wanglab/gogpt-training-data huggingface dataset:
Protein: TRUD domain-containing protein (Q4GZ59)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKKTLSCRRRLILGMSIEDAQSKFDSPESRVALRLAHERHNQGVYHELNLAQRLRNRLPSERKYHLVRHTKPSVKGFQAYIKSSPDDYVVKELWYGKKATLPKLAGDVGAAAAITSGQSVVDSSPNVIPSIIQEKGVGGPVPCDPLYNGYSNPSGVGAVVDNQTGPVCGVNSSDECARDDTSAASVEGSSMSSQASVEAYIGPQLGEEMDAYSRHRTIFMAELKRVAKTLSNEAKRQLLIRRSKGAAPSARQMSVVDRLVEEVREAEEKGYTSLSSSSHLLEPLGLSLNVCTKRDKRVLEAFRSPLLCVPAEENYISISLWVAGALIENNELATEFPYYIAKHASPDLDECDVITSPNSVPRASIDVYFSLELYKLQQSIGVDGVLALRRFIGRAMIRQHDPLPTTPSIAFNMRLKQRECGGLCSGESTQIPWLHVIKAKVASISGTVLEVSSDDSPSTTVMREAIGHVWRTWGNLVKDLHVHGDLDYLYVSVRPEVDVQVGMPLLGDSTGGVLNCSKGKVLSTSTSLGNSSQQLLQGQDGQDWKGQNGGSNGANLGRAISGKGGKNGSLWNGFNSRKTRATNVILPTDFVVVECLLEKRGLPHRLVVEDITESLTEMQRQAMEVQRLAVIDEAHQQSQQYVTENEEDESCDEGIAQFPVDVRPVLYAPTITVSHAGVIDSASHSFQRIRIRGSCLAHIEALAKALGSGEHFVEREGIHLYATKTSSQGTSLPQLPPNLHFSRTHADVNEHAATKRLIGHHASSSHAVMEQRAASGYFHPYQTLKPMQYMIADHDEREFWREHFYKLSDITLVFHDRVCAADINNSRQWSSTLKSQLLSIGRQRSGQMGLEDESDDTAVNGPKDEEGDSAGRARKKKPKKGRGKRAAQGDLEDVVSTMSPEKIFEYLCFDMEVTSASYDLRMGDNDGYDYRVKLRRIPQSHFPLVKPAMVSLQKHGFINYFGPQRFSSYTRYNMHPGLHLLKGEFHAAASIIVQQFYMDSDLAAEKRRNGHTIEKMYSSKGAGFRLPDIDRSFGGRRSVTENGSALQSVLSNALQASSLLGLNENSAEMESYSSSPKDQQIMNVTNGASVLDPCGEAFLRVVGPKACSMLVHEFLAFLWNDIVNQRLQRYGTFAILPGDLVRLNPLASPHSNEFGRVVYASKNSIEKGKYTCYDVVLPVPGAGVELPDNHTADLYVVTLKRMGILFNPESKQWDIFRSRSNFGNDGALHDGEAAFASSPYNRFSTSFALMEEELGGETSVMNFAHESQVGEEGDAGGMVTEGVLSDGRGLRRDLRHEGNMGNLLGVNIWCSYRHMLVNPSSQLRWRFQSGRTGDPYQRWAFGVRNTFMGRETNVSSLSGALLDKGTLGRSAEQPQQQLLLLGNGAPGRSGKDSRGGKRRARTLPAAPYWLPEKNNGCLELSFQLPSSVYPSMLLREVTKSDVNSPDVVDLDRPLIDTRAESWNGLTADQQQTYRRYLAKKRQKLFTEAPRAINIALLHQHIFRSGGMRRGLIPSMRGYDNVSK
Protein: Alpha-tubulin N-acetyltransferase 1 (Alpha-TAT) (Alpha-TAT1) (TAT) (EC 2.3.1.108) (Acetyltransferase mec-17 homolog) (Q8K341)
Organism: Mus musculus (Mouse)
Function: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. Required for normal sperm flagellar function. Promotes directional cell locomotion and chemotaxis, through AP2A2-dependent acetylation of alpha-tubulin at clathrin-coated pits that are concentrated at the leading edge of migrating cells. May facilitate primary cilium assembly.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Membrane, clathrin-coated pit {ECO:0000255|HAMAP-Rule:MF_03130}. Cell junction, focal adhesion {ECO:0000255|HAMAP-Rule:MF_03130}. Cell projection, axon {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Note=In primary root dorsal ganglion neurons, localizes with acetylated tubulin in axons. Recruited to the mitotic spindle during cell division. {ECO:0000269|PubMed:23275437}.
Interaction partners:
- Protein deacetylase HDAC6
- NAD-dependent protein deacetylase sirtuin-2
Sequence:
MEFPFDVDALFPERITVLDQHLRPPARRPGTTTPARVDLQQQIMTIVDELGKASAKAQHLPAPITSALRMQSNRHVIYILKDTSARPAGKGAIIGFLKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQHMLQKERVEPHQLAIDRPSPKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHRPPTSSLRATRHSRAAVADPIPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSSSLGNSPDRGPLRPFVPEQELLRSLRLCPPHPTARLLLATDPGGSPAQRRRTRGTPWGLVAQSCHYSRHGGFNTSFLGTGNQERKQGEQEAEDRSASEDRVLLLDGSGEEPTQTGAPRAQAPPPQSWTVGGDIMNARVIRNLQERRSTRPW
Protein: Probable NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial (Complex I-13kD-A) (CI-13kD-A) (NADH-ubiquinone oxidoreductase 13 kDa-A subunit) (Q19724)
Organism: Caenorhabditis elegans
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH-ubiquinone oxidoreductase 75 kDa subunit
- NADH dehydrogenase iron-sulfur protein 5
- Acyl carrier protein
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 beta subcomplex subunit 10
Sequence:
MNRLLQQSVSRGPLAVRASSTITTKPPTPNQITKNNAQFDKVTHTGQAWDQSDYRLQRFDISKKSVNPNVAMHLIDQRPPEDCGDKRVVFCDGGHPALGHPKVYINLDKPGVHACGYCGNRFYNSHATKAEDMKIQHLNC
Protein: PEX5-related protein (PEX5-like protein) (Peroxin-5-related protein) (TPR-containing Rab8b-interacting protein) (Tetratricopeptide repeat-containing Rab8b-interacting protein) (Pex5Rp) (TRIP8b) (Q925N3)
Organism: Rattus norvegicus (Rat)
Function: Accessory subunit of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, regulating their cell-surface expression and cyclic nucleotide dependence.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11278749}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Some fraction is membrane associated via its interaction with RAB8B.
Interaction partners:
- Peroxisomal targeting signal 2 receptor
- Peroxisomal membrane protein PEX14
- Ras-related protein Rab-8B
- Cyclic nucleotide-gated channel alpha-1
- Peroxisomal targeting signal 1 receptor.
- Peroxisomal membrane protein PEX13
- Cyclic nucleotide-gated channel subunit beta 1.
- Cyclic nucleotide-gated channel alpha-4
- Cyclic nucleotide-gated channel alpha-2
- Peroxisome assembly protein 12
Sequence:
MYQGHMQGKGSRAADKAVAMVMKEIPREESAEEKPLLTMTSQLVNEQQESRPLLSPSIDDFLCETKSEAIAKPVTSNTAVLTTGLDLLDLSEPVSQTQTKAKKSESSSKSSSLKKKADGSDLISADAEQRAQALRGPETSSLDLDIQTQLEKWDDVKFHGDRTSKGHLMAERKSCSSRAGSKELLWSSEHRSQPELSTGKSALNSESASELELVAPAQARLTKEHRWGSALLSRNHSLEEEFERAKAAVESDTEFWDKMQAEWEEMARRNWISENQEAQNQVTVSASEKGYYFHTENPFKDWPGAFEEGLKRLKEGDLPVTILFMEAAILQDPGNAEAWQFLGITQAENENEQAAIVALQRCLELQPNNLKALMALAVSYTNTSHQQDACEALKNWIKQNPKYKYLVKNKKGSPGLTRRMSKSPVDSSVLEGVKDLYLEAAHQNGDMIDPDLQTGLGVLFHLSGEFNRAIDAFNAALTVRPEDYSLWNRLGATLANGDRSEEAVEAYTRALEIQPGFIRSRYNLGISCINLGAYREAVSNFLTALSLQRKSRNQQQVPHPAISGNIWAALRIALSLMDQPELFQAANLGDLDVLLRAFNLDP
Protein: Moesin/ezrin/radixin homolog 1 (Q9VFU8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell projection, rhabdomere {ECO:0000256|ARBA:ARBA00043944}.
Interaction partners:
- Protein crumbs
- Neurexin-4
- Atypical protein kinase C
- Peripheral plasma membrane protein CASK
Sequence:
MLRFLSRRKVRNNYVDNSREGGGATSSAVGVAGGGGAITSGGSSQIKPQRIVVNKNKIDCRVILLDNTDLSIELSKKALGSFLYEQVFYALDIIEKDYFGLQFMDANHVKHWLDPTKPIKKQVKIGPPYTFRLKVKFYSSEPNTLREELTRYLFFLQLKQDLLEGRLDCPEDKATELCALALQSELGDYDNQEHSAATVSEFRFVPEQTEDLEIAILDEYKTCRGLTPAQAETAFLNKAKWLDMYGVDMHTVLGKDGCEYHLGLTPTGILVFERDQKIGLFFWPKISKLDFKKKKLTLIVIEDDDEGREQEHTFVFRLYNEKACKHLWKCAVEHHTFFRLRAPVKGPSARQNFFRMGSRFRYSGRTEFQTTQQSRARRTVQFERRPSQRFASRQSHLLRERQKASQEAAVSAVASVNARAAAAAAAAAASQSPAPATPLVSSQVSTPTPNNDNNNDAFDSLISTDQFITVTPSPSVLTVIQNSAIIEPDAACSGSISSSSQAAANFASLGRNSLKSNFSNEDPAYSKIGSIGKASGLTVKLDPDYTPPYSPNATKNFDETNPFRNATSSHHGSFGKASISSGQLSVKSGLSDKDRELDSLLKSIVKDPSPSVLANEAINDANSIRVTINKTFDMDHNTETLKRLSNANEKPNNQVKLANVNTTALPPGNIKCNILKARVEEELGAGGNAKLTNQMFVPAAHSSNMHTSNTNSSNNHAHSDGPDSLNATYISVGGDKLTLSIPEQKPSTGSSSSSSTSSTATTTTNGNGPYSNATFVSGFSAPLTPPSSLPANLNNTGSGCNTTLTSVTTISTPSSPTATVSTTASESVAPALSNASAAEILINEIFINNIINNNASGSITAETAAKPAGSSTPSAGTLLFSTLSEQERLESQKTNQQMNQSLNLNQNHSEVDAPPSEKKTPSNYPDSSRIPFPSSSNSKDMVSPWLVSSEVVSAPKGRESAIIRKSVITTQL
Protein: Amphiphysin (A0A0R4INS3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAEIKTGIFAKNVQKRINRAQEKVLQKLGKADETKDEQFEQCVQNFKRQEFEGSRLQREMKAYIAAVKGMQQASMNLTESLHEVYEPDWHGKDDVMTIGKNCDALWEDFHQKLVDSTINTLETYLTQFPDLKVRVAKRSRKLIDYDSARHHLETLQTSTMRNEKRIAKAEEDLKKAQRVFDDLNVGLQDELPTLWDSRVGFYVSTFKNVSSLEARFHREISFLCHKLYEVMNKLAEQHSDKMFTIQGAPSDSGPLRLARTPSPPDDESPDSSPAASPNHTLRPTSPGPPRPKSPSQLKMGPPKPPPPKVTPTRELQQEQIIDLFDGGFPEISVTSPQPNERPGESLLDLDFDPFKPDTSTPIGQTQSPVSQTLPWDLWTGDAAQPAQPATDAGFTANWAADFGSSATTVTDESANTQPAADGQGWPPADGWPTDSTPQPQGETATDEDATVPTFMADFDKMPEAEAEAPEGDVAEGEGEASPASEPEGGEGPVTTPPTDTQPEEITASSPPAETPTSTVESPVSAEPEAAEQAEDSVPVQETEKESPTEAALASVEDKESPIEETPEKMPIPSVVIEPASSNEGDDDRDGDITSPIATGDNGMIADCQTTKDSSGMPPRFLFKVETMHDFEAANPDELELKKGDIVLVVPTELAEDQDAGWLTGIRESDWQQRGASAKKGLFPENFTQRLE
Protein: Cobyrinate a,c-diamide synthase (EC 6.3.5.11) (Cobyrinic acid a,c-diamide synthetase) (Q72F13)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Precorrin-8X methylmutase
- Cobyric acid synthase
- Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase
- corrinoid adenosyltransferase
- Cobalt-precorrin-5B C
- Cobyrinate a,c-diamide synthase
- Precorrin-6Y C5,15-methyltransferase
- CobS protein, putative
- Cobalamin biosynthesis protein CbiG
- Cobalamin biosynthesis protein CobD
Sequence:
MSSARLVIAGLNGGTGKTILSLGTVRALTNAGHSVKPFKKGPDYIDAEWLGLAAGRAATNLDPFFLDAARLQSLFLHASAGASISIIEGNRGLYDGRDVTGSCSTAELARILDSPVVLAMDCTKMTRTAAAILSGVAAFEPGVKLAGVVLNRTANERHRSMLRQCIEHYTDIPVLGALPRLRDNPIPERHMGLVSDREFAQCAGELDRVAQFVAQHVDVERMAEIARSAQPLASNEPFWPVVAEGDGVRPRIGYVRDAALWFYYEENLEALRQAGADLVELRIIDGDPWPTLDGLYLGGGFPETLASELSACRERLAGIREAALAGLPVYAECGGFMVLGESIVMDGVEYPMSGVFPVQTVFHPKPQGLGYVEAEVVAENPFFPQGMVFRGHEFHYSACRPRDGGAVTHALRLNPGTGMGGGADGLVQANTFAAYTHIFGPAVQGWAERFVRAARGHRDQLNKGTDLS
Protein: Spn43Ac (Q6V6U5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FSSELFKEIIKSQSQQNVVFSPFSVHALLALIYGASDGKTFRELQKAGEFSKNAMAVAQDFESVIKYKKHLEGADLTLATKVYYNRELGGVNHSYDEYAKFYFSAGTEAVDMQNAKDTAAKINAWVMDTTRNKIRDLVTPTDVDPQTQALLVNAVYFQGRWEHEFATMDTSPYDFQHTNGRISKVAMMFNDDVYGLAELPELGATALELAYKDSATSMLILLPNETTGLGKMLQQLSRPEFDLNRVAHRLRRQSVAVRLPKFQFEFEQDMTEPLKNLGVHQMFTPNSQVTKLMDQPVRVSKILQKAYINVGEAGTEASAASYAKFVPLSLPPKPTEFVANRPFVFAVRTPASVXL
Protein: Calpain clp-1 (EC 3.4.22.-) (P34308)
Organism: Caenorhabditis elegans
Function: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates (By similarity). Required for assembly and maintenance of integrin attachment complexes which are essential for maintenance of adult muscle. Proteolytic activity is activated in response to increased intracellular Ca(2+) levels during cell degeneration and promotes necrotic cell death.
Subcellular location: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:22479198}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:22479198}. Note=In body wall muscle cells, localizes at M-lines extending over the H-zone, and at adhesion plaques which form between adjacent cells. {ECO:0000269|PubMed:22479198}.
Interaction partners:
Sequence:
MADDEEEIIQKVEVKPDEFNGLIGSIAGNLIRDKVGGAGGDILGGLASNFFGGGGGGGGGGGGGGFGGGNGGFGGGSNYDQGGNGNSGDQQKRKRDMAKDLIGGIFDNVVNRKGKKEQDNYGGGGNYGGGGGNQGGGGGGGFNFNDIGGLINSMGGGGGGGQRQGGGGGGFGDILGGIGSLIGGGGGGQYNGGGGNVNPNNLNGGMVNVIGNLIGEAAHRFLGVDPGTGRIIGAVAGNVIMGLGGKDNSLGNIGKVILDNIISGKFRRDVDPFVRPGPDPDRGGGGSGPSPISPRPTTEPQDFYELRDQCLESKRLFEDPQFLANDSSLFFSKRPPKRVEWLRPGEITREPQLITEGHSRFDVIQGELGDCWLLAAAANLTLKDELFYRVVPPDQSFTENYAGIFHFQFWQYGKWVDVVIDDRLPTSNGELLYMHSASNNEFWSALLEKAYAKLFGSYEALKGGTTSEALEDMTGGLTEFIDLKNPPRNLMQMMMRGFEMGSLFGCSIEADPNVWEAKMSNGLVKGHAYSITGCRIVDGPNGQTCILRIRNPWGNEQEWNGPWSDNSREWRSVPDSVKQDMGLKFDHDGEFWMSFDDFMRNFEKMEICNLGPDVMDEVYQMTGVKAAGMVWAANTHDGAWVRNQTAGGCRNYINTFANNPQFRVQLTDSDPDDDDELCTVIFAVLQKYRRNLKQDGLDNVPIGFAVYDAGNNRGRLSKQFFAANKSAMRSAAFINLREMTGRFRVPPGNYVVVPSTFEPNEEAEFMLRVYTNGFIESEEL
Protein: Halotolerance protein 9 (Q12180)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Putative transcription factor involved in halotolerance.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MENQGGDYSPNGFSNSASNMNAVFNNEITGRSDISNVNHQTGTPRLVPETQIWSMPVPDQLMTMPNRENTLMTGSTIGPNIPMNVAYPNTIYSPTEHQSQFQTQQNRDISTMMEHTNSNDMSGSGKNLKKRVSKACDHCRKRKIRCDEVDQQTKKCSNCIKFQLPCTFKHRDEILKKKRKLEIKHHATPGESLQTSNSISNPVASSSVPNSGRFELLNGNSPLESNIIDKVSNIQNNLNKKMNSKIEKLDRKMSYIIDSVARLEWLLDKAVKKQEGKYKEKNNLPKPARKIYSTALLTAQKLYWFKQSLGVKASNEEFLSPISEILSISLKWYATQMKKFMDLSSPAFFSSEIILYSLPPKKQAKRLLENFHATLLSSVTGIISLKECLDLAEKYYSESGEKLTYPEHLLLNVCLCSGASATQSIIRGDSKFLRKDRYDPTSQELKKIENVALLNAMYYYHKLSTICSGTRTLQALLLLNRYFQLTYDTELANCILGTAIRLAVDMELNRKSSYKSLDFEEAIRRRRMWWHCFCTDKLYSLMLSRPPIVGERDMDMLTDQNYYEVIKTNILPDLIDKKEDLDKITDVNSALNVVVNFCQHISLFISYYVSKLVSIESKIYSTCFAVRSTLDLSFDAMLDKIKDLNDSLNNWRDNLHVSMKLKSYKQYLSVLYAQKSQENPALSFEIACSRVLNCHFRALYSKVILSMMTTSLLIDNERLYKGSRHDIPQLFILFSSQYLNASKEMLQLFQGINYQAHMYNEVMYQFSTAMFVLFFYVVDNMNDLKKKGEVKEIIDILKKSYDRLVGENDEQLLFDNVKWNTLIVFYSHFLKYVLQRYHALNDSTSIFDSKPYDETITKVIMHSRKIKDETVDQLIMSLKSYGSLHSLQKGNEADLADDGLNTNDISSEDFAEEAPINLFGELSVEILKLLKSHSPISNFGDLSPSSNRKGISDDSSLYPIRSDLTSLVYPIHSSDTGDTLSSGLETPENSNFNSDSGIKEDFEAFRALLPLGKLIYDRDYSFVNTFRDYE
Protein: Atrial natriuretic peptide-converting enzyme (EC 3.4.21.-) (Corin) (Pro-ANP-converting enzyme) [Cleaved into: Atrial natriuretic peptide-converting enzyme, N-terminal propeptide; Atrial natriuretic peptide-converting enzyme, activated protease fragment; Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment] (Q80YN4)
Organism: Rattus norvegicus (Rat)
Function: Serine-type endopeptidase involved in atrial natriuretic peptide (NPPA) processing. Converts through proteolytic cleavage the non-functional propeptide NPPA into the active hormone, thereby regulating blood pressure in heart and promoting natriuresis, diuresis and vasodilation (By similarity). Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus (By similarity). Also acts as a regulator of sodium reabsorption in kidney. May also process pro-NPPB the B-type natriuretic peptide (By similarity).
Subcellular location: Cell membrane; Single-pass type II membrane protein. Cytoplasmic vesicle.; SUBCELLULAR LOCATION: [Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment]: Secreted {ECO:0000250}. Note=Soluble form produced following cleavage by ADAM10. {ECO:0000250}.
Interaction partners:
- Natriuretic peptides A
Sequence:
MGRVSFNVRVSSVRRARCSCPGRCYLSCRVPPTTALHALNGFGRAGVLGETAGGTVGLGPSGTRGFLSGSKFQASGSLKDCFGAPPAPDVLRADSSVGEGCPQKLVTANLLRFLLLVLIPCICALIVLLAILLSFVGTLKKVYFKSNDSEPLVTDGEVRVPGVIHVNRYENTGAPSMPPSQSIPAWTPRAPSLEDQSHGNTSTCVNITHRQCQILPYHSTLAPLLPIVKNMDTEKFLKFFTYLHRLGCYQHILLFGCSLAFPKCIVDGDDRHGLLPCRSFCEAAKEGCESVLGMVNSSWPDSLRCSQFRYHTENNSDASRICFSLQQEHGKQSLCGGGESFLCTSGLCISKKLQCNGYNDCDDWSDEAHCNCSEDLFHCGTGKCLHHSLVCDGYDDCGDLSDEQNCDCNLTKEHRCGDGRCIAAEWVCDGDHDCVDKSDEVNCSCPSQGLVECRSGQCIPSTFQCDGDEDCKDGSDEENCSDRPTPCPGGDRGCLDSSCVESCAGSSLCDSDSSLSNCSHCEPITLELCMNLPYNLTHYPNYLGHRTQKEASISWESALFPALVQTNCYKYLMFFACTILVPKCDVNTGQRVPPCRLLCEHSKERCESVLGIVGLQWPEDTDCSQFPEQSSDNQTCLLPNEDVEECSPSHFKCRSGRCVLGSRRCDGQADCDDDSDEENCGCKERDLWECPLNKQCLKHTLICDGFPDCSDSMDEKNCSFCQDDELECANHECVPRDLWCDGWTDCSDSSDEWGCVTLSKNGNSSSFLTVHRSARDHHVCADGWQETLSQLACRQMGLGEPSVTELVQGQEGQQWLRLHSSWENLNGSTLQELLVHRRSCPSGSEISLLCTKQDCGRRPAARMNKRILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGREDADVWKVVFGINNLDHPSGFMQTRFVKTILLHPRYSRAVVDYDISVVELSDDINETSYVRPVCLPSPREFLEPDTYCYITGWGHMGNKMPFKLQEGEVRIIPLEQCQSYFDMKTITNRMICAGYESGTVDSCMIDSGGPLVCERPGGQWTLFGLTSWGSVCFSKVLGPGVYSNVSYFVDWIERQIYIQTFLQKKSQG
Protein: T-cell surface glycoprotein CD1a (T-cell surface antigen T6/Leu-6) (hTa1 thymocyte antigen) (CD antigen CD1a) (P06126)
Organism: Homo sapiens (Human)
Function: Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11231314, ECO:0000269|PubMed:11600221, ECO:0000269|PubMed:18178838}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:18178838}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:11231314}; Single-pass type I membrane protein {ECO:0000255}. Note=Subject to intracellular trafficking between the cell membrane and endosomes (PubMed:11231314). Localizes to cell surface lipid rafts (PubMed:18178838). {ECO:0000269|PubMed:11231314, ECO:0000269|PubMed:18178838}.
Interaction partners:
- Beta-2-microglobulin
- C-type lectin domain family 4 member K
- T-cell surface glycoprotein CD1b
- Macrosialin
- T cell receptor delta variable 1
- CD83 antigen
- T-cell surface glycoprotein CD1c
- T-lymphocyte activation antigen CD86
- T-lymphocyte activation antigen CD80
- T-cell surface glycoprotein CD5
Sequence:
MLFLLLPLLAVLPGDGNADGLKEPLSFHVTWIASFYNHSWKQNLVSGWLSDLQTHTWDSNSSTIVFLCPWSRGNFSNEEWKELETLFRIRTIRSFEGIRRYAHELQFEYPFEIQVTGGCELHSGKVSGSFLQLAYQGSDFVSFQNNSWLPYPVAGNMAKHFCKVLNQNQHENDITHNLLSDTCPRFILGLLDAGKAHLQRQVKPEAWLSHGPSPGPGHLQLVCHVSGFYPKPVWVMWMRGEQEQQGTQRGDILPSADGTWYLRATLEVAAGEAADLSCRVKHSSLEGQDIVLYWEHHSSVGFIILAVIVPLLLLIGLALWFRKRCFC
Protein: Uncharacterized protein (Q585I5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- NEDD8-activating enzyme E1 regulatory subunit
Sequence:
MSVLVKGWGRGTCKINHIRDDDISSSESEGDDANVAVPLEELNVGTQHMITEEMRFRLRRKEKLSVQDDELGRLREAMRRQVFASGLLQPGQSAGVAPRRAEIIFSCAVEIQSSGLMEEAPTASPRVGDTSAWLKQLRKFILDRVPFQRSVRVMVPRTWLARAQETDVV
Protein: Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130) (P40190)
Organism: Rattus norvegicus (Rat)
Function: Signal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST for initiating signal transmission. Binding of IL6 to IL6R induces IL6ST homodimerization and formation of a high-affinity receptor complex, which activates the intracellular JAK-MAPK and JAK-STAT3 signaling pathways. That causes phosphorylation of IL6ST tyrosine residues which in turn activates STAT3 (By similarity). In parallel, the IL6 signaling pathway induces the expression of two cytokine receptor signaling inhibitors, SOCS1 and SOCS3, which inhibit JAK and terminate the activity of the IL6 signaling pathway as a negative feedback loop. Also activates the yes-associated protein 1 (YAP) and NOTCH pathways to control inflammation-induced epithelial regeneration, independently of STAT3 (By similarity). Mediates signals which regulate immune response, hematopoiesis, pain control and bone metabolism (By similarity). Has a role in embryonic development (By similarity). Essential for survival of motor and sensory neurons and for differentiation of astrocytes (By similarity). Required for expression of TRPA1 in nociceptive neurons (By similarity). Required for the maintenance of PTH1R expression in the osteoblast lineage and for the stimulation of PTH-induced osteoblast differentiation (By similarity). Required for normal trabecular bone mass and cortical bone composition (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P40189}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Tyrosine-protein kinase JAK2
- Suppressor of cytokine signaling 3
- Interleukin-6
- Leukemia inhibitory factor receptor
- Interleukin-6 receptor subunit alpha
- Tyrosine-protein kinase JAK3
- Cardiotrophin-1
- Oncostatin-M
- Tyrosine-protein kinase
- Ciliary neurotrophic factor
Sequence:
MSALRIWLMQALLIFLTTESIGQLVEPCGYIYPEFPVVQRGSNFTATCVLKEKCLQVYSVNATYIVWKTNHVAVPKEQVTVINRTASSVTFTDVVFQNVQLTCNILSFGQIEQNVYGITILSGYPPDIPTNLSCIVNEGKNMLCQLDPGRETYLETNYTLKSEWATEKFPDCRTKHGTSSCMMGYTPIYFVNIEVWVEAENALGNVSSEPINFDPVDKVKPSPPHNLSVTNSEELSSILKLAWVNSGLDSILRLKSDIQYRTKDASTWIQVPLEDTVSPRTSFTVQDLKPFTEYVFRIRSIKENGKGYWSDWSEEASGTTYEDRPSKAPSFWYKVNANHPQEYRSARLIWKTLPLSEANGKILDYEVVLTQSKSVSQTYTVNGTELIVNLTNNRYVASLAARNVVGKSPATVLTIPGSHFKASHPVVDLKAFPKDNLLWVEWTPPSKPVNKYILEWCVLSENSPCIPDWQQEDGTVNRTHLRGSLLESKCYLITVTPVFPGGPGSPESMKAYLKQAAPSKGPTVRTKKVGKNEAVLEWDHLPVDVQNGFIRNYSISYRTSVGKEMVVRVDSSHTEYTLSSLSSDTLYMVHMAAYTEEGGKDGPEFTFTTLKFAQGEIEAIVVPVCLAFLLTTLLGVLFCFNKRDLIKKHIWPNVPDPSKSHIAQWSPHTPPRHNFNSKDQMYSDANFTDVSVVEIEANNKKPCPDDLKSLDLFKKEKISTEGHSSGIGGSSCMSSSRPSISSSEENESAQSTASTVQYSTVVHSGYRHQVPSVQVFSRSESTQPLLDSEERPEDLQLVDSVDSGDEILPRQQYFKQSCSQPGASPDVSHFGRSSQVPSGSEEDFVRLKQQQVSDHISEPYGSEQRRLFQEGSVADALGTGTDGQIERFESVGMETAMDEDISKSYLPQTVRQGGYMPQ
Protein: Ephrin type-B receptor 3 (EC 2.7.10.1) (Developmental kinase 5) (mDK-5) (Tyrosine-protein kinase receptor SEK-4) (P54754)
Organism: Mus musculus (Mouse)
Function: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance also plays an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14691139}; Single-pass type I membrane protein {ECO:0000269|PubMed:14691139}. Cell projection, dendrite {ECO:0000269|PubMed:14691139}.
Interaction partners:
- Ephrin-B3
- Ephrin-B2
- Ephrin-B1
- Tyrosine-protein kinase ABL1
- Ephexin-1
- Ras GTPase-activating protein 1
- Ephrin-A5
- Ephrin-A1
- Ephrin-A2
- Ephrin-A3
Sequence:
MAGARPPPGLLPLLAPLLLPLLLPAGCWALEETLMDTKWVTSELAWTSHPESGWEEVSGYDEAMNPIRTYQVCNVRESSQNNWLRTGFIWRREVQRVYVELKFTVRDCNSIPNIPGSCKETFNLFYYEADSDVASASSPFWMENPYVKVDTIAPDESFSRLDAGRVNTKVRSFGPLSKAGFYLAFQDQGACMSLISVRAFYKKCASTTAGFALFPETLTGAEPTSLVIAPGTCIANAVEVSVPLKLYCNGDGEWMVPVGACTCATGHEPAAKESQCRACPPGSYKAKQGEGPCLPCPPNSRTTSPAASICTCHNNFYRADSDSADSACTTVPSPPRGVISNVNETSLILEWSEPRDLGGRDDLLYNVICKKCRGSSGAGGPATCSRCDDNVEFVPRQLGLTERRVHISHLLAHTRYTFEVQAVNGVSGKSPLPPRYAAVNITTNQAAPSEVPTLHLHSSSGSSLTLSWAPPERPNGVILDYEMKYFEKSKGIASTVTSQKNSVQLDGLQPDARYVVQVRARTVAGYGQYSHPAEFETTSERGSGAQQLQEQLPLIVGSTVAGFVFMVVVVVIALVCLRKQRHGPDAEYTEKLQQYIAPGMKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLKLPGRREVFVAIKTLKVGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMILTEFMENCALDSFLRLNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDPSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAVEQDYRLPPPMDCPTALHQLMLDCWVRDRNLRPKFSQIVNTLDKLIRNAASLKVTASAPSGMSQPLLDRTVPDYTTFTTVGDWLDAIKMGRYKESFVGAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILCSIQDMRLQMNQTLPVQV