wanglab/gogpt-training-data huggingface dataset:
Protein: 17-beta-hydroxysteroid dehydrogenase type 3 (17-beta-HSD 3) (Estradiol 17-beta-dehydrogenase 2) (EC 1.1.1.62) (Testicular 17-beta-hydroxysteroid dehydrogenase) (Testosterone 17-beta-dehydrogenase 3) (EC 1.1.1.64) (O54939)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of 17-oxosteroids to 17beta-hydroxysteroids. Favors the reduction of androstenedione to testosterone. Testosterone is the key androgen driving male development and function (By similarity). Uses NADPH while the two other EDH17B enzymes use NADH. Androgens such as epiandrosterone, dehydroepiandrosterone, androsterone and androstanedione are accepted as substrates and reduced at C-17. Can reduce 11-ketoandrostenedione as well as 11beta-hydroxyandrostenedione at C-17 to the respective testosterone forms (By similarity). Plays a role in the rate-limiting-step for the maximum level of testosterone production by the testis but does not affect basal testosterone production (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P37058}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Aromatase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
- Estradiol 17-beta-dehydrogenase 2
- (3R)-3-hydroxyacyl-CoA dehydrogenase (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (KAR alpha subunit) (Estradiol 17-beta-dehydrogenase 8) (Testosterone 17-beta-dehydrogenase 8)
- Polyprenal reductase
- Aldo-keto reductase family 1 member C15
Sequence:
MEQFLLSVGLLVCLVCLVKCVRFSRYLFLSFCKALPGSFLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQVISEEIERTTGSRVKVVQADFTREDIYDHIEEQLKGLEIGVLVNNVGMLPNLLPSHFLSTSGESQSVIHCNITSVVKMTQLVLKHMESRRRGLILNISSGVGVRPWPLYSLYSASKAFVCTFSKALNVEYRDKGIIIQVLTPYSVSTPMTKYLNTSRVTKTADEFVKESLKYVTIGAETCGCLAHEILAIILNLIPSRIFYSSTTQRFLLKQFSDYLKSNISNR
Protein: Ladinin-1 (Lad-1) (Linear IgA disease antigen) (LADA) (O00515)
Organism: Homo sapiens (Human)
Function: Anchoring filament protein which is a component of the basement membrane zone.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}.
Interaction partners:
- Ephrin type-A receptor 4
Sequence:
MAVSRKDWSALSSLARQRTLEDEEEQERERRRRHRNLSSTTDDEAPRLSQNGDRQASASERLPSVEEAEVPKPLPPASKDEDEDIQSILRTRQERRQRRQVVEAAQAPIQERLEAEEGRNSLSPVQATQKPLVSKKELEIPPRRRLSREQRGPWALEEESLVGREPEERKKGVPEKSPVLEKSSMPKKTAPEKSLVSDKTSISEKVLASEKTSLSEKIAVSEKRNSSEKKSVLEKTSVSEKSLAPGMALGSGRRLVSEKASIFEKALASEKSPTADAKPAPKRATASEQPLAQEPPASGGSPATTKEQRGRALPGKNLPSLAKQGASDPPTVASRLPPVTLQVKIPSKEEEADMSSPTQRTYSSSLKRSSPRTISFRMKPKKENSETTLTRSASMKLPDNTVKLGEKLERYHTAIRRSESVKSRGLPCTELFVAPVGVASKRHLFEKELAGQSRAEPASSRKENLRLSGVVTSRLNLWISRTQESGDQDPQEAQKASSATERTQWGQKSDSSLDAEV
Protein: Zinc finger protein 341 (Q9BYN7)
Organism: Homo sapiens (Human)
Function: Transcriptional activator of STAT3 involved in the regulation of immune homeostasis. Also able to activate STAT1 transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:29907690, ECO:0000269|PubMed:29907691}.
Interaction partners:
Sequence:
MAQAIFEALEGMDNQTVLAVQSLLDGQGAVPDPTGQSVNAPPAIQPLDDEDVFLCGKCKKQFNSLPAFMTHKREQCQGNAPALATVSLATNSIYPPSAAPTAVQQAPTPANRQISTYITVPPSPLIQTLVQGNILVSDDVLMSAMSAFTSLDQPMPQGPPPVQSSLNMHSVPSYLTQPPPPPPPPPPLPPPPPPQPPPPPPQSLGPPGRPNPGGNGVVEVYSAAAPLAGSGTVEIQALGMQPYPPLEVPNQCVEPPVYPTPTVYSPGKQGFKPKGPNPAAPMTSATGGTVATFDSPATLKTRRAKGARGLPEAAGKPKAQKLKCSYCDKSFTKNFDLQQHIRSHTGEKPFQCIACGRAFAQKSNVKKHMQTHKVWPPGHSGGTVSRNSVTVQVMALNPSRQEDEESTGLGQPLPGAPQPQALSTAGEEEGDKPESKQVVLIDSSYLCQFCPSKFSTYFQLKSHMTQHKNEQVYKCVVKSCAQTFPKLDTFLEHIKSHQEELSYRCHLCGKDFPSLYDLGVHQYSHSLLPQHSPKKDNAVYKCVKCVNKYSTPEALEHHLQTATHNFPCPHCQKVFPCERYLRRHLPTHGSGGRFKCQVCKKFFRREHYLKLHAHIHSGEKPYKCSVCESAFNRKDKLKRHMLIHEPFKKYKCPFSTHTGCSKEFNRPDKLKAHILSHSGMKLHKCALCSKSFSRRAHLAEHQRAHTGNYKFRCAGCAKGFSRHKYLKDHRCRLGPQKDKDLQTRRPPQRRAAPRSCGSGGRKVLTPLPDPLGLEELKDTGAGLVPEAVPGKPPFAEPDAVLSIVVGGAVGAETELVVPGHAEGLGSNLALAELQAGAEGPCAMLAVPVYIQASE
Protein: Si:dkey-19f23.3 (Transmembrane 6 superfamily member 2b) (A1L2E0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MVQEICVFIFSLTALGVLYTMNNVPAFQEPVVILEIGVAVLVAVFLLVYLATRFNPPKDPLFYVFAEFSFTCVIDLTSALEYDGFASGFMEFYQKTGEPYLGTPYAIMMCYWDGIVHFILYLILIHRMSSRQQYRTLGLFWAGSLCANMIVFVPGIVVGKYGSEIRPAFWLNMPFLLVPIWGAVSFFSRPRDMRLVGADKAEREQKKALIWRPLDLLFVVYLLAAMGFTIFRGLAVLDCPLEILNKYVTEYEPYLKDPVGFPKVMMLLLLFHALPMLASFAYGLCTPGCTWMLDRTVFFAGVILQCEWSHIGASLHPRTAEVYRIPSTALLSVLLLNLLYAVGPVLLALRCKREPDYFLPILPMGQTNNEKKLS
Protein: Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20) (Tyrosylprotein sulfotransferase 2) (TPST-2) (O88856)
Organism: Mus musculus (Mouse)
Function: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:O60704}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O60704}.
Interaction partners:
- Coagulation factor VIII
- Podocalyxin-like protein 2
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
Sequence:
MRLSVRKVLLAAGCALALVLAVQLGQQVLECRAVLGGTRNPRRMRPEQEELVMLGADHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWTKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLARLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGRDKCLPVYYEQLVLHPRRSLKRILDFLGIAWSDTVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPRDVVRDMAQIAPMLARLGYDPYANPPNYGNPDPIVINNTHRVLKGDYKTPANLKGYFQVNQNSTSPHLGSS
Protein: Appetite-regulating hormone isoform X1 (Ghrelin/obestatin prepropeptide) (F1QKX9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Growth hormone secretagogue receptor type 1
- Growth hormone secretagogue receptor type 1
- Glucagon b
- Insulin
- Membrane-bound ghrelin O-acyltransferase mboat4
- Agouti-related neuropeptide.
- Leptin
- Cholecystokinin a
- Peptide YY-A
- Pro-neuropeptide Y
Sequence:
MPLRCRASSMFLLLCVSLSLCLESVSGGTSFLSPTQKPQGRRPPRVGRREAADPEIPVIKEDDRFMMSAPFELSMSLSEAEYEKYGPVLQNLLENLLRDSSFEF
Protein: Putative cytidine deaminase (CDA) (EC 3.5.4.5) (Cytidine aminohydrolase) (Q09190)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Interaction partners:
- Uridine kinase
- Putative purine nucleoside phosphorylase
- 5-azacytidine resistance protein azr1
- Thymidylate kinase
- Uncharacterized protein C1683.06c
- Uridylate kinase
- Probable thymidylate synthase
- Putative uridine kinase C227.14
Sequence:
MEKEDIEKLFQEVKKSLQYSYCPYSNFAVGACVVSDDKNTYIYGANVENASYGNCICAERVAITKAVSMGYTKFMAIGVMSAKGRVTPCGICRQVIREFSKDINVYMFHDDGGYDMKTIEELLPDSFGPDDLK
Protein: Glucocorticoid modulatory element binding protein 1, isoform CRA_a (cDNA, FLJ96492, Homo sapiens glucocorticoid modulatory element binding protein 1(GMEB1), transcript variant 2, mRNA) (B1AT47)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MANAEVSVPVGDVVVVPTEGNEGENPEDTKTQVILQLQPVQQGIYEAGSENNTAVVAVETHTIHKIEEGIDTGTIEANEDMEIAYPITCGESKAILLWKKFVCPGINVKCVKFNDQLISPKHFVHLAGKSTLKDWKRAIRLGGIMLRKMMDSGQIDFYQHDKVCSNTCRSTKFDLLISSARAPVPGQQTSVVQTPTSADGSITQIAISEESMEEAGLEWNSALTAAVTMATEEGVKKDSEEISEDTLMFWKGIADVGLMEEVVCNIQKEIEELLRGVQQRLIQAPFQVTDAAVLNNVAHTFGLMDTVKKVLDNRRNQVEQGEEQFLYTLTDLERQLEEQKKQGQDHRLKSQTVQNVVLMPVSTPKPPKRPRLQRPASTTVLSPSPPVQQPQFTVISPITITPVGQSFSMGNIPVATLSQGSSPVTVHTLPSGPQLFRYATVVSSAKSSSPDTVTIHPSSSLALLSSTAMQDGSTLGNMTTMVSPVELVAMESGLTSAIQAVESTSEDGQTIIEIDPAPDPEAEDTEGKAVILETELRTEEKVVAEMEEHQHQVHNVEIVVLED
Protein: Tubulin tyrosine ligase 3 (EC 6.3.2.-) (Tubulin--tyrosine ligase protein 3) (B2GUB3)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction. Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases. Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions. Together with TTLL8, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28576883}. Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A4Q9E5}.
Interaction partners:
Sequence:
MAHHTAVNPDRLKHAKALVEKAIKQKKIFAIHGPYPVIRSCLRSRGWVEKKFPKSGKAKQKKEKASDEDMEDDDGDGSSNDDDDGENSDEEENGDPDGTCDLMSRLLRNEDPNFFWTTKRDAVDCRFLKKDQMLNHYAKAGSFTTKVGLCLNLRNLHWFDDADPDSFFPRCYRLGAEDEKQSFKEDFWHTAARSILKRVANRRDICSPAATGGAKASHREPGANNGAQLLAKRGSRKRAESVPVQIILTALEACERYLNSLEHNDIDMETEATPAMTDTQWEEFLHGYYQVIHDGATIEHSEYYVDQCSEVLHKLEAVNPQLDIEGGRNIWIVKPGAKSRGRGIICMDRLEEILKLVDCDPMIVKDGKWVVQKYIERPLLIFGTKFDVRQWFLVTDWNPLTIWFYKECYVRFSSQPFSLENLDTSIHLCNNSIQKHYENSQSRHPLVPTDNMWSSRQLQVHLHKLGAPHAWEAVIVPGMKAAIIHAMQSAQDIVEYRKSSFELYGADFMFGENFHPWLIEINASPTMAASTTVTSRLCAEVQEDTLRIVLDRKLDRNCDIGAFELIYKQCAVDIPQYLGINLLVEGSMVKKPRQLQQPNPNGAFNLSIVQSNKRSVSLLNAKTSGSNPGVGSQDSVKVAVPTRTAPAVMGNDFWTSRTHGTIGRAKTTAAGKENKAAEGGQRNSVMVELVRLPSKRALEQSKEGTNPRQRLFPAPKSCTLEKPIRVRQPIRLKNGGFVDLKFTSLDSGQVQLLRNMKTGMTDPNKMPCLFCKGPSSLTGLHAMCSCSRAGKQAAKPTCLKLSKRIIIGKFHGSSAALSARGTAILTSLLP
Protein: Proteasome subunit alpha type-2 (PROS-Dm25) (Proteasome 25 kDa subunit) (P40301)
Organism: Drosophila melanogaster (Fruit fly)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome regulatory subunit 7
- Proteasome subunit beta
- Proteasome subunit beta type-4
- Proteasome subunit beta type-3
- Proteasome subunit beta
- 26S proteasome non-ATPase regulatory subunit 6
- Proteasome subunit beta type-1
- 26S proteasome non-ATPase regulatory subunit 14
Sequence:
MATERYSFSLTTFSPSGKLVQLEYALAAVSGGAPSVGIIASNGVVIATENKHKSPLYEQHSVHRVEMIYNHIGMVYSGMGPDYRLLVKQARKIAQTYYLTYKEPIPVSQLVQRVATLMQEYTQSGGVRPFGVSLLICGWDNDRPYLYQSDPSGAYFAWKATAMGKNAVNGKTFLEKRYSEDLELDDAVHTAILTLKEGFEGKMTADNIEIGICDQNGFQRLDPASIKDYLASIP
Protein: dipeptidyl-peptidase IV (EC 3.4.14.5) (M0R2A8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRKVKKLRLDKENTGSWRSFSLNSEGAERMATTGTPTADRGDAAATDDPAARFQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLLSWKQMLDHFQATPHHGVYSREEELLRERKRLGVFGITSYDFHSESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCSGPRMDPKICPADPAFFSFINNSDLWVANIETGEERRLTFCHQGLSNVLDDPKSAGVATFVIQEEFDRFTGYWWCPTASWEGSEGLKTLRILYEEVDESEVEVIHVPSPALEERKTDSYRYPRTGSKNPKIALKLAEFQTDSQGKIVSTQEKELVQPFSSLFPKVEYIARAGWTRDGKYAWAMFLDRPQQWLQLVLLPPALFIPSTENEEQRLASARAVPRNVQPYVVYEEVTNVWINVHDIFYPFPQSEGEDELCFLRANECKTGFCHLYKVTAVLKSQGYDWSEPFSPGEGEQSLTNAVDSSR
Protein: Aurora kinase B (EC 2.7.11.1) (Serine/threonine kinase A) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase aurora-B) (Q6NW76)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis (By similarity). The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly (By similarity). Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis (By similarity). Required for central/midzone spindle assembly and cleavage furrow formation (By similarity). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage (By similarity). Phosphorylates 'Ser-10' of histone H3 during mitosis (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96GD4}. Chromosome {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere {ECO:0000250|UniProtKB:Q96GD4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96GD4}. Midbody {ECO:0000250|UniProtKB:Q96GD4}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Localization (and probably targeting of the CPC) to the inner centromere occurs predominantly in regions with overlapping mitosis-specific histone phosphorylations H3pT3 and H2ApT12. {ECO:0000250|UniProtKB:Q96GD4}.
Interaction partners:
- Uncharacterized protein.
- Borealin
- Cell division cycle 20 homolog
- Kinesin family member 11
- Kinetochore protein NDC80 homolog
- Baculoviral IAP repeat-containing 5b.
- Cyclin B1
- Kinesin-like protein
- Baculoviral IAP repeat-containing 5a.
- Serine/threonine-protein kinase PLK
Sequence:
MQNKENREPRVQQTPSAGVGPLRVEMNPDTHAVSGPGRVPVKSNSKVLSIDDFDIGRPLGKGKFGNVYLARERKLKVVIALKVLFKSQMVKEGVEHQLRREIEIQSHLRHPNILRFYNYFHDDTRVFLILEYAPRGEMYKELQRYGRFDDQRTATYMEEVSDALQYCHEKKVIHRDIKPENLLLGYRGELKIADFGWSVHAPSLRRRTMCGTLDYLPPEMIEGHSHDEKVDLWSIGVLCYECLVGNPPFETASHAETYKRITKVDLQFPKLVSEGARDLISKLLRHSPSMRLPLRSVMEHPWVKANSRRVLPPVCSSEPH
Protein: Xylan O-acetyltransferase 14 (EC 2.3.1.-) (Protein trichome birefringence-like 3) (OsTBL3) (Q84TV3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Xylan acetyltransferase required for 2-O- and 3-O-monoacetylation of xylosyl residues in xylan. Catalyzes the 2-O-acetylation of xylan, followed by nonenzymatic acetyl migration to the O-3 position, resulting in products that are monoacetylated at both O-2 and O-3 positions (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q2QYU2}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTTTGSTPPRKNRSNVTGGEGGSLEEYAWRAAGEAAAAKKATRAWGVSVSLRSHFSSLVLLLLLLLVALAVSATTKNGDPAETPHAPPLPPPASIKLPSSSSSGGGECDLFSGRWVYDEAAYPLYRESACRVMSEQSACEKYGRTDLRYQHWRWQPHGCDLPRFDAEKFLGKLRNKRLVFVGDSLNRNQWASMLCLIDTGAPELHTSINSSRSLTTFKIHEYNASVDFYWSPLLVESNSDHPLRHRVADRTVRAASINKHAAHWTNADVLVFNSYLWWQRPAMKVLWGSFDNPAAVVAAAAEEGDEYAVSKVIDSLRAYELAVRTWADWMEFHVDRARTQLFFMTMSPTHLRSDEWEDAAAAAAGGNHGCYGETEPIAAEEYRGTSGTDMAFARAVEAEARRLGERSVAVRLINVTRLSERRKDAHPSVHRRYWDPVTDEQRRNPSSYADCIHWCLPGVPDVWNQLLYAHIVS
Protein: CYFIP-related Rac1 interactor B (L1) (Q9NUQ9)
Organism: Homo sapiens (Human)
Function: Negatively regulates RAC1 signaling and RAC1-driven cytoskeletal remodeling. Regulates chemotaxis, cell migration and epithelial polarization by controlling the polarity, plasticity, duration and extent of protrusions. Limits Rac1 mediated activation of the Scar/WAVE complex, focuses protrusion signals and regulates pseudopod complexity by inhibiting Scar/WAVE-induced actin polymerization. Protects against Salmonella bacterial infection. Attenuates processes such as macropinocytosis, phagocytosis and cell migration and restrict sopE-mediated bacterial entry. Restricts also infection mediated by Mycobacterium tuberculosis and Listeria monocytogenes (By similarity). Involved in the regulation of mitochondrial dynamics and oxidative stress.
Subcellular location: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:29059164}.
Interaction partners:
- Ras-related C3 botulinum toxin substrate 3
Sequence:
MGNLLKVLTCTDLEQGPNFFLDFENAQPTESEKEIYNQVNVVLKDAEGILEDLQSYRGAGHEIREAIQHPADEKLQEKAWGAVVPLVGKLKKFYEFSQRLEAALRGLLGALTSTPYSPTQHLEREQALAKQFAEILHFTLRFDELKMTNPAIQNDFSYYRRTLSRMRINNVPAEGENEVNNELANRMSLFYAEATPMLKTLSDATTKFVSENKNLPIENTTDCLSTMASVCRVMLETPEYRSRFTNEETVSFCLRVMVGVIILYDHVHPVGAFAKTSKIDMKGCIKVLKDQPPNSVEGLLNALRYTTKHLNDETTSKQIKSMLQ
Protein: Growth/differentiation factor 8 (GDF-8) (Myostatin) (O42221)
Organism: Meleagris gallopavo (Wild turkey)
Function: Acts specifically as a negative regulator of skeletal muscle growth.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MQKLAVYVYIYLFMQILVHPVALDGSSQPTENAEKDGLCNACTWRQNTKSSRIEAIKIQILSKLRLEQAPNISRDVIKQLLPKAPPLQELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLVQMEGKPKCCFFKFSSKIQYNKVVKAQLWIYLRQVQKPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKAFDENGRDLAVTFPGPGEDGLNPFLEVRVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
Protein: ORF 57 (P88945)
Organism: Human herpesvirus 8 type M
Interaction partners:
Sequence:
MIIDGESPRFDDSIIPRHHGACFNVFIPAPPSHVPEVFTDRDITALIRAGGKDDELINKKISAKKIDHLHRQMLSFVTSRHNQAYWVSCRRETAAAGGLQTLGAFVEEQMTWAQTVVRHGGWFDEKDIDIILDTAIFVCNAFVTRFRLLHLSCVFDKQSELALIKQVAYLVAMGNRLVEACNLLGEVKLNFRGGLLLAFVLTIPGMQSRRSISARGQELFRTLLEYYRPGDVMGLLNVIVMEHHSLCRNSECAAATRAAMGSAKFNKGLFFYPLS
Protein: Aquaporin TIP3-1 (Alpha-tonoplast intrinsic protein) (Alpha-TIP) (Tonoplast intrinsic protein 3-1) (AtTIP3;1) [Cleaved into: Aquaporin TIP3-1, N-terminally processed] (P26587)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Water channel required to facilitate the transport of water from the vacuolar compartment to the cytoplasm.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:16668923}; Multi-pass membrane protein {ECO:0000269|PubMed:16668923}. Note=Tonoplast. It is specifically located in the tonoplast of protein storage vacuoles (PSV) of the embryo and endosperm.
Interaction partners:
- Probable aquaporin SIP2-1
- Protein S-acyltransferase 24
- Aquaporin SIP1-1
- NAC domain-containing protein 91
- V-type proton ATPase subunit a3
- Calcineurin B-like protein 6
- Late embryogenesis abundant protein
Sequence:
MATSARRAYGFGRADEATHPDSIRATLAEFLSTFVFVFAAEGSILSLDKLYWEHAAHAGTNTPGGLILVALAHAFALFAAVSAAINVSGGHVNPAVTFGALVGGRVTAIRAIYYWIAQLLGAILACLLLRLTTNGMRPVGFRLASGVGAVNGLVLEIILTFGLVYVVYSTLIDPKRGSLGIIAPLAIGLIVGANILVGGPFSGASMNPARAFGPALVGWRWHDHWIYWVGPFIGSALAALIYEYMVIPTEPPTHHAHGVHQPLAPEDY
Protein: Glycine oxidase (GO) (EC 1.4.3.19) (Q88Q83)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Catalyzes the oxidation of glycine, leading to glyoxyl imine and hydrogen peroxide as primary products; glyoxyl imine is used for the biosynthesis of the thiazole ring of thiamine. Otherwise, glyoxyl imine is spontaneously hydrolyzed in water to produce glyoxylate and ammonia. Can also use sarcosine (N-methylglycine) as substrate, and, to a lesser extent, N-ethylglycine and D-proline. Has no activity towards other amino-acids D-Asp, D-Glu, D-Gln, D-His, D-Leu, D-Lys, D-ornithine, D-Trp, D-Val, L-Ala, L-Asp, L-Glu, L-His, L-Leu, L-Lys, L-Met and L-Pro.
Interaction partners:
- Thiazole synthase
- Type IV pili biogenesis protein PilE
- hydroxymethylpyrimidine kinase
- Opine oxidase subunit A
- Sarcosine oxidase subunit alpha
Sequence:
MSKQVVVVGGGVIGLLTAFNLAAKVGQVVVCDQGEVGRESSWAGGGIVSPLYPWRYSPAVTALAHWSQDFYPQLGERLFASTGVDPEVHTTGLYWLDLDDEAEALAWAAREQRPLSAVDISAAYDAVPVLGPGFKHAIYMAGVANVRNPRLVKSLKAALLALPNVSLREHCQITGFVQEKGRVTGVQTADGVLAADEVVLSAGAWSGDLLRTLGLELPVEPVKGQMILFKCAEDFLPSMVLAKGRYAIPRRDGHILVGSTLEHAGYDKTPTADALESLKASAVELLPELEGATVVAHWAGLRPGSPEGIPYIGPVPGHEGLWLNCGHYRNGLVLAPASCQLFTDLLTGAEPIIDPAPYAPEGRLG
Protein: Syncytin-A [Cleaved into: Surface protein (SU); Transmembrane protein (TM)] (Q5G5D5)
Organism: Mus musculus (Mouse)
Function: This endogenous retroviral envelope protein has retained its original fusogenic properties. Together with Synb, participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. Syna is essential for placental development and is specifically required for formation of syncytiotrophoblast layer I (SynT-I). Promotes muscle myoblast fusion. Does not have immunosuppressive activity.
Subcellular location: [Transmembrane protein]: Cell membrane {ECO:0000305|PubMed:17762178}; Single-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Surface protein]: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM. {ECO:0000250|UniProtKB:Q9UQF0}.
Interaction partners:
- Plasminogen
- Angiotensin-converting enzyme 2
- Fibronectin
- Cadherin-1
- Albumin
- Integrin beta-1
- Complement factor H
- Chorion-specific transcription factor GCMa
- Toll-like receptor 4
- Sodium-dependent lysophosphatidylcholine symporter 1
Sequence:
MVRPWVFCLLLFPCSSAYSDSWMPLVNLTQHLLQEANSSFSSNCWVCLSIQTQRSLAMPAPLRTWTETPMKLRIMYSARTLSGPYPITDLERRLQNFQPLTPHSSFVNPDQRAIAFLQITSVTGILPILSRITSVRYPDDHVYESAQRPIWGSLSTQTILTSQAPLCISRFFKNSNHATFVGKLPASLCNHTFQLSPSANHQSIDLSSSYAFAPLMAMPGSKWRNPLRFSGPPSLNSGMPHYSCPIDDIHCHTYPTTPWRSCPSFPASTCYNLTLFEPDNSSHPITLSVDTTYFKIKLQGHKDPYPLFQYQPLMGAALSGQYSIWEYEPTVKKNGGITPNIFSHLVSLTYSFCLNSSGVFFLCGNSTYVCLPANWSGVCTLVFQYPDIELLPNNQTISVPLFATVPSSVPASRRKRALPLLPLLAGLGIASALGLGIAGITTSTVYFQQLSKALSDSLDEIATSIISLQDQIDSLAGVVLQNRRALDLIVAERGGTCLFLQEECCFYINQSGVVRHAARKLRERASELGTSSSSWIQWLGLGPWLPSWLTSLMAPILFILVLLVFRPCLLNCLTHSVSRRMSSFIHTTTEGHVDKILLLRESQYKRLPQEPPEEDAV
Protein: Nuclear transport factor 2 (NTF-2) (P61972)
Organism: Rattus norvegicus (Rat)
Function: Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:9822603}. Nucleus outer membrane {ECO:0000269|PubMed:10543952, ECO:0000269|PubMed:11846560, ECO:0000269|PubMed:15522285, ECO:0000269|PubMed:9822603}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10543952, ECO:0000269|PubMed:11846560, ECO:0000269|PubMed:15522285}. Nucleus inner membrane {ECO:0000269|PubMed:10543952, ECO:0000269|PubMed:11846560}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61970}. Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. {ECO:0000250|UniProtKB:P61970}.
Interaction partners:
- GTP-binding nuclear protein Ran
- Nuclear pore glycoprotein p62
- Nuclear pore complex protein Nup54
- NTF2-related export protein
- Ran-specific GTPase-activating protein
- RNA helicase
- FA complementation group G
- Regulator of chromosome condensation
- Nuclear pore complex protein Nup153
- NTF2-related export protein 2
Sequence:
MGDKPIWEQIGSSFIQHYYQLFDNDRTQLGAIYIDASCLTWEGQQFQGKAAIVEKLSSLPFQKIQHSITAQDHQPTPDSCIISMVVGQLKADEDPIMGFHQMFLLKNINDAWVCTNDMFRLALHNFG
Protein: Integrin beta 1 binding protein 1, isoform CRA_g (Integrin subunit beta 1 binding protein 1) (A8MPU2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLVRLRYFG
Protein: GTP cyclohydrolase 1 feedback regulatory protein (GFRP) (GTP cyclohydrolase I feedback regulatory protein) (p35) (P70552)
Organism: Rattus norvegicus (Rat)
Function: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine.
Subcellular location: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- GTP cyclohydrolase 1
- 6-pyruvoyl tetrahydrobiopterin synthase
- Dihydropteridine reductase
Sequence:
MPYLLISTQIRMEVGPTMVGDEHSDPELMQQLGASKRRVLGNNFYEYYVNDPPRIVLDKLECRGFRVLSMTGVGQTLVWCLHKE