:0045493; GO:0072330
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31792788}.
|
SIGNAL 1..20; /evidence="ECO:0000255"
| null |
PF01764;
|
IPR029058;IPR051299;IPR002921;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Penicillium (genus)
|
fae1
| false |
515 |
A0A6I8PUB9
|
MSNFTPDACNVDSGLDSVLPPSLYALVFTLGLPANLLALWAAWLQVRKGRELGVYLLNLSLSDLLLICALPPWTDYYLRRDVWGYGPGACRLFGFVFYTNLYVGAAFLSCVSADRYLAVAHPLRFPGARPIRSAAAVSALIWMLELAANAPPLLGEAIHRDRYNHTFCYESYPLSGRGAALANVGRVLAGFLLPWGVMMLCYAGLLRALRGSASCEQRERRRVRRLALGLPCVALLCYGPYHALLLLRSLVFLVGGGSVDAGGGCALEERLFPAYHASLALATLNCLADPALYCLACPGARGEVAKVVGGVVAWAMGKERRAWGERGGNGRGCGEGEEVGMVELRGNGREFVV
|
G-protein coupled receptor 4 (XtGPR4)
|
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
| 8,364 | 353 | 38,045 |
Cell membrane;Disulfide bond;G-protein coupled receptor;Glycoprotein;Membrane;Receptor;Reference proteome;Transducer;Transmembrane;Transmembrane helix
|
GO:0004930; GO:0005886; GO:0007189; GO:0071468
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P46093}; Multi-pass membrane protein {ECO:0000269|PubMed:39753131}.
| null |
TRANSMEM 9..45; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:39753131"; TRANSMEM 50..80; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:39753131"; TRANSMEM 86..121; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:39753131"; TRANSMEM 130..156; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:39753131"; TRANSMEM 173..211; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:39753131"; TRANSMEM 216..251; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:39753131"; TRANSMEM 268..296; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:39753131"
|
PF00001;
|
IPR000276;IPR017452;IPR002276;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Pipoidea (superfamily), Pipidae (family), Xenopodinae (subfamily), Xenopus (genus), Silurana (subgenus)
|
gpr4
| false |
516 |
A0A6I8TCE0
|
MNSAPRNAGAARSVDRRGFIAACGLLVLLVVRMLGAADATRIFDIENIPVVKYVAVAGRNVTLNCPGVTEHSLVDTLVWRTSQTIAEYVDGGLPLVSSLRITLLPDNFSLHFNPAFASDTDEYSCLVNDRHSPDALVDLLVQDVPDPPGRPLVLSFTSRTVNLSWAYTQDPRNAPINNFVIETRVGENGEWDQVDPLYTNSNEAFYQVTGLVPFTVYSFRVIAVNELGHSPPSKESYYFVTLREAPTGKPVTTIAHNTSATSVYISWKPPPAETILGEFLGYRITYRARDKGTDDDVKEIYIRDSTVESHEIHHLETYTQYLASIQVFNPEGLGPPTTVLVMTDEGVPSKPLNLSVLEVTSTTIKITWREPEKLNGAIHGYRVYYVHQNQTLLHLPILKADAAVNSVYTYTLSNLKPYTDYKIIVAAFTKKFDGEPSEVSQRTDISGPSAPKVVNLTCHSQHELLFGWHIPQTYYNTIDYYIISYRNLEHSEYKDIRLTANSSIVETSMIIPNLTTNMVYEVKVRAASASVINPKQIILGSYSEPKKISLQLHCEKIPQPSQRQVYDDYNLAVLGGIVFSCFGLLLIVLSFLLWKKCFHAAYYYLDDPPACQGANTAGLIDWEAPCEVAGEVRGPIPVTEFAKHVASLHVDGDIGFSKEYEAIQGEALNDEYPSEHSQHPDNKGKNRYLNVIAYDHSRVHLRQVPGQKKHLDYINANYIDGYQRPRSFIGTQGPLPGTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGAEMYGVIQVRLIREDVMATYTVRTLQIKHTKLKKKKASQSEKLVYQYHYTNWPDHGTPDHPLPVINFVKKSTAANPSDAGPIVVHCSAGVGRTGTYIVLDAMLKQIESKGMLNVFGFLRYIRAQRNYLVQTEEQYIFIHDALVEAIDSGETNIKMDAIGGLVNNIDFIDNQYKLITSYQPKEINLTSALKSVNAIKNRSSLVPLEGSRVHLTPKPGVEGSDYINASWLHGFRRLRDFVVTQHPLIETFKDFWQMVWDHNAQTVVLLSSADNMSFLQFWPNESEPMESDYYRIRMVSETSENNYIVRNFVIQSIQDDYELSVRMFENPMWPDMANPRSIYDFAVRVHERCAQYRNGPIVVVDRYGGFQACQFCCISSLAMQLEYDQTANVYTYAKLYHNKRPGIWSSYEDIRQIYRILSYMPKDLGLLKCTELRTEFDDAAIMTATPDLYSKICSNGSINTHLNSGDGGGNGNDGVPTGNGTNGGLPMSGGGTTTAATIQNGGTVIVKMNGEDNDELSVVVATSNHLNLDHNQS
|
Putative receptor-type tyrosine-protein phosphatase mosPTP-1 (mosPTP-1) (EC 3.1.3.48)
|
Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
| 7,159 | 1,309 | 147,143 |
Cell membrane;Glycoprotein;Hydrolase;Membrane;Protein phosphatase;Reference proteome;Signal;Transmembrane;Transmembrane helix
|
GO:0004725; GO:0005886; GO:0009653; GO:0048666
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20797779}; Single-pass type I membrane protein {ECO:0000255}.
|
SIGNAL 1..36; /evidence="ECO:0000255"
|
TRANSMEM 573..593; /note="Helical"; /evidence="ECO:0000255"
|
PF00041;PF00102;
|
IPR003961;IPR036116;IPR036179;IPR013783;IPR003599;IPR029021;IPR000242;IPR050713;IPR006311;IPR016130;IPR003595;IPR000387;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Diptera (order), Nematocera (suborder), Culicomorpha (infraorder), Culicoidea (superfamily), Culicidae (family), Culicinae (subfamily), Aedini (tribe), Aedes (genus), Stegomyia (subgenus)
| null | false |
517 |
A0A6J2ATK2
|
MGPPSSSGFYVSRAVALLLAALAAALLLALAVLAALYGRCARVQPSDLHHGGVPDAASSPRGTQEEQLPTWPPRPTREPAGTATPGHWRPPGPWDQLRLPPWLVPLHYELELWPRLRPNEFQSPTLSFTGRVNITVRCTAATARLLLHSLFLDCESAEVRGPLSSGPRDGAVGRVPVDDVWFAFDMQYMVLELGATLQPGSRYELQLSFSGLVYRDLREGLFFSIYTDQGERRALLASQMEPTFARSVFPCFDEPALKATFNITIIHHPSYGALSNMPKLGQSEKRDVNGSVWTITTFSTTPHMPTYLVALAICDYDHVSRTERGQEIRIWARKDAIANGNAAFALNITGPIFSFLEDLFNISYPLPKTDIIALPTFDNSAMENWGLLIFDESLLLMQPNDQVTDKKAVISFILSHEIGHQWFGNLVTMNWWNDIWLKEGFASYFEFGVINYFNPKFRRNEVFFSNILHHVLSEDHALVSRAVSLKVENFTETSEINELFDLFTYNKGASLARMLSSFLNENVFISALKSYLKTFSYSTAEQDDLWRHFQMVVDDQSKILLPAPVKSIMDRWTHQSGFPVITLNVSTGAMKQEPFYLGKVKNQTLLTHNDTWIVPILWIKNGITQSLVWLDKSSKIFPEMQVSDSDHDWVILNLNMTGYYRVNYDKVGWKKLKQQLEKDPKAIPVIHRLQMIDDAFSLSKNNYVEIETALDLTKYLAEEDEIIVWYAVLVNLVTKDLVFDVNNYDMYPLLKKYLLKRLISIWNMYSTVIRENVAALQDDYLALVALEKLFETACWLGLEDCLQLSRELFKNWTNHPENEIPYPIKSVVLCYGVAFGSDEEWDFLLNMYSNKTKEEERIQLTYAMSCSKDPWILHRYLEYAVTAAPFTFNETNIMEVVAESEVGRYIVKDFLINNWQAVSERYGTQSLVNLMYIIGRTISTDLQITELQQFFSNMLEEHQKLTVRAKLQTIKNKNLGNKKLNARMTAWLRKNT
|
Aminopeptidase Q (EC 3.4.11.-) (Laeverin) (Tabulin) (Transmembrane Aminopeptidase Q)
|
Acinonyx jubatus (Cheetah)
| 32,536 | 992 | 113,497 |
Aminopeptidase;Developmental protein;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc
|
GO:0005615; GO:0005737; GO:0006508; GO:0008270; GO:0016020; GO:0042277; GO:0043171; GO:0070006
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6Q4G3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6Q4G3}.
| null |
TRANSMEM 14..34; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"
|
PF11838;PF01433;PF17900;
|
IPR045357;IPR042097;IPR024571;IPR034016;IPR001930;IPR050344;IPR014782;IPR027268;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Feliformia (suborder), Felidae (family), Felinae (subfamily), Acinonyx (genus)
|
LVRN TAQPEP
| false |
518 |
A0A6M7H989
|
MKRSAINDILGHTRQFFSQHDVHLPPFASFSPAQWQQLDTAAWEEVFDLKLGWDVTAFGRNNFAAHGLTLFTLRNGSAKGMPYVKCYAEKIMHVRDAQVTPMHFHWRKREDIINRGGGNLIVELWNADSNEQTADSDITVVIDGCRQKHTAGSQLRLSPGESICLPPGLYHSFWAEAGFGDVLVGEVSSVNDDDHDNHFLQPLDRYNLIDEDEPAQLVLCNEYRQFR
|
D-lyxose/D-mannose isomerase (EC 5.3.1.15) (EC 5.3.1.7)
|
Escherichia coli O157:H7
| 83,334 | 227 | 25,798 |
3D-structure;Carbohydrate metabolism;Disulfide bond;Isomerase;Manganese;Metal-binding
|
GO:0016853; GO:0046872
|
Evidence at protein level
| 5 | null | null | null |
PF07385;
|
IPR010864;IPR047581;IPR014710;IPR011051;
|
3KMH;3MPB;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Escherichia (genus), Escherichia coli (species)
|
Z5688
| false |
519 |
A0A6N3IN21
|
MEGASAECVRAEPFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGCRHLVCSSGGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNASLVRELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEVGWQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVARSLGAKTVAARTLECAKECEVLSEVVEDREAVRAVQRFLDDERMLVEPACGAALAAVYSGILGRLQTEGRLSPALDSVVVIVCGGNNISSQQLQELKTQLNCS
|
Serine dehydratase-like (Glutamate racemase) (EC 5.1.1.3) (L-serine deaminase) (EC 4.3.1.17) (L-serine dehydratase/L-threonine deaminase) (L-threonine dehydratase) (TDH) (EC 4.3.1.19)
|
Rattus norvegicus (Rat)
| 10,116 | 329 | 34,953 |
Acetylation;Isomerase;Lipid metabolism;Lyase;Pyridoxal phosphate;Reference proteome
|
GO:0003941; GO:0004794; GO:0006629; GO:0008881; GO:0030170; GO:0042802
|
Evidence at protein level
| 5 | null | null | null |
PF00291;
|
IPR050147;IPR001926;IPR036052;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Rattus (genus)
|
Sdsl Sdhl Stdhgr
| false |
520 |
A0A6P3CW73
|
MKFIIVLLLLTALTLTSIPVIEGILKRCKTYDDCKDVCKARKGKCEFGICKCMIKSGK
|
Cyclotide trypsin inhibitor TopI1
|
Tityus obscurus (Amazonian scorpion) (Tityus cambridgei)
| 1,221,240 | 58 | 6,482 |
3D-structure;Amidation;Direct protein sequencing;Disulfide bond;Knottin;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
|
GO:0004867; GO:0005576
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32787139}.
|
SIGNAL 1..23; /evidence="ECO:0000255"
| null | null | null |
6MRQ;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Chelicerata (subphylum), Arachnida (class), Scorpiones (order), Buthida (parvorder), Buthoidea (superfamily), Buthidae (family), Tityus (genus)
| null | false |
521 |
A0A6P3HVI0
|
MRNQDKRAAHKDSEPSTEVNHTASSYQGRQQETGMNLRGIDGNEPTEGSNLLNNNEKMQGTPAEPNHLQRRRQIHACPPRGLLARVITNVTMVILLWAVVWSVTGSECLPGGNLFGIIMLFYCAIIGGKLFGLIKLPTLPPLPPLLGMLLAGFLIRNVPVISDNIQIKHKWSSALRSIALSVILVRAGLGLDSNALKKLKGVCVRLSLGPCLIEACTSAVLAYFLMGLPWQWGFMLGFVLGAVSPAVVVPSMLLLQEGGYGVEKGIPTLLMAAGSFDDILAITGFNTCLGMAFSTGSTVFNVLKGVLEVIIGVVTGLVLGFFIQYFPSSDQDNLVWKRAFLVLGLSVLAVFSSTYFGFPGSGGLCTLVTAFLAGRGWASTKTDVEKVIAVAWDIFQPLLFGLIGAEVLITALRPETIGLCVATLGIAVLIRILVTYLMVCFAGFNIKEKIFISFAWLPKATVQAAIGSVALDTARSHGEKQLEGYGMDVLTVAFLSIIITAPVGSLLIGLLGPRLLQKAEQNKDEEDQGETSIQV
|
Sodium/hydrogen exchanger 9B2 (Na(+)/H(+) exchanger NHA2) (Na(+)/H(+) exchanger-like domain-containing protein 2) (NHE domain-containing protein 2) (Sodium/hydrogen exchanger-like domain-containing protein 2) (Solute carrier family 9 subfamily B member 2)
|
Bison bison bison (North American plains bison)
| 43,346 | 535 | 57,374 |
3D-structure;Cell membrane;Cell projection;Cilium;Cytoplasmic vesicle;Endosome;Flagellum;Lysosome;Membrane;Metal-binding;Mitochondrion;Reference proteome;Sodium;Synapse;Transmembrane;Transmembrane helix
|
GO:0005765; GO:0005886; GO:0006814; GO:0010008; GO:0010348; GO:0010351; GO:0015385; GO:0016323; GO:0016324; GO:0030317; GO:0030672; GO:0031966; GO:0042802; GO:0046872; GO:0055037; GO:0055038; GO:0055078; GO:0061178; GO:0072583; GO:0097228; GO:2001206
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35173351}; Multi-pass membrane protein {ECO:0000269|PubMed:35173351}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000269|PubMed:35173351}. Endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000269|PubMed:35173351}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000269|PubMed:35173351}. Lysosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000269|PubMed:35173351}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000269|PubMed:35173351}. Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000269|PubMed:35173351}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000269|PubMed:35173351}. Apical cell membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000269|PubMed:35173351}.
| null |
TRANSMEM 86..103; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 113..132; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 144..160; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 171..188; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 200..226; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 233..241; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 270..289; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 300..323; /note="Helical; Name=8"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 339..356; /note="Helical; Name=9"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 361..372; /note="Helical; Name=10"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 390..410; /note="Helical; Name=11"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 417..439; /note="Helical; Name=12"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 461..472; /note="Helical; Name=13"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"; TRANSMEM 486..508; /note="Helical; Name=14"; /evidence="ECO:0000269|PubMed:35173351, ECO:0007744|PDB:7P1I"
|
PF00999;
|
IPR006153;IPR051843;IPR038770;
|
7P1I;7P1J;7P1K;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Ruminantia (suborder), Pecora (infraorder), Bovidae (family), Bovinae (subfamily), Bison (genus), Bison bison (species)
|
SLC9B2 NHA2 NHEDC2
| false |
522 |
A0A6P6DKR7
|
MKVLCTVLVVTLLAGCRADVEPEPEVLEPAVWKSGQPWELALGRFWDYVRWVQTLSDQVQEELLSSQVTQELTVLMEDTMKAVKAYKSELEQELVPMAEDTKARLSKELQAAQARLGADMEEVRNRLAQYRNEMQAMLGQSADELRARLASHLRKLRKRMLRDAEDLQKRLAVYKDGASEGAERGVSAIRERLGSLVEQSRVRAALTGQPLQERAQAWGKQLRGRLEEVRGQAQDRLEEMREQMEEVRVKIEEQAEAFQTRLKGWFEPMVEDMRRQWADLIEKVQAAVGASTPVPSQKP
|
Apolipoprotein E (Apo-E)
|
Octodon degus (Degu) (Sciurus degus)
| 10,160 | 299 | 34,183 |
Chylomicron;Endosome;Extracellular matrix;Glycoprotein;HDL;Heparin-binding;Lipid transport;Lipid-binding;Oxidation;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal;Transport;VLDL
|
GO:0001540; GO:0001937; GO:0002021; GO:0005543; GO:0005783; GO:0005794; GO:0005886; GO:0006641; GO:0006707; GO:0006874; GO:0006898; GO:0006979; GO:0007186; GO:0007616; GO:0008201; GO:0010467; GO:0010544; GO:0010629; GO:0010875; GO:0010877; GO:0010976; GO:0010977; GO:0015909; GO:0016209; GO:0017038; GO:0019068; GO:0019899; GO:0031012; GO:0031175; GO:0032438; GO:0032489; GO:0032805; GO:0033344; GO:0033700; GO:0034360; GO:0034361; GO:0034362; GO:0034363; GO:0034364; GO:0034372; GO:0034374; GO:0034375; GO:0034380; GO:0034382; GO:0034384; GO:0034447; GO:0035641; GO:0038060; GO:0042158; GO:0042159; GO:0042311; GO:0042470; GO:0042632; GO:0042803; GO:0042981; GO:0042982; GO:0043083; GO:0043254; GO:0043395; GO:0043537; GO:0043691; GO:0044794; GO:0045088; GO:0045429; GO:0045541; GO:0045807; GO:0045893; GO:0046889; GO:0046911; GO:0048018; GO:0048156; GO:0048662; GO:0048844; GO:0050709; GO:0050728; GO:0050750; GO:0051044; GO:0051651; GO:0055089; GO:0060228; GO:0060999; GO:0061136; GO:0061771; GO:0070062; GO:0070326; GO:0070328; GO:0070374; GO:0071402; GO:0071813; GO:0071831; GO:0090090; GO:0090205; GO:0090209; GO:0097113; GO:0097114; GO:0097487; GO:0098978; GO:0120020; GO:0140077; GO:1900223; GO:1900272; GO:1902430; GO:1902952; GO:1902995; GO:1903002; GO:1905890; GO:1905907; GO:2000822
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P02649}. Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes. {ECO:0000250|UniProtKB:P02649}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
| null |
PF01442;
|
IPR000074;IPR050163;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Hystricomorpha (suborder), Octodontidae (family), Octodon (genus)
|
APOE
| false |
523 |
A0A6P6W6H5
|
MAIINLPVPTNSSSEVNKHNHLRSCLPSGRATFTTLSAAAMRSATMAAANVREQSGQKQQLINRRSGNYEAPLWEFDYIQSLKNEYAGDIYVSRANELKEQVKMMLDEEDMKLLDCMELVDGLERLGLAYHFEGRINRLLSSDYKAIHEGNHQRNKEDLYAAALEFRIFRQNGFNVPQDIFNDFITEDGEFDESLSEDTMGLLSLYEASFLSLEGEATLDLAREFTTKHLNNYLGKENTDQNLRILVYHALELPLRWRAPRIEARWYIDAYERSPNVNPTLLELAKIDFNIVQAIHQQDLKHVSWWWKNIRIAEKLTFIRDRIVENFFWAIGAVFEPQYGSCRRMLTKVFALITMIDDIYDVYGTLEELELFTDAVDRWDVKAIDQLPDYMRVGYLGFFNSINEMAYDALKEQGVHIVEYLRKVWADLCKAYLQEAKWYYAGYTPTVEEYLENAWVSMSVPVMLMHAYAGVTNPMNKEAMDVLDTHDIVRCSSYLLRFADDLGTSPGEMKRGDVPKLVQCYMKEAGCSEEESREHVWFLLRETWKKMNKDSEWAESPFSKTFVTAAKNFGRVALVMYQYGDGHGLHSNPEAKDRILASLFSPVPPA
|
Limonene synthase, chloroplastic (EC 4.2.3.-) (Alpha-pinene synthase, chloroplastic) (EC 4.2.3.-) (Beta-farnesene synthase, chloroplastic) (EC 4.2.3.47) (Beta-myrcene synthase, chloroplastic) (EC 4.2.3.15) (Beta-pinene synthase, chloroplastic) (EC 4.2.3.-) (Sabinene synthase, chloroplastic) (EC 4.2.3.-) (Terpinolene synthase, chloroplastic) (EC 4.2.3.113)
|
Coffea arabica (Arabian coffee)
| 13,443 | 606 | 69,977 |
Chloroplast;Lyase;Magnesium;Metal-binding;Plastid;Reference proteome;Transit peptide
|
GO:0000287; GO:0009507; GO:0016098; GO:0016102; GO:0046248; GO:0046250; GO:0050550; GO:0050551; GO:0080015
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
| null | null |
PF01397;PF03936;
|
IPR008949;IPR044814;IPR001906;IPR036965;IPR050148;IPR005630;IPR008930;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Gentianales (order), Rubiaceae (family), Ixoroideae (subfamily), Gardenieae complex (clade), Bertiereae - Coffeeae clade (clade), Coffeeae (tribe), Coffea (genus)
|
TPS1 LOC113729710
| false |
524 |
A0A6P7EFR0
|
MAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSANTETTKVTGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFDSSFSPNTGKKNAKIKTGYKREHINLGCDVDFDIAGPSIRGALVLGYEGWLAGYQMNFETAKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNKKLETAVNLAWTAGNSNTRFGIAAKYQIDPDACFSAKVNNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA
|
Non-selective voltage-gated ion channel VDAC1 (Outer mitochondrial membrane protein porin 1) (Voltage-dependent anion-selective channel protein 1) (VDAC-1)
|
Ovis aries (Sheep)
| 9,940 | 283 | 30,741 |
Acetylation;Apoptosis;ATP-binding;Cell membrane;Ion transport;Isopeptide bond;Membrane;Mitochondrion;Mitochondrion outer membrane;NAD;Nucleotide-binding;Phosphoprotein;Porin;Reference proteome;Transmembrane;Transmembrane beta strand;Transport;Ubl conjugation
|
GO:0005244; GO:0005524; GO:0005741; GO:0005886; GO:0006820; GO:0006915; GO:0008308; GO:0015288; GO:0022832; GO:0045121; GO:0046930
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P21796}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21796}. Cell membrane {ECO:0000250|UniProtKB:P21796}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21796}. Membrane raft {ECO:0000250|UniProtKB:P21796}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21796}. Note=Found in a complex with HSPA9 and VDAC1 at the endoplasmic reticulum-mitochondria contact sites. {ECO:0000250|UniProtKB:Q9Z2L0}.
| null |
TRANSMEM 26..35; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 39..47; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 54..64; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 69..76; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 80..89; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 95..104; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 111..120; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 123..130; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 137..145; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 150..158; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 163..175; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 178..185; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 189..198; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 202..211; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 218..227; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 231..238; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 242..251; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 254..263; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"; TRANSMEM 273..282; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P21796"
|
PF01459;
|
IPR023614;IPR001925;IPR027246;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Ruminantia (suborder), Pecora (infraorder), Bovidae (family), Caprinae (subfamily), Ovis (genus)
|
VDAC1
| false |
525 |
A0A7E6FSU6
|
MVKIAVIGAGVVGLSTALQVKQNFPFCSVTVVAEKFNTETTSDGAGGLFRPNFLTLSANPLESIKQWSQDTFSHFNNLFNSPEASDCGIALMSGFLLSNKEKLDMIEDISLGQSKMTAEQIAKMGFDCKHVTKVLTYTMECRRYMPWLTSKFLSLGGSMHHHRLKSLEELVGVYDVVVNCSGLGAKDLVPDPLVYPVKGQLIQVEAPWVKHFYFFEDDTYVIPNINRTSLGGIRIKNDYSTEVDPEISKSIWQRCTSRIPSLQKAKVLWEWAGLRPHRDPIRIEQDVMNFPKGTLKVVHNYGHGANGVSLSWGTAKHATRLVRQFLENDPELRSKL
|
D-aspartate oxidase (DASOX) (DASPO) (DDO) (EC 1.4.3.1)
|
Octopus vulgaris (Common octopus)
| 6,645 | 336 | 37,653 |
Direct protein sequencing;FAD;Flavoprotein;Oxidoreductase;Peroxisome;Reference proteome
|
GO:0005782; GO:0008445; GO:0019478; GO:0071949
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:Q99489}.
| null | null |
PF01266;
|
IPR006181;IPR023209;IPR006076;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Spiralia (clade), Lophotrochozoa (clade), Mollusca (phylum), Cephalopoda (class), Coleoidea (subclass), Octopodiformes (superorder), Octopoda (order), Incirrata (suborder), Octopodidae (family), Octopus (genus)
|
DDO LOC115226122
| false |
526 |
A0A7G5KET3
|
MSLSNKLAITDVDLKDKRVLIRVDFNVPLDADKKITNNQRIVGALPTIKYAIENGAKAVVLMSHLGRPDGKANPKYSLKPVATELEKLLSKSVIFAENCVGKETEEIVNKATGGQVILLENLRFHAEEEGSSKDAEGKKVKADKEKVEEFRKGLTALGDVYINDAFGTAHRAHSSMVGVDLPQKASGFLVKKELEYFAKALESPQRPFLAILGGAKVSDKIQLIDNLLPKVNSLIITGAMAFTFKKTLENVKIGNSLFDEAGSKIVGDIVEKAKKNNVKIVLPVDYVTADKFAADAKTGYATDADGIPDGYMGLDVGEKSVELYKKTIAEAKTILWNGPPGVFELEPFANATKKTLDAAVAAAQSGSIVIIGGGDTATVAAKYGAEAKLSHVSTGGGASLELLEGKVLPGVDALSSK
|
Phosphoglycerate kinase (EC 2.7.2.3)
|
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
| 332,952 | 417 | 44,369 |
ATP-binding;Cytoplasm;Glycolysis;Kinase;Magnesium;Metal-binding;Mitochondrion;Nucleotide-binding;Phosphoprotein;Reference proteome;Transferase
|
GO:0004618; GO:0005524; GO:0005739; GO:0005829; GO:0006094; GO:0006096; GO:0043531; GO:0046872; GO:0160218
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:37754565}. Mitochondrion {ECO:0000269|PubMed:37754565}. Note=Localizes to the mitochondrion when phosphorylated. {ECO:0000269|PubMed:37754565}.
| null | null |
PF00162;
|
IPR001576;IPR015911;IPR015824;IPR036043;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Aspergillus (genus), Aspergillus subgen. Circumdati (subgenus), Aspergillus flavus (species)
|
pgk1 F9C07_8361
| false |
527 |
A0A7G6KN55
|
MRLLYLLFAAVMLLFLQAVPANGSYYSTLQCRNNHGHCRRLCFHGEQWIGNCNGRHQHCCK
|
Beta-defensin 13 (CpoBD13)
|
Crocodylus porosus (Saltwater crocodile) (Estuarine crocodile)
| 8,502 | 61 | 7,095 |
3D-structure;Antibiotic;Antimicrobial;Defensin;Disulfide bond;Fungicide;Lipid-binding;Reference proteome;Secreted;Signal
|
GO:0005615; GO:0031640; GO:0031731; GO:0042056; GO:0042742; GO:0042802; GO:0050832; GO:0060326; GO:0070300
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33309943, ECO:0000305|PubMed:36859344}.
|
SIGNAL 1..21; /evidence="ECO:0000255"
| null |
PF00711;
|
IPR001855;
|
7T9Q;7T9R;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Archelosauria (clade), Archosauria (clade), Crocodylia (order), Longirostres (clade), Crocodylidae (family), Crocodylus (genus)
|
BD13
| false |
528 |
A0A7J6JXB6
|
MAAKAIQYNIKVDLHEVKDLSFREAAGEKEIVPNPYIEVTVNGVTKTTIQKTQVVSATFNTSFNFTAYLTPDEFARSYVEVAVLHKYMLIGGVGLQSAVIGKYVFSFAYVYTKSQHWIYRQWVTLRNLDQPQDETGLLLITVGVFGPGDAMPVVDETVCVVNEGERTSTDVNVKLTHYSLSVNIFKGQDIPSVAGQFSTVLEPYVKVKHGGAELQTRPLPDSNPDWLASISIPACVPCFDGNVLVELWNGQDSSTAAGTLMGTVVLDYFQLIKNDLPPRWFNFYWRPPAEGLLGAVTDMMASAELREPIAYGGRILLSASAAKVQTPLPLGVRSARPIPDPATQECVWWLDLYEMTSATGYTSELRIEIAFGPHVIKTASLEANALGTYVIGDNLGRLPEMKIFAPVDEVQVWDVMMYVCSPPATTVAAGIADISNWFSGWGGSPTATQNTPEPAETPWTRLAWVRIPYDSRQFQNGKPQWYSLRSLDGSGTDMFSVLLGMEMFPTKAGKQRAPRLEYKLARFYFRALIYEGLHLPAVGYDVFPDPYIQVELASKTLRTSTIRQTLNPSYYEAYEIEIRLPENISLAPDINVEVISESNSLLSSDVVLGSVQYPIQKVPKEWTKAPVWLQLHSKAYPRCKARVLVAFELVPAEKAEDDTYPFYDDIRPSTKEGNIRLFLVGVRLFKPITQPFVTVCFGRDVENTAEPLWSQESSAPRTGEGGNWNFLEEFTVSVSLPKRMQHHSFLEVKIQDRTQGIGGESNVDVGMAYITLNPLLPWLDSRERAESLETFRLQMLEEVLIEDAENARRSADGGLAARTGGGSFDEDATKKKEMLAAERSRKMAIPYNDPDMANLKIEEVDDYVSFKVAPRPQASRLSREGTSRDERGKAPGKSLSGMPGPVARASPGAGEETEKKGDPVAEKKEGGAQAAPPVAPSAHQREALAASPEEETYGFTPEQLNFVLADLEEDDAEEMTRDEVPYELEADFTVDDLPYLRTPIFRPTDAGVPETVGYLKYVCRVFQSTDEDEGAEMDAVCKSLIETYNSTRDLVVRAYVLAARGLVPPSGASDIQTYVWIQDSENAATLPGGLSYNIRDTGYTKKQGFKPEFNRCYTLACSLPENSIVQIAVMNMGRLTDECIGRTYLDVEDRFFNKKVEQMVIEESTPIELRTLKNEGSTVSHGSLRGFFEIMRADYAQLHPPYTLASAEPDEYQLRVVIWRVKAVPLDDNSSISLFVRTIYQLEDSSEIVKDTDTHYNSTDGTAVYNWRMVFDVLIPAQIPVLKLQIWNYALLSSTEPIGEANFDLTADFFRARKRQQHYRVPRMWVRCSHPAHKGKLRGTIEIEASILPREEAEYTPVGNGRDEPNRDPFLPAVTTNRTYIDWQQIGETVGAASSAIMSGLKWTGVWMTVAGIIALVIFVMFLLK
|
Ferlin 1 (FER1) (TgFER1)
|
Toxoplasma gondii
| 5,811 | 1,425 | 158,917 |
Cytoplasm;Endosome;Exocytosis;Golgi apparatus;Membrane;Reference proteome;Repeat;Transmembrane;Transmembrane helix
|
GO:0007009; GO:0010008; GO:0032588; GO:0045055; GO:0099500
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:39294204}; Single-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:39294204}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:39294204}. Note=In intracellular parasites localizes to the trans-Golgi-endosome network; upon egress disperses into the cytoplasm (PubMed:39294204). In extracellular parasites, localizes throughout the cytoplasm (PubMed:39294204). {ECO:0000269|PubMed:39294204}.
| null |
TRANSMEM 1404..1424; /note="Helical"; /evidence="ECO:0000255"
|
PF00168;
|
IPR000008;IPR035892;IPR037724;IPR012968;IPR037721;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Conoidasida (class), Coccidia (subclass), Eucoccidiorida (order), Eimeriorina (suborder), Sarcocystidae (family), Toxoplasma (genus)
|
TGRH88_049110
| false |
529 |
A0A7J6K7I9
|
MMFPAVAAPPRRLPGERLQRSQNPVETSWLSFRILATRGPCVTSTFLFLTVAFLGLSWVSVAVAAHAEHPEDSATNFLFSFAENSLANREPPEDSAARPSSRSGGAERRRLDSLIPGFLKRRRIFKQLRPVDEFQLREFQEASSKVKAQFFSAGHSKVTFVDRPSAALLSFLHLEEEDVPYGVVIKAIPYDAFDFYESVAEPYIHRMFDDPRKFPYVVPVLAALRSTSKRVLYLVLPLYRELPETVDEEARSLDFVLLLAEMAMAVCQLHERNLAHRDLKEDNFLVSPEGHIVVSDLATLDITDNKSFLIGTSGYMPPETRSSYLLRKGYKRSRYGEKTDVYSLGVAFRHLAFMLEGLGVQVPHRTQLAKLIKKMTSPDPEKRPLIGEVMEDPFFASVDFRLVRQRAGKHPFKKLPGADLLAERQRARLEAREKADAAAKAADNAEVPAAKSPAGKTGGAGTLSGDRDRAGSGEKPAERAEEEKGRGRGAQTHEGNHDRTDDAGREELREGPGDQKPSGEENREGGQPPGQREEQREGTGLEEGFNKEDAQES
|
Serine/threonine-protein kinase WNG2 (EC 2.7.11.1) (Rhoptry kinase family protein ROP34) (With-No-Gly-loop kinase 2)
|
Toxoplasma gondii
| 5,811 | 553 | 61,601 |
ATP-binding;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Reference proteome;Secreted;Signal;Transferase
|
GO:0004674; GO:0005524; GO:0005576; GO:0046872
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:30850550}. Secreted {ECO:0000269|PubMed:30850550}. Parasitophorous vacuole lumen {ECO:0000269|PubMed:30850550}. Note=In tachyzoites, localizes to dense granules. {ECO:0000269|PubMed:30850550}.
|
SIGNAL 1..64; /evidence="ECO:0000269|PubMed:30377279"
| null |
PF00069;
|
IPR011009;IPR050660;IPR000719;IPR008271;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Conoidasida (class), Coccidia (subclass), Eucoccidiorida (order), Eimeriorina (suborder), Sarcocystidae (family), Toxoplasma (genus)
|
ROP34 WNG2 TGRH88_030990
| false |
530 |
A0A7J6K7Y0
|
MPEQDLASGFLLRFQNARPVCLSVGSFVSFRTVQPRKMRDRGWRCVWHRMAGVGALFGIFGVLCTVEAGATVAAPQVETGPLLSVRAPRSPLHLRDVDAPEVTHASSEGSPQFESSLSQQRLRRPADRGEAHNGEEPRKDAATQTVRGYGGQSTEPPPASIVPVSSEAPQDGAEQRQASSAAESLAGLDPDAGDTGLRSQEMDEEGSGAAQDMERAHAAQPTVSTWDDAHLVQVSTSHPDMFPVDGSFSKKQEGRRERRLAVRGDDSFARGHNRDRDASNGRSILRRAPGWAKIAALATGLLVSAFGYSSYKHGGPRVALRIHKLHLKRKLPISWRRYLNNLPVLDERLFPEFEDILPWLRRGARLVKRVPHVSEALADFIGLDEETRRTGIVIKVKSSTDAEARRLVYEVNAHANMVPDNPFFLPIIGAYQGASKRAVYMILPRARADVADYVRARPYDVDVRLAAAEMVYSNYILHTHGFLHRDIKAHNYFVTFDGHVVLADFEGVGVLQQRTPVVGTRGYFAPELSRATDHTEKSDVFALGQTLKRLVKYMRPTVRVPHLRELWALTKRMTAKDPEERPTLKQVMEDPYFDGIDFERLEAKDQGVPFRGDFSIDDPDAGGKMYIPPSKEQDHEQENE
|
Serine/threonine-protein kinase WNG1 (EC 2.7.11.1) (Rhoptry kinase family protein ROP35) (With-No-Gly-loop kinase 1)
|
Toxoplasma gondii
| 5,811 | 640 | 71,272 |
ATP-binding;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Reference proteome;Secreted;Serine/threonine-protein kinase;Signal;Transferase
|
GO:0004674; GO:0005524; GO:0005576; GO:0035556; GO:0046872
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:30850550}. Secreted {ECO:0000269|PubMed:30850550}. Parasitophorous vacuole lumen {ECO:0000269|PubMed:30850550}. Note=In tachyzoites, localizes to dense granules. {ECO:0000269|PubMed:30850550}.
|
SIGNAL 1..70; /evidence="ECO:0000269|PubMed:30377279"
| null |
PF00069;
|
IPR011009;IPR000719;IPR008271;IPR050236;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Conoidasida (class), Coccidia (subclass), Eucoccidiorida (order), Eimeriorina (suborder), Sarcocystidae (family), Toxoplasma (genus)
|
ROP35 WNG1 TGRH88_033260
| false |
531 |
A0A7J6KDB0
|
MRGGTSALLHALTFSGAVWMCTPAEALPIQKSVQLGSFDKVVPSREVVSESLAPSFAVTETHSSVQSPSKQETQLCAISSEGKPCRNRQLHTDNGYFIGASCPKSACCSKTMCGPGGCGEFCSSNWIFCSSSLIYHPDKSYGGDCSCEKQGHRCDKNAECVENLDAGGGVHCKCKDGFVGTGLTCSEDPCSKRGNAKCGPNGTCIVVDSVSYTCTCGDGETLVNLPEGGQGCKRTGCHAFRENCSPGRCIDDASHENGYTCECPTGYSREVTSKAEESCVEGVEVTLAEKCEKEFGISASSCKCDNGYSGSASATSHHGKGESGSEGSLSEKMNIVFKCPSGYHPRYHAHTVTCEKIKHFALDGAGNHDTTTYVARRRYPASL
|
Micronemal protein 3
|
Toxoplasma gondii
| 5,811 | 383 | 40,528 |
Cell adhesion;Cytoplasmic vesicle;Disulfide bond;EGF-like domain;Endoplasmic reticulum;Glycoprotein;Golgi apparatus;Reference proteome;Secreted;Signal
| null |
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, microneme {ECO:0000269|PubMed:18390648, ECO:0000269|PubMed:1944419}. Secreted {ECO:0000269|PubMed:11207591}. Golgi apparatus {ECO:0000269|PubMed:18390648}. Endoplasmic reticulum {ECO:0000303|PubMed:18390648}. Note=In dividing and recently replicated parasites, MIC3 is not immediately targeted to micronemes but is retained into the secretory pathway. {ECO:0000269|PubMed:18390648}.
|
SIGNAL 1..26; /evidence="ECO:0000255"
| null |
PF12947;
|
IPR000742;IPR024731;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Conoidasida (class), Coccidia (subclass), Eucoccidiorida (order), Eimeriorina (suborder), Sarcocystidae (family), Toxoplasma (genus)
|
MIC3 TGRH88_007550
| false |
532 |
A0A7M6UMR7
|
MRYFIILLALVALGVCAPNVKQRAADQDLLNKQQDVIQLLQKISQPIPNQELQNLGASYDIESNSHQYKNPIIVMYYAGAVKAGLVQPQGTTFSNSISQLRKEVSLLYRILLGAKDYQTFLKTAAWARVHVNEGQFLKAFVAAVLTRQDTQSVIFPPVYEILPQHHLDSRVIQEAQNIAIQNTQGKNNQQNILIPVNYSALLSHDEQQLSYFTQDIGLAAYYAQVNLAGYIQEQNQQQQQQPLTQQQYQQQIVGKYLQQQAGQQDQQANIGRGAQYLYLHQQLLARYELNRLSNGLGPIKDIDYENVQSLYQPHLRGLNGLEFAGRPQNLQLQSQRNQLIQYVATLEKRLRDAIDSGNVITPQGVFLSLYQPQGMNILGDLIEGTGRSVNPRYYGSLQAAARKLLGNAPEVENIWDYTPSSLELGEVAVHDPVFYQLYKKVMNLYQQYQQSLPVYQYNDLILPGVTIQNVDVSQLVTLFTDFYVDLDAVTGHQSQQQQEEQTQSRVRAHLKRLDHQPYQYKIAVHSEQNVPGAVVRVFLGPKHDHQGRPISISKNQHLFVELDQFIQNLHAGENTIIRNSQQAPGQSPDWPSTSQIQRGVNAAIRSQEPFYITEPHQIFSFPARLSLPKGQPQGFPLQFLVVISSSNPLNVPYGPVIPEQSLTYQDQQYQVVSVEQYQQLKEQGQISQVGGGIQQNVEVLPENLVNAQQQVQAVRNYYANLYTKYHGQYPNTQIQNPVGQGQDMTYSVQGVGVVNAGGWLGQQGNSWSQQQVQQAQQVQQQMQAAMAAVQQSQQRHQHAAQMIYGHQQSHHGLHINSSPSSVQSGQQQQSVLQGLGVQGVQQGVQGVQTAQGVQGVQGVQGVQGVQGVQGVQGVPGLLQGVQQVFGQGVQGMNVPYGMQRGQSGGQTWSNSQVQGVAVPGSGIVASGQQHAGGWQSIYAQPQTVQDQIVSEYYQNKPISEVIGGAISLDGKPLGFPLDRPLSLGALSVPNIFVKDVLVFHQGQPTNDITQ
|
Hexamerin 110 (High Glx storage protein)
|
Apis mellifera (Honeybee)
| 7,460 | 1,010 | 112,188 |
Cytoplasm;Direct protein sequencing;Glycoprotein;Nucleus;Reference proteome;Secreted;Signal;Storage protein
|
GO:0005615; GO:0005634; GO:0005730; GO:0030139; GO:0045735
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26466725}. Nucleus {ECO:0000269|PubMed:26466725, ECO:0000269|PubMed:26954256, ECO:0000269|PubMed:34309096}. Nucleus, nucleolus {ECO:0000269|PubMed:26954256}. Cytoplasm {ECO:0000269|PubMed:26466725, ECO:0000269|PubMed:26954256}. Cytoplasmic granule {ECO:0000269|PubMed:26466725}. Note=Localizes to the nucleus in a punctate pattern closely associated with chromatin (PubMed:26466725). Localizes in foci within the cytoplasm of some cells of the fat body; these are probably cytoplasmic granules formed by endocytosis of hexamerins (PubMed:26466725). Colocalizes with RNA and the nucleolus marker fibrillarin in the nucleus (PubMed:26954256). Localizes to the nucleolus in the precursors of oocytes, nurse cells and follicle cells during oogenesis; this localization is maintained in differentiated nurse cells and follicle cells but not in the oocyte (PubMed:26954256). Punctate localization in the nucleus of brain cells (PubMed:34309096). {ECO:0000269|PubMed:26466725, ECO:0000269|PubMed:26954256, ECO:0000269|PubMed:34309096}.
|
SIGNAL 1..16; /evidence="ECO:0000269|PubMed:9692239"
| null |
PF03723;PF00372;PF03722;
|
IPR008922;IPR013788;IPR000896;IPR005203;IPR037020;IPR005204;IPR036697;IPR014756;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Hymenoptera (order), Apocrita (suborder), Aculeata (infraorder), Apoidea (superfamily), Anthophila (clade), Apidae (family), Apinae (subfamily), Apini (tribe), Apis (genus)
|
Hex110 551648
| false |
533 |
A0A7U2MSD6
|
MGQTLSEPVVDKTSSEGEDDCCIYGVSAMQGWRISMEDAHAAVLDLHAKYTSPEETSTDPAKRLAFFGVYDGHGGDKVALFAGENVHKIVAKQDSFAKGDIEQALKDGFLATDRAILEDPKYEEEVSGCTAAVSVISKHKIWVANAGDSRSVLGVKGRAKPLSFDHKPQNEGEKARISAAGGFVDFGRVNGNLALSRAIGDFEFKKSPELAPEQQIVTAYPDVTVHELSDDDEFLVIACDGIWDCQSSQAVVEFVRRGIAAKQELYRICENMMDNCLASNSETGGVGCDNMTMIIIGLLNGRTKEECGDAAEFRGPGIRNQFEENPDDYDMENDRARGFSVRSGRIILLGDGTELVPDQNDEELFDQTEEDRDLPSQVQRELPDSARNEREGTPGPQSKTDATSKSEEGSSASTSESTVTPAGSSTSGAPEKSTS
|
Protein phosphatase 2C homolog 2 (PP2C-2) (EC 3.1.3.16)
|
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
| 332,952 | 435 | 46,987 |
Cytoplasm;Hydrolase;Magnesium;Manganese;Metal-binding;Nucleus;Protein phosphatase;Reference proteome
|
GO:0004722; GO:0005634; GO:0005737; GO:0046872; GO:1903215
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:37754565}. Nucleus {ECO:0000269|PubMed:37754565}. Note=Nuclear following induction of autophagy and DNA damage. {ECO:0000269|PubMed:37754565}.
| null | null |
PF00481;
|
IPR015655;IPR000222;IPR036457;IPR001932;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Aspergillus (genus), Aspergillus subgen. Circumdati (subgenus), Aspergillus flavus (species)
|
ptc2 F9C07_2102428
| false |
534 |
A0A7U2QYM2
|
MASENNKRKASEEALSPDSQLQSKKARTDSPEREPKSEGGPLGKPPLRIVPFPEKPAVLEERRGEIEFRVVNNDGSRDSFVVLTGLKCIFQKQLPKMPKDYIARLVYDRSHLSIAIVKHPLEVVGGITYRPFNSRRFAEIVFCAISSDQQVKGYGAHLMSHLKDYVKATSPIMHFLTYADNYAIGYFKKQGFTKEITLDKSIWMGYIKDYEGGTIMQCTMLPKIRYLEIGRMLLKQKEAVHAKIRAFSRSHIIHAPPKEWKNGACKIDPLSIPAIKQSGWSPDMDELARQPRHGPNYNQLLHLLNDMQNHSAAWPFTQPVNRDEVPDYYEVIKEPMDLSTMEEKHEKDMYPTPQDFIKDAMLIFDNCRRYNNENTPYAKSANKLEKFMWQQIRNIPEWSVST
|
Histone acetyltransferase gcnE (EC 2.3.1.48) (Benzoyltransferase gcnE) (EC 2.3.1.-)
|
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
| 332,952 | 402 | 46,366 |
Activator;Acyltransferase;Bromodomain;Chromatin regulator;Nucleus;Reference proteome;Transcription;Transcription regulation;Transferase
|
GO:0000124; GO:0000775; GO:0003712; GO:0005634; GO:0005829; GO:0010515; GO:0032968; GO:0036408; GO:0043992; GO:0043993; GO:0045815; GO:0046695; GO:0070577; GO:0140068; GO:0140566; GO:0140671
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03330}.
| null | null |
PF00583;PF00439;
|
IPR016181;IPR001487;IPR036427;IPR018359;IPR037800;IPR000182;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Aspergillus (genus), Aspergillus subgen. Circumdati (subgenus), Aspergillus flavus (species)
|
gcnE F9C07_11133
| false |
535 |
A0A7U9P668
|
MRKEAIHHRSTDNFAYAYDSETLHLRLQTKKNDVDHVELLFGDPYEWHDGAWQFQTMPMRKTGSDGLFDYWLAEVKPPYRRLRYGFVLRAGGEKLVYTEKGFYHEAPSDDTAYYFCFPFLHRVDLFQAPDWVKDTVWYQIFPERFANGNPAISPKGARPWGSEDPTPTSFFGGDLQGIIDHLDYLADLGITGIYLTPIFRAPSNHKYDTADYFEIDPHFGDKETLKTLVKRCHEKGIRVMLDAVFNHCGYEFGPFQDVLKNGAASRYKDWFHIREFPLQTEPRPNYDTFAFVPQMPKLNTAHPEVKRYLLDVATYWIREFDIDGWRLDVANEIDHQFWREFRQAVKALKPDVYILGEIWHDAMPWLRGDQFDAVMNYPLADAALRFFAKEDMSASEFADRLMHVLHSYPKQVNEAAFNLLGSHDTPRLLTVCGGDVRKVKLLFLFQLTFTGSPCIYYGDEIGMTGGNDPECRKCMVWDPEKQNKELYEHVKQLIALRKQYRALRRGDVAFLAADDEVNHLVYAKTDGNETVMIIINRSNEAAEIPMPIDARGKWLVNLLTGERFAAEAETLCVSLPPYGFVLYAVESW
|
Cyclomaltodextrinase (CDase) (EC 3.2.1.54) (Cyclomaltodextrin hydrolase, decycling)
|
Geobacillus thermopakistaniensis (strain MAS1)
| 1,408,282 | 588 | 68,157 |
Carbohydrate metabolism;Glycosidase;Hydrolase
|
GO:0042802; GO:0042803; GO:0047798; GO:0051678
|
Evidence at protein level
| 5 | null | null | null |
PF00128;PF02903;PF16657;
|
IPR006047;IPR004185;IPR013780;IPR017853;IPR013783;IPR032091;IPR045857;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Anoxybacillaceae (family), Geobacillus (genus)
|
T260_08735
| false |
536 |
A0A858E6N7
|
MKPLPSTNGKVNGNGKHHDSSLSSTSSTSSSSSSDTQFNISDRYGDFLHRLDTLDTWPKSNEQILLEPYTYLNNIPGKEIRSMMIDAFNHWLQIPRPALEIIKKIVGQLHTASLLMDDVEDDSDLRRGVPVTHKIYGIPQTINTANYVYFLAYQELSKLKPCLSSNASTDLWSLVNDELLQLHRGQGMDLYWRDSLTCPTEEEYLQMVNNKTGGLFRIAIKLMIALSPLTETPDYLPLVNLVGIIFQIRDDLLNLSSVYTKNKGFCEDLTEGKFSFPIVHSIRADSSNHQLMNILRQKPTDIGTKTFAVSYMKDQTKSLQYTREVLTCLEEQAIEEVTRLGGNPALESIFELMHVLPSPPATDQH
|
Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
|
Melampsora lini (Rust fungus)
| 5,261 | 365 | 41,213 |
Isoprene biosynthesis;Lyase;Magnesium;Metal-binding;Multifunctional enzyme;Transferase
|
GO:0004659; GO:0008299; GO:0016829; GO:0046872
|
Evidence at protein level
| 5 | null | null | null |
PF00348;
|
IPR008949;IPR000092;IPR033749;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Pucciniomycotina (subphylum), Pucciniomycetes (class), Pucciniales (order), Melampsoraceae (family), Melampsora (genus)
|
GGDPS
| false |
537 |
A0A8C0N8E3
|
MSTRSVSSSSYRRMFGGPGTGSRPSSTRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGAYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQDQHVQIDMDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRIALPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE
|
Vimentin
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 466 | 53,598 |
Acetylation;Cell membrane;Coiled coil;Cytoplasm;Cytoskeleton;Glycoprotein;Intermediate filament;Isopeptide bond;Membrane;Nucleus;Phosphoprotein;Reference proteome;S-nitrosylation;Ubl conjugation
|
GO:0005737; GO:0005882; GO:0005886; GO:0010634; GO:0016363
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19386766}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus matrix {ECO:0000250|UniProtKB:P31000}. Cell membrane {ECO:0000250|UniProtKB:P20152}.
| null | null |
PF00038;PF04732;
|
IPR018039;IPR039008;IPR006821;IPR050405;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
VIM
| false |
538 |
A0A8C0NGY6
|
MDPGPPPPAAPPQAQGPPSAPPPPGQAPPSAPGPPAPPGSQAAPQAPPAGHQIVHVRGDSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPEPKAHSRQASTDAGTAGALTPQHVRAHSSPASLQLGAVSPGTLTPTGVSSGPAAAPSAQHLRQSSFEIPDDVPLPAGWEMAKTSSGQRYFLNHIDQTTTWQDPRKAMLSQMSVTAPTSPPVQQSMMTSASGPLPDGWEQAMTQDGEIYYINHKNKTTSWLDPRLDPRFAMNQRISQSAPVKQPPPLAPQSPPGVLGGGGSSQQQQMRLQQLQMEKERLRLKQQELLRQVRPQAMRNISPSTANSPKCQELALRSQLPTLEQDGGTPNPVPSPGMSQELRTMTTSGSDPFLNSGTYHSRDESTDSGLSMSSYSVPRTPDDFLNSVDEMDTGDTINQSTLPSQQNRFPDYLEAIPGTNVDLGTLEGDGMNIEGEELMPSLQEALSSDILNDMESVLAATKLDKESFLTWL
|
Transcriptional coactivator YAP1 (Yes-associated protein 1)
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 506 | 54,151 |
Activator;Cell junction;Cytoplasm;Nucleus;Phosphoprotein;Reference proteome;Repeat;Repressor;Tight junction;Transcription;Transcription regulation;Ubl conjugation
|
GO:0000122; GO:0000902; GO:0000978; GO:0001570; GO:0001674; GO:0001829; GO:0001894; GO:0002067; GO:0003015; GO:0003143; GO:0003682; GO:0003713; GO:0003714; GO:0005634; GO:0005654; GO:0005737; GO:0005739; GO:0005829; GO:0005886; GO:0005923; GO:0006974; GO:0010628; GO:0010629; GO:0010837; GO:0030216; GO:0030307; GO:0030857; GO:0030903; GO:0032570; GO:0035019; GO:0035265; GO:0035329; GO:0042060; GO:0045599; GO:0045669; GO:0045747; GO:0045944; GO:0048339; GO:0048368; GO:0050673; GO:0050679; GO:0050767; GO:0060045; GO:0060070; GO:0060449; GO:0060487; GO:0060576; GO:0061026; GO:0065003; GO:0070064; GO:0070102; GO:0070160; GO:0071300; GO:0071480; GO:0072091; GO:0072307; GO:0090263; GO:0097191; GO:0140297; GO:0140552; GO:1900182; GO:1902018; GO:1902459; GO:1903703; GO:1904036; GO:2000737; GO:2001237
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21205866, ECO:0000269|PubMed:33730553}. Nucleus {ECO:0000269|PubMed:33730553}. Cell junction, tight junction {ECO:0000269|PubMed:21205866}. Note=Both phosphorylation and cell density can regulate its subcellular localization (By similarity). Phosphorylation sequesters it in the cytoplasm by inhibiting its translocation into the nucleus (By similarity). At low density, predominantly nuclear and is translocated to the cytoplasm at high density (By similarity). PTPN14 induces translocation from the nucleus to the cytoplasm (By similarity). In the nucleus, phosphorylation by PRP4K induces nuclear exclusion (By similarity). Localized mainly to the nucleus in the early stages of embryo development with expression becoming evident in the cytoplasm at the blastocyst and epiblast stages (By similarity). Localizes to the cytoplasm and tight junctions following interaction with AMOT (By similarity). Localizes to tight junctions following interaction with AMOTL2 (PubMed:21205866). Translocates to the nucleus in the presence of SNAIL1 (PubMed:33730553). {ECO:0000250|UniProtKB:P46937, ECO:0000250|UniProtKB:P46938, ECO:0000269|PubMed:21205866, ECO:0000269|PubMed:33730553}.
| null | null |
PF15238;PF00397;
|
IPR053819;IPR001202;IPR036020;IPR051583;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
YAP1
| false |
539 |
A0A8C0TYJ0
|
MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCIDRSKQSEPIQPVNTWEISSLPSTTVTSETLPSSLSPSVEKYRYQDEDTPPQEHISPQITNEVIGPELVHVSEKNLSEIENVHGFVSHSHISPIKPTEAVPPSSPTVPVIPVLPVPAENTVILPTIPQANPPPVLVNTDSLETSTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIIAGGAAAQDGRLRVNDCILRVNEVDVRDVTHSKAVEALKEAGSIVRLYVKRRKPVSEKIMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAVNSVCLEEVTHEEAVTALKNTSDFVYLKVAKPTSMYMNDGYAPPDITNSSSQPVDNHVSPSSYLGHTPASPARYSPVSKAMLGDDEITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRTASHEQAAAALKNAGQAVTIVAQYRPEEYSRFEAKIHDLREQMMNSSISSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVTPDGESDEVGVIPSKRRVEKKERARLKTVKFNSKTRGDKGQSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQHITSNASDSESSYRGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCILDVSGNAIKRLQIAQLYPISIFIKPKSMENIMEMNKRLTEEQARKTFERAMKLEQEFTEHFTAIVQGDTLEDIYNQVKQIIEEQSGPYIWVPAKEKL
|
Disks large homolog 1 (Synapse-associated protein 97) (SAP-97) (SAP97)
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 927 | 103,441 |
Cell junction;Cell membrane;Cytoplasm;Endoplasmic reticulum;Membrane;Phosphoprotein;Reference proteome;Repeat;SH3 domain;Synapse;Ubl conjugation
|
GO:0000122; GO:0001658; GO:0001771; GO:0001772; GO:0001935; GO:0002088; GO:0005604; GO:0005634; GO:0005789; GO:0005794; GO:0005874; GO:0005923; GO:0007268; GO:0008284; GO:0008360; GO:0009898; GO:0010669; GO:0014069; GO:0015459; GO:0016323; GO:0016324; GO:0016328; GO:0019900; GO:0019902; GO:0030041; GO:0030432; GO:0030838; GO:0030866; GO:0030953; GO:0031253; GO:0031579; GO:0031594; GO:0031641; GO:0033268; GO:0035748; GO:0042098; GO:0042130; GO:0042383; GO:0042982; GO:0043219; GO:0043268; GO:0043491; GO:0043622; GO:0044325; GO:0045121; GO:0048471; GO:0048608; GO:0048704; GO:0048745; GO:0050680; GO:0051660; GO:0051898; GO:0060022; GO:0060090; GO:0070373; GO:0070830; GO:0072659; GO:0097016; GO:0097025; GO:0097060; GO:0098609; GO:0098911; GO:0098915; GO:0098919; GO:0098978; GO:0099645; GO:1902473; GO:1903078; GO:1903286; GO:1903753; GO:1903764; GO:2000134
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21849460}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q12959}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q12959}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q62696}. Postsynaptic density {ECO:0000250|UniProtKB:Q62696}. Synapse {ECO:0000250|UniProtKB:Q62696}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q12959}. Apical cell membrane {ECO:0000250|UniProtKB:Q12959}. Cell junction {ECO:0000250|UniProtKB:Q12959}. Cytoplasm {ECO:0000250|UniProtKB:Q12959}. Note=Colocalizes with EPB41 at regions of intercellular contacts. Basolateral in epithelial cells (By similarity). May also associate with endoplasmic reticulum membranes. Mainly found in neurons soma, moderately found at postsynaptic densities (By similarity). {ECO:0000250|UniProtKB:Q12959, ECO:0000250|UniProtKB:Q62696}.
| null | null |
PF00625;PF09058;PF10608;PF00595;PF10600;PF00018;
|
IPR019583;IPR016313;IPR019590;IPR008145;IPR008144;IPR020590;IPR015143;IPR004172;IPR036892;IPR027417;IPR001478;IPR036034;IPR036028;IPR001452;IPR050614;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
DLG1
| false |
540 |
A0A8C2LVE3
|
MGLLRIMMPPKLQLLAVVAFAVAMLFLENQIQKLEESRAKLERAIARHEVREIEQRHTMDGPRQDAAVDEEEDIVIIYNRVPKTASTSFTNIAYDLCAKNRYHVLHINTTKNNPVMSLQDQVRFVKNITTWNEMKPGFYHGHISYLDFAKFGVKKKPIYINVIRDPIERLVSYYYFLRFGDDYRPGLRRRKQGDKKTFDECVAEGGSDCAPEKLWLQIPFFCGHSSECWNVGSRWAMDQAKYNLINEYFLVGVTEELEDFIMLLEAALPRFFRGATDLYRTGKKSHLRKTTEKKLPTKQTIAKLQQSDIWKMENEFYEFALEQFQFIRAHAVREKDGDLYILAQNFFYEKIYPKSN
|
Heparan sulfate 2-O-sulfotransferase 1 (EC 2.8.2.-) (2-O-sulfotransferase) (2-OST) (2OST) (HS 2-O-sulfotransferase) (Heparan sulfate 2-sulfotransferase)
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
| 10,029 | 356 | 41,831 |
Coiled coil;Disulfide bond;Glycoprotein;Golgi apparatus;Membrane;Signal-anchor;Transferase;Transmembrane;Transmembrane helix
|
GO:0000139; GO:0004394; GO:0010467; GO:0015012; GO:0030202; GO:0050656; GO:0060676
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8R3H7}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8R3H7}.
| null |
TRANSMEM 12..28; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"
|
PF03567;
|
IPR007734;IPR027417;IPR005331;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Cricetidae (family), Cricetinae (subfamily), Cricetulus (genus)
|
HS2ST1 LOC100760748
| false |
541 |
A0A8C2MDK8
|
MAALVVSETAEPGSRVGPGRGRISRGRLANQIPPEILNNPQLQAAVQALPSNYNFEIPKTIWRIQQAQAKKVALQMPEGLLLFACTIVDILERFTKAEVMVMGDVTYGACCVDDFTARALGVDFLVHYGHSCLVPMDTSVQDFRVLYVFVDIRIDTAHLLDSVRLTFAPGSSLALVSTIQFVSTLQAAAQELKAEYHVSVPQCKPLSPGEILGCTSPRLPKEVEAVVYLGDGRFHLESVMIANPNVPAYRYDPYSKVLSREHYDHQRMQATRQEAIAAARSAKTWGLILGTLGRQGSPKILEHLESRLKGLGLPFVRLLLSEIFPSKLSLLPMVDVWVQVACPRLSIDWGSAFPKPLLTPYEAAVALKDISWQQPYPMDFYAGNSLGPWTVNHGRDPGPRGLGQPASGKVQQGFRGQSPAPACEGCSCADLKAALPAS
|
2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 (EC 2.5.1.108) (Diphthamide biosynthesis protein 1) (Diphtheria toxin resistance protein 1) (Ovarian cancer-associated gene 1 protein homolog) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1)
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
| 10,029 | 438 | 47,771 |
Cytoplasm;Iron;Iron-sulfur;Metal-binding;Nucleus;Phosphoprotein;S-adenosyl-L-methionine;Transferase
|
GO:0005654; GO:0005737; GO:0017183; GO:0030054; GO:0046872; GO:0048144; GO:0051539; GO:0090560; GO:0120513
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5NCQ5}. Cytoplasm {ECO:0000250|UniProtKB:Q5NCQ5}. Note=Punctate, primarily perinuclear localization. {ECO:0000250|UniProtKB:Q5NCQ5}.
| null | null |
PF01866;
|
IPR016435;IPR042263;IPR042264;IPR042265;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Cricetidae (family), Cricetinae (subfamily), Cricetulus (genus)
|
DPH1 OVCA1
| false |
542 |
A0A8H8CMW1
|
MSTEQFVLPDLLESCPLKDATNPYYKEAAAESRAWINGYDIFTDRKRAEFIQGQNELLCSHVYWYAGREQLRTTCDFVNLLFVVDEVSDEQNGKGARETGQVFFKAMKYPDWDDGSILAKVTKEFMARFTRLAGPRNTKRFIDLCESYTACVGEEAELRERSELLDLASYIPLRRQNSAVLLCFALVEYILGIDLADEVYEDEMFMKAYWAACDQVCWANDIYSYDMEQSKGLAGNNIVSILMNENGTNLQETADYIGERCGEFVSDYISAKSQISPSLGPEALQFIDFVGYWMIGNIEWCFETPRYFGSRHLEIKETRVVHLRPKEVPEGLSSEDCIESDDE
|
Cubebol synthase cubA (EC 4.2.3.-) (EC 4.2.3.127) (EC 4.2.3.128) (EC 4.2.3.129) (EC 4.2.3.91) (EC 4.2.3.98) (Sesquiterpene synthase cubA)
|
Psilocybe cubensis (Psychedelic mushroom) (Stropharia cubensis)
| 181,762 | 343 | 39,317 |
Lyase;Magnesium;Metal-binding;Reference proteome
|
GO:0008299; GO:0010333; GO:0046872
|
Evidence at protein level
| 5 | null | null | null |
PF19086;
|
IPR008949;IPR034686;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Agaricomycotina (subphylum), Agaricomycetes (class), Agaricomycetidae (subclass), Agaricales (order), Agaricineae (suborder), Strophariaceae (family), Psilocybe (genus)
|
cubA JR316_004838
| false |
543 |
A0A8I3NFE2
|
MASACGAPGPGGAGPGGALGSPAPAWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCVLYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEREREPDPPDDRDVSDGEDEKPPLPPRSGSTSISAPVGPGSPPAAPETPTTPAAESAPNGLSTVSHEYLKGSYGLDLEAVRGGASNLPHLTRTLATSCRRLHSEVDKVLAGLEILSKVFDQQSSPMVTRLLQQQNPAQTGEQELESLVLKLSVLKDFLSGIQKKALKVLQDMSSTAPPAPPQPAIRKAKTVPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFTHDRIRQLIKSQRVQNKLGVVFEKEKDRTQRKDFIFVSARKREAFCQLLQLMKNKHSKQDEPDMISVFIGSWNMGSVPPPKNVTSWFTSKGLGKTLDEVTVTIPHDIYVFGTQENSVGDREWLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTARRNQNYLDILRLLSLGDRQLSAFDISLRFTHLFWFGDLNYRLDMDIQEILNYISRKEFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPTYRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSYPETHIICNSYGCTDDIVTSDHSPVFGTFEVGVTSQFISKKGLSKTSDQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKSFENDAQSSDNINFLKVQWSSRQLPTLKPILADIEYLQDQHLLLTVKSMDGYESYGECVVALKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDEAGAKSKAPSVSRGSQDPRSGNRKPAPAEASCPLSKLFEEPEKPPPTGRPPAPPRAASREEPLTPRLKAEGAPEPEGVAAPPPKNSFNNPAYYVLEGVPHQLLPPEPPSPARAPVPPATKNKVAITVPAPQLGRHRPPRVGEGSSSDEESGGTLPPPDFPPPPLPDSAIFLPPSLDPLPGPVVRGRSGGEARGPPPPKAHPRPPLPPGPSPTSTFLGEVASGDDRSCSVLQMAKTLSEVDYAPAGPGRSVLLPGPLELQPPRGLPSDYGRPLSFPPPRIRESIQEDLAEEAPCPQGGRAGGLGEAGMGAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK
|
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (Protein 51C) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 1,264 | 138,815 |
Actin-binding;Cell membrane;Cell projection;Cytoplasm;Cytoskeleton;Hydrolase;Immunity;Lipid metabolism;Membrane;Nucleus;Phosphoprotein;Reference proteome;SH2 domain;SH3-binding
|
GO:0000132; GO:0000922; GO:0001958; GO:0002376; GO:0003779; GO:0004445; GO:0005794; GO:0005829; GO:0006006; GO:0006661; GO:0006897; GO:0006915; GO:0007015; GO:0008285; GO:0009791; GO:0009925; GO:0010467; GO:0010629; GO:0016607; GO:0017124; GO:0030027; GO:0030175; GO:0032868; GO:0032880; GO:0042169; GO:0043491; GO:0043569; GO:0046856; GO:0050776; GO:0070371; GO:0097178; GO:0110053
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15357}. Membrane {ECO:0000250|UniProtKB:O15357}; Peripheral membrane protein. Cell projection, filopodium {ECO:0000250|UniProtKB:O15357}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O15357}. Basal cell membrane {ECO:0000269|PubMed:27926875}. Nucleus {ECO:0000250|UniProtKB:D7PF45}. Nucleus speckle {ECO:0000250|UniProtKB:D7PF45}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:27926875}. Note=Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type (By similarity). Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B). Tyrosine phosphorylation may also participate in membrane localization. Insulin specifically stimulates its redistribution from the cytosol to the plasma membrane. Recruited to the membrane following M-CSF stimulation. In activated spreading platelets, localizes with actin at filopodia, lamellipodia and the central actin ring (By similarity). {ECO:0000250|UniProtKB:O15357, ECO:0000250|UniProtKB:Q6P549}.
| null | null |
PF24147;PF24150;PF22669;PF00536;PF00017;
|
IPR036691;IPR000300;IPR001660;IPR013761;IPR000980;IPR036860;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
INPPL1 SHIP2
| false |
544 |
A0A8I3NQW8
|
MSTNNMSDPRRPNKVLRYKPPPSECNPALDDPTPDYMNLLGMIFSMCGLMLKLKWCAWVAVYCSFISFANSRSSEDTKQMMSSFMLSISAVVMSYLQNPQPMTPPW
|
PAT complex subunit Asterix (Protein WDR83OS homolog)
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 106 | 12,068 |
3D-structure;Acetylation;Chaperone;Endoplasmic reticulum;Membrane;Reference proteome;Transmembrane;Transmembrane helix
|
GO:0005789; GO:0044183; GO:0045048; GO:0101031; GO:0160063; GO:0160064
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:36261528}; Multi-pass membrane protein {ECO:0000269|PubMed:36261528}.
| null |
TRANSMEM 33..51; /note="Helical"; /evidence="ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TM3, ECO:0007744|PDB:7TUT"; TRANSMEM 53..70; /note="Helical"; /evidence="ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TM3, ECO:0007744|PDB:7TUT"; TRANSMEM 75..95; /note="Helical"; /evidence="ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TM3, ECO:0007744|PDB:7TUT"
|
PF03669;
|
IPR005351;
|
7TM3;7TUT;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
WDR83OS
| false |
545 |
A0A8I3P7X4
|
MKASLAFCVVLLVFGSVSEAKFDDFEDEEDIVEYDDNDFAEFEDVTEDSVTESPQRVITTEDDEDETTVELEGQDENQEGDFEDADTQEGDTESEPYDDEEFEGYEDKPDTSSSKNKDPITIVDVPAHLQNSWESYYLEILMVTGLLAYIMNYIIGKNKNSRLAQAWFNTHRELLESNFTLVGDDGTNKEATSTGKLNQENEHIYNLWCSGRVCCEGMLIQLRFLKRQDLLNVLARMMRPVSDQVQIKVTMNDEDMDTYVFAVGTRKALVRLQKEMQDLSEFCSDKPKSGAKYGLPDSLAILSEMGEVTEGMMDTKMVHFLTHYADKIESVHFSDQFSGPKIMQEEGQPLKLPDTKRTLLFTFNVPGSGNTYPKDMEALLPLMNMVIYSIDKAKKFRLNREGKQKADKNRARVEENFLKLTHVQRQEAAQSRREEKKRAEKERIMNEEDPEKQRRLEEAALRREQKKLEKKQMKMKQIKVKAM
|
PAT complex subunit CCDC47 (Coiled-coil domain-containing protein 47)
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 483 | 55,732 |
3D-structure;Chaperone;Coiled coil;Endoplasmic reticulum;Glycoprotein;Membrane;Reference proteome;Signal;Transmembrane;Transmembrane helix
|
GO:0005509; GO:0005783; GO:0005789; GO:0006983; GO:0009791; GO:0030867; GO:0032469; GO:0036503; GO:0043022; GO:0044183; GO:0101031; GO:0160063; GO:0160064
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:36261528}; Single-pass type I membrane protein {ECO:0000269|PubMed:36261528}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9D024}; Single-pass type I membrane protein {ECO:0000269|PubMed:36261528}.
|
SIGNAL 1..20; /evidence="ECO:0000255"
|
TRANSMEM 136..156; /note="Helical"; /evidence="ECO:0000305|PubMed:36261528, ECO:0007744|PDB:7TM3, ECO:0007744|PDB:7TUT"
|
PF07946;
|
IPR012879;
|
7TM3;7TUT;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
CCDC47
| false |
546 |
A0A8I3PDQ1
|
MWARNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPIQETPSGQDQPTSGLMHQTFGQQKLYQVPNPHSAPRDTIYQVPPSYQHQGIYQVPTSHGIQEQDVYQVPPSVQRSIGAANGPHLSKKVVTPVRTGQGYVYEYPSRHQKDIYDIPPSHTTQGVYDIPPSSVKVPVFSLPVGEIKPQGVYDIPPTKGLYAIPPSACRDEAGLREKEYDFPPPMRQAGRLDVRPEGVYDIPPTSTKPTGKDLHIKYNCDAPGAAELATRRHQSVLLNHAPSQLGQSPGAQNDAYDVPRGVQFLEPPAETSEKANPEERDGVYDVPLHNPPDAKGSQDVVDGMNRLSFSSTGSTRSNMSTSSTTSKESSVSASPSQDKRLLLDPDTAIERLHRLQQTLEVGVSSLMALVTTDWRCYGYMDRHINEIRTSVDKVELFVRDYLHFARGAVANASCLPELTLHNKMKRELQRVEDSHQILSQTSHDLNECSWSLNILAVNKPQNKCDDLDRFVMVAKTVPDDAKQLTTTINTNAEALFRPGPGSSHVKSGSENIMNSTEYPHAASQMPLLHPGDHKAQGLNKPLPPSLGKDQPPDCSSSDGSERSWMDDYDYVHLQGKEEFERQQKELLEKENIIKQNKLQLEHHQLSQFQLLEQEITKPVENDISKWKPSQSLPTTNSSVGAQDRQLLCFYYDQCETHYISLLNAIDALFSCVSSAQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVAAQDICHKVMNSSNQLCEQLKTIVMATKMAALHYPSTTALQEMVHQVTDLSRNAQLFKRSLLEMATF
|
Enhancer of filamentation 1 (CRK-associated substrate-related protein) (CAS-L) (Neural precursor cell expressed developmentally down-regulated protein 9) (NEDD-9) (p105)
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 834 | 92,936 |
Alternative splicing;Cell adhesion;Cell cycle;Cell division;Cell junction;Cell membrane;Cell projection;Cytoplasm;Cytoskeleton;Golgi apparatus;Growth regulation;Membrane;Mitosis;Nucleus;Phosphoprotein;Reference proteome;SH3 domain;Ubl conjugation
|
GO:0000922; GO:0001772; GO:0005654; GO:0005737; GO:0005794; GO:0005829; GO:0005925; GO:0005938; GO:0007155; GO:0007169; GO:0007611; GO:0016323; GO:0016477; GO:0030027; GO:0030336; GO:0032956; GO:0036064; GO:0045672; GO:0051301; GO:0061523; GO:0072686; GO:0097021; GO:0140131; GO:1900026; GO:1902952; GO:1903829; GO:1990782; GO:2000522
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14511}. Nucleus {ECO:0000250|UniProtKB:Q14511}. Golgi apparatus {ECO:0000250|UniProtKB:Q14511}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q14511}. Cytoplasm {ECO:0000250|UniProtKB:Q14511}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q14511}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14511}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:27926875}. Cell projection, cilium {ECO:0000250|UniProtKB:Q14511}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q14511}. Basolateral cell membrane {ECO:0000269|PubMed:27926875}.
| null | null |
PF12026;PF08824;PF14604;
|
IPR021901;IPR037362;IPR035746;IPR014928;IPR038319;IPR036028;IPR001452;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
NEDD9 CASL
| false |
547 |
A0A8I3PI99
|
MSTMFADTLLIVFISVCTALLAEGITWVLVYRTDKYKRLKAEVEKQSKKLEKKKETITESAGRQQKKKIERQEEKLKNNNRDLSMVRMKSMFAIGFCFTALMGMFNSIFDGRVVAKLPFTPLSYIQGLSHRNLLGDDTTDCSFIFLYILCTMSIRQNIQKILGLAPSRAATKQAGGFLGPPPPSGKFS
|
Calcium load-activated calcium channel (CLAC channel) (GEL complex subunit TMCO1) (Transmembrane and coiled-coil domain-containing protein 1)
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 188 | 21,175 |
3D-structure;Calcium;Calcium channel;Calcium transport;Coiled coil;Endoplasmic reticulum;Golgi apparatus;Ion channel;Ion transport;Membrane;Mitochondrion;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix;Transport
|
GO:0000139; GO:0001503; GO:0005262; GO:0005737; GO:0005783; GO:0005789; GO:0006983; GO:0031966; GO:0032469; GO:0043022; GO:0160063; GO:0160064
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:36261528}; Multi-pass membrane protein {ECO:0000269|PubMed:36261528}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UM00}; Multi-pass membrane protein {ECO:0000269|PubMed:36261528}. Mitochondrion membrane {ECO:0000250|UniProtKB:C5HGF3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UM00}. Note=The first transmembrane region is required for localization to the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9UM00}.
| null |
TRANSMEM 5..32; /note="Helical"; /evidence="ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TUT"; TRANSMEM 87..106; /note="Helical"; /evidence="ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TUT"; TRANSMEM 141..162; /note="Helical"; /evidence="ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TUT"
|
PF01956;
|
IPR002809;IPR008559;
|
7TUT;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
TMCO1
| false |
548 |
A0A8I3PQN6
|
MNPASVPPALPPPGQQVIHVTQDLDTDLEALFNSVMNPKPSSWRKKILPESFFKEPDSGSHSRQSSTDSSGGHAGPRLAGGAQHVRSHSSPASLQLGPGAGAAGSPAQQHAHLRQQSYDVTDELPLPPGWEMTFTATGQRYFLNHIEKITTWQDPRKAMNQSLNPMNLHPAATSTPASQRSMAVSQPNLVMNHQHQQQMAPTNLSQQNHPTQNPPAGLMSMPNALTTQQQQQQKLRLQRIQMERERIRMRQEELMRQEAALCRQLPMEAETLATVQAAVNPPAMTPDMRSITNNSSDPFLNGGPYHSREQSTDSGLGLGCYSVPTTPEDFLSNVDEMDTGENAGQTPMNINPQQTRFPDFLDCLPGTNVDLGTLESEDLIPLFNDVESALNKSEPFLTWL
|
WW domain-containing transcription regulator protein 1 (Transcriptional coactivator with PDZ-binding motif)
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 400 | 43,972 |
Activator;Cell junction;Cell membrane;Cytoplasm;Isopeptide bond;Membrane;Nucleus;Phosphoprotein;Reference proteome;Tight junction;Ubl conjugation
|
GO:0000122; GO:0001649; GO:0001894; GO:0003015; GO:0003713; GO:0003714; GO:0005634; GO:0005667; GO:0005829; GO:0005886; GO:0005923; GO:0008284; GO:0010718; GO:0016567; GO:0016604; GO:0017145; GO:0031146; GO:0032835; GO:0035264; GO:0035329; GO:0042803; GO:0045599; GO:0045669; GO:0045944; GO:0048762; GO:0060271; GO:0060395; GO:0060993; GO:0070160; GO:0072307; GO:0090090; GO:1900182
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21205866}. Nucleus {ECO:0000250|UniProtKB:Q9GZV5}. Cell membrane {ECO:0000250|UniProtKB:Q9GZV5}. Cell junction, tight junction {ECO:0000269|PubMed:21205866}. Note=Concentrates along specific portions of the plasma membrane, and accumulates in punctate nuclear bodies (By similarity). When phosphorylated, is retained in the cytoplasm by YWHAZ (By similarity). Can be retained in the nucleus by MED15 (By similarity). Localized in the cytoplasm in areas of epithelial cell high density (By similarity). At blastocyst stage expressed in the nucleus in trophectodermal cells, however expressed in the cytoplasm in the inner cell mass (By similarity). In the nucleus, phosphorylation by PRP4K induces nuclear exclusion (By similarity). Interaction with AMOTL2 results in localization to the cytoplasm and tight junctions (PubMed:21205866). {ECO:0000250|UniProtKB:Q9EPK5, ECO:0000250|UniProtKB:Q9GZV5, ECO:0000269|PubMed:21205866}.
| null | null |
PF00397;
|
IPR001202;IPR036020;IPR051583;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
WWTR1 TAZ
| false |
549 |
A0A8I3QA39
|
MRTLEDSSGTVLHRLIQEQLRYGNLTETRTLLAIQQQALRGGAGAGGTGSPQASAEILAPEDTQVLQQATRQEPQGQEHQGGESHLAENTLYRLCPQPGKGEELPTYEEAKAHSQYYAAQQAGPRPHVGDRDPRGAPGGHRSQDEALRELRHGHVRSLSERLLQLSLERNGARAPSHMSSSHSFPQLARNQQGPAPRGPPAEGPEPRGPPPQYPHVVLAHETATAVTDPRYRTRGSPHFQHAEVRILQAQVPPVFLQQQQQYQYLQQPQEHPLPPHPAVLSHGPLGALSPPEVEGPASTQTSSAPSGSAHLAQMETLLRENARLQRDNERLQRELESSAEKAGRIEKLEGEIQRLSEAHESLMRASSKREALEKTMRNKMDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALSNAQGRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKRELLELRLRTRLEQELKALRAQQRQAGTPTGASGGSPELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKDAVIKVLQQRSRKDPGKATQGSLRPAKSVPSVFVAAAAGTQGWQSLSSSERPADAPARLATDRAPEEEPVAAAPLPAHAKHGSRDGSTQTDGPTEGASACLGLDPDSLLGYSGGQRTASLDSVAASRVQDLSDMVEILI
|
Angiomotin-like protein 2
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 776 | 85,463 |
Cell junction;Cell projection;Coiled coil;Cytoplasm;Endosome;Isopeptide bond;Phosphoprotein;Reference proteome;Ubl conjugation;Wnt signaling pathway
|
GO:0000122; GO:0001525; GO:0002102; GO:0003365; GO:0005886; GO:0005923; GO:0016055; GO:0030036; GO:0030334; GO:0031410; GO:0035329; GO:0042995; GO:0055037; GO:1903829
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Recycling endosome. Cytoplasm {ECO:0000250|UniProtKB:Q9Y2J4}. Cell projection, podosome {ECO:0000250|UniProtKB:Q8K371}. Cell junction {ECO:0000250|UniProtKB:Q8K371}.
| null | null |
PF12240;
|
IPR009114;IPR051747;IPR024646;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
AMOTL2
| false |
550 |
A0A8I3S724
|
MDKSKENCIAGPVKTAIALGDGPKRVLVTQQVPSQNPLSANSGQAQRVLCPSNSSQRVPPQTQKLVSSHKPAQNLKQKQLQATGVPRPASRSLNNTQKSEQPSSSAPGNNSEKELATKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILAIKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGAVYRELQKLSKFDEQRTATYITELADALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEASTYQETYKRISRVEFTFPDFVPEGARDLISRLLKHNPSQRPTLKDVLEHPWIMANSSKPSSSQKSKDSTSKQS
|
Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (Ipl1- and aurora-related kinase 1) (Serine/threonine-protein kinase 15) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase Ayk1) (Serine/threonine-protein kinase aurora-A)
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 405 | 45,598 |
ATP-binding;Cell cycle;Cell division;Cell membrane;Cell projection;Cytoplasm;Cytoskeleton;Isopeptide bond;Kinase;Membrane;Microtubule;Mitosis;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase;Ubl conjugation
|
GO:0000212; GO:0000776; GO:0000922; GO:0004674; GO:0005524; GO:0005634; GO:0005737; GO:0005813; GO:0005814; GO:0005876; GO:0005929; GO:0007052; GO:0007100; GO:0016323; GO:0032133; GO:0032465; GO:0043005; GO:0045931; GO:0051233; GO:0051301
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O14965}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:27926875}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P97477}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P97477}. Cell projection, cilium {ECO:0000250|UniProtKB:O14965}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P97477}. Basolateral cell membrane {ECO:0000269|PubMed:27926875}. Note=Detected at the neurite hillock in developing neurons (By similarity). Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase (By similarity). Moves to the midbody during both telophase and cytokinesis (By similarity). Associates with both the pericentriolar material (PCM) and centrioles (By similarity). Colocalized with SIRT2 at centrosome. The localization to the spindle poles is regulated by AAAS (By similarity). {ECO:0000250|UniProtKB:O14965}.
| null | null |
PF00069;
|
IPR030616;IPR030611;IPR011009;IPR000719;IPR017441;IPR008271;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
AURKA AIK AIRK1 ARK1 AURA AYK1 BTAK IAK1 STK15 STK6
| false |
551 |
A0A8I3S9V6
|
MSGGRRKEEPPQPQLANGALKVSVWSKVLRSDAAWEDKDEFLDVIYWFRQIIAVVLGVIWGVLPLRGFLGIAGFCVINAGVLYLYFSNYLQIDEEEYGGTWELTKEGFMTSFALFMVIWIIFYTAIHYD
|
GEL complex subunit OPTI (Obligate partner of TMCO1 insertase) (Rab5-interacting protein) (RIP5) (Respirasome Complex Assembly Factor 1) (RCAF1)
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 129 | 14,811 |
3D-structure;Endoplasmic reticulum;Membrane;Mitochondrion;Mitochondrion inner membrane;Reference proteome;Transmembrane;Transmembrane helix
|
GO:0005743; GO:0005789; GO:0097250; GO:0160063; GO:0160064
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:36261528}; Multi-pass membrane protein {ECO:0000269|PubMed:36261528}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9BUV8}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 45..65; /note="Helical"; /evidence="ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TM3, ECO:0007744|PDB:7TUT"; TRANSMEM 67..84; /note="Helical"; /evidence="ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TM3, ECO:0007744|PDB:7TUT"; TRANSMEM 104..127; /note="Helical"; /evidence="ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TM3, ECO:0007744|PDB:7TUT"
|
PF07019;
|
IPR029008;IPR010742;
|
7TM3;7TUT;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
RAB5IF OPTI
| false |
552 |
A0A8I5ZN27
|
MLGWVQRVLPQPPGTPQKTEEGAGPQPETESKPEANPQPEPEVQPEPEPEPEPAPEEAAPEVQTLPPEEPVEGEDVAEAGPSLQETQEADPPQPTSQAQVAVVKVNRPSSWMLSWFWKGMEKVVPQPVYSSSGGQNLAAGEGGPDQDGAQTLEPCGTGDPGSEDGSDKTSKTQDTEPSLWLLRWLELNLEKVLPQPPTPSQAWKVEPEGAVLEPDPPGTPMEVEPTENPSQPNPGPVEPEEEPAAEPQPGFQASSLPPPGDPVRLIEWLLHRLEMALPQPVLHGKAAEQEPSCPGTCDVQTISILPVEQAEHDLVLEDVDSCWEDTQQEDGASLQETELAPIYEDESEAMVEMPRELPQIQEEEEEEKEEKEEKEEEEEKEEEEKREEEKKKEKEEEKKEKEKEEKEEKEEKEEEEKEEKEEEEKEEKEEEEKEEKEEEEEEEEEEEEEEPIVLLDSCLVVQADVDQCQLERAQPETASIQELPEEEEEKEEEKKEEEEEKEEEEEKEEEEEKEEEGEATNSTVPATKEHPELQVEDTDAEAGPLIPEETIPPPERPPVSPAKSDTLAVPGAATHRKKLPSQDDEAEELKALSPAESPVVAWSDPTTPQEADGEDRAASTASQNSAIINDRLQELVKMFKERTEKVKEKLIDPDVTSDEESPKPSPAKKAPDSAPAQKPAEAEAAEEEHYCDMLCCKFKRRPWKMYQFPQSIDPLTNLMYILWLFFVVLAWNWNCWLIPVRWAFPYQRADNIHLWLLMDYLCDFIYLLDITVFQMRLQFVKGGDIITDKKEMRNNYLKSQRFKMDLLCLLPLDFLYLKLGVNPLLRLPRCLKYMAFFEFNNRLEAILSKAYVYRVIRTTAYLLYSLHLNSCLYYWASAFQGIGSTHWVYDGVGNSYIRCYYWAVKTLITIGGLPDPQTLFEIVFQLLNYFTGVFAFSVMIGQMRDVVGAATAGQTYYRSCMDSTVKYMNFYKIPRSVQNRVKTWYEYTWHSQGMLDESELMVQLPDKMRLDLAIDVNYNIVSKVALFQGCDRQMIFDMLKRLRSVVYLPNDYVCKKGEIGREMYIIQAGQVQVLGGPDGKAVLVTLKAGSVFGEISLLAVGGGNRRTANVVAHGFTNLFILDKKDLNEILVHYPESQKLLRKKARRMLRNNNKPKEEKSVLILPPRAGTPKLFNAALAAAGKMGPRGAKGGKLAHLRARLKELAALEAAARQQQLLEQAKSSQEAGGEEGSGATDQPAPQEPSEPKEPPEPPAPSSPPPASAKPEGSTEEAAGPPEPSVRIRVSPGPDPGEQTLSVEMLEEKKEEVE
|
Cyclic nucleotide-gated channel beta-1 (Cyclic nucleotide-gated cation channel 4) (CNG channel 4) (CNG-4) (CNG4)
|
Rattus norvegicus (Rat)
| 10,116 | 1,307 | 147,160 |
Alternative initiation;Alternative splicing;Calcium;Calcium channel;Calcium transport;cAMP;cAMP-binding;Cell membrane;Cell projection;cGMP;cGMP-binding;Ion channel;Ion transport;Ligand-gated ion channel;Membrane;Nucleotide-binding;Olfaction;Reference proteome;Sensory transduction;Sodium;Sodium channel;Sodium transport;Transmembrane;Transmembrane helix;Transport;Vision
|
GO:0001750; GO:0001895; GO:0005221; GO:0005222; GO:0005223; GO:0005262; GO:0005272; GO:0005886; GO:0006812; GO:0006813; GO:0006814; GO:0006816; GO:0007601; GO:0007602; GO:0007608; GO:0010628; GO:0016020; GO:0017071; GO:0021630; GO:0030552; GO:0030553; GO:0033365; GO:0035845; GO:0043195; GO:0043855; GO:0044877; GO:0045494; GO:0050908; GO:0050911; GO:0051480; GO:0051899; GO:0098655; GO:0098804; GO:0120200; GO:1902495; GO:1990834
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium membrane {ECO:0000269|PubMed:10377344}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 721..742; /note="Helical; Name=S1"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 752..773; /note="Helical; Name=S2"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 789..808; /note="Helical; Name=S3"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 825..837; /note="Helical; Name=S4"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 850..872; /note="Helical; Name=S5"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 896..922; /note="Helical; Name=P-helix"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 923..948; /note="Helical; Name=S6"; /evidence="ECO:0000250|UniProtKB:Q14028"
|
PF00027;
|
IPR050866;IPR018488;IPR000595;IPR018490;IPR014710;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Rattus (genus)
|
Cngb1 CNCG2 CNCG3L CNCG4 RCNC2
| false |
553 |
A0A8I5ZNK2
|
MSEDSSALPWSINRDDYELQEVIGSGATAVVQAAYCAPKKERVAIKRINLEKCQTSMDELLKEIQAMSQCHHPNIVSYYTSFVVKDELWLVMKLLSGGSVLDIIKHIVAKGEHKGGVLDESTIATILREVLEGLEYLHKNGQIHRDVKAGNILLGEDGSVQIADFGVSAFLATGGDITRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPSLDTGVQDKEMLKKYGKSFRKMISLCLQKDPEKRPTAAELLRHKFFQKAKNKEFLQEKILQRAPTISERSKKVRRVPGSSGRLHKTEDGGWEWSDDEFDEESEEGKAAISQLRSCPTQQHCLCLLQLFSAADPMGTLLQVPEQISAHLPQPASQMPTQPAQVSLLPPAEPAKPAQARSSGERSQETKVPISLVLRLRNSKKELNDIRFEFTPGRDTAEGVSQELISAGLVDGRDLVIVAANLQKIVEEPQSNRSVTFKLASGVEGSDIPDDGKLIGFAQLSIS
|
Serine/threonine-protein kinase OSR1 (EC 2.7.11.1) (Oxidative stress-responsive 1 protein)
|
Rattus norvegicus (Rat)
| 10,116 | 528 | 58,360 |
Acetylation;ATP-binding;Cytoplasm;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase
|
GO:0000287; GO:0004674; GO:0005524; GO:0005737; GO:0005829; GO:0006884; GO:0006979; GO:0007165; GO:0007231; GO:0009410; GO:0010820; GO:0019901; GO:0035556; GO:0038116; GO:0038146; GO:0042802; GO:0070294; GO:0071474; GO:0071476; GO:1901380; GO:1990869
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95747}.
| null | null |
PF12202;PF00069;
|
IPR011009;IPR024678;IPR000719;IPR017441;IPR050629;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Rattus (genus)
|
Oxsr1 Osr1
| false |
554 |
A0A8I6G705
|
MNGGGKAEKENTPSEANLQEEEVRTLFVSGLPLDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVSFDSRSEAEAAKNALNGIRFDPEIPQTLRLEFAKANTKMAKNKLVGTPNPSTPLPNTVPQFIAREPYELTVPALYPSSPEVWAPYPLYPAELAPALPPPAAFTYPASLHAQMRWLPPSEATSQGWKSRQFC
|
RNA-binding protein with multiple splicing (RBP-MS) (RBPMS)
|
Rattus norvegicus (Rat)
| 10,116 | 197 | 21,816 |
Acetylation;Alternative splicing;Cytoplasm;Nucleus;Phosphoprotein;Reference proteome;RNA-binding
|
GO:0000381; GO:0000932; GO:0003713; GO:0003723; GO:0003730; GO:0005634; GO:0005654; GO:0005737; GO:0005829; GO:0006979; GO:0010494; GO:0036002; GO:0042802; GO:0042803; GO:0060090; GO:0060395; GO:0065003; GO:0097157; GO:1990715
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93062}. Cytoplasm {ECO:0000250|UniProtKB:Q93062}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q93062}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q93062}.
| null | null |
PF00076;
|
IPR012677;IPR035979;IPR000504;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Rattus (genus)
|
Rbpms
| false |
555 |
A0A8I6GM68
|
MTSTGQDSSTRQRKSRHNPQSPLQDSSATLKRGGKKGAVPHSSPNLAEVKKKGKMKKLSQPAEEDLIVGLQGLDLNSETRVPVGTGLVFDEQLNDFHCLWDDSFPENPERLHAIKEQLILEGLLGRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLAGTYDSVYLHPNSYSCACLATGSVLRLVDAVMGAEIRNGMAVIRPPGHHAQRSLMDGYCMFNHLAVAARYAQKKHRIQRILIVDWDVHHGQGTQFIFDQDPSVLYFSIHRYEHGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVSFCSHKLSLACFPRGSREMTDYYIAFLCLQVGMRDADYIAAFLHILLPVAFEFQPQLVLVAAGFDALHGDPKGEMSATPAGFAHLTHFLMGLAGGKLILSLEGGYNLHALAKGVSGSLHTLLGDPCPMLESPVAPCASAQTSISCTLEALEPFWEVLERSVEPQDEDEVEGDMLEDEEEEGHWEATALPMDTWPLLQNRTGLVYDERMMSHCNLWDNHHPETPQRILRIMCHLEEVGLAARCLILPARPALDSELLTCHSAEYVERLRATEKMKTRDLHREGANFESIYICPSTFACAQLATGAACRLVEAVLSGEVLNGIAIVRPPGHHAEPDAACGFCFFNSVAVAARHAQVIAGRALRILIVDWDVHHGNGTQHIFEEDPSVLYVSLHRYDRGTFFPMGDEGASSQVGRAAGTGFTVNVPWNGPRMGDADYLATWHRLVLPIAYEFNPELVLISAGFDAAQGDPLGGCQVTPEGYAHLTHLLMGLAGGRIILILEGGYNLTSISESMAACTHSLLGDPPPQLTSLRPPQSGALASISEVIQVHRKYWRSLRLMKMEDKEERSSSRLVIKKLPQSASPVSAKGMTTPKGKVLEAGMRKPTAALPTKESTLGQAKAKTAKALLAQGQSSEQAAKGTTLDLATSKDTVGGATTDQCASVAATENSANQTTSGEEASGETESFGTSPSSNASKQTTGASPLHGAAAQQSPELGLSSTLELSSEAQEVQESEEGLLGEAAGGQDMNSLMLTQGFGDFNTQDVFYAVTPLSWCPHLMAVCPIPAAGLDVSQPCKTCGSVQENWVCLTCYQVYCSRYVNAHMVCHHEASEHPLVLSCVDLSTWCYLCQAYVHHEDLQDVKNAAHQNKFGEGMPHLQ
|
Protein deacetylase HDAC6 (EC 3.5.1.-) (E3 ubiquitin-protein ligase HDAC6) (EC 2.3.2.-) (Tubulin-lysine deacetylase HDAC6) (EC 3.5.1.-)
|
Rattus norvegicus (Rat)
| 10,116 | 1,183 | 129,064 |
Actin-binding;Autophagy;Cell projection;Chromatin regulator;Cytoplasm;Cytoskeleton;Hydrolase;Metal-binding;Methylation;Nucleus;Phosphoprotein;Reference proteome;Repeat;Repressor;Transcription;Transcription regulation;Transferase;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger
|
GO:0000118; GO:0000209; GO:0000978; GO:0001222; GO:0001975; GO:0004407; GO:0005634; GO:0005737; GO:0005813; GO:0005829; GO:0005874; GO:0005875; GO:0005901; GO:0006511; GO:0006515; GO:0006886; GO:0007015; GO:0007026; GO:0007173; GO:0008013; GO:0008017; GO:0008270; GO:0010634; GO:0010727; GO:0010821; GO:0010977; GO:0015630; GO:0016234; GO:0016235; GO:0016241; GO:0019213; GO:0019896; GO:0019899; GO:0030182; GO:0030424; GO:0030425; GO:0031252; GO:0031333; GO:0031593; GO:0031625; GO:0031647; GO:0031648; GO:0032418; GO:0032461; GO:0032984; GO:0032991; GO:0033148; GO:0033558; GO:0035902; GO:0035967; GO:0036064; GO:0036479; GO:0042030; GO:0042826; GO:0042903; GO:0043005; GO:0043014; GO:0043025; GO:0043130; GO:0043131; GO:0043162; GO:0043204; GO:0043242; GO:0045598; GO:0045814; GO:0045861; GO:0048156; GO:0048471; GO:0048487; GO:0048668; GO:0048843; GO:0050775; GO:0051412; GO:0051646; GO:0051787; GO:0051788; GO:0051879; GO:0051968; GO:0060997; GO:0061523; GO:0061734; GO:0070201; GO:0070301; GO:0070507; GO:0070840; GO:0070842; GO:0070845; GO:0071218; GO:0071374; GO:0071548; GO:1900409; GO:1904056; GO:1904115; GO:1905091; GO:1905336
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBN7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UBN7}. Nucleus {ECO:0000250|UniProtKB:Q9UBN7}. Perikaryon {ECO:0000250|UniProtKB:Q9Z2V5}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9Z2V5}. Cell projection, axon {ECO:0000250|UniProtKB:Q9Z2V5}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9UBN7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UBN7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9UBN7}. Note=Mainly cytoplasmic where it is associated with microtubules (By similarity). Can shuttle between the cytoplasm and the nucleus. Found exclusively in the cytoplasm in proliferative cells with a fraction found in the nucleus during differentiation (By similarity). May translocate to the nucleus following DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9UBN7, ECO:0000250|UniProtKB:Q9Z2V5}.
| null | null |
PF00850;PF02148;
|
IPR050284;IPR000286;IPR023801;IPR037138;IPR023696;IPR013083;IPR001607;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Rattus (genus)
|
Hdac6
| false |
556 |
A0A8M1NHK4
|
MTAEDSASAVAMSNPSPSSSSKSSSGHPQHHCTVPEGVAGAPNEAALVSLMERSGYGMVQENGQRKYGPPPGWQGTSPPRGCEIFVGKIPRDVYEDELVPVFESVGRIYEMRLMMDFDGKNRGYAFVMYTQKHEAKRAVRELNNFEIRPGRLLGVCSSVDNCRLFIGGIPKTKKREEILEEVSKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETSEEILRQTFGQFNPGCVERVKKIRDYAFVHFASRDDAVVAMDNLNGTEIEGSRIEVTLAKPVDKEQYTRYQKASKGTAAATTVESTQQSYVYQCDPYTLAYYGYPYNTLIGPNRDYFIKGTVRGRGRAGASSRGPGPRGSYLGGYSAGRGIYSRYHEGKTKLPDKPYEIMSNLELAAVNPVGIKPGTMALPALGAQYPTVFSAAPATKLMEEGKIHPVEHLINPLALQHDPTAASATAAVIPAVSTPPPFQGRPITPVYAMAHNIQRIPAAAASLYGAGYMPIAAHANTATLAALQKNAAVAAAYGGYAGYMPQAFPAATFQMPIHDVYQTY
|
RNA-binding protein 47 (RNA-binding motif protein 47)
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 600 | 65,521 |
Cytoplasm;Methylation;mRNA processing;mRNA splicing;Nucleus;Reference proteome;Repeat;RNA-binding
|
GO:0003729; GO:0005634; GO:0005764; GO:0006397; GO:0008380; GO:0060322; GO:0140374; GO:1905146; GO:2000742
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0AV96}. Cytoplasm {ECO:0000250|UniProtKB:A0AV96}.
| null | null |
PF00076;
|
IPR006535;IPR012677;IPR035979;IPR047044;IPR034440;IPR000504;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
rbm47 si:ch211-241e15.2
| false |
557 |
A0A8M2
|
MSGGTPYIGSKISLISKAEIRYEGILYTIDTENSTVALAKVRSFGTEDRPTDRPIPPRDEIFEYIIFRGSDIKDLTVCEPPKPQCSLPQDPAIVQSSLGSSSASSFQSVSSYGPFGRMPAYSQFNTGPLVGPQFGAVGVGSSLTSFGAETTSSTSLPPSSAVGTSFTQEARTLKTQSSQGQSSSPLDSLRKSPNIEQAVQTAAAPHAPSTATVGRRSPVLSRPVPSSIQKTAESPEQRKGELHKMQRPDIDQLKNDKNDPSKRQPVLSALQPRRGRGGNRGGRGRFGVRRDGPMKFEKDFDFESANAQFNKEEIDREFHNKLKIKDDKPEKPVNGEDKTDSVVDTQNSEGNAEEEEVLAGGVCYYDKTKSFFDNISCDDNRDRRQTWAEERRINVETFGLPLRSNRGRGGFRGRGGGMGFRGGRGRGGERRGAPGGGGFGPARGFRGGFRGGRGGREFADYEYRKDNKVAA
|
Protein LSM14 homolog A-A (RNA-associated protein 55A-A) (RAP55A-A) (xRAP55) (xRAP55A)
|
Xenopus laevis (African clawed frog)
| 8,355 | 471 | 51,168 |
Cytoplasm;Developmental protein;Phosphoprotein;Reference proteome;Repressor;Ribonucleoprotein;Translation regulation
|
GO:0000932; GO:0003723; GO:0003729; GO:0005737; GO:0010494; GO:0017148; GO:0017151; GO:0032991; GO:0033962; GO:0034063; GO:1990904
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17074753}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q8ND56}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q8ND56}. Note=Localizes to cytoplasmic particles in stage VI oocytes and eggs. {ECO:0000269|PubMed:17074753}.
| null | null |
PF09532;PF12701;
|
IPR025762;IPR019050;IPR025761;IPR025609;IPR010920;IPR047575;IPR025768;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Pipoidea (superfamily), Pipidae (family), Xenopodinae (subfamily), Xenopus (genus), Xenopus (subgenus)
|
lsm14a-a lsm14a rap55a-a
| false |
558 |
A0A8M2BID5
|
MSLSGSQTRLHQISRRSSSRPDLTAVGYSLPRNDGAQFFTSGNGYQSDYNDGYMQTYTQTFSKNSQGGGAGGAQSMSSMAVQKRAQMLYSDCMGFLQRAQGLLETMGPASEVDKNMMAAQDAMDQLRKCAVDMRNAGLPNDMILRSLEDCHSFYADIRNSITGTTIRRTGGTVSGTIGGTISGTIGGTVGGWDDPSKSFQDALSWINQKKRLIETSGFGENSEAISQQILNHNKFHSSIQRSQEVDRARDDLMQSREKAGLHALDQEWDSLQKMSHARMDHLRDLQSIIEEISRAIMWVNDREEEELVFDWGDKNIDNYIPQKQESYSKLMSDLEEKEKELNKLKAKVDMLLKNQHPASDKIEAYMDTLQTQWSWLLQITKCIHVHLKENAAYSQFFKEANETYSRLQKDHENIRKKFGCDKTTPLENLNDMLKNLEKEKEKVIENKRQVQTLVSKSKNIVCLKPRNPEEKSSSPVIVQALCDFKQDQKGIMKGNEGILKDNSQRSKWHVTGPGGLEMLIPSVCLIIPPPNPLSISLANKNEQYYEAIMSIWSQLYINIKSLISWQYCLRDIQHINSLTLSMLTQMRPEEYRQTIKNLEIHYQEFLRNSLGSEMFGDDDKRKMELQYAGAQSHYDQLVIQLPNYRENGVIREVVMVETDSKLKSEVSSGKTATGVSSGKTATGVSSGKTSSSVSVSGLNVSLLSDLSALRRRLETAESGLTKHLHVPLKENSVQECSQRLAQLQAVHRDLDSIRDEYLHLREKIMRELEGSSDPEQSRYLRAELDLINQKLGSLQGFSSAYIQRLGALQALLQHLLQAEDIIKVHEARLTEKETSSLDLNEVEKYCMTLKTMKAELEQKKGVLKAMETELSKAVHWNSQIDQSFHQCDVDLSRYTELVGQMTDRWRRIVTQIDSRTWDLEKQEKQLNHYQQTSSTINRWIQDTRQRQDTLQITKFNSVDNLMDHLNQQKALYSEIKGKKEKVDAVVKDSDTCAASIKDYELQLASYSAGLETLLNIPIKKTMLQSPATVLREEATDLQSRYIELLTRSSDYYKFLGEMLKNMEELKMRNTKIELLEEELRRLKDNLKDQNQKNKSLEDSLTRFRLELTQSKEQLISMEEVKRTQARQCNTAQESLDSTQNQLKSLQDEMSRLTFLIEEEKRKRRLAEERYTNQQEEYELAMRKRQKELEELTLSKSQFERAIKEKEREIERLKLQLQDEASRRSAAELETSKTSMMIQRSDSNYKDIVQERDSLLIKLKLLQQDKDKQQRYEEELRRIKLTLESETKQKQRLQDEIDKITKDFKYWKSQYELKEGQIRQSEMDRDRVERDRASLQSEIQRLTAELRSVEERYRGRLQSSDKEISELMRKKESLEIELRRLQQRPAATWKQTQTDEISKPVVEQKLTVQGLRGEVSLTELVESDLLDQTDLDKINRGQLTSKDIEHKLKSYLGGSDCIAGIYDEAKDRVMPFYQAMKDGLLRRGTTLELLEAQAASGFIIDPVNNVCMTVEEAWKRGLVGKEFKDKLLSAEKAVTGYKDPATGKIISLFQAIEKEIIEKGHGIRLLEAQIASGGIIDPKGSHRIDVEVAYRKGYFDREMNEILSYEGDDTKGFFDPNTHENLTYLELKKRCIKDPKTGLMLLPLNDKQKPKQTTTQKNTLRKRRVVIVDPDTGKEMTVREAYHRELIDYDTFLELSEQECEWEEITIETSDGNKRLLIVDRKTGIQYDIQESLQRGIINKQTLEKYRAGTMTLTEFAALITSKSNSSELAIFSSSPEDVATCSSPTQPSSPTVRKRFASVSITLSPPSDIFDDQSPVGAIFDTETLEKITIPEAQRRGIVDNITAQRLLEAQVCSGGIINPATGQRLSLKDAVQQSLIDEDMSVKLKPAQKAYDGFEDVKTKRKLSAAEAMKEKWLPYEAGQRFLEFQYLTGGLIEPGTGRRVSIEEAIRKGWLDGKGAQKLQDTRNYIKNLTCPKTKLKISYKEAMDNCMVEENNGMKMLQATSMSTKGISSPYNVSSGPSSRSGSRAGSRTGSRSGSRRGSVDYSSSSVSYTFFSSAS
|
Desmoplakin-A (Desmoplakin isoform X2)
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 2,059 | 235,142 |
Cell junction;Cell membrane;Coiled coil;Membrane;Phosphoprotein;Reference proteome;Repeat
|
GO:0002934; GO:0005198; GO:0005856; GO:0005886; GO:0007507; GO:0014704; GO:0030057; GO:0031101; GO:0042060; GO:0043588; GO:0045104; GO:0060047; GO:0061436; GO:0098609
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250|UniProtKB:E9Q557}. Cell membrane {ECO:0000250|UniProtKB:E9Q557}.
| null | null |
PF00681;PF17902;PF18373;PF21019;PF21097;
|
IPR041615;IPR041573;IPR043197;IPR035915;IPR001101;IPR018159;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
dspa
| false |
559 |
A0A8M3B525
|
MWKCSTVINKNKLIKAEYHTFYTLLFAMAVNAVHLESDAFLVCMNHALSTEKEEVMGLCIGEVDTNRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAEMTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSVQAQKGSEYERIEIPIHVVPHEAIGKVCLESAVELPRILCQEEQDTYRRIHSLTHLDPITKIHNGSVFTKNLCSQMSAISGPLLQWLEDRLEQNKQSIITLQKEKELLTQELAAL
|
Lys-63-specific deubiquitinase (EC 3.4.19.-)
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 287 | 32,858 |
3D-structure;Cell cycle;Cell division;Coiled coil;Cytoplasm;Cytoskeleton;Hydrolase;Metal-binding;Metalloprotease;Mitosis;Nucleus;Protease;Reference proteome;Ubl conjugation pathway;Zinc
|
GO:0000922; GO:0001525; GO:0004843; GO:0005737; GO:0006302; GO:0006508; GO:0008237; GO:0031593; GO:0046872; GO:0051301; GO:0070531; GO:0070536; GO:0070552
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU367116}. Cytoplasm {ECO:0000255|RuleBase:RU367116}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|RuleBase:RU367116}.
| null | null |
PF18110;PF01398;
|
IPR040749;IPR000555;IPR050242;IPR037518;IPR033860;
|
5CW6;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
brcc3
| false |
560 |
A0A8M9PDM1
|
MFVFIAKLLIFSSVITSAFTCYQCFIDENDSRRLCLGHILTEYNVRNVDSCYKTLDRIFNNEEKVIEAGKVGRGYDLTLKNILMAEIMPIVEEFDQQLNYDTEYESRLQAAANNFIAAASSLPRVSGCLPPCGFQVQGAVYNCVTCQYDSCEFPLDCPGKEITVQENNRTQMWCSVPFLLPADVEIVWRYAQDRTMLRERFDDVTVGVDPLYSIPSARPEQSGTYQCEVLSQEQSLVRLYFYLTVVPVAQTYHVHLQDLCAQALRPEPQFPPSFSFWLPRPALLITCLTATMLLIFLSLGAMCRLWYQIRTNVSNPA
|
Sperm acrosome membrane-associated protein 6
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 317 | 36,158 |
Cytoplasmic vesicle;Disulfide bond;Fertilization;Glycoprotein;Immunoglobulin domain;Membrane;Reference proteome;Signal;Transmembrane;Transmembrane helix
|
GO:0002080; GO:0007342; GO:0035036; GO:0043012
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000250|UniProtKB:W5XKT8}; Single-pass type I membrane protein {ECO:0000255}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
|
TRANSMEM 282..302; /note="Helical"; /evidence="ECO:0000255"
| null |
IPR007110;IPR036179;IPR013783;IPR003599;IPR034549;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
spaca6
| false |
561 |
A0A8M9PFP2
|
MARMSFLSFLLFCLTSVAHGNKANKHKPWIETEYQGIVMENDNTVLLNPPLFALDKDAPLHYAGEICGFRVHNGPGGSGSAQFEAVVLDRSTGEGLVRSKEPLDCESQKEHSFTIQAYDCGEGPDGTNSKKSHKATVHVRVNDVNEFSPVFVERRYEASVPEGRLFDRIVRVEAVDADCSPQYSQICFYDIITPNVPFTIDNDGNIKNTEPLDSKRQRVHSFWVTAFDCGKNRAQADAQVIVTVKPSCKPGWIGWTKRIEYTPGSGSIPLFPNLHLETCEETVWNIQATVELQTSHIGKGCDRDSYSDRSVRRLCGAVRGEVDLLPPPSPATNWTAALPTLPSSDSSLVFSFNGSTHVAVVPDSVASAVSGDHFTLQLWMRRGGASTQPPANQARGTRKEEETIVCSTVKNDDSYSHYSLSVHGCRLSLFYWPDVSAARPVKFLWKLEQVCDSEWHHLSLSVQFPSVTLYVDGVTFDPALIHDNGAIPNPAPHQRLVIGACWEPEEKPKDIVNNTMPENKDTGKFVSGYKGLLSGVTVRPGNVEPHSVVECLYACREGLDFGDLETLGSGMKVHVNPSQSVLVLEGDDIESFNRAVQQVTYRNSLRFATPGVRPLKLTTSLRCFSEESCLSLRQLEGYLVVLQPDAPQISLSGVGPHLARPAAEFEGPQGVPLFPELRIVCSLSHAVNTAAQGMEGGALMSDAVAHTLDGCEVQPLGEELNTEREELLVDMESLRERGLDIINTTAYIAITGAESISVYEDVLRSIHYRLAKGSARFERRFRLSCSEMNGRYTSNELTLEVNFLHSLDSLYHPSHLLASQQQFLHPSHHTGELSGHTLPNPHRNSVVPGAATVIIMVCVGFLVVMVILGVFRIRSIHRRGEGARGGGKEGGNQWDDSALTIIVNPMETYENRMGITTDMEGECEDEEEVVDSPDDTSDDQRIIIKKEGRDSAPRRY
|
Calsyntenin-3
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 956 | 105,444 |
Calcium;Cell adhesion;Cell membrane;Endoplasmic reticulum;Glycoprotein;Golgi apparatus;Membrane;Postsynaptic cell membrane;Reference proteome;Repeat;Signal;Synapse;Transmembrane;Transmembrane helix
|
GO:0000139; GO:0005509; GO:0005789; GO:0007156; GO:0009986; GO:0042043; GO:0045211; GO:0050806; GO:0051965; GO:0098632; GO:1904861; GO:1904862; GO:1904889; GO:1904890; GO:1905704
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Note=Most prominent in the postsynaptic specializations of asymmetric (type I) synapses. {ECO:0000250|UniProtKB:Q99JH7}.
|
SIGNAL 1..20; /evidence="ECO:0000255"
|
TRANSMEM 851..871; /note="Helical"; /evidence="ECO:0000255"
|
PF00028;PF19699;
|
IPR002126;IPR015919;IPR045588;IPR013320;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
clstn3
| false |
562 |
A0A8M9PQ61
|
MDMQVPSVCLLVPPPNPLAISLASKNSQYYEAILSVWNQLYINVKSMISWQYCLLDIGRINSLTMSMLSKMGPDESNNILRSLEMHFQEFKRHSQGSELFGAEDQKLIENQFAGAQQHFDKLVVDLPTYAARGEGSEYSAAVSVKMLNELNALRLKLDGAESSLISFLYIALGDDGLEECGQHISSTQAFQKNIQGLRGEFVSLRDGIQAELKDAGNSDKGRYLSGQLDIMNQRLLNLDNYFTTHLQRLDSVKSLLKDMMKAEDVVKVYEARLTEKETASSDPEEVQRYQKVLLSMRSDLEQKQDLLNSLVVDLNQMQKVNDQRDQGRYQCIINLTQYADHVHQLSDRWKRIHVQINNRLVDLDSYLPQLKRYMQSSSQLSGWIDETQKQIDSQHSVKMEDSAAYTQLLNQQKALNSDIKAKRELMETVHKDGETCISAIKNYELELATYSAGLETLLNIPIKRTVLQSPSSSIAEEVSSLNAHYLELLTRSSDYYKLLLASQKNMEELKIRNTRIELLEEELEQLRDAIKDQTANNASLQDALLQYQQELNNSQSHLLSLEEVKRTETMKCMATQESLDSSKDRLEELTEEVRRLKLQLEDMERKKKIVEERYTFLQEEHDETMRKKLKELEQASWAKMELEKTVSERNRELERLRKELEDEARRIKEAQTELAKVRQEHSTEIREVKQTYESQILVAQSSMQKLSQEKESDSAAMSLEFERLEGESSELKEQLKRLRISLSQEEAQRRILEEEVKRLTALNTEESRKRHELESQIQVMMSQKREGDNKMREVQESSSRTLQDKINEINRLTRNFEEERRLKRSLETDKRRLEGDLAVLKSKNETTNEELVQLRSSHRELSLIRVELEAHALEKGRSEQTIARLQARIQELQEELKRLEGELEKQRQVAEEEAGKRRRTESQLEKSSQAMREYTTTITTLRTSQEETNIGAKHADEKCKQLQEALDRASKENKVTSQNLAALKAEINTLKLQLTQEQGRVQDSNQRYEALHRSMEEKSCALNVSSGETERLQRLTETLTKDRQRVEEELRAVRLEHEELLKNKKRGDREMTEQITALQKQLDSSQRAGAEHDRLMRQLSREREKLQVEIENVQKQARETSSVIQTSQSQCSSLSQERDDLLKKITTMEQEIVRLKRLEDELARIKLSLESELRFKSQLQEENNKIKKDFTQWKTKCASHEEQLRQHASERSGLESQFSSVRTELERLRTQLREAEERYRLLLQNFEQERTEMQALRDSKQELLRLQQKPDGATKYTQTDQTDPSSLVFEGVRKNITAQQLQDCGVIDKVIFEQLMTGKRTVQDVSVDIRLNLKGTGAIAGLAAGPKGKMTFTEAKKQNLISDKSGNMLLEAQAATGYIIDPQANTKMTVEEACLNGVVDEADKKQLLIAEAACVGFRDPKTAKLLPVSQAMKKGIIDRETTLRLLQAQEAAGGILDPILSVYLPKDTAMDRDLVDEDLYQALNAKPDCYIDPDTDLRASYVTLKKQCKADLNTGLLLLPAPEKPITVQGLRSEVNVSDLVDAKLLEPSDMNHLREGKITSQEIEHRLRAYLRGSTCIAGIYDEAGECTLPIYQAMKNGLLRPGTTLELLEAQAASGFVIDPINNEYYTVEEACQKGLVGVEFKDKLLSAEKAVTGYKEPGTNKLISLFEAIERGLIEKGHGIRLLEAQIASGGIIDPKHSHRIDVDVAYQRGYFDQGMNQILKDEGDDTKGFFDPNTEDNLTYLELKSRCTIDKKTGLVLLPIHDKKKAQQKNSTRKRRVLIVDPDSNKEMTVREAYEKKLIDYETFLELSQQECEWEETTITAPDGSTSTAIMDMQTGIQYNLKELLAQGVIDQDVFNKYRSGGISVTELAGMITKKTKMLTNPVSSSSSSSLSSSSSSFTSQTTTKSQIVKTETIKSIESTSEYLQQDQSSANSSKHISSMSVKLSPLVESIEEQNPVGAIFDTEKLEKITVCDALKRGMIDSITAQRLLEAQACTGGIVSPDNGRRMSIQEATRVGVLDDEMANRIKPAQKAYIGFEDVKTKRKMSAAEAVKEKWLPYEAGQRFLEFQYLTGGLFDPELGCRRSLEEALQMGWLDMRAAQRLQDTRHHPKTLTCPKTKLRISYKEAMEACMNEENTGVRMLPAATVSSRGISSPYNLSNPGSASGSRSGSRRGSVDYSLSPSSSSRYSSFSYSRTSFSSRSLS
|
Desmoplakin-B (Desmoplakin isoform X1)
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 2,207 | 251,066 |
Cell junction;Cell membrane;Coiled coil;Membrane;Phosphoprotein;Reference proteome;Repeat
|
GO:0002934; GO:0005198; GO:0005856; GO:0005886; GO:0007507; GO:0014704; GO:0030057; GO:0031101; GO:0042060; GO:0043588; GO:0045104; GO:0060047; GO:0061436; GO:0098609
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250|UniProtKB:E9Q557}. Cell membrane {ECO:0000250|UniProtKB:E9Q557}.
| null | null |
PF00681;PF18373;PF21097;
|
IPR041573;IPR043197;IPR035915;IPR001101;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
dspb
| false |
563 |
A0A8P0N4K0
|
MLKCIPLWRCNRHVESVDKRHCSLQAVPEEIYRYSRSLEELLLDANQLRELPKPFFRLLNLRKLGLSDNEIQRLPPEVANFMQLVELDVSRNDIPEIPESIKFCKALEIADFSGNPLSRLPEGFTQLRSLAHLALNDVSLQALPGDVGNLANLVTLELRENLLKSLPSSLSFLVKLEQLDLGGNELEVLPDTLGALPNLRELWLDRNQLSALPPELGNLRRLVCLDVSENRLEELPAELGGLLLLTDLLLSQNLLQRLPDGIGQLKQLSILKVDQNRLCEVTEAIGDCENLSELILTENLLTALPRSLGKLTKLTNLNADRNRLEVLPPEIGGCAALSVLSLRDNRLATLPAELAHTAELHVLDVAGNRLQSLPFALTHLNLKALWLAENQAQPMLRFQTEDDAQTGEKVLTCYLLPQQPPPSLEESGLQSSPSESWSDAPPSRVSVIQFLEVPMCSDDAEGAAAEKRGLQRRATPHPSELKVMKRGVEERRGEAYSWKPESRLPSPLEEDKRLSTESGLSEDSQPSTGTASQGEPEGSLADTQGLSQQEAAPNAQEEAVEEETYEEPTVRFAEDTLLLPPAGEDGESEEGQLEAPWPLPGGRQRLIRKDTPHYKKHFKISKLPQPEAVVALLQGAQPDGEGPAGAGGWHNGPHTPWAPRAEEEDEEDEEEDEEEEEVAVAEEDKEEAVVSAPSIKGVSFDQANNLLIEPARIEEEELTLTIVRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAAQAGVRVGDKLLEVNGVALHGAEHHQAVEALRGAGTTVQMRLWRERMVEPENAVTVTPLRPEDDYSPRERRGAGLRLPLLQPEAAGPLRQRHVACLVRSEKGLGFSIAGGKGSTPYRAGDGGIFISRIAEGGAAHRAGTLQVGDRVLSINGVDMTEARHDHAVSLLTAASPTIALLLEREAGGPLPPSPLPHSPPPPVTAPSTVVTASPGESGPLRLAPSLLAATLEGPYPVEEICLPRAGGPLGLSIVGGSDHSSHPFGIQEPGVFISKVLPRGLAARSGLRVGDRILAVNGQDIREATHQEAVSALLRPCLELVLLVRRDPPPPGMRELCIQKAPGEKLGISVRGGAKGHAGNPCDPTDEGIFISKVSPTGAAGRDGRLRVGLRLLEVNQQSLLGLTHGEAVQLLRSVGDTLTVLVCDGFDTSTVAPAEVSPGVIANPFAAGVGRRNSLESVSSIDRELSPEGCGKEKEPPGPTPQWGLEAMVPPGTTGGKMAEGPHSSSCQQPPSPPSPDTLPTNVKQAYRTFAAVPGPHPLQDTPAQPPTPGPMASPEQLSFRERQKYFELEVRMPQAEGPPKRVSLVGADDLRKMQEEEARKLQQKRAQLMREAEDGALSLDLDGEAPDDEEPEEPPPWAGPAAGLSPSSPQPLGGGAPVRTAKAERRHQERLRVQSPELSTPLPDRALSPAERRALEAEKRALWRAARMKSLEQDALRAQMVLSKSQEGRSRRGPLERLAEAPSPAPTPSPTPVEDLGLQTSTSPGRLALSGRKFDYRVFAALPSSRPVCELQSPDFAEELRSLEPSPSPGLQEEDGEVAMVLLGRPSPGTVGPEEVTLCSSRRPVRPGRRGLGPVPS
|
Protein scribble homolog (Scribble)
|
Canis lupus familiaris (Dog) (Canis familiaris)
| 9,615 | 1,614 | 173,907 |
Cell junction;Cell membrane;Cell projection;Coiled coil;Cytoplasm;Developmental protein;Differentiation;Leucine-rich repeat;Lipoprotein;Membrane;Palmitate;Phosphoprotein;Reference proteome;Repeat;Synapse;Ubl conjugation
|
GO:0005737; GO:0005886; GO:0005912; GO:0010634; GO:0010669; GO:0030027; GO:0030054; GO:0030154; GO:0098793; GO:0098794
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19386766, ECO:0000269|PubMed:33730553}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q80U72}. Cell junction {ECO:0000269|PubMed:33730553}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q14160}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q14160}. Cytoplasm {ECO:0000269|PubMed:19386766, ECO:0000269|PubMed:33730553}. Postsynapse {ECO:0000250|UniProtKB:Q14160}. Presynapse {ECO:0000250|UniProtKB:Q14160}. Note=Targeting to cell-cell junctions which is CDH1-dependent is required for the pro-apoptotic activity (By similarity). In a subset of CD4+ T-cells, colocalizes with CRTAM at the immunological synapse during the late phase of T-cell activation (By similarity). Localized to small puncta throughout the cytoplasm and cell membrane when in the presence of SNAIL1 (PubMed:33730553). Localized along the length of perinuclear emanating vimentin bundles and at vimentin-positive fibrils at the cell periphery (PubMed:19386766). Localized to the lateral plasma membrane during the establishment and maturation of cell-cell contacts (PubMed:19386766). {ECO:0000250|UniProtKB:Q14160, ECO:0000250|UniProtKB:Q80U72, ECO:0000269|PubMed:19386766, ECO:0000269|PubMed:33730553}.
| null | null |
PF23598;PF13855;PF00595;
|
IPR001611;IPR003591;IPR032675;IPR055414;IPR001478;IPR036034;IPR050614;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Canidae (family), Canis (genus), Canis lupus (species)
|
SCRIB
| false |
564 |
A0A8U0WQF3
|
MFIPSHQVWLVGLLAFSLVGAEYYDTKTADKDFLLKQKKVYNLLYRVAQPALANITWYNEGQAWNIEANIDSYTNAAAVKEFLSIYKHGMLPRGELFSLYYPQLLREMSALFKLFYHAKDFDIFFKTALWAKNNINEAQYIYSLYTAVITRPDTKFIQLPPLYEMCPYFFFNSEVLQKANHALIFGKLDTKTSGKYKEYIIPANYSGWYLNHDYNLENKLIYFIEDIGLNTYYFFLRQAFPFWLPSKEYDLPDYRGEEYLYSHKLLLNRYYLERLSNDLPHLEEFDWQKPFYPGYYPTMTYSNGLPFPQRPIWSNFPIYKYKYIREIMNKESRISAAIDSGYILNNDGKWHNIYSEKGLNILGNIIEGNADSYNTEFYGSIDTLARKILGYNLEAASKYQIVPSALEIFSTSMKDPAFYRIYKRIIDYYHSYKMHQKPYNKDEIIYPNLKIESFTVDKLITYFEQFDTTINNGLLLEEQRNDDKPFLIKIRQYRLNHKPFNFHITINADKPMKAAIRIFIGPKYDSHHKLIEIPEDLKYFYEIDNWMLDLNSGLNKITRNSLDCFFTMNDLEPSEIFYEKIETSLNSDKPFTYNERIFGFPGRLLLPRGKKEGMPFQLFLYVSPVSSEYNQYNSRIWGGYKFDKRSFGFPLDKPLYDFNYEGPNMLFKDILIYHKDEFDMNITY
|
Hexamerin 70a (Arylphorin Hex70a)
|
Apis mellifera (Honeybee)
| 7,460 | 684 | 81,460 |
Chromosome;Cytoplasm;Direct protein sequencing;Glycoprotein;Nucleus;Reference proteome;Secreted;Signal;Storage protein
|
GO:0005576; GO:0005694; GO:0005730; GO:0005737; GO:0045735
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26466725}. Nucleus {ECO:0000269|PubMed:22205988, ECO:0000269|PubMed:26466725, ECO:0000269|PubMed:36630080}. Cytoplasm {ECO:0000269|PubMed:22205988, ECO:0000269|PubMed:26466725, ECO:0000269|PubMed:36630080}. Cytoplasmic granule {ECO:0000269|PubMed:26466725, ECO:0000269|PubMed:36630080}. Nucleus, nucleolus {ECO:0000269|PubMed:36630080}. Chromosome {ECO:0000269|PubMed:36630080}. Note=Localizes to the nucleus in a punctate pattern closely associated with chromatin (PubMed:22205988, PubMed:26466725). Localizes to the nucleus in ovarian germline and somatic cells, and to the posterior extremity of nuclei in spermatid syncytia and individualised spermatozoa (PubMed:22205988). Localizes in foci within the cytoplasm of some cells of the fat body and gonads; these are probably cytoplasmic granules formed by endocytosis of hexamerins (PubMed:22205988, PubMed:26466725, PubMed:36630080). Localizes to the nucleus of neuronal cells (PubMed:36630080). Localizes to nuclear foci in trophoblasts and oenocytes of the fat body, which colocalize with fibrillarin and histones (PubMed:36630080). {ECO:0000269|PubMed:22205988, ECO:0000269|PubMed:26466725, ECO:0000269|PubMed:36630080}.
|
SIGNAL 1..21; /evidence="ECO:0000269|PubMed:9692239"
| null |
PF03723;PF00372;PF03722;
|
IPR008922;IPR013788;IPR000896;IPR005203;IPR037020;IPR005204;IPR036697;IPR014756;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Hymenoptera (order), Apocrita (suborder), Aculeata (infraorder), Apoidea (superfamily), Anthophila (clade), Apidae (family), Apinae (subfamily), Apini (tribe), Apis (genus)
|
Hex70a GB30362 hex71
| false |
565 |
A0A8V0ZB02
|
MLPYVIATLGSAGSTCKASTCSNSTKDYCYSARIRSTVLQGLPFGGVPTVLALDFMCFLALLFVFSILRKVAWDYGRLALVTDADSIASALHSDNHDRYERLTSVSSSVDFDQRDNGFCSWLTAIFRIKDDEIRDKCGGDAVHYLSFQRHIIGLLVAVGVLSVGIVLPVNFSGDLLENNAYSFGRTTIANLNSGNNLLWLHTSFAFLYLLLTVYSMRRHTSKMRYKEDDLVKRTLFINGISKYAEPEKIKKHFEEAYANCTVLEARPCYDVARLMFLDAERRKAERGRIYFTNLQSKENTPSMINPKPCGHLCCCVIRGCEEVEAIEYYTKLEEKLKDDYKREKEKVNEKPLGMAFVTFHNETITAIILKDFNACKCQGCACRGEPRASSCSESLHVSNWTVSYAPDPQNIYWEHLSIRGFIWWIRCLVINVVLFILLFFLTTPAIIITTMDKFNVTKPVEYLNNPIITQFFPTLLLWCFSALLPTIVYYSAFFEAHWTRSGENRTTMHKCYTFLIFMVLLLPSLGLSSLDVFFRWLFDKKFLAEAAVRFECVFLPDNGAFFVNYVIASAFIGNAMDLLRIPGLLMYMIRLCLARSAAERRNVKRHQAYEFQFGAAYAWMMCVFTVVMTYSITCPIIVPFGLMYMLLKHLVDRYNLYYAYLPAKLDKKIHSGAVNQVVAAPILCLFWLLFFSTMRTGFLAPTSMFTFVVLVITIVICLCHVCFGHFKYLSAHNYKIEHTEVDTTESRQNGRPATNLPAPKSAKYIAQVLQDSSPEGEATESEEQGSQDEELITTDGMNDTDFQSCEDSLIENEIRQ
|
Mechanosensitive cation channel TMEM63B (Transmembrane protein 63B)
|
Gallus gallus (Chicken)
| 9,031 | 816 | 92,953 |
Calcium;Cell membrane;Endosome;Ion channel;Ion transport;Lipoprotein;Lysosome;Membrane;Palmitate;Reference proteome;Transmembrane;Transmembrane helix;Transport
|
GO:0005227; GO:0005765; GO:0005886; GO:0007605; GO:0015629; GO:0017128; GO:0031901; GO:0036335; GO:0042756; GO:0120019; GO:0140135; GO:0140338; GO:0160069; GO:1990760
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T3F8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T3F8}. Lysosome membrane {ECO:0000250|UniProtKB:Q5T3F8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T3F8}. Early endosome membrane {ECO:0000250|UniProtKB:Q5T3F8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T3F8}.
| null |
TRANSMEM 47..71; /note="Helical; Name=TM0"; /evidence="ECO:0000250|UniProtKB:Q3TWI9"; TRANSMEM 139..171; /note="Helical; Name=TM1"; /evidence="ECO:0000250|UniProtKB:Q3TWI9"; TRANSMEM 196..220; /note="Helical; Name=TM2"; /evidence="ECO:0000250|UniProtKB:Q3TWI9"; TRANSMEM 421..450; /note="Helical; Name=TM3"; /evidence="ECO:0000250|UniProtKB:Q3TWI9"; TRANSMEM 466..495; /note="Helical; Name=TM4"; /evidence="ECO:0000250|UniProtKB:Q3TWI9"; TRANSMEM 500..536; /note="Helical; Name=TM5"; /evidence="ECO:0000250|UniProtKB:Q3TWI9"; TRANSMEM 560..592; /note="Helical; Name=TM6"; /evidence="ECO:0000250|UniProtKB:Q3TWI9"; TRANSMEM 613..631; /note="Helical; Name=TM7"; /evidence="ECO:0000250|UniProtKB:Q3TWI9"; TRANSMEM 635..659; /note="Helical; Name=TM8"; /evidence="ECO:0000250|UniProtKB:Q3TWI9"; TRANSMEM 667..695; /note="Helical; Name=TM9"; /evidence="ECO:0000250|UniProtKB:Q3TWI9"; TRANSMEM 701..721; /note="Helical; Name=TM10"; /evidence="ECO:0000250|UniProtKB:Q3TWI9"
|
PF14703;PF02714;PF13967;
|
IPR045122;IPR003864;IPR027815;IPR032880;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Archelosauria (clade), Archosauria (clade), Dinosauria (clade), Saurischia (clade), Theropoda (clade), Coelurosauria (clade), Aves (class), Neognathae (infraclass), Galloanserae (superorder), Galliformes (order), Phasianidae (family), Phasianinae (subfamily), Gallus (genus)
|
TMEM63B
| false |
566 |
A0A8V1ABE9
|
MWLGALLDTLPTPALTIDRTTAHRNAERMRERCRALGVRLRPHVKTHKTLEGGLLATGGTRRGIAVSTLAEARFFADGGFDDILLAYPVPTARLEECAGLARRLDAFHVLLDRPEALASLRQRPLGHGKRWLVWLKLDCGNGRAGVRPTDPAALELAQAIANDAPEEVTLVGVYAHCGNTYGCSGADTIQAIARTTTNAVLSFVAALRQAGVPCPQASIGSTPSCSHPIPEMSQLTELHPGNYIFYDLQQTQLGSCQPQDVAIRVLTRVIGHYAHRGQLLVDCGWAALSLHGAGAGQGPQGCAAIDGHPELRLVGLTQEHGLLEHAGGQMDFGRFPVGSVLALIPYHACATAAMHPVYYVHEEGKVVALWHPVRGW
|
D-serine dehydratase (EC 4.3.1.18) (D-serine deaminase)
|
Gallus gallus (Chicken)
| 9,031 | 376 | 40,379 |
3D-structure;Cell projection;Cytoplasm;Direct protein sequencing;Lyase;Metal-binding;Pyridoxal phosphate;Reference proteome;Zinc
|
GO:0005737; GO:0008270; GO:0008721; GO:0030170; GO:0030425; GO:0036088
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24529545}. Cell projection, dendrite {ECO:0000269|PubMed:24529545}.
| null | null |
PF01168;PF14031;
|
IPR001608;IPR051466;IPR026956;IPR042208;IPR029066;
|
3ANU;3ANV;3AWN;3AWO;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Archelosauria (clade), Archosauria (clade), Dinosauria (clade), Saurischia (clade), Theropoda (clade), Coelurosauria (clade), Aves (class), Neognathae (infraclass), Galloanserae (superorder), Galliformes (order), Phasianidae (family), Phasianinae (subfamily), Gallus (genus)
|
DSD
| false |
567 |
A0A9E7S4M3
|
MEMMQLSFASAVVYSLIFFVFLLVKQLLKPKSHKKLPPGPWTLPIIGNLHQILGALPHRIFKDLSDKYGPLMRIMMGERTTIIVSSATMAKVVLHTHGLAVANRPINSVAKVICYNNLGVTFAEYGEYLKQLRQLYMLELLSPKRVQSFSAVFEDELQTFVKSIKSEVGQPMIIYEKSVTYLYSTICRVMLGNVCNEREKLIKICKKVSFYSAAPIRIEDLFPSMKFIISRIFSTNSILKDLLKDLDDVLDIVIAERENSQYAQEEEDMLGILLKHKRSDGNNSKLKITNKDIKAIIFELLLAATLSVADVVEWAMVEILRHPKVLKQVHDEVRQAFKGQKTITGSDLGKLEYLHMCFKESTRLHPAAPLLFPREAREEFEIDGYTIPKGSWVLTNYWAVGRDPRIWPKPDEFDPERFRNSDIEFYGNHFELIPFGTGRRGCPGILFGITEALYLLAALFYHFDWKLAGGITPEEIDMTEVFGAGCILKNPLNLIPRLAEN
|
Rhazimal synthase (AsRHS) (EC 1.14.14.187) (Cytochrome P450 RHS) (Geissoschizine oxidase RHS) (EC 1.14.19.80)
|
Alstonia scholaris (Dogbane) (Echites scholaris)
| 52,822 | 501 | 57,128 |
Alkaloid metabolism;Glycoprotein;Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Transmembrane;Transmembrane helix
|
GO:0004497; GO:0005506; GO:0016020; GO:0016705; GO:0020037; GO:0035835
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 4..24; /note="Helical"; /evidence="ECO:0000255"
|
PF00067;
|
IPR001128;IPR017972;IPR002401;IPR036396;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Gentianales (order), Apocynaceae (family), Rauvolfioideae (subfamily), Alstonieae (tribe), Alstonia (genus)
|
RHS
| false |
568 |
A0A9E7S4M4
|
MEFSFSSPLLYILYFLLFFIVRQLLKPKSNRKLPPGPRTLPIIGNLHQLRGSLPHRTLKKLSDKHGPLMHLKMGERSAIIVSDARMAKIVLHNHGLAVADRSVNTVASIMTYNSLGVTFAQYGDYLTKLRQIYTLELLSPKKVRSFYNCFEDELDVFVKSIRSQVGQPMVLYEKVSTYLYATICRTIFGSVCKEREKMIKIVKRTSLLSGTPLRMEDLFPSMRVFCRFSKTLNQLRGLLQEMDGILEDIIVEREKTTEILKEAKDDEDMLSVLLRHKWYNPSGARFRITNADIKAIIFELILAATLSVADVVEWAMVEILRHPAILKKVYDEGRGICKEKKRVTGYDVEKMEYMRLCVKESTRVHPAAPLLVPRECREDFEVDGYTVPKGAWVLTNCWAIQMDPEIWPEPEKFDPERYIRNPMDFYGSNFELIPFGTGRRGCPGILYGVTNAELLLAAMFYHFDWEIADGKKPEDIDLTENFGAGCIMKYPLTLVPHLANE
|
Geissoschizine oxidase (AsGO) (EC 1.14.19.80) (Cytochrome P450 GO)
|
Alstonia scholaris (Dogbane) (Echites scholaris)
| 52,822 | 501 | 57,554 |
Alkaloid metabolism;Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Transmembrane;Transmembrane helix
|
GO:0004497; GO:0005506; GO:0016020; GO:0016705; GO:0020037; GO:0035835
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 1..21; /note="Helical"; /evidence="ECO:0000255"
|
PF00067;
|
IPR001128;IPR017972;IPR002401;IPR036396;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Gentianales (order), Apocynaceae (family), Rauvolfioideae (subfamily), Alstonieae (tribe), Alstonia (genus)
|
GO
| false |
569 |
A0A9E8G339
|
METFLYTSESVNEGHPDKLCDQISDAVLDACLEQDPDSKVACETCTKTNMVMVFGEITTKANVDYEKIVRNTCRNIGFVSDDVGLDADNCKVLVNIEQQSPDIAQGVHGHLTKRPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCPWLRPDGKTQVTVEYYNDKGAMVPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSIVANGLARRCLVQVSYAIGVPEPLSVFVDSYGTGKIPDKEILKIVKENFDFRPGMISIHLDLKRGGNGRFLKTAAYGHFGREDPDFTWETVKPLKWEKPQA
|
S-adenosylmethionine synthase (AdoMet synthase) (SAM-synthetase) (EC 2.5.1.6)
|
Acacia koa (Koa tree)
| 468,172 | 393 | 43,180 |
ATP-binding;Cobalt;Cytoplasm;Magnesium;Metal-binding;Nucleotide-binding;One-carbon metabolism;Potassium;Transferase
|
GO:0004478; GO:0005524; GO:0005737; GO:0006556; GO:0006730; GO:0046872
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9LUT2}.
| null | null |
PF02773;PF02772;PF00438;
|
IPR022631;IPR022630;IPR022629;IPR022628;IPR002133;IPR022636;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Fabales (order), Fabaceae (family), Caesalpinioideae (subfamily), mimosoid clade (clade), Acacieae (tribe), Acacia (genus)
|
KSAMS
| false |
570 |
A0A9J9HGY6
|
MNKVRTCWNEGRPALAGWLQLPGTLHAEALARLDYDAVVIDMQHSPIDFGQVAPMLIAIELGGAEPFVRTQVNDPSDIMKLLDAGAYGIIAPMVNTRAEAQTLASALHYSPRGLRSFGPRRPSLRYGSGYLAQASETVVGLAMIETREALANIDEILSVDGIDGVFIGPTDLALDLGHAPLVDTEEAEVVSAIAHVRERAHAAGKRVGIFCGSGGFARVKLAEGFDFVTAAPDLAMLSAAARQVIADARAL
|
Hydroxypyruvate/pyruvate aldolase (HPA/PA aldolase) (EC 4.1.2.-) (Hydroxy ketoacid aldolase) (SwHKA)
|
Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1) (Sphingomonas wittichii)
| 392,499 | 251 | 26,612 |
3D-structure;Cobalt;Lyase;Magnesium;Manganese;Metal-binding;Plasmid;Pyruvate;Reference proteome;Zinc
|
GO:0005737; GO:0016832; GO:0046872
|
Evidence at protein level
| 5 | null | null | null |
PF03328;
|
IPR005000;IPR050251;IPR015813;IPR040442;
|
6R62;7NNK;7NR1;7NUJ;7O5I;7O5R;7O5V;7O5W;7O87;7O9R;7OBU;8ADQ;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Alphaproteobacteria (class), Sphingomonadales (order), Sphingomonadaceae (family), Rhizorhabdus (genus), Rhizorhabdus wittichii (species)
|
Swit_5035
| false |
571 |
A0AA51VIL7
|
MGSYHDEKNVMGGSDQGELCSLAMTIASGSVPAMVLKALIELDVLELIKRAGPGAQLSPAQIVAQLPTKNPDAGTMLDRMLRLLASYEILSCSTQTLPDGRVERLYGLAPVCQFFTNNEDGATLGAIVQLSQEKLVVESWYHLKDAVLDGGIPFKKAQGMTIYEYPKTDPRFNQVFNSGMSNYSTIIMRDLLERYKGFEGISTLVDIAGGTGASINMVVSKYPTIKGINFDLPHVIKDAPSYDGVEHVGGDMFESVTKADAMLIKWTLCDWSDEHCLKLLKNCYNALPDNGKVIVCDYVLPMAPETSNAAKTVFLLDAIMLANFVGGKGRTKQEFEALARKVGFEGFEVPCSSYDFSVMELFKKKNN
|
Tyramine N-methyltransferase 1 (LwNMT1) (EC 2.1.1.27) (O-methyltransferase 4) (LwOMT4)
|
Lophophora williamsii (Peyote) (Echinocactus williamsii)
| 130,138 | 367 | 40,190 |
Alkaloid metabolism;Methyltransferase;S-adenosyl-L-methionine;Transferase
|
GO:0008171; GO:0032259; GO:0046983
|
Evidence at protein level
| 5 | null | null | null |
PF08100;PF00891;
|
IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), Caryophyllales (order), Cactineae (suborder), Cactaceae (family), Cactoideae (subfamily), Cacteae (tribe), Lophophora (genus)
|
NMT1 OMT4
| false |
572 |
A0AAQ4VMX2
|
MRLLWGLAWVFSFCASSLQKPRLLLFSPSVVNLGTPLSVGVQLLDAPPGQEVKGSVFLRNPKGGSCSPKKDFKLSSGDDFVLLSLEVPLEDVRSCGLFDLRRAPYIQLVAQSPWLRNTAFKATETQGVNLLYSSRRGHIFVQTDQPIYNPGQRVRYRVFALDQKMRPSTDFLTITVENSHGLRVLKKEIFTSTSILQDTFTIPDISEPGTWKISARFSDGLESNRSTHFEVKKYVLPNFEVKITPWKPYILMVPSNSDEIQLDIQARYIYGKPVQGVAYTRFALMDEQGKRTFLRGLETQAKLVEGRTHISISKDQFQAALDKINIGVRDLEGLRLYAATAVIESPGGEMEEAELTSWRFVSSAFSLDLSRTKRHLVPGAHFLLQALVREISGSEASNVIVKVSPTLVSGSDSQVLNVQQSTNRIGQVSISFPIPPTVTGLRLLVSAGSLYPMIARLTVQSPPSRGTGFLSIEPLDPRSPRVGDTFILNLQAVGIPAPTFSHYYYMIISRGQIMAMSREARRTVTSVSVLVDHQLAPSFYFVAYFYHQGHPVANSLLINIQPRDCEGKLQLKVVGAKEYHNGDMMKLRIQTDSKALVALGAVDTALYAVGGWSHKPLDMSKVFEVINSYNVGCGPGGGDDAPQVFQDAGLAFSDGDRLTQTREDLSCPKEKKSRQKRNVNFLKALSEKLGQYSSPDAKRCCQDGMTKLPMKRTCEQRAARVPQQACREPFLSCCKFAEDLRRNQTRSQAPLARKVRDMVNLIEEDDILVRTSFPENWLWRVEPVDSSKLLTVRLPDSMTTWEIHGVSLSKSKGLCVAKPTRVRVFRKFHLHLRLPISVRRFEQLELRPVLYNYLNDDKNVSVHVTPVEGLCMAGGGMMAQWVIVPAGSALPVAFSVVPTASTNVPLKLVAKGTLDSSDSVSKILQIEKEGAIHREEIVYNLDPLNNLGQMLEIPGSSDPNIVPEGDFSTFVKVTASEPLETLGSEEALSPGGVASLLRLPGCAEQTMIYLAPTLTASNYLDRTKQWSKLSPETKDHAVHLIQKGHVRIQQFRKKDGSFGAWLHRDSSTWLTAFVLKILSLAQEQVGNSPEKLQETASWLLAQQLGDGSFHDPCPVIHRAMQGGLVGSNETVALTAFVVIALHHGLNVFREGHAKQLKNRVEASITKANSFLGQKASAGLLGAHAAAITAYALTLTKASEDLRNVAHNSLMAMAEETGENLYWGLVLGSQDKVVLRPADPRSPTEPVPQAPALWIETTAYALLHLLLREGKGKMADKAASWLTHQGNFHGAFRSTQDTVVTLDALSAYWIASHTTEEKALKVTLSSMGRNGLKTHVLHLNNHQVKGLEEELKFSLGSTISVKVEGNSKGTLKILRTYNVLDMKNTTCQDLQIEVKVTDAVEYAWSAYEDYEDDYNMPATDDPSVPLQPVTPLQLFEGRRSRRRREAPKVAEERESRVHYTVCIWRNGKLGLSGMAIADITLLSGFHALRADLEKLTSLSDRYVSHFETDGPHVLLYFDSVPTTRECVGFGASQEVVVGLVQPASAVLYDYYSPDHKCSVFYAAPTKSQLLATLCSGDVCQCAEGKCPRLLRSLERRVEDKDGYRMRFACYYHQVEYGFTVKVLREDGRAAFRFFESKITQVLHFRTDTMASIGQTRNFLSRTSCRLRLEPNKEYLIMGMDGETSDNKGDPQYLLDSNTWIEEMPSEQMCKSTRHRAACFQLKDFLMEFSSRGCQV
|
Complement C4-A (Sex-limited protein) [Cleaved into: Complement C4 beta chain; Complement C4-A alpha chain; C4a anaphylatoxin; Complement C4b-A; Complement C4 gamma chain]
|
Mus musculus (Mouse)
| 10,090 | 1,734 | 192,883 |
Alternative splicing;Cell projection;Cleavage on pair of basic residues;Complement pathway;Disulfide bond;Glycoprotein;Immunity;Inflammatory response;Innate immunity;Phosphoprotein;Reference proteome;Secreted;Signal;Sulfation;Synapse;Thioester bond
|
GO:0004866; GO:0005615; GO:0006954; GO:0006956; GO:0006958; GO:0030424; GO:0030425; GO:0045087; GO:0045202
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C0L4}. Synapse {ECO:0000250|UniProtKB:P0C0L4}. Cell projection, axon {ECO:0000250|UniProtKB:P0C0L4}. Cell projection, dendrite {ECO:0000250|UniProtKB:P0C0L4}.; SUBCELLULAR LOCATION: [C4a anaphylatoxin]: Secreted {ECO:0000250|UniProtKB:P0C0L4}.; SUBCELLULAR LOCATION: [Complement C4b-A]: Secreted {ECO:0000250|UniProtKB:P0C0L4}. Cell surface {ECO:0000250|UniProtKB:P0C0L4}. Note=Covalently associated with the surface of pathogens: the internal thioester bond reacts with carbohydrate antigens on the target surface to form amide or ester bonds. {ECO:0000250|UniProtKB:P0C0L4}.
|
SIGNAL 1..19; /evidence="ECO:0000255"
| null |
PF00207;PF07703;PF07677;PF01821;PF21145;PF22661;PF01835;PF17791;PF01759;PF07678;
|
IPR009048;IPR036595;IPR050473;IPR011625;IPR047565;IPR011626;IPR000020;IPR018081;IPR001840;IPR048847;IPR054587;IPR013783;IPR001599;IPR002890;IPR041555;IPR001134;IPR018933;IPR008930;IPR008993;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Mus (genus), Mus (subgenus)
|
C4a Slp
| false |
573 |
A0AAR7
|
MGYDQTRKLSDEYEISEILGRGGFSVVRKGTKKSGNEKTQVAIKTLRRLGSSPSGTGGGQKSTATVMGFPSLRQVSVSDALLTNEILVMRRIVENVSPHPNVIDLYDVCEDSNGVHLVLELCSGGELFDRIVAQDKYAETEAAAVVRQIAAGLEAVHKADIVHRDLKPENCLFLDSRKDSPLKIMDFGLSSVEEFTDPVVGLFGSIDYVSPEALSQGKITAKSDMWSLGVILYILLSGYPPFIAQNNRQKQQMIINGNFSFYEKTWKGITQSAKQLISSLLTVDPSKRPSAQELLSHPWVRGDKAKDEQMDPEIVSRLQSFNARRKLRAAAIASVWSSTIFLRTKKLRSLVGTYDLKEEEIESLRIHFKKICGNGDNATLSEFVEVLKAMKMPSLIPLAPRIFDLFDNNRDGTIDMREILCGFSSLKNSKGDDALRLCFQMYDTDRSGCITKEEVASMLCALPEECLPADITEPGKLDEIFDLMDANSDGKVTFEEFKAAMQRDSSLQDMLLSSLRPS
|
Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase (LjCCaMK) (EC 2.7.11.17)
|
Lotus japonicus (Lotus corniculatus var. japonicus)
| 34,305 | 518 | 57,480 |
ATP-binding;Calcium;Calmodulin-binding;Coiled coil;Kinase;Metal-binding;Nodulation;Nucleotide-binding;Nucleus;Phosphoprotein;Repeat;Serine/threonine-protein kinase;Transferase
|
GO:0004683; GO:0005509; GO:0005516; GO:0005524; GO:0005634; GO:0009608; GO:0009877; GO:0106310
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19074278, ECO:0000269|PubMed:21209278}.
| null | null |
PF13202;PF13499;PF00069;
|
IPR050205;IPR011992;IPR018247;IPR002048;IPR011009;IPR000719;IPR017441;IPR008271;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Fabales (order), Fabaceae (family), Papilionoideae (subfamily), 50 kb inversion clade (clade), NPAAA clade (clade), Hologalegina (clade), robinioid clade (clade), Loteae (tribe), Lotus (genus)
|
CCAMK
| false |
574 |
A0AAS4
|
MSASTMKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGRDLINLTQEDFTKPPLCRVSSDNGQRLLDMIETLKMEHHMEAHKNGHANGHLSIGTDVPAPDGSFSIKVKPNGMPNGYRKEMIKIPMPEPERSQYPMEWGKTFLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFFDHFNRVQWAFSICEINGMILVGLWLIQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTTLPVPGMHFNCSPKLFGDWEAQLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYLFIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQVLKEASQMNLLARVWWYRPFQYFEKNVQGIVPRSYHWPFPWPVVHLGRQVKYSRLVNDT
|
Phosphatidylcholine:ceramide cholinephosphotransferase 1 (EC 2.7.8.27) (Sphingomyelin synthase 1)
|
Sus scrofa (Pig)
| 9,823 | 418 | 48,984 |
Apoptosis;Golgi apparatus;Kinase;Lipid metabolism;Membrane;Phosphoprotein;Reference proteome;Sphingolipid metabolism;Transferase;Transmembrane;Transmembrane helix
|
GO:0000138; GO:0000139; GO:0002950; GO:0005789; GO:0005886; GO:0006686; GO:0006915; GO:0016301; GO:0033188; GO:0046513; GO:0047493
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86VZ5}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 141..161; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 189..209; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 220..240; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 281..301; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 309..329; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 335..352; /note="Helical"; /evidence="ECO:0000255"
|
PF14360;
|
IPR001660;IPR013761;IPR045221;IPR025749;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Suina (suborder), Suidae (family), Sus (genus)
|
SGMS1 SMS1
| false |
575 |
A0AAW1JA93
|
MELITLLSALLVLAIVSLSTFFVLYYNTPTKDGKTLPPGRMGWPFIGESYDFFAAGWKGKPESFIFDRLKKFAKGNLNGQFRTSLFGNKSIVVAGAAANKLLFSNEKKLVTMWWPPSIDKAFPSTAQLSANEEALLMRKFFPSFLIRREALQRYIPIMDDCTRRHFATGAWGPSDKIEAFNVTQDYTFWVACRVFMSIDAQEDPETVDSLFRHFNVLKAGIYSMHIDLPWTNFHHAMKASHAIRSAVEQIAKKRRAELAEGKAFPTQDMLSYMLETPITSAEDSKDGKAKYLNDADIGTKILGLLVGGHDTSSTVIAFFFKFMAENPHVYEAIYKEQMEVAATKAPGELLNWDDLQKMKYSWCAICEVMRLTPPVQGAFRQAITDFTHNGYLIPKGWKIYWSTHSTHRNPEIFPQPEKFDPTRFEGNGPPAFSFVPFGGGPRMCPGKEYARLQVLTFVHHIVTKFKWEQILPNEKIIVSPMPYPEKNLPLRMIARSESATLA
|
Beta-amyrin 28-monooxygenase CYP716A379 (EC 1.14.14.126) (Cytochrome P450 716A379) (SoCYP716A379) (Oleanolic acid 16-monooxygenase CYP716A379) (EC 1.14.14.-)
|
Saponaria officinalis (Common soapwort) (Lychnis saponaria)
| 3,572 | 502 | 56,964 |
Glycoprotein;Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Signal-anchor;Transmembrane;Transmembrane helix
|
GO:0004497; GO:0005506; GO:0016020; GO:0016104; GO:0016125; GO:0016135; GO:0020037; GO:0102373
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}.
| null |
TRANSMEM 3..23; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"
|
PF00067;
|
IPR001128;IPR017972;IPR002401;IPR036396;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), Caryophyllales (order), Caryophyllaceae (family), Caryophylleae (tribe), Saponaria (genus)
|
CYP716A379 Saoffv11043486m RND81_08G189800
| false |
576 |
A0AUJ5
|
MPTRYRGADRYGNLGYDKVLQSKADAAKRRGLLFDHGSETYECPRCGEIWRNLDDYMAEGGKMHPKKCLPEECDSDEEQISSCNAALIHEKWGDLDSDTSSKLSEFYKEPSILTYTTRTHCVVEKMRSMTAPQCIEDIVGVRLHGRTAWFFSKDPTLQYGHHPIYYDTHPWNDELDKYLGGAKYNTALVQVYDGTRDLPYHKDDEPCYDITNNPIRTVNVTGTGDLCISKDKRRLYETIPMTSGTVITFPATMQENFYHAVRNPSAGRISITFRNQIRTVERQVAHSANKRWVPIVEARVTTNESRRGDNKQFQEAQSKLQTKTTINFGEFAAEVDGYYPTLSQDHKPALPKIIPELGLPTVDFIYVGNMRVPIDFKKNNVPAIVDTARHVAKIIDSQALTSEPIKVFTEQREVVGNVVTCTGTGFSVADAKEAKALLNGLMYNRASNLFICPSCSDAAVLPEALLTLEHKRSCELASMKKISLARNMQVHVKQEAVARLISQQNSISVPIATLSSCVRGSADTTQVSLHIDEEDSIVDAIHLPNDFITCDHEHAFETDSASDNDVETMKKSEKRRKRRKRNPPPVRQVITRAPVSNIICDVILTCLETQIPVEFIGKSCITFKPVRVGPVHTVGIQLKHQLHKTGFEVDDLPDRETTSDIILAATRALRRLRHAHSNAQQVHNSDITFGTSGAILPWSWLAHDVIVEGPVQDSLVVRGRNVVSGHVTNALNLQQDCLADDYLQYSEELQPLHDDLSELKPLNVINNELIRQNMHITTLYSNMSKLQNDALATKAEMKLPLFGVAQLVVNQLKYNTTTHEWGERGDYVRKFVGKFFADFPTTQVPKQYMTRTTNGHIRITAYKALSLTSDPEIMMSRRMTQPMLTTAKQADCVFQSTTGATCTSASCTTNSSGVVLSNKCADPAPNTLRVRTMWDDIIIELPLQGGRVHVPLEGLCFSTIFLHMYLLVPDESVKLFHRTVTERAMPSLGQWPTLRHLATWVLNLVAMFPVLSTTPMPEILVHHESQSVHIPDCLGTATSGYHRLNIVTPYDFIIFATEIGRNGCQEYRVGGFAHDIKYTVSLMQDKRKLLHELMLTPTWAFYALSSPTLLKILYRSGALKRTYEHAVMANHNAVDLVHELNFLPERVSRAQTLQDEITAWEANVGRVLQQVDGYLTRNHDPPLQRWYADASARLQHLKIDVDLLKNGFRSSQREHVEKKEQLLCDSFERLYNEQNSSLESLKTRCGMGSARALIKPSGKCESPEPAKQLSCKDLICSTKDKYALMLYTQADALKRKIVAGSQSAFTTVCAGVAYRATKVMLRTPFNLLNALNTYSLLIAAVNVMVLVQNYRRDQRKRAQYVNNLETQSMIRHYFAHLEQYIVNYVPRDEQFEVIKAKFDEEFPEYNVMFKEVYKERIQFQSADEGKNMCKIFASAILVMMVFDAHRADLMYKSFSQVRALFNTLYDSGNPFNIIFQAERTIAPTMDVIIQEPKPAIPSTSSCTFETWFRNCVNANNVIPVIPECDLLDFTRDTASSVVATLTSSVKREFVIRGFVGSGKSTYLPHLLTKHGKVLLCEPVRVLASNVFEALSGSPFYQSPTLLMRGTTKFGSGKITVATSGYAANYYNANRHRLNEFAYIIFDESHQHTAHNFLLRSILDVIGYEGTVLHVSATPIGKEIPFRTMHPVEVVNMSTLSFEDFAIGQRKQVRCDVFNKGANILVYVASYNDVDRMSTLLLERGLRVKKIDARTVANVNNITCDGSDGEPLYLVATNIVENGVTLNVDVVVDFGLCVKPVINALQRRVDYVKTPITWGQRIQRNGRVGRYKNGFCLNVGDVYKTPPIISEDVALESALMCFAANVPPIFDNVDPALFGQVTRPQVQTAQMFELPIYITTPMISDAGALQSDIYQVIKKFVLREGSIQLTQDATYLSNMSNWKTIADYFPDISDTHAMRHEKVPFFVKDFGENSYIALAEAIRKARNKSLGARGKLYGDVDATALLLQTDPGSLDRSIMIVETELVAQRSKLEDLNHHVHESTGMFQRYVSHLNHCLRGRYQTDQIQKNIEVLSNMRSTLVGYRQVVDKVEPEEIPHFVQQNPNITMIIDFQSDRTKADGFVKHGINGIYNYTKIASDTFSLLLIACVVIYYVVQYFFREMKSHITFEASGSRRNRLHLRDNKLIKGGYTWAGPSDDMEREFGPEYALKRDKFSEKKARKHMRERIQPRTNMGVKLAPFQVFYGFDVADYDVLQLFDPITGVKIDMDPRATAKEITEEVEDTPFNKEVWSDTHMPEKIQATFVKKGGVNREDVLKQVRVDMTTHNPTMVTGSGGIMGYPEHKGDFRQTGPPKFSIVPEGRSTIKSGNNIAPFISAMGTIKNVYMNGDFDTLACTQIGNKLVVNAHIFMEPVKKQELILQHGVYELPNNGTINIKHVPGIDMVIQTLPMDVPLARQIKAYRGPIPGELIRLLKIERNTKTNSTSLSDPGTARVGPGTIWYHNITTKHGDCGSLVLSEKDNKIVGIHTGQQDGTNLNLFAPITKDAIVAIETVLPGELNDWVFTPDMLDVGSNNAIRKQASDPFPVVKKLLEGITFQNNRTTTTDSVSNTAILPARKYWVASDLPVNIKYQCDMPTFFNTRHTYEGESQPFMAYLRECGDAETFFRPLLSHYIPSNLNGDAFKKDFFKYGKPVPVGLVHGPSFKIASDRVIKRFERVGYERHSIPFEFDAEAIRDDLNKHAAMGAQYVGKKEQHLDGISEEQFCDEFVASCCRLANNCDGVWKGSLKAELRSKEKVQENKTRVFTSAPYDVLLGGKACVMHFNKKFYANNTKGPWTVGINKLGLGWHRLLKSLPEGFVYGTGDGSQFDSSLTPLLINEVCRIRMYFMQDDELGQAMLRGLYRQIIWTLISMPDGSVVRKAKGNPSGQPSTVDDNTIMVMLAVEYVFAYLGITQEEMDTIFKYYANGDDLIFAIHPDRESILNEFTHLFAHLGLNYIFEDRTRNRAELEYMSLTGIEREGFYIPKLSRERISSIVQWRRKGDTRAMFDALNAAILESWGYDDLTYWLRKYYEWLIINRYDIDLPEGEKLPYHTETAVETLYTCDDNTTVYDGRYDFEVPTDASGGVFIIDFQSSSGTDTPPVIPPATSEPALQPVLTRQTSRPPTPPNTILTGQQQQQLMPKSSQPYQLEPLLAPTGVQQPTFGTFGMPQAQQTTTEPVVAAARVRGKQKEGDTSLSQVRDHRRLSPERIVRHDDDLAPPNESTSGESSHYDELTLPDVPRDKRKGLGARLKGKPIITQTQIYNYRPAFGSIHNNKATDIELEAWKKQIADYFQVDDVSTLILGFMAYVIENGTSPEIFTNQKFVMATSSGEQREYPLAPFRSRSVELRKIMRRFSEEAIDYIQIQREHNPQYVPRQAVVRNVKRAIYFPYCFDFIDETILTPDALEIVHQMKAAALESASSKVLGLDGGSARAIDTERHTTEDATARTHNLRGAAMMA
|
Genome polyprotein [Cleaved into: P1 protease (EC 3.4.21.-) (Leader protease P1) (N-terminal protein) (P1 proteinase); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
|
Blackberry virus Y (isolate Blackberry plant/USA:Arkansas/C3ARK/2005) (BVY)
| 686,949 | 3,491 | 393,838 |
ATP-binding;Capsid protein;Covalent protein-RNA linkage;Dioxygenase;Helical capsid protein;Helicase;Host cytoplasmic vesicle;Host-virus interaction;Hydrolase;Inhibition of host innate immune response by virus;Iron;Metal-binding;Nucleotide-binding;Nucleotidyltransferase;Oxidoreductase;Phosphoprotein;Protease;Reference proteome;RNA-directed RNA polymerase;Serine protease;Suppressor of RNA silencing;Thiol protease;Transferase;Viral immunoevasion;Viral RNA replication;Virion
|
GO:0003723; GO:0003968; GO:0004197; GO:0004386; GO:0005198; GO:0005524; GO:0006351; GO:0006508; GO:0008236; GO:0016818; GO:0019029; GO:0039694; GO:0044161; GO:0046872; GO:0051213; GO:0052170
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate with host chloroplasts. {ECO:0000250|UniProtKB:P09814}.; SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
| null | null |
PF00270;PF00271;PF00863;PF00851;PF01577;PF00767;PF08440;PF13608;PF00680;
|
IPR037151;IPR011545;IPR043502;IPR001456;IPR031159;IPR042308;IPR014001;IPR001650;IPR005123;IPR027417;IPR002540;IPR009003;IPR043504;IPR001592;IPR001730;IPR039560;IPR013648;IPR043128;IPR001205;IPR007094;
| null |
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Pisuviricota (phylum), Stelpaviricetes (class), Patatavirales (order), Potyviridae (family), Brambyvirus (genus), Blackberry virus Y (species)
| null | false |
577 |
A0AV02
|
MTQMSQVQELFHEAAQQDALAQPQPWWKTQLFMWEPVLFGTWDGVFTSCMINIFGVVLFLRTGWLVGNTGVLLGMFLVSFVILVALVTVLSGIGVGERSSIGSGGVYSMISSVLGGQTGGTIGLLYVFGQCVAGAMYITGFAESISDLLGLGNIWAVRGISVAVLLALLGINLAGVKWIIRLQLLLLFLLAVSTLDFVVGSFTHLDPEHGFIGYSPELLQNNTLPDYSPGESFFTVFGVFFPAATGVMAGFNMGGDLREPAASIPLGSLAAVGISWFLYIIFVFLLGAICTREALRYDFLIAEKVSLMGFLFLLGLYISSLASCMGGLYGAPRILQCIAQEKVIPALACLGQGKGPNKTPVAAICLTSLVTMAFVFVGQVNVLAPIVTINFMLTYVAVDYSYFSLSMCSCSLTPVPEPVLREGAEGLHCSEHLLLEKAPSYGSEGPAQRVLEGTLLEFTKDMDQLLQLTRKLESSQPRQGEGNRTPESQKRKSKKATKQTLQDSFLLDLKSPPSFPVEISDRLPAASWEGQESCWNKQTSKSEGTQPEGTYGEQLVPELCNQSESSGEDFFLKSRLQEQDVWRRSTSFYTHMCNPWVSLLGAVGSLLIMFVIQWVYTLVNMGVAAIVYFYIGRASPGLHLGSASNFSFFRWMRSLLLPSCRSLRSPQEQIILAPSLAKVDMEMTQLTQENADFATRDRYHHSSLVNREQLMPHY
|
Solute carrier family 12 member 8 (Cation-chloride cotransporter 9)
|
Homo sapiens (Human)
| 9,606 | 714 | 78,239 |
Alternative splicing;Chloride;Glycoprotein;Ion transport;Membrane;Potassium;Potassium transport;Proteomics identification;Reference proteome;Symport;Transmembrane;Transmembrane helix;Transport
|
GO:0006884; GO:0015379; GO:0016020; GO:0055064; GO:0055075; GO:1902476; GO:1990573
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null |
TRANSMEM 37..60; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 72..93; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 99..116; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 123..142; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 154..173; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 185..205; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 233..254; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 266..289; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 309..331; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 360..377; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 383..403; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 593..616; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 622..643; /note="Helical"; /evidence="ECO:0000255"
|
PF00324;
|
IPR004841;IPR004842;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Homo (genus)
|
SLC12A8 CCC9
| false |
578 |
A0AV96
|
MTAEDSTAAMSSDSAAGSSAKVPEGVAGAPNEAALLALMERTGYSMVQENGQRKYGGPPPGWEGPHPQRGCEVFVGKIPRDVYEDELVPVFEAVGRIYELRLMMDFDGKNRGYAFVMYCHKHEAKRAVRELNNYEIRPGRLLGVCCSVDNCRLFIGGIPKMKKREEILEEIAKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETTEDTIKKSFGQFNPGCVERVKKIRDYAFVHFTSREDAVHAMNNLNGTELEGSCLEVTLAKPVDKEQYSRYQKAARGGGAAEAAQQPSYVYSCDPYTLAYYGYPYNALIGPNRDYFVKAGSIRGRGRGAAGNRAPGPRGSYLGGYSAGRGIYSRYHEGKGKQQEKGYELVPNLEIPTVNPVAIKPGTVAIPAIGAQYSMFPAAPAPKMIEDGKIHTVEHMISPIAVQPDPASAAAAAAAAAAAAAAVIPTVSTPPPFQGRPITPVYTVAPNVQRIPTAGIYGASYVPFAAPATATIATLQKNAAAAAAMYGGYAGYIPQAFPAAAIQVPIPDVYQTY
|
RNA-binding protein 47 (RNA-binding motif protein 47)
|
Homo sapiens (Human)
| 9,606 | 593 | 64,099 |
3D-structure;Alternative splicing;Cytoplasm;Methylation;mRNA processing;mRNA splicing;Nucleus;Proteomics identification;Reference proteome;Repeat;RNA-binding
|
GO:0000381; GO:0002244; GO:0003723; GO:0003729; GO:0003730; GO:0005634; GO:0005737; GO:0006397; GO:0008380; GO:0016554; GO:0019899; GO:0030895; GO:0032733; GO:0060340; GO:0070935; GO:0140767
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24038582, ECO:0000269|PubMed:24916387}. Cytoplasm {ECO:0000269|PubMed:24916387}.
| null | null |
PF00076;
|
IPR006535;IPR012677;IPR035979;IPR047044;IPR034440;IPR034445;IPR000504;
|
2DIS;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Homo (genus)
|
RBM47
| false |
579 |
A0AVF1
|
MMLSRAKPAVGRGVQHTDKRKKKGRKIPKLEELLSKRDFTGAITLLEFKRHVGEEEEDTNLWIGYCAFHLGDYKRALEEYENATKEENCNSEVWVNLACTYFFLGMYKQAEAAGFKASKSRLQNRLLFHLAHKFNDEKKLMSFHQNLQDVTEDQLSLASIHYMRSHYQEAIDIYKRILLDNREYLALNVYVALCYYKLDYYDVSQEVLAVYLQQIPDSTIALNLKACNHFRLYNGRAAEAELKSLMDNASSSFEFAKELIRHNLVVFRGGEGALQVLPPLVDVIPEARLNLVIYYLRQDDVQEAYNLIKDLEPTTPQEYILKGVVNAALGQEMGSRDHMKIAQQFFQLVGGSASECDTIPGRQCMASCFFLLKQFDDVLIYLNSFKSYFYNDDIFNFNYAQAKAATGNTSEGEEAFLLIQSEKMKNDYIYLSWLARCYIMNKKPRLAWELYLKMETSGESFSLLQLIANDCYKMGQFYYSAKAFDVLERLDPNPEYWEGKRGACVGIFQMIIAGREPKETLREVLHLLRSTGNTQVEYMIRIMKKWAKENRVSI
|
Intraflagellar transport protein 56 (Tetratricopeptide repeat protein 26) (TPR repeat protein 26)
|
Homo sapiens (Human)
| 9,606 | 554 | 64,178 |
Alternative splicing;Cell projection;Ciliopathy;Cilium;Disease variant;Protein transport;Proteomics identification;Reference proteome;Repeat;TPR repeat;Transport
|
GO:0005813; GO:0005929; GO:0007224; GO:0015031; GO:0030992; GO:0035082; GO:0035720; GO:0035735; GO:0036064; GO:0042073; GO:0043005; GO:0060271; GO:0061512; GO:0097542; GO:0097546; GO:0120170; GO:1905198
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q8BS45}. Note=Localizes at the base to the ciliary transition zone. {ECO:0000250|UniProtKB:Q8BS45}.
| null | null |
PF12895;
|
IPR011990;IPR019734;IPR030511;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Homo (genus)
|
IFT56 TTC26
| false |
580 |
A0AVI4
|
MDSPEVTFTLAYLVFAVCFVFTPNEFHAAGLTVQNLLSGWLGSEDAAFVPFHLRRTAATLLCHSLLPLGYYVGMCLAASEKRLHALSQAPEAWRLFLLLAVTLPSIACILIYYWSRDRWACHPLARTLALYALPQSGWQAVASSVNTEFRRIDKFATGAPGARVIVTDTWVMKVTTYRVHVAQQQDVHLTVTESRQHELSPDSNLPVQLLTIRVASTNPAVQAFDIWLNSTEYGELCEKLRAPIRRAAHVVIHQSLGDLFLETFASLVEVNPAYSVPSSQELEACIGCMQTRASVKLVKTCQEAATGECQQCYCRPMWCLTCMGKWFASRQDPLRPDTWLASRVPCPTCRARFCILDVCTVR
|
E3 ubiquitin-protein ligase TM129 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TM129)
|
Homo sapiens (Human)
| 9,606 | 362 | 40,464 |
Alternative splicing;Endoplasmic reticulum;Membrane;Metal-binding;Proteomics identification;Reference proteome;Transferase;Transmembrane;Transmembrane helix;Ubl conjugation pathway;Unfolded protein response;Zinc;Zinc-finger
|
GO:0000209; GO:0005783; GO:0005789; GO:0006511; GO:0006986; GO:0008270; GO:0016567; GO:0030970; GO:0036503; GO:0061630
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24807418}; Multi-pass membrane protein {ECO:0000269|PubMed:24807418}.
| null |
TRANSMEM 7..27; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 57..77; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 95..115; /note="Helical"; /evidence="ECO:0000255"
|
PF10272;
|
IPR018801;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Homo (genus)
|
TMEM129
| false |
581 |
A0AVK6
|
MENEKENLFCEPHKRGLMKTPLKESTTANIVLAEIQPDFGPLTTPTKPKEGSQGEPWTPTANLKMLISAVSPEIRNRDQKRGLFDNRSGLPEAKDCIHEHLSGDEFEKSQPSRKEKSLGLLCHKFLARYPNYPNPAVNNDICLDEVAEELNVERRRIYDIVNVLESLHMVSRLAKNRYTWHGRHNLNKTLGTLKSIGEENKYAEQIMMIKKKEYEQEFDFIKSYSIEDHIIKSNTGPNGHPDMCFVELPGVEFRAASVNSRKDKSLRVMSQKFVMLFLVSTPQIVSLEVAAKILIGEDHVEDLDKSKFKTKIRRLYDIANVLSSLDLIKKVHVTEERGRKPAFKWTGPEISPNTSGSSPVIHFTPSDLEVRRSSKENCAKNLFSTRGKPNFTRHPSLIKLVKSIESDRRKINSAPSSPIKTNKAESSQNSAPFPSKMAQLAAICKMQLEEQSSESRQKVKVQLARSGPCKPVAPLDPPVNAEMELTAPSLIQPLGMVPLIPSPLSSAVPLILPQAPSGPSYAIYLQPTQAHQSVTPPQGLSPTVCTTHSSKATGSKDSTDATTEKAANDTSKASASTRPGSLLPAPERQGAKSRTREPAGERGSKRASMLEDSGSKKKFKEDLKGLENVSATLFPSGYLIPLTQCSSLGAESILSGKENSSALSPNHRIYSSPIAGVIPVTSSELTAVNFPSFHVTPLKLMVSPTSVAAVPVGNSPALASSHPVPIQNPSSAIVNFTLQHLGLISPNVQLSASPGSGIVPVSPRIESVNVAPENAGTQQGRATNYDSPVPGQSQPNGQSVAVTGAQQPVPVTPKGSQLVAESFFRTPGGPTKPTSSSCMDFEGANKTSLGTLFVPQRKLEVSTEDVH
|
Transcription factor E2F8 (E2F-8)
|
Homo sapiens (Human)
| 9,606 | 867 | 94,166 |
3D-structure;Activator;Cell cycle;DNA-binding;Nucleus;Phosphoprotein;Proteomics identification;Reference proteome;Repressor;Transcription;Transcription regulation
|
GO:0000122; GO:0000785; GO:0000978; GO:0000981; GO:0000987; GO:0001217; GO:0001227; GO:0001890; GO:0002040; GO:0003700; GO:0005654; GO:0005730; GO:0005829; GO:0006357; GO:0032466; GO:0032877; GO:0033301; GO:0042802; GO:0045944; GO:0048144; GO:0060707; GO:0060718; GO:0070365; GO:0090575; GO:1990837
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15897886}.
| null | null |
PF02319;
|
IPR015633;IPR003316;IPR036388;IPR036390;
|
4YO2;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Homo (genus)
|
E2F8
| false |
582 |
A0AVT1
|
MEGSEPVAAHQGEEASCSSWGTGSTNKNLPIMSTASVEIDDALYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVNKRNRAEAVLKHIAELNPYVHVTSSSVPFNETTDLSFLDKYQCVVLTEMKLPLQKKINDFCRSQCPPIKFISADVHGIWSRLFCDFGDEFEVLDTTGEEPKEIFISNITQANPGIVTCLENHPHKLETGQFLTFREINGMTGLNGSIQQITVISPFSFSIGDTTELEPYLHGGIAVQVKTPKTVFFESLERQLKHPKCLIVDFSNPEAPLEIHTAMLALDQFQEKYSRKPNVGCQQDSEELLKLATSISETLEEKPDVNADIVHWLSWTAQGFLSPLAAAVGGVASQEVLKAVTGKFSPLCQWLYLEAADIVESLGKPECEEFLPRGDRYDALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTSKEKGMITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKIDAHLNKVCPTTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPHLTESYNSHRDPPEEEIPFCTLKSFPAAIEHTIQWARDKFESSFSHKPSLFNKFWQTYSSAEEVLQKIQSGHSLEGCFQVIKLLSRRPRNWSQCVELARLKFEKYFNHKALQLLHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLHLSFLQNAAKLYATVYCIPFAEEDLSADALLNILSEVKIQEFKPSNKVVQTDETARKPDHVPISSEDERNAIFQLEKAILSNEATKSDLQMAVLSFEKDDDHNGHIDFITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTTATVSGLVALEMIKVTGGYPFEAYKNCFLNLAIPIVVFTETTEVRKTKIRNGISFTIWDRWTVHGKEDFTLLDFINAVKEKYGIEPTMVVQGVKMLYVPVMPGHAKRLKLTMHKLVKPTTEKKYVDLTVSFAPDIDGDEDLPGPPVRYYFSHDTD
|
Ubiquitin-like modifier-activating enzyme 6 (Ubiquitin-activating enzyme 6) (EC 6.2.1.45) (Monocyte protein 4) (MOP-4) (Ubiquitin-activating enzyme E1-like protein 2) (E1-L2)
|
Homo sapiens (Human)
| 9,606 | 1,052 | 117,970 |
3D-structure;Acetylation;Alternative splicing;ATP-binding;Ligase;Magnesium;Metal-binding;Nucleotide-binding;Phosphoprotein;Proteomics identification;Reference proteome;Ubl conjugation pathway
|
GO:0004839; GO:0005524; GO:0005634; GO:0005737; GO:0005829; GO:0006511; GO:0006974; GO:0016567; GO:0019780
|
Evidence at protein level
| 5 | null | null | null |
PF16191;PF16190;PF09358;PF00899;PF10585;
|
IPR032420;IPR032418;IPR042302;IPR045886;IPR000594;IPR018965;IPR042449;IPR038252;IPR019572;IPR042063;IPR035985;IPR018075;IPR000011;
|
7PVN;7PYV;7SOL;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Homo (genus)
|
UBA6 MOP4 UBE1L2
| false |
583 |
A0AVX7
|
MGSAQSVPPEMRALAERTGFTSEQIEQLHRRFKQLNHNRKTIRKEDFDTIPDLEFNPIRARIVHAFFDKRNLRKAPAGLAEEINFEDFLTIMSYFRPIEMDMDEERLESFRKEKLKFLFHMYDADYDGIITLQEYKNVLDELMSGNPHLEKESLRAIAEGAMLEAASACMARTGPDEVYEGITFEDFLKVWKGIDIETKMHVRFLTMEAIAHCY
|
Calcineurin B homologous protein 3 (Tescalcin) (TSC)
|
Gallus gallus (Chicken)
| 9,031 | 214 | 25,051 |
Calcium;Cell membrane;Cell projection;Cytoplasm;Differentiation;Lipoprotein;Membrane;Metal-binding;Myristate;Nucleus;Protein kinase inhibitor;Reference proteome
|
GO:0000287; GO:0001726; GO:0004860; GO:0005509; GO:0005634; GO:0005737; GO:0005886; GO:0019212; GO:0030027; GO:0030154; GO:0030854; GO:0032417; GO:0032587; GO:0033628; GO:0042803; GO:0050821; GO:0051604; GO:0071300; GO:0072659
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19345287}. Cytoplasm {ECO:0000269|PubMed:19345287}. Membrane {ECO:0000250|UniProtKB:Q96BS2}; Lipid-anchor {ECO:0000250|UniProtKB:Q96BS2}. Cell membrane {ECO:0000250|UniProtKB:Q96BS2}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q96BS2}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q9JKL5}. Note=Expressed in both the nucleus and cytoplasm of the embryonic testis. {ECO:0000269|PubMed:19345287}.
| null | null | null |
IPR052490;IPR011992;IPR002048;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Archelosauria (clade), Archosauria (clade), Dinosauria (clade), Saurischia (clade), Theropoda (clade), Coelurosauria (clade), Aves (class), Neognathae (infraclass), Galloanserae (superorder), Galliformes (order), Phasianidae (family), Phasianinae (subfamily), Gallus (genus)
|
TESC CHP3
| false |
584 |
A0FGR8
|
MTANRDAALSSHRHPGCAQRPRTPTFASSSQRRSAFGFDDGNFPGLGERSHAPGSRLGARRRAKTARGLRGHRQRGAGAGLSRPGSARAPSPPRPGGPENPGGVLSVELPGLLAQLARSFALLLPVYALGYLGLSFSWVLLALALLAWCRRSRGLKALRLCRALALLEDEERVVRLGVRACDLPAWVHFPDTERAEWLNKTVKHMWPFICQFIEKLFRETIEPAVRGANTHLSTFSFTKVDVGQQPLRINGVKVYTENVDKRQIILDLQISFVGNCEIDLEIKRYFCRAGVKSIQIHGTMRVILEPLIGDMPLVGALSIFFLRKPLLEINWTGLTNLLDVPGLNGLSDTIILDIISNYLVLPNRITVPLVSEVQIAQLRFPVPKGVLRIHFIEAQDLQGKDTYLKGLVKGKSDPYGIIRVGNQIFQSRVIKENLSPKWNEVYEALVYEHPGQELEIELFDEDPDKDDFLGSLMIDLIEVEKERLLDEWFTLDEVPKGKLHLRLEWLTLMPNASNLDKVLTDIKADKDQANDGLSSALLILYLDSARNLPSGKKISSNPNPVVQMSVGHKAQESKIRYKTNEPVWEENFTFFIHNPKRQDLEVEVRDEQHQCSLGNLKVPLSQLLTSEDMTVSQRFQLSNSGPNSTIKMKIALRVLHLEKRERPPDHQHSAQVKRPSVSKEGRKTSIKSHMSGSPGPGGSNTAPSTPVIGGSDKPGMEEKAQPPEAGPQGLHDLGRSSSSLLASPGHISVKEPTPSIASDISLPIATQELRQRLRQLENGTTLGQSPLGQIQLTIRHSSQRNKLIVVVHACRNLIAFSEDGSDPYVRMYLLPDKRRSGRRKTHVSKKTLNPVFDQSFDFSVSLPEVQRRTLDVAVKNSGGFLSKDKGLLGKVLVALASEELAKGWTQWYDLTEDGTRPQAMT
|
Extended synaptotagmin-2 (E-Syt2) (Chr2Syt)
|
Homo sapiens (Human)
| 9,606 | 921 | 102,357 |
3D-structure;Alternative splicing;Calcium;Cell membrane;Endocytosis;Endoplasmic reticulum;Lipid transport;Lipid-binding;Membrane;Metal-binding;Phosphoprotein;Proteomics identification;Reference proteome;Repeat;Transmembrane;Transmembrane helix;Transport
|
GO:0005509; GO:0005544; GO:0005789; GO:0005829; GO:0005886; GO:0006869; GO:0006897; GO:0008429; GO:0009898; GO:0016020; GO:0031210; GO:0035091; GO:0042802; GO:0044232; GO:0045296; GO:0061817; GO:0140268
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:20833364, ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:29469807}; Peripheral membrane protein {ECO:0000269|PubMed:17360437}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:29469807}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS) (PubMed:23791178, PubMed:27044890, PubMed:29469807, PubMed:30220461). Recruited to the cell membrane via the third C2 domain (PubMed:17360437). {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:29469807, ECO:0000269|PubMed:30220461}.
| null |
TRANSMEM 104..124; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 128..148; /note="Helical"; /evidence="ECO:0000255"
|
PF00168;PF17047;
|
IPR000008;IPR035892;IPR037752;IPR037733;IPR037749;IPR051634;IPR031468;IPR039010;
|
2DMG;4NPJ;4NPK;4P42;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Homo (genus)
|
ESYT2 FAM62B KIAA1228
| false |
585 |
A0FGR9
|
MRAEEPCAPGAPSALGAQRTPGPELRLSSQLLPELCTFVVRVLFYLGPVYLAGYLGLSITWLLLGALLWMWWRRNRRGKLGRLAAAFEFLDNEREFISRELRGQHLPAWIHFPDVERVEWANKIISQTWPYLSMIMESKFREKLEPKIREKSIHLRTFTFTKLYFGQKCPRVNGVKAHTNTCNRRRVTVDLQICYIGDCEISVELQKIQAGVNGIQLQGTLRVILEPLLVDKPFVGAVTVFFLQKPHLQINWTGLTNLLDAPGINDVSDSLLEDLIATHLVLPNRVTVPVKKGLDLTNLRFPLPCGVIRVHLLEAEQLAQKDNFLGLRGKSDPYAKVSIGLQHFRSRTIYRNLNPTWNEVFEFMVYEVPGQDLEVDLYDEDTDRDDFLGSLQICLGDVMTNRVVDEWFVLNDTTSGRLHLRLEWLSLLTDQEVLTEDHGGLSTAILVVFLESACNLPRNPFDYLNGEYRAKKLSRFARNKVSKDPSSYVKLSVGKKTHTSKTCPHNKDPVWSQVFSFFVHNVATERLHLKVLDDDQECALGMLEVPLCQILPYADLTLEQRFQLDHSGLDSLISMRLVLRFLQVEERELGSPYTGPEALKKGPLLIKKVATNQGPKAQPQEEGPTDLPCPPDPASDTKDVSRSTTTTTSATTVATEPTSQETGPEPKGKDSAKRFCEPIGEKKSPATIFLTVPGPHSPGPIKSPRPMKCPASPFAWPPKRLAPSMSSLNSLASSCFDLADISLNIEGGDLRRRQLGEIQLTVRYVCLRRCLSVLINGCRNLTPCTSSGADPYVRVYLLPERKWACRKKTSVKRKTLEPLFDETFEFFVPMEEVKKRSLDVAVKNSRPLGSHRRKELGKVLIDLSKEDLIKGFSQWYELTPNGQPRS
|
Extended synaptotagmin-3 (E-Syt3) (Chr3Syt)
|
Homo sapiens (Human)
| 9,606 | 886 | 100,035 |
Alternative splicing;Calcium;Cell membrane;Endoplasmic reticulum;Lipid transport;Lipid-binding;Membrane;Metal-binding;Proteomics identification;Reference proteome;Repeat;Transmembrane;Transmembrane helix;Transport
|
GO:0005509; GO:0005544; GO:0005789; GO:0005886; GO:0006869; GO:0008429; GO:0009898; GO:0031210; GO:0035091; GO:0044232; GO:0061817; GO:0140268
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:29469807}; Peripheral membrane protein {ECO:0000269|PubMed:17360437}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:29469807}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS) (PubMed:29469807, PubMed:30220461). Recruited to the cell membrane via the third C2 domain. {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:29469807, ECO:0000269|PubMed:30220461}.
| null |
TRANSMEM 30..50; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 51..71; /note="Helical"; /evidence="ECO:0000255"
|
PF00168;PF17047;
|
IPR000008;IPR035892;IPR037752;IPR037733;IPR037749;IPR051634;IPR031468;IPR039010;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Homo (genus)
|
ESYT3 FAM62C
| false |
586 |
A0FI79
|
MPSKAENLRPSEPAPQPPEGRTLQGQLPGAPLAQRAGSPPDVPGSESPALACSTPATPSGEDPPARAAPIAPRPPARPRLERALSLDDKGWRRRRFRGSQEDLEARNGTSPSRGSVQSEGPGAPAHSCSPPCLSTSLQEIPKSRGVLSSERGSPSSGGNPLSGVASSSPNLPHRDAAVAGSSPRLPSLLPPRPPPALSLDIASDSLRTANKVDSDLADYKLRAQPLLVRAHSSLGPGRPRSPLACDDCSLRSAKSSFSLLAPIRSKDVRSRSYLEGSLLASGALLGADELARYFPDRNVALFVATWNMQGQKELPPSLDEFLLPAEADYAQDLYVIGVQEGCSDRREWETRLQETLGPHYVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTSGDGKVAERLLDYTRTVQALALPRNVPDTNPYRSSAADVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRVKVRPGRDNIPLAAGKFDRELYLLGIKRRISKEIQRQQALQSQNSSTICSVS
|
Phosphatidylinositol polyphosphate 5-phosphatase type IV (72 kDa inositol polyphosphate 5-phosphatase) (Inositol polyphosphate-5-phosphatase E) (Phosphatidylinositol 4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase) (EC 3.1.3.86)
|
Pan troglodytes (Chimpanzee)
| 9,598 | 644 | 70,221 |
Cell membrane;Cell projection;Cilium;Cytoplasm;Cytoskeleton;Golgi apparatus;Hydrolase;Lipid metabolism;Lipoprotein;Membrane;Methylation;Nucleus;Phosphoprotein;Prenylation;Reference proteome;Repeat
|
GO:0001726; GO:0004439; GO:0004445; GO:0005634; GO:0005794; GO:0005886; GO:0005930; GO:0032580; GO:0034485; GO:0043813; GO:0046856
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9JII1}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9JII1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JII1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9JII1}. Cell membrane {ECO:0000250|UniProtKB:Q9WVR1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9WVR1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9WVR1}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9WVR1}. Cytoplasm {ECO:0000250|UniProtKB:Q9WVR1}. Nucleus {ECO:0000250|UniProtKB:Q9JII1}. Note=Peripheral membrane protein associated with Golgi stacks. {ECO:0000250|UniProtKB:Q9JII1}.
| null | null |
PF22669;
|
IPR036691;IPR042478;IPR000300;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Pan (genus)
|
INPP5E
| false |
587 |
A0FIN4
|
MPITRMRMRPWLEMQINSNQIPGLIWINKEEMIFQIPWKHAAKHGWDINKDACLFRSWAIHTGRYKAGEKEPDPKTWKANFRCAMNSLPDIEEVKDQSRNKGSSAVRVYRMLPPLTKNQRKERKSKSSRDAKCKAKKKSCGESSPDTFSDGLSSSTLPDDHSSYTAQGYIGQDLDIEQALTPALSPCAISSTLPEWRIPVEIVPDSTSDLYNFQVSPMPSTSEAATDEDEEGKLTEDIMKLLEQSGWQQTNVDGKGYLLNEPGAQPTAVYGDFSCKEEPEVESPGGYTGLISSDLKNVDTSWLDNLLTPVRLPSIQAIPCAP
|
Interferon regulatory factor 1 (IRF-1)
|
Sus scrofa (Pig)
| 9,823 | 322 | 35,999 |
Acetylation;Activator;Antiviral defense;Cytoplasm;DNA-binding;Immunity;Innate immunity;Isopeptide bond;Nucleus;Phosphoprotein;Reference proteome;Repressor;Transcription;Transcription regulation;Tumor suppressor;Ubl conjugation
|
GO:0000785; GO:0000976; GO:0000978; GO:0000981; GO:0001228; GO:0005634; GO:0005737; GO:0006366; GO:0006915; GO:0032481; GO:0032728; GO:0032735; GO:0034124; GO:0035458; GO:0043374; GO:0045590; GO:0045892; GO:0045893; GO:0045944; GO:0051607; GO:0051726; GO:0060333; GO:0071260; GO:2000564
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15314}. Cytoplasm {ECO:0000250|UniProtKB:P15314}. Note=MYD88-associated IRF1 migrates into the nucleus more efficiently than non-MYD88-associated IRF1. {ECO:0000250|UniProtKB:P15314}.
| null | null |
PF00605;
|
IPR019817;IPR001346;IPR017431;IPR036388;IPR036390;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Suina (suborder), Suidae (family), Sus (genus)
|
IRF1
| false |
588 |
A0FKN5
|
MEDAQESGECLVQNQKYCVERPIYNQEILQGQLHKRERTPQSLRQKIEHSCRCSSKKAKSHLYSFLPILKWLPRYPVKEYLLGDIISGISTGVMQLPQGLAYALLAAVPPVFGLYSSFYPVFLYTFFGTSKHISIGTFAVISMMVGGVAVRQVPDEVISVGYNSTNATDASDYYSLRDDKRVQVAVTLAFLSGIIQLCLGFLRFGFVAIYLTEPLVRGFTTAAAVHVFTSQLKYLLGVKTSRYSGPLSVVYSLVAVFSKITTTNIAALIVGLTCIALLLIGKEINLRFKKKLPVPIPMEIIVVIIGTGVSAGMNLTESYGVDVVGKIPQGLSAPAVPEIQLIPAIFIDAVAIAIVGFSMAVSMAKIFALKHGYTIDGNQELIALGICNSVGSFFQSFPITCSMSRSLVQESTGGKTQIAGALSSIMVLLVIVAIGYLFEPLPQTVLAAIVMVNLKGMFKQFADVAHFWRTSKIELAIWVVAFVASLFLGLDYGLLTAVAFAMITVIYRTQRPQYRILGQIPDTDIYCDVEEYEEVKEYPGIKIFQANTSLYFANSESYTSALKKKTGVDPCAILAARRKAQKKHAREIKKANKVKKKAVLKLVNSSTNDVEASVKHEIANDGLPANGKFAFVDAGVQDGSPDELEHFVEPKTNVHSLILDFAPVNFVDSVGAKTLKSVIKEYNEVGVCVCIASCSGPVMNELTRLNFFDNTVTRELLFHSIHDAVLACQGKDRSASQTALDH
|
Prestin (Solute carrier family 26 member 5)
|
Gallus gallus (Chicken)
| 9,031 | 742 | 81,113 |
3D-structure;Cell membrane;Glycoprotein;Membrane;Metal-binding;Reference proteome;Transmembrane;Transmembrane helix;Zinc
|
GO:0005886; GO:0046872; GO:0160044; GO:0160046
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17442754}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 77..106; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 110..127; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 139..152; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 169..202; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 213..236; /note="Helical; Name=5a"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 265..288; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 298..313; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 339..373; /note="Helical; Name=8"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 377..394; /note="Helical; Name=9"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 403..412; /note="Helical; Name=10"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 417..438; /note="Helical; Name=11"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 443..470; /note="Helical; Name=12"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 472..487; /note="Helical; Name=13"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 490..510; /note="Helical; Name=14"; /evidence="ECO:0000250|UniProtKB:P58743"
|
PF01740;PF00916;
|
IPR018045;IPR011547;IPR001902;IPR002645;IPR036513;
|
5EZB;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Archelosauria (clade), Archosauria (clade), Dinosauria (clade), Saurischia (clade), Theropoda (clade), Coelurosauria (clade), Aves (class), Neognathae (infraclass), Galloanserae (superorder), Galliformes (order), Phasianidae (family), Phasianinae (subfamily), Gallus (genus)
|
SLC26A5
| false |
589 |
A0JLT2
|
MENFTALFGAQADPPPPPTALGFGPGKPPPPPPPPAGGGPGTAPPPTAATAPPGADKSGAGCGPFYLMRELPGSTELTGSTNLITHYNLEQAYNKFCGKKVKEKLSNFLPDLPGMIDLPGSHDNSSLRSLIEKPPILSSSFNPITGTMLAGFRLHTGPLPEQCRLMHIQPPKKKNKHKHKQSRTQDPVPPETPSDSDHKKKKKKKEEDPDRKRKKKEKKKKKNRHSPDHPGMGSSQASSSSSLR
|
Mediator of RNA polymerase II transcription subunit 19 (Lung cancer metastasis-related protein 1) (Mediator complex subunit 19)
|
Homo sapiens (Human)
| 9,606 | 244 | 26,273 |
3D-structure;Activator;Alternative splicing;Nucleus;Phosphoprotein;Proteomics identification;Reference proteome;Transcription;Transcription regulation
|
GO:0003712; GO:0005634; GO:0005654; GO:0016592; GO:0032968; GO:0045944; GO:0051123; GO:0060261; GO:0070847
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null |
PF10278;
|
IPR019403;
|
7EMF;7ENA;7ENC;7ENJ;7LBM;7NVR;8GXQ;8GXS;8TQW;8TRH;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Catarrhini (parvorder), Hominoidea (superfamily), Hominidae (family), Homininae (subfamily), Homo (genus)
|
MED19 LCMR1
| false |
590 |
A0JMD4
|
MEEEPLLAGSINQGSGDYGAHSESCLHYPDEHTPRSRRLSYSVTDDSCNVEEDADADLYVQQAVVFIEDAIKYRSINHRVDSGSLRLYRWYYSNLCQWGLGLTIAVVLALAFIERPSSLTYTSDIRVKPKPWEPPCGMTEGIEIVCLCIFILDVTAKGYLIGWEEFRMNKWLLAYLIVITASVIDWMLSISMLCDENLRVRRLIRPFFLLQNSSLMKKTLKCIKRTLPEIASVILLLALHICLFTMIGMLIFAKSDDPKQNGEWQTYFRNLPKALSSLLVLLTTANNPDVMIPAYSLNRGYSIFFILFSVFGTYLLMNLMTAIIYNQFRGYLLMSVQTSIIRRRLGIRAAFEVLCCPGRGHTSTQAEGHVERVAVSMFLKVMERVHMKSYCRQAIVKAARRFPDGFISGEDFQRLFNELDKDFVKEHPPKPEYSSSGLQHIQYVYSHYYISVLGNAVALANVICICTVLVLNAEKSASEKNYFYMEIINCIFILYYLIEMLLKIVAFGWKGYLSYRNNIFDGFLTVLLLAIQIVIFITFKIPYVDVDPVPRHVMALWEMIRLVNMLIVFRFLRIIPEIKLMAVVASTIVDLVKNLRAFAGILLVVYYMFAVLGIWLFQGAISPPSNMSLVSNSSLENITGPYSMECGTFEQLEYWPNNFDDFASSLILLYNIMVVNNWHVFTDAYARYTTDWSLVYFVVWWLTSSVMWVNLFVALILENFTYKWDRSNGLSVEDVERIAYQSTVQLMFKEHVKEPTEEELLAQLHQHPHLHLSW
|
Two pore channel protein 2 (Two pore calcium channel protein 2) (Voltage-dependent calcium channel protein TPC2)
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 774 | 89,184 |
Calcium;Calcium channel;Calcium transport;Endosome;Glycoprotein;Ion channel;Ion transport;Lysosome;Membrane;Reference proteome;Repeat;Transmembrane;Transmembrane helix;Transport;Voltage-gated channel
|
GO:0005245; GO:0005764; GO:0005765; GO:0006939; GO:0014866; GO:0015280; GO:0019722; GO:0031902; GO:0034702; GO:0035725; GO:0042802; GO:0072345; GO:0075509; GO:0080025; GO:0097682; GO:2000290
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q8NHX9}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8NHX9}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 93..113; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 141..161; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 171..191; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 198..218; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 233..253; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 303..323; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 453..475; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 487..507; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 519..539; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 565..585; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 597..617; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 697..717; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000255"
|
PF00520;
|
IPR005821;IPR028798;IPR027359;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
tpcn2 tpc2 zgc:152898
| false |
591 |
A0JMQ9
|
MTDLGLKWSCEYCTYENWPSAIKCTMCRAQRHNAPIITEEPFKSSSSLDPSLCTTQGGSTLLICPDSSARPRVRIADELPETSSKWSCHMCTYLNWPRAIRCTQCLSQRQQGSQQHSPLSPSETPQTSGSRPSPVTSDPCEEYNDRNRLNMHAQRWPCSACTYENWPKSLRCVVCDHPKPSGSPETPQQDSEAESATSPSIVNEQERENVRTAGGGGGGSRGRLRKLSPPMCKGQAEVKIELASGAVGSDNEQEADFKKLKQIRNRMRRSDWLFLNACAGVVEGDLAAVEAYKSSGGDIARQLTADEVRILNRPSAFDAGFTLVHLAIRFQRQDMLAVLLTEVSQQTAKCIPALVCPELTEQIRREVAAALHRRKGEFPCYFFTDLVTFTLPADIEDLPPNVQEKLFDEVLDRDVQKELEEESPIINWSLELGTRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKSLNDSLHDCSHWFYTRWKEWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHVFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYDNRGAGANLNTDDDVTVTFLPLVDSERKLLHIHFLSAQEMGTEEQQERMLRQWMDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDGYRQLAACPTLSDGEEEEEDEDE
|
Ubiquitin thioesterase zranb1-B (EC 3.4.19.12) (Zinc finger Ran-binding domain-containing protein 1-B)
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 716 | 81,193 |
ANK repeat;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Protease;Reference proteome;Repeat;Thiol protease;Ubl conjugation pathway;Wnt signaling pathway;Zinc;Zinc-finger
|
GO:0004843; GO:0005634; GO:0005737; GO:0007010; GO:0007420; GO:0008270; GO:0016055; GO:0016477; GO:0021551; GO:0022604; GO:0030177; GO:0035523; GO:0070530; GO:0070536; GO:0071947; GO:1990168
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UGI0}. Nucleus {ECO:0000250|UniProtKB:Q9UGI0}. Note=Enriched in punctate localization in the cytoplasm. {ECO:0000250|UniProtKB:Q9UGI0}.
| null | null |
PF18418;PF02338;PF00641;
|
IPR041294;IPR051346;IPR003323;IPR001876;IPR036443;IPR049768;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
zranb1b zranb1 zgc:154177
| false |
592 |
A0JMZ4
|
MGSNRLTARELCENDDLATSLVLDPYLGFRTHKMNVSAMPTIRRQHHLREALQTFCKKKDLEAAYQSLTAGGWARHYFHSRTRQQESLLKTHIFRYLRMFLPESGFMILSCSRYSLEMNGAKVVSTKSWSKNEKIELLVGCIAELSKADETLLRFGDNDFSVMYSTRKKCAQLWLGPAAFINHDCRPNCKFVPTEGNTACVKVLREIKTGEEITCFYGDSFFGEKNEMCECCTCERKGDGAFKQQNTEQTVSTSLEKYQLRETDGRLKRLSESACKPSPQVTTKKKGSKLRLSLRLKRIPASRRKGAFYRRVKTFASSRYFYKSHLMKHIPLKPVKIALPRGTVLRDVRIILHNCKKCNQASRPKSQHERQCCKLGKEPLVSLRREDLSPERLKFRLSCPGGSCPPIIQTANVGCNAKDCSQTEAGKSNLEQITTAELCEHLSFSPVPSHNEDDNSFYEPEIPGSLLGPESPSSEPLSNNLNLECNSPEPIVINTVYPHYNGGVTSDSHPHALKQFGITHYIQVDLRKDVTLEPGRSQPDKSSLEAEKKQIPNNKHSQHPVISDDHLVANLNAETQSNAVSPPTNTPICEALNGSLEHKVFSLRSRPVSFRPRKTSDNKITLFKRRRSSVKQGVRCVKLNGHVKLTGQLVPSKLHPPPGAGANHLTDAMHSDPKLLLKPYVELGLNNNLKRQSLTGLPPSTVLTGDAFNILHSPPASKQSTEGATKNVAFNPFTPSKRLRLVVSHGSIALDMASTSSEETS
|
Histone-lysine N-methyltransferase KMT5C (Lysine-specific methyltransferase 5C) (Suppressor of variegation 4-20 homolog 2) (Su(var)4-20 homolog 2) (Suv4-20h2) ([histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B) (EC 2.1.1.362) ([histone H4]-lysine20 N-methyltransferase KMT5B) (EC 2.1.1.361)
|
Xenopus laevis (African clawed frog)
| 8,355 | 761 | 85,058 |
Chromatin regulator;Chromosome;Metal-binding;Methyltransferase;Nucleus;Reference proteome;Repressor;S-adenosyl-L-methionine;Transcription;Transcription regulation;Transferase;Zinc
|
GO:0003682; GO:0005634; GO:0005694; GO:0006281; GO:0032259; GO:0042799; GO:0045830; GO:0046872; GO:0140941; GO:0140944; GO:1904047; GO:2001034
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}. Note=Associated with pericentric heterochromatin. {ECO:0000250}.
| null | null |
PF00856;
|
IPR041938;IPR001214;IPR046341;IPR039977;IPR025790;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Pipoidea (superfamily), Pipidae (family), Xenopodinae (subfamily), Xenopus (genus), Xenopus (subgenus)
|
kmt5c suv420h2
| false |
593 |
A0JN54
|
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAEYLQGDAIGYEGFQQFLKIYLEVDNVPDHLSQALFQSFQTGYYIEDTVREDVVCLSDVSCYFSLLEGGRPEDKLEFTFKLYDTDRNGILDSSEVDRIIIQMMRMAEYLDWDVSELRPILQEMMKEIDYDGSGSVSLAEWLRAGATTVPLLVLLGLEMTLKDNGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKYIVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLVGLHCVWCHLEIHDDCLPAMGHECDCGLLRDHILPPSSIYPSVLASGQERKTSKISQKTMDDLSLSTSEALRIDPVSNTHPLLVFVNPKSGGKQGERVLWKFQYLLNPRQVFNLLKDGPEPGLRFFRDVPDYRILVCGGDGTVGWILESIDKANLPFVPPVAVLPLGTGNDLARCLRWGGGYEGQNLGKILKDLETSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVLNIPSTHGGSNLWGDTKRPHGDIHGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLEGAIEIGQIYTKLKNAGHRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHRNQMPMLVGPPPRSSNFFGFLC
|
Diacylglycerol kinase alpha (DAG kinase alpha) (EC 2.7.1.107) (EC 2.7.1.93) (Diglyceride kinase alpha) (DGK-alpha)
|
Bos taurus (Bovine)
| 9,913 | 734 | 82,672 |
Acetylation;ATP-binding;Calcium;Cytoplasm;Kinase;Lipid metabolism;Metal-binding;Nucleotide-binding;Reference proteome;Repeat;Transferase;Zinc;Zinc-finger
|
GO:0004143; GO:0005509; GO:0005524; GO:0005829; GO:0005886; GO:0006654; GO:0007200; GO:0008270; GO:0035556; GO:0046339; GO:0046834; GO:0047649
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P23743}.
| null | null |
PF00130;PF14513;PF00609;PF00781;PF13499;
|
IPR017438;IPR046349;IPR047469;IPR029477;IPR037607;IPR038199;IPR000756;IPR001206;IPR011992;IPR018247;IPR002048;IPR016064;IPR002219;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Ruminantia (suborder), Pecora (infraorder), Bovidae (family), Bovinae (subfamily), Bos (genus)
|
DGKA
| false |
594 |
A0JN74
|
MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELFPQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCAAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPLQDAAEDLKSKLEKSLEHLRKQMEDALLFQAQAEETCSLWQKMVETQRQNVLTEFERLRRLLVEEEQLLLQRLEEEELEVLPPLRESAARLGQQSAQLAELITELEGRCQLPALGLLQDIRDTLRRVQDVKLQPPEVVPMEMRTVCRVPGLVEALRRFRGDMTLDPDTANPELVLSEDRRSVRRGDLRQALPDSPERFDPGPCVLGREPLTSGRHYWEVEVGERASWALGVCRENANRKEKGELFAGNGFWILVFLGSYYNSSERAFAPLRDPPRRVGIFLDYEAGHLSFYSANDGSLLYTFPETPFSGTLRALFSPLSSSPTPMTICRLKGGPGDGLAPQ
|
E3 ubiquitin-protein ligase TRIM11 (EC 2.3.2.27) (Tripartite motif-containing protein 11)
|
Bos taurus (Bovine)
| 9,913 | 468 | 52,947 |
Antiviral defense;Coiled coil;Cytoplasm;Isopeptide bond;Metal-binding;Nucleus;Phosphoprotein;Reference proteome;Transferase;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger
|
GO:0004842; GO:0005634; GO:0005737; GO:0005829; GO:0008270; GO:0010468; GO:0016567; GO:0030674; GO:0032897; GO:0044790; GO:0045087; GO:0046597; GO:0061630; GO:0140972
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96F44}. Nucleus {ECO:0000250|UniProtKB:Q96F44}.
| null | null |
PF13765;PF00622;PF00643;PF15227;
|
IPR001870;IPR043136;IPR003879;IPR013320;IPR006574;IPR003877;IPR050143;IPR000315;IPR001841;IPR013083;IPR017907;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Ruminantia (suborder), Pecora (infraorder), Bovidae (family), Bovinae (subfamily), Bos (genus)
|
TRIM11
| false |
595 |
A0JNB0
|
MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHGAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGENL
|
Tyrosine-protein kinase Fyn (EC 2.7.10.2) (Proto-oncogene c-Fyn) (p59-Fyn)
|
Bos taurus (Bovine)
| 9,913 | 537 | 60,718 |
Adaptive immunity;ATP-binding;Cell membrane;Cytoplasm;Developmental protein;Immunity;Kinase;Lipoprotein;Manganese;Membrane;Metal-binding;Myristate;Nucleotide-binding;Nucleus;Palmitate;Phosphoprotein;Proto-oncogene;Reference proteome;SH2 domain;SH3 domain;Transferase;Tyrosine-protein kinase
|
GO:0001664; GO:0001764; GO:0002250; GO:0003015; GO:0004713; GO:0004715; GO:0005102; GO:0005524; GO:0005634; GO:0005768; GO:0005829; GO:0005884; GO:0005886; GO:0007169; GO:0007216; GO:0008360; GO:0010467; GO:0010629; GO:0010976; GO:0014069; GO:0016004; GO:0016525; GO:0016567; GO:0018108; GO:0030101; GO:0030154; GO:0030163; GO:0030425; GO:0030900; GO:0031397; GO:0035556; GO:0036120; GO:0038026; GO:0042177; GO:0042802; GO:0043014; GO:0043204; GO:0043274; GO:0044325; GO:0045121; GO:0045471; GO:0046872; GO:0046875; GO:0048156; GO:0048813; GO:0050798; GO:0050804; GO:0050852; GO:0050966; GO:0070851; GO:0071560; GO:0090314; GO:0097110; GO:0097386; GO:0097718; GO:0098685; GO:1900182; GO:1900449; GO:1902951; GO:1904646; GO:1905664
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06241}. Nucleus {ECO:0000250|UniProtKB:P06241}. Cell membrane {ECO:0000250|UniProtKB:P06241}. Perikaryon {ECO:0000250|UniProtKB:Q62844}. Note=Present and active in lipid rafts (By similarity). Palmitoylation is crucial for proper trafficking (By similarity). {ECO:0000250|UniProtKB:P06241}.
| null | null |
PF07714;PF00017;PF00018;
|
IPR047924;IPR035750;IPR011009;IPR050198;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR036028;IPR001452;IPR008266;IPR020635;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Ruminantia (suborder), Pecora (infraorder), Bovidae (family), Bovinae (subfamily), Bos (genus)
|
FYN
| false |
596 |
A0JNC1
|
MTELRQRVAREPEAPPEDKESESEAKADGETASDSESRVEAVTQPPSADDTPEVLNRALSNLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMMIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLTGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSGLFRLQEYNIPGVIQSIIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLVQQFLTLRPDQQLHIFNTLKSHLTDKGMLTAATEDK
|
Phosphatidate cytidylyltransferase 2 (EC 2.7.7.41) (CDP-DAG synthase 2) (CDP-DG synthase 2) (CDP-diacylglycerol synthase 2) (CDS 2) (CDP-diglyceride pyrophosphorylase 2) (CDP-diglyceride synthase 2) (CTP:phosphatidate cytidylyltransferase 2)
|
Bos taurus (Bovine)
| 9,913 | 445 | 51,357 |
Endoplasmic reticulum;Lipid biosynthesis;Lipid metabolism;Membrane;Nucleotidyltransferase;Phospholipid biosynthesis;Phospholipid metabolism;Phosphoprotein;Reference proteome;Transferase;Transmembrane;Transmembrane helix
|
GO:0004605; GO:0005783; GO:0005789; GO:0016020; GO:0016024; GO:0140042
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95674}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 79..99; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 132..152; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 166..186; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 213..233; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 262..282; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 340..360; /note="Helical"; /evidence="ECO:0000255"
|
PF01148;
|
IPR000374;IPR016720;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Ruminantia (suborder), Pecora (infraorder), Bovidae (family), Bovinae (subfamily), Bos (genus)
|
CDS2
| false |
597 |
A0JNC4
|
MAFSDLTSRTVRLYDNWIKDADPRVEDWLLMSSPLPQTIILGFYVYFVTSLGPKLMENRKPFELKKVMITYNFSIVLFSVYMFYEFIMSGWGTGYSFRCDIVDYSQSPTALRMVRTCWLYYFSKFIELLDTIFFILRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHAFLNTAVHVVMYSYYGLCALGPDYQKYLWWKKYLTSLQLIQFVLITIHISQFFFMEDCKYQFPVFQYIIMSYGCIFLLLFLHFWYRAYTKGQRLPKTVKHGICKNKDH
|
Very long chain fatty acid elongase 7 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL7) (ELOVL fatty acid elongase 7) (ELOVL FA elongase 7) (Elongation of very long chain fatty acids protein 7) (Very long chain 3-ketoacyl-CoA synthase 7) (Very long chain 3-oxoacyl-CoA synthase 7)
|
Bos taurus (Bovine)
| 9,913 | 281 | 33,639 |
Acetylation;Disulfide bond;Endoplasmic reticulum;Fatty acid biosynthesis;Fatty acid metabolism;Lipid biosynthesis;Lipid metabolism;Membrane;Reference proteome;Transferase;Transmembrane;Transmembrane helix
|
GO:0005783; GO:0005789; GO:0006636; GO:0009922; GO:0019367; GO:0030148; GO:0034625; GO:0034626; GO:0035338; GO:0042761
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03207}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03207}.
| null |
TRANSMEM 28..48; /note="Helical; Name=1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03207"; TRANSMEM 67..87; /note="Helical; Name=2"; /evidence="ECO:0000255|HAMAP-Rule:MF_03207"; TRANSMEM 116..136; /note="Helical; Name=3"; /evidence="ECO:0000255|HAMAP-Rule:MF_03207"; TRANSMEM 143..162; /note="Helical; Name=4"; /evidence="ECO:0000255|HAMAP-Rule:MF_03207"; TRANSMEM 172..194; /note="Helical; Name=5"; /evidence="ECO:0000255|HAMAP-Rule:MF_03207"; TRANSMEM 207..227; /note="Helical; Name=6"; /evidence="ECO:0000255|HAMAP-Rule:MF_03207"; TRANSMEM 237..257; /note="Helical; Name=7"; /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
|
PF01151;
|
IPR030457;IPR002076;IPR033670;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Ruminantia (suborder), Pecora (infraorder), Bovidae (family), Bovinae (subfamily), Bos (genus)
|
ELOVL7
| false |
598 |
A0JNH9
|
MSGGFELQPQDGGPRVALAPGETVIGRGPLLGLHRNPCYYQSSEKSQLLPLKTNIWCWLNPGDHFSLLVDKYIFCVLSTHSEMEMECTLRNSQMLDEDDILNEIPKSSSADLPDKTPSAPRRERSTETAKPQAAANNMSFIGESRDLSKQQPNPSERKRILPAWMLTENSSDQNLSVISGGNNVTWESEKERVCKDKTQVNITQPGKKRLISSGSSESTSAKQDTGKKCKNDDQEESIISSKEMPQSFSAAMLHNTEIDNTKTNPQRSKVPVEALGKVSEHKIITKGSSNEDSTARSCSESYSSTQSKSFCDKPQKSHPEPSSNPPSPECVQAKATDSVPNGSEENKVQRTSCMYGANCYRKNPVHFQHFSHPGDSDYGGVNITCQDEADDRPECPYGASCYRKNPQHKIEYRHSTFPVRSISDEDDNVGQPNEYNLNDSFIDDEEEEYEPTDEDSDWEPEKEDLEKEDMEGLLKEAKKFMKRKK
|
Aprataxin and PNK-like factor (EC 3.1.1.-) (Apurinic-apyrimidinic endonuclease APLF)
|
Bos taurus (Bovine)
| 9,913 | 485 | 54,326 |
ADP-ribosylation;Chromosome;Coiled coil;Cytoplasm;DNA damage;DNA repair;Hydrolase;Metal-binding;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Zinc;Zinc-finger
|
GO:0000012; GO:0000166; GO:0003906; GO:0004520; GO:0005634; GO:0005829; GO:0006302; GO:0006303; GO:0006974; GO:0007566; GO:0008270; GO:0008408; GO:0010717; GO:0035861; GO:0042393; GO:0072572; GO:0090734; GO:0140713; GO:0140861; GO:0160002
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9D842}. Chromosome {ECO:0000250|UniProtKB:Q8IW19}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9D842}. Note=Localizes to DNA damage sites. Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers. {ECO:0000250|UniProtKB:Q8IW19}.
| null | null |
PF10283;
|
IPR039253;IPR019406;IPR008984;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Ruminantia (suborder), Pecora (infraorder), Bovidae (family), Bovinae (subfamily), Bos (genus)
|
APLF
| false |
599 |
A0JNI4
|
MCDQYCISFADVEKAHINIRDFIHLTPVLTSSILNQITGRNLFFKCELFQKTGSFKIRGALNAIRGLISAHPEEKPRAVVAHSSGNHGQALSFAARLEGIPAYVIVPETAPNCKKLAIQAYGASIVYSEQSEESRENITKRIAEETEGIMVHPNQEPAVIAGQGTIAMEVLNQVPLVDALVVPVGGGGMLAGIAVTVKALRPSVKVYAAEPLNADDCYQSKLKGELTPNPYPPETIADGIKSSIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGVAVVLSQHFRTVPAEVKNICIVLSGGNVDLTSLTWVKKQDEKAAP
|
Serine racemase (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (EC 4.3.1.18) (L-serine ammonia-lyase) (L-serine dehydratase) (EC 4.3.1.17)
|
Bos taurus (Bovine)
| 9,913 | 334 | 36,181 |
Allosteric enzyme;ATP-binding;Calcium;Isomerase;Lyase;Magnesium;Manganese;Metal-binding;Nucleotide-binding;Pyridoxal phosphate;Reference proteome;S-nitrosylation
|
GO:0000287; GO:0003941; GO:0005524; GO:0005737; GO:0006563; GO:0008721; GO:0018114; GO:0030170; GO:0030378; GO:0070178; GO:0070179
|
Evidence at transcript level
| 5 | null | null | null |
PF00291;
|
IPR000634;IPR001926;IPR036052;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Ruminantia (suborder), Pecora (infraorder), Bovidae (family), Bovinae (subfamily), Bos (genus)
|
SRR
| false |
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