wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome P450 4F3 (CYPIVF3) (Leukotriene-B(4) omega-1/omega-2 hydroxylase) (Q99N16)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase involved in the metabolism of the pro-inflammatory lipid mediator leukotriene B4 (LTB4). Hydroxylates at the omega-1 and omega-2 positions LTB4. This oxidation step leads to LTB4 inactivation, which is postulated to be a crucial part of the resolution of inflammation. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:16380383}; Single-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305|PubMed:16380383}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome P450 2U1
- Cytochrome P450 2E1
- Leukotriene A-4 hydrolase
- Polyunsaturated fatty acid lipoxygenase ALOX12
- Polyunsaturated fatty acid 5-lipoxygenase
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Polyunsaturated fatty acid lipoxygenase ALOX8
- Polyunsaturated fatty acid
- Prostaglandin G/H synthase 2
- Prostaglandin G/H synthase 1
Sequence:
MSQLSMSWMGLGHTAASPWLLLLLAGASCLLAYILTPIYGVFENSLRLRCFPQPPKRNWILGHLGLIQSSEEGLLYIQSLVRTFRDACCWWVGPLHPVIRIFHPAFIKPVVLAPALVAPKDTVFYRFLKPWLGDGLLMSTGDKWSRHRRMLTPAFHFNILKPYVKVFNDSTNIMHAKWQRLASKGSAYLNMFEHISLMTLDSLQKCVFSFDSNCQEKPSEYITAILELSTLVARRHQRLLLHVDLFYYLTHDGMRFRKACRLVHDFTDAVIRERRRTLLDQGGVDVLKAKAKAKTLDFIDVLLLSKDEHGKALSDEDIRAEADTFMFGGHDTTASGLSWILYNLARHPEYQERCRQEVRELLRDREPEEIEWDDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLPDGRVIPKGVISRISIFGTHHNPAVWPDPEVYDPFRFDADNVKGRSPLAFIPFSAGPRNCIGQTFAMSEMKVALALTLLRFRVLPDDKEPRRKPELILRAEGGLWLKVEPLSAGAQ
Protein: Gamma-aminobutyric acid receptor subunit rho-1 (GABA(A) receptor subunit rho-1) (GABAAR subunit rho-1) (GABA(C) receptor) (P50572)
Organism: Rattus norvegicus (Rat)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-1 GABA receptor could play a role in retinal neurotransmission.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P56475}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P24046}. Cell membrane {ECO:0000250|UniProtKB:P24046}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P24046}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit rho-2
- Gamma-aminobutyric acid receptor subunit rho-3
- Gamma-aminobutyric acid receptor subunit alpha-4
- Gamma-aminobutyric acid receptor subunit alpha-6
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit gamma-3
- Gamma-aminobutyric acid receptor subunit alpha-5
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit gamma-1
- Gamma-aminobutyric acid receptor subunit alpha-3
Sequence:
MLAVRNMKFGIFLLWWGWVLAAESTVHWPGREVHEPSKKGSRPQRQRRGAHDDAHKQGSPILKRSSDITKSPLTKSEQLLRIDDHDFSMRPGFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSTNNLSMTFDGRLVKKIWVPDMFFVHSKRSFIHDTTTDNVMLRVQPDGKVLYSLRVTVTAMCNMDFSRFPLDTQTCSLEIESYAYTEDDLMLYWKKGNDSLKTDERISLSQFLIQEFHTTTKLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVPLGITTVLTMSTIITGVNASMPRVSYIKAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQERKERKLREKISCTCGLPQPRGVMLDSSYSDGEVNDLGGYMPENGEKPDRMMVQLTLASERGSPQRKSQRGSYVSMRINTHAIDKYSRIIFPAAYILFNLIYWSIFS
Protein: Probable WRKY transcription factor 45 (AT.I.24-4) (WRKY DNA-binding protein 45) (Q9S763)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9SI37}.
Interaction partners:
- DELLA protein RGL1
- Inorganic phosphate transporter 1-1
- Transcription factor MYB62
- Protein PHOSPHATE STARVATION RESPONSE 1
- Brassinosteroid-related acyltransferase 1
- Inorganic phosphate transporter 1-4
- Regulatory protein NPR1
- Zinc finger protein ZAT6
Sequence:
MEDRRCDVLFPCSSSVDPRLTEFHGVDNSAQPTTSSEEKPRSKKKKKEREARYAFQTRSQVDILDDGYRWRKYGQKAVKNNPFPRSYYKCTEEGCRVKKQVQRQWGDEGVVVTTYQGVHTHAVDKPSDNFHHILTQMHIFPPFCLKE
Protein: Outer kinetochore KNL1 complex subunit knl-1 (Kinetochore null protein 1) (P34278)
Organism: Caenorhabditis elegans
Function: Proposed to be part of the KMN network incorporating the MIS12 complex and NDC80 complex that is required for establishing the kinetochore-microtubule interface that aids in chromosome segregation during meiotic and mitotic cell division. Appears to function downstream of hcp-3 (CENP-A) and hcp-4 (CENP-C) in the kinetochore assembly hierarchy. Has a role in the correct localization of the spindly-like protein spdl-1 and the RZZ complex that is composed of rod-1, czw-1 and zwl-1 to kinetochores. Required for the recruitment of spindle-assembly checkpoint components bub-1 and mdf-1/2 to unattached kinetochores.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:20729837}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14522947, ECO:0000269|PubMed:15371340, ECO:0000269|PubMed:16273096, ECO:0000269|PubMed:17339379, ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:22331849, ECO:0000269|PubMed:24567362}. Note=Also found on the surface of chromosomes (PubMed:14522947). Subcellular localization dependent on expression of hcp-3, hcp-4, knl-3 and knl-2 (PubMed:14522947, PubMed:15371340, PubMed:16273096, PubMed:17339379). During anaphase of meiosis I, localized also to spindle-associated rod-shaped structures which depends on zwl-1 (PubMed:20729837). {ECO:0000269|PubMed:14522947, ECO:0000269|PubMed:15371340, ECO:0000269|PubMed:16273096, ECO:0000269|PubMed:17339379, ECO:0000269|PubMed:20729837}.
Interaction partners:
- Kinetochore NuLl
- KNL
- Mitotic checkpoint serine/threonine-protein kinase bub-1
- Kinetochore protein ndc-80
- Kinetochore null protein 2
- Kinetochore protein Nuf2 homolog
- KNL
- BUB1 N-terminal domain-containing protein
- Spindle and Kinetochore-Associated protein homolog
- Kinesin-like protein
Sequence:
MSMEPRKKRNSILKVRQAVETIEETVMNSGPSSTTTNRRVSFHNVKHVKQYDRDHGKILDATPVKEKITDTIGSDGILTPRGGNMDISESPACTSSFQVFGGGNLDKTMDMSLETTINENNETARLFETTRDPTLLYEKIVETTTKVTERIVSMPLDDTLAMFNTTNQEDKDMSVDRSVLFTIPKVPKHNATMNRTIPMDLDESKAAGGQCDETMNVFNFTNLEAAEMDTSKLDENNTMNAIRIPINSNVMPVDMDITEHHTLIEEKKNDTFGPSQLMDISAPQVQVNDTLAIFNSPRDICNKGLGVPQNLINIASNVVPVDMDITDQAVLNAEKKNDQFETSQLMDISIPKVLVNDTMAMFNSPKHVSKSSMDLEKTIEAADKSTKYPSIADEVEDLDMDMDITEQQPCEAGNQQNDGLQLQKEDLMDISVIRDSPAVNDTMAVFQSPARVKIGANNSIIDSQKSIVFGDEMSIDETQNDGTLTLPKSNVEVTTTNDVYTSLERQEENASENVSMINESSVHSEIDKKSFMLIEEERAFMHSSMIDVAQKLEDDGSSKTPVILASQSASLATKEPSALHNSSATLNNSMELDNNTLLKTMQITTCEDISMVHESIAVELNSNKEQEQFGDETLQKNDTSNTGANFTFQGHNETSQIMNNVDSEAVNTSKISTYSAFNLSINQSISKRRRSLLNSARESPRRVALENSIMSMNGQTMEALTEYRQNKTMQTSQDSMPSMSLNDSGRDILAMNTSVRSPHLNSSKTAAPGTPSLMSQNVQLPPPSPQFEMPDFDPAVVNVVYLTSEDPSTEQHPEALKFQRIVENEKMKVQHEIDSLNSTNQLSAEKIDMLKTKELLKFSHDEREAIMIARKDAEIKFLELRLKFALEKKIESDQEIAELEQGNSKMAEQLRGLDKMAVVQKELEKLRSLPPSREESGKIRKEWMEMKQWEFDQKMKALRNVRSNMIALRSEKNALEMKVAEEHEKFAQRNDLKKSRMLVFSKAVKKIVNF
Protein: Transcriptional regulator of yeast form adherence 4 (Q5ANC8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor required for yeast cell adherence to silicone substrate.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSLPMSPVSPINTTTSTSTTTTPLSPPSSIENSSHPLSTSISNNSITSDSSLDSNTSTSSTTTTNYGTKTPSGNARIFNCTLCQRAFTREEHLTRHTLSTHNKLKPFTCGICSRPFSRRDLLLRHAKNLHQGSEVAVSRIRKSYKHCNKDNDSKSGSDSNTNKTNKNGKKQEQEDDEEEGSRSDSSSGADDEDSNTSSGGSNYHAIGSGNKRFVNNSPQLKKILTNGSVPSTTTTSTTTVPTSTNNDTASITNSSTSHIHQRSLNVEDYDTPEKKRLKMSVNMLVS
Protein: 72 kDa type IV collagenase (EC 3.4.24.24) (72 kDa gelatinase) (Matrix metalloproteinase-2) (Q7SZM5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MLSVKFFRCRHIVLKVFLVQFLASLQTFAAPSPIIKFPGDDTAHTDKEVALHYLNKFYGCPKDRCNLMVLKDTLKKMQKFFALPETGEIDQKTVEIMKKPRCGVPDVANYNFFHRKPKWGQKNVTYRILGHTPDLDEDTIDDAFYRAFKVWSDVTPLKFTRIMDGEADIMINFGRNEHGDGYPFDGKDGLLAHAFAPGPGIGGDSHFDDDEQWTLGEGQVVKVKYGNAEGEFCKFPFLFMGKEYNSCTSQGRDDGFLWCSTTYNFDDDGKYGFCPHELLFTLGGNADGAPCKFPFTFQGDKYDSCTTSGRDDGYRWCATTEDYDKDKTYGFCPETAMSTSGGNSDGAPCVFPFKFLGDSYDSCTTSGRNDGKMWCAVTKSFDDDRKWGFCPDQGYSLFLVAAHEFGHALGLEHSDDPGALMAPIYTFTKTLRLSDDDVKGIQELYGEPTDKPLATHTPPVTPMDVCNENIIFDAVAQIRGEIFFFKDRFLFRTADVRKKPTGPMLVATFWSELPEKIDAAYENPLEERTVFFAGDEMWVYSASTLEREYPKKISSMGLPSDLHGIDAAYSFHKTKKTYIFAGNKFWRYNEAKKKMDPGFPKIIADSWTAVPDDLDGALSLNGDGHSYFFKDSHYLKMDDSTLKIIKVGEVKKDWLRC
Protein: 1-aminocyclopropane-1-carboxylate synthase 9 (ACC synthase 9) (EC 4.4.1.14) (Ethylene-overproduction protein 3) (S-adenosyl-L-methionine methylthioadenosine-lyase 9) (Q9M2Y8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene.
Interaction partners:
- 5'-methylthioadenosine nucleosidase
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
- 1-aminocyclopropane-1-carboxylate oxidase 4
- Ethylene-overproduction protein 1
- 1-aminocyclopropane-1-carboxylate oxidase
- S-adenosylmethionine synthase 1
- 1-aminocyclopropane-1-carboxylate oxidase 1
- 1-aminocyclopropane-1-carboxylate oxidase 5
- S-adenosylmethionine synthase 4
- 1-aminocyclopropane-1-carboxylate oxidase 2
Sequence:
MKQLSRKVTSNAHGQDSSYFLGWEEYEKNPYDEIKNPNGIIQMGLAENQLCFDLIETWLAKNPDAAGLKKDGQSIFKELALFQDYHGLPEFKKALAEFMEEIRGNRVTFDPSKIVLAAGSTSANETLMFCLAEPGDAFLLPTPYYPGFDRDLKWRTGAEIVPIHCSSSNGFQITESALQQAYQQAQKLDLKVKGVLVTNPSNPLGTMLTRRELNLLVDFITSKNIHLISDEIYSGTVFGFEQFVSVMDVLKDKNLENSEVSKRVHIVYSLSKDLGLPGFRVGAIYSNDEMVVSAATKMSSFGLVSSQTQYLLSALLSDKKFTSTYLDENQKRLKIRQKKLVSGLEAAGITCLKSNAGLFCWVDMRHLLDTNTFEAELELWKKIVYDVKLNISPGSSCHCTEPGWFRVCFANMSEDTLDLAMKRLKEYVESTDSRRVISKSSHDRIKSLRKRTVSNWVFRVSWTDRVPDER
Protein: Ubiquitin-conjugating enzyme E2 D3 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D3) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D3) (Ubiquitin carrier protein D3) (Ubiquitin-conjugating enzyme E2(17)KB 3) (Ubiquitin-conjugating enzyme E2-17 kDa 3) (Ubiquitin-protein ligase D3) (P61077)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction. Together with RNF135, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18508924}; Peripheral membrane protein {ECO:0000269|PubMed:18508924}. Endosome membrane {ECO:0000269|PubMed:18508924}; Peripheral membrane protein {ECO:0000269|PubMed:18508924}.
Interaction partners:
Sequence:
MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM
Protein: Sidestep II, isoform A (Sidestep II, isoform B) (Q59DZ1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Seminal fluid protein 36F
- Seminal fluid protein 51E
- Glial cell line-derived neurotrophic family receptor-like, isoform E
Sequence:
MVLLLAMALLMPVTLARLHSTSGVGMSGGGSSMGPGGGGSGSGGISSKDSHVKTKDIDAVEGKSVSLPCPITEPLDNVYMVLWFRDNAGIPLYSFDVRDKESREQPRHWSAPEVFGSRAKFHFDSQPATLEIKRHDQGIYRCRVDFRTSQTQSFRFNLSVIILPEQPIIMDRWGRQLNGTQLGPKQEGDDIVITCRVVGGRPQPQVRWLVNGLLVDNQNEHNSGDVIENRLLWPSVQRNDLNSVFTCQALNTQLDKPKEKSFILDMHLKPLVVKILEPPSSMIADRRYEVSCESSGSRPNAIITWYKGKRQLRRTKDDISKNSTRSELSFVPTTDDDGKSITCRAENPNVNGLYLETMWKLNVVYPPLVTLRLGSTLTPDDIKEGDDVYFECHVQSNPQWRKLLWLHNGIHLEHNTSARVIRSNQSLVLQKITKHYAGNYACSAINDEGETVSNQLPLRVKYTPMCKHADRVILIGASKDETVEVVCEIQADPPPRTFRWKFNNSGETLDVGSERFSVNGSRSILKYTPVTDQDYGTLSCWASNEVGTQQHPCLFQVVLAALPNAVSNCTVFNRTELSVDIQCIPGYDGGLPQIFVLEMFSTRTGITRFNLSNAEEALFSLENLDTLTSMMVQENNSLRLRIYSYNQKGRSAAYLLTDFIIGSTAYKTDDDVTLTLSPVIVGSVLTIIIIGVAIAIRIFVVTFVHNLRRNRHHGSKATAAGVTAQPSDVFKGGNLEKPRWQHTDIKTKSSEDLVEDERDPDVIPSQYVGGSSAGSSGSNASNVGSTTAGTATGSSTSTAVVANANAAASAMAGPGGATSSASATDGHQFASGTAAAGGGASKWSPNGNVTTTMLTGDAVNATVTYNQINAQRAQLLAAVAAVGGGCSSTVISPSSSILGGLGKPLGMGMGMGLGMGVGGTVIGSPTSLSSTATLAAHLQPAHSSGVGTLPPGLGSGGGYILNAYASGRLHHPPGGGVPGGATHTATLNRHHHQQQQLHHHPHHQQPHHSGSSLLMGSAGSVMGVVGSTTTATTSCNSSQDLDDNININAIKDCLMTQRVPESCV
Protein: Ras-like protein family member 11A (EC 3.6.5.2) (Q6T310)
Organism: Homo sapiens (Human)
Function: Regulator of rDNA transcription. Acts in cooperation UBF/UBTF and positively regulates RNA polymerase I transcription (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}. Note=Associates with rDNA transcription unit throughout the cell cycle. {ECO:0000250}.
Interaction partners:
- ADP-ribosylation factor-like protein 9
- ADP-ribosylation factor-like protein 10
Sequence:
MRPLSMSGHFLLAPIPESSSDYLLPKDIKLAVLGAGRVGKSAMIVRFLTKRFIGDYEPNTGKLYSRLVYVEGDQLSLQIQDTPGGVQIQDSLPQVVDSLSKCVQWAEGFLLVYSITDYDSYLSIRPLYQHIRKVHPDSKAPVIIVGNKGDLLHARQVQTQDGIQLANELGSLFLEISTSENYEDVCDVFQHLCKEVSKMHGLSGERRRASIIPRPRSPNMQDLKRRFKQALSPKVKAPSALG
Protein: Uncharacterized protein (Q384U6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDVVEKFLSLRREGRGEEAYKMLAPGAAMGCPWGGMHHGETVQELLRDETRFVKRGYLDHVPIEKIDENTFQRKFKWDRGMSEYGNSGFKGVGILPVWREIYFVDNGSIRLVTANKQLKNRSLWHVLGVS
Protein: Thiamine-repressible mitochondrial transport protein THI74 (Q04083)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in thiaminediphosphate transport across the mitochondrial membrane.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:16850348}; Multi-pass membrane protein {ECO:0000269|PubMed:16850348}.
Interaction partners:
- UDP-N-acetylglucosamine transporter YEA4
- UDP-galactose transporter homolog 1
- Putative nucleotide-sugar transporter YMD8
- Vitamin B6 transporter TPN1
Sequence:
MNRVGIDVDHMIGVLLLAVVVVFWVGASCLTNELLETNAYNKPFFLTYLNISSFALYLTPDLWRIIQSRRKSLQERTERTLPIHTQESFSEFLPLLSSTPSTSSNLSSIADTKVKDTMRLSLLFCVLWFVANLAANAALSYTTVASSTILSSTSSFFTLFLATSLGIETFSTKKLLGLFVSLFGIILIVMQSSKQQDSVSASSFLVGNTLALLGSLGYSVYTTLLKYEISSKGLRLDIQMFLGYVGIFTFLLFWPILIILDITHMETFELPSNFHISFLVMLNCIIIFVSDYFWCKALILTSPLVVTVALTFTIPLAMFADFVWREAFFTPWYIIGVIFIFVSFFLVNHRGESAVEKDCAAVEKGPILDA
Protein: E3 ubiquitin-protein ligase MARCHF8 (EC 2.3.2.27) (Cellular modulator of immune recognition) (c-MIR) (Membrane-associated RING finger protein 8) (Membrane-associated RING-CH protein VIII) (MARCH-VIII) (RING-type E3 ubiquitin transferase MARCHF8) (Q9DBD2)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination of CD86 and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. May also promote ubiquitination and endocytosis of TFRC and FAS (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5T0T0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5T0T0}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q5T0T0}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q5T0T0}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q5T0T0}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Bone marrow stromal antigen 2
Sequence:
MSMPLHQISAIPSQDAISARVYRSKTKDKEQNEKTLGHSMSHPSNISKAGSSPPSTTAPVSAFSRTSVTPSNQDICRICHCEGDDESPLITPCHCTGSLHFVHQACLQQWIKSSDTRCCELCKYEFIMETKLKPLRKWEKLQMTASERRKIMCSVTFHVIAITCVVWSLYVLIDRTAEEIKQGQVTGILEWPFWTKLVVVAIGFTGGLLFMYVQCKVYLQLWKRLKAYNRVIYVQNCPETSKKNIFEKSALTEPTLENKEGHGMCHSTTNSSCTEPEDTGAEIINV
Protein: Calponin-1 (Basic calponin) (Calponin H1, smooth muscle) (Q9GK38)
Organism: Mustela putorius furo (European domestic ferret) (Mustela furo)
Function: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity (By similarity).
Interaction partners:
- Dystonin
- Myosin-11
- Mas-related G-protein coupled receptor member F
- Calbindin 2
- Calmodulin-like protein 4
- Calmodulin like 5
- Abnormal spindle-like microcephaly-associated protein homolog
- Smoothelin
- Nuclear receptor binding protein 2
- Transgelin
Sequence:
MSSAHFNRGPAYGLSAEVKNKLAQKYDHQREQELREWIEGVTGRRIGSNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTKGNKVNVGVKYAEKQERKFEPEKLREGRNIIGLQMGTNKFASQQGMTAYGTRRHLYDPKLGTDQPLDQATISLQMGTNKGASQAGMTAPGTKRQIFEPGLGMEHCDTLNVSLQMGSNKGASQRGMTVYGLPRQVYDPKYCLTPEYPELGEPTHNHHAHNYYNSA
Protein: Mating-type protein ALPHA1 (MATalpha1 protein) (Alpha-1 activator) (P0CY06)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional coactivator that, in alpha-cells, binds cooperatively with MCM1 and STE12 to a DNA sequence termed the QP' element, to activate the transcription of alpha-specific genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00655}.
Interaction partners:
Sequence:
MFTSKPAFKIKNKASKSYRNTAVSKKLKEKRLAEHVRPSCFNIIRPLKKDIQIPVPSSRFLNKIQIHRIASGSQNTQFRQFNKTSIKSSKKYLNSFMAFRAYYSQFGSGVKQNVLSSLLAEEWHADKMQHGIWDYFAQQYNFINPGFGFVEWLTNNYAEVRGDGYWEDVFVHLAL
Protein: Receptor tyrosine-protein kinase erbB-3 (EC 2.7.10.1) (Proto-oncogene-like protein c-ErbB-3) (Q62799)
Organism: Rattus norvegicus (Rat)
Function: Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. May also be activated by CSPG5. Involved in the regulation of myeloid cell differentiation.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Pro-neuregulin-1, membrane-bound isoform
- Receptor tyrosine-protein kinase erbB-2
- Pro-neuregulin-2, membrane-bound isoform
- Receptor protein-tyrosine kinase
- Pro-epidermal growth factor
- Receptor tyrosine-protein kinase erbB-4
- Protransforming growth factor alpha
- SHC-transforming protein 1
- Growth factor receptor-bound protein 2
- Phosphatidylinositol 3-kinase regulatory subunit alpha
Sequence:
MRATGTLQVLCFLLSLARGSEMGNSQAVCPGTLNGLSVTGDADNQYQTLYKLYEKCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSVLPLPNLRVVRGTQVYDGKFAIFVMLNYNTNSSHALRQLKFTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRVRGAEIVVKNNGANCPPCHEVCKGRCWGPGPDDCQILTKTICAPQCNGRCFGPNPNQCCHDECAGGCSGPQDTDCFACRRFNDSGACVPRCPEPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTFCVRACPPDKMEVDKHGLKMCEPCGGLCPKACEGTGSGSRYQTVDSSNIDGFVNCTKILGNLDFLITGLNVDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGGRSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRVYISANQQLCYHHSLNWTRLLRGPSEERLDIKYDRPLGECLAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSREGVCVTHCNFLQGEPREFVHEAQCFSCHPECLPMEGTSTCNGSGSDACARCAHFRDGPHCVNSCPHGILGAKGPIYKYPDAQNECRPCHENCTQGCNGPELQDCLGQAEVLMSKPHLVIAVTVGLAVILMILGGSFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVFGTVHKGIWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAVGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVKQHRETLGPQLLLNWGVQIAKGMYYLEEHSMVHRDLALRNVMLKSPSQVQVADFGVADLLPPDDKQLLHSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAEPYAGLRLAEIPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIKRASGPGTPPAAEPSVLTTKELQEAELEPELDLDLDLEAEEEGLATSLGSALSLPTGTLTRPRGSQSLLSPSSGYMPMNQSSLGEACLDSAVLGGREQFSRPISLHPIPRGRPASESSEGHVTGSEAELQEKVSVCRSRSRSRSPRPRGDSAYHSQRHSLLTPVTPLSPPGLEEEDGNGYVMPDTHLRGASSSREGTLSSVGLSSVLGTEEEDEDEEYEYMNRKRRGSPPRPPRPGSLEELGYEYMDVGSDLSASLGSTQSCPLHPMAIVPSAGTTPDEDYEYMNRRRGAGGAGGDYAAMGACPAAEQGYEEMRAFQGPGHHAPHVRYARLKTLRSLEATDSAFDNPDYWHSRLFPKANAQRT
Protein: Late embryogenesis abundant protein 17 (OsLEA17) (Late embryogenesis abundant protein 1) (OsLEA3-2) (A3AHG5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in abiotic stress responses. May function as chaperone and contribute to prevent the formation of damaging protein aggregates.
Subcellular location: Nucleus {ECO:0000269|PubMed:23024799}.
Interaction partners:
- DNA polymerase delta small subunit
- DNA polymerase delta catalytic subunit
- Os01g0749000 protein
- Crossover junction endonuclease MUS81
Sequence:
MASRQDRREARAEADARRAAEEIARARDERVMQAEVDARSAADEIARARADRGAATMGADTAHHAAGGGGILESVQEGAKSFVSAVGRTFGGARDTAAEKTSQTADATRDKLGEYKDYTADKARETNDSVARKTNETADASRDKLGEYKDYTADKTRETKDAVAQKASDASEATKNKLGEYKDALARKTRDAKDTTAQKATEFKDGVKATAQETRDATADTARKAKDATKDTTQTAADKARETAATHDDATDKGQGQGLLGALGNVTGAIKEKLTVSPAATQEHLGGGEERAVKERAAEKAASVYFEEKDRLTRERAAERVDKCVEKCVEGCPDATCAHRHGKM