wanglab/gogpt-training-data huggingface dataset:
Protein: Transposon Ty1-GR2 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q12269)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPGINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (B2RYC7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNFNTILEEILIKRSQQKKKTSPLNYKERLFVLTKSVLTYYEGRAEKKYRKGFIDISKIKCVEIVKNDDGIIPCQNKFPFQVVHDANTLYIFAPSPQSRDRWVKKLKEEIKNNNNIMIKYHPKFWADGSYQCCRQTEKLAPGCEKYNLFESSIRKTLPPAPEIKRRPPPPIPPEEENTEEIVVAMYDFQATEAHDLRLERGQEYIILEKNDTHWWRARDKYGSEGYIPSNYVTGKKSNNLDQYEWYCRNTNRSKAEQLLRTEDKEGGFMVRDSSQPGLYTVSLYTKFGGEGSSGFRHYHIKETATSPKKYYLAEKHAFGSIPEIIEYHKHNAAGLVTRLRYPVSTKGKNAPTTAGFSYDKWEINPSELTFMRELGSGLFGVVRLGKWRAQYKVAIKAIREGAMCEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMERGCLLNFLRQRQGHFSRDVLLSMCQDVCEGMEYLERNSFIHRDLAARNCLVNEAGVVKVSDFGMARYVLDDQYTSSSGAKFPVKWCPPEVFNYSRFSSKSDVWSFGVLMWEIFTEGRMPFEKNTNYEVVTMVTRGHRLPRPKLASKYLYEVMLRCWQERPEGRPSFEDLLRTIDELVECEETFGR
Protein: Zinc metalloproteinase/disintegrin-like HR1a (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP) [Cleaved into: Disintegrin-like 1a] (Q8JIR2)
Organism: Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
Function: Zinc protease that induces hemorrhage and has proteolytic activity. Has preference for Ala, His, Pro, Met, and Tyr at the P1 position, in descending order (in vitro). Predominantly prefers Val and Asp at the P3 and P2 positions, respectively.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MIQVLLVTICLAVFPYQGSSIILGSGNVNDYEVVYPRKVTAVPKGAVQPKYEDTMQYEFKVNGEPVVLHLEKNKGLFSKDYSETHYSPDGREITTYPSVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGEMYLIEPLRFSDSEAHAVFKYENVEKEDEAPKMCGVTQTNWESDEPIKKASKLVVTAEQQRYLNNFRFIELVIVADYRMFTKFNSNLNEVKTWVYEIVNTLNEIYRYLYVRVALVALEVWSNGDLSSVTLSAYDTLDSFGEWRKRDLLKRKSHDNAQLLTAIDFNGTIIGLAHVASMCDPKCSTGIVQDYSSRNLVVAVIMAHEMGHNLGIRHDRENCTCHANSCIMSAVISDQPSKYFSNCSHVQYWNYINDDEPQCILNEPLRTDIVSPPVCGNELLEVGEECDCGSPATCRYPCCDAATCKLHSWVECESGECCEQCRFRTAGTECRARRSECDIAESCTGHSADCPTDRFHRNGQPCLHNFGYCYNGNCPIMYHQCYALWGANATVAKDSCFEDNQKGNDYGYCRKENGRKIPCEPQDVKCGRLYCSLGNQLPCRFFYTPTDENIGMVDTGTKCGDKKVCSNRQCVDVNTAY
Protein: Acidic fibroblast growth factor intracellular-binding protein (aFGF intracellular-binding protein) (FGF-1 intracellular-binding protein) (O43427)
Organism: Homo sapiens (Human)
Function: May be involved in mitogenic function of FGF1. May mediate with IER2 FGF-signaling in the establishment of laterality in the embryo (By similarity).
Subcellular location: Nucleus. Endomembrane system; Peripheral membrane protein. Note=Also associated with cytoplasmic membranes, particularly of mitochondria.
Interaction partners:
- Fibroblast growth factor 1
- C2 domain-containing protein 5
- Cyclin-dependent kinase 5
- CDK5 and ABL1 enzyme substrate 1
- CDK5 and ABL1 enzyme substrate 2
- Transmembrane protein 94
Sequence:
MTSELDIFVGNTTLIDEDVYRLWLDGYSVTDAVALRVRSGILEQTGATAAVLQSDTMDHYRTFHMLERLLHAPPKLLHQLIFQIPPSRQALLIERYYAFDEAFVREVLGKKLSKGTKKDLDDISTKTGITLKSCRRQFDNFKRVFKVVEEMRGSLVDNIQQHFLLSDRLARDYAAIVFFANNRFETGKKKLQYLSFGDFAFCAELMIQNWTLGAVGEAPTDPDSQMDDMDMDLDKEFLQDLKELKVLVADKDLLDLHKSLVCTALRGKLGVFSEMEANFKNLSRGLVNVAAKLTHNKDVRDLFVDLVEKFVEPCRSDHWPLSDVRFFLNQYSASVHSLDGFRHQALWDRYMGTLRGCLLRLYHD
Protein: EF-hand domain-containing family member C2 (Q5JST6)
Organism: Homo sapiens (Human)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9D485}.
Interaction partners:
- Parkin coregulated gene protein
- Enkurin
- Cilia- and flagella-associated protein 161
- Tektin-2
- EF-hand domain-containing family member B
- Cilia- and flagella-associated protein 45
- Tektin-1
- Cilia- and flagella-associated protein 20
- Probable G-protein coupled receptor 82
- EF-hand domain-containing protein 1
Sequence:
MALPLLPGNSFNRNVGKEKFHKSQHWGFCNNVMMLVSDEKPGIGGEPLLGQKIKPKCSIYPKGDGSDVPSWVAFDKQVLSFDAYLEEEVLDKSQTNYRIRYYKIYFYPEDDTIQVNEPEVKNSGLLQGTSIRRHRITLPPPDEDQFYTVYHFNVGTEVVFYGRTFKIYDCDAFTRNFLRKIGVKVNPPVQCPEDPYMKIRREVVEHVEPLRPYESLDTLKQFLQYHGKILCFFCLWDDSVSMFGDRRELILHYFLCDDTIEIKELLPHSSGRDALKMFLRRSKLPKNCPPRVYQPGQITDRAVLNSYGDFIKNQADGYLFDRYKLGKVDQEFYKDSDLSLGVTINVWGRKVLLYDCDEFTKSYYKSKYGIENFTSVSCKPPSPPPKIERKFPPYNGFGSEEDSLRNCIDLKPTPHRRNFKKFMEKDSYGSKSNILRFFAKLVTDKCVDLDRMFVISYYLGDDTISVFEPIERNSGIAGGMFLKRSRVKKPGQEVFKSELSEYIKAEELYIGVTVNVNGYLFRLLNADEYTLNYMEQNTDKYPFSNLKLALQKLKQEEGKSRELKQVFKAADSKHTNMVDYNTFRDILMSLTVGNLAEQEFVTIARHYRVPEGTCSDMDFLIALAHEKFKKNMFENFDTFIYSCVYEDREKKNVLPTKDIKRLCKSSRLPLSDDLLESLLSRFEDSEKQIDYKSFFSALNWRKNPVPELQPASYLKERCEDVWLGMPSPIPAKYIDYWTFLKDAFGLEEE
Protein: Syncytin-2 (ERV-FRD provirus ancestral Env polyprotein) (Envelope polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)] (P61553)
Organism: Callithrix jacchus (White-tufted-ear marmoset)
Function: This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. The interaction with MFSD2A is apparently important for this process (By similarity).
Subcellular location: Virion {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}.; SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium-dependent lysophosphatidylcholine symporter 1
- RNA helicase
Sequence:
MGLLLLLLILTPLLAAYCHPDFRLLEKAQQLLQSTGSPYSTNCWLCTSSSSKTPGRAYPASSREWTTIEAELHISYQWDPNLKGLIRLANSLLSKVKQDFPDIRKEPPIFGPIFTNVNLIGIAPICVTAKRKDGTNVGTLPSTVCNVTLTVDPNQQTYQKYAHNQFHHQPRFPKPPNITFPQGTLLDKSTRFCQGRPSSCSTRNFWFQPADYNQCLQIPNLSSTAEWVLLDQTRNSLFWENKTKGANQSQTPCVQVLAGMTIATSYLSTSAVSEFSGTSVTSLFSFHISTCLKTQGAFYICGQSIHQCLPTNWTGTCTIGYVSPDIFIAPGNLSLPIPIYGNFHFPRVKRAIHLIPLLVGLGIVGSAGTGIAGIAKASFTYSQLSKEIANNIEAMAKTLTTVQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNRASTLQEQATQGWLNWEGTWKWFSWVLPFTGPLVSLLLLLLFGPCLLNLITQFVSSRLQATKLQMKLNKRVHPRNSQESPF
Protein: Hyperkinetic, isoform F (M9NEC7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTPPRLSRYLMAVRGGRDGEQHSKNSQTDEEKQRDRQRNEREAKKEEQDAINYKRDKEQREARLLDFEIRRQQKRDEQQQQRQQQQQLQQHREHLQQQHRDQQQSSEKSPPTSSTAAAAHQTHSHSQQQQQRQHLHLQQQHLQQQQQQQQQQSTGSGSSNTPVTPKLQTPPPDRSLPPAFRSRSIEREILYERKRFSQPETGEIKELDSTTSSSSTQQTFPGSAVGAGRGASAAVPGSGTAIAVAVAGAGAGQSATLAGPPATAAAATAAIIPILPLGVATLRDDSTESEQSVTCAHNQLDAYHRIMCRAPIASLDCMEEFSGTGGHLDFGRSISLGSNPALPLRHGSTPTPGLRYKNLGKSGLRISNVGLGTWPVFSPGVSDDQAEAILKLAIESGINLFDISEAHSETEIGKILQRAGWKRTAYVITTKVYWSTKSEERGLSRKHIIECVRASLQRLQLQYIDIVIIHKADPMCPMEVVRAMSYVIQQGWAMYWGTARWSQVEIMEAYTNCRQFNCITPIVEQSEYHMFCREKCELYLPEMYNKIGVGLMAWGPLSMALSDTQNGDKLFLPKGSFKTKSFSWTEDEINRNAALSPQGSWGKDRIDEGRRHCDRLRDLAALAEKLGCSPTQLSIAWSLKHEPVQCLLLGATSAEQLHQSLQSLQLLPRLSSSVMLELERILENKPVRPPMISTLALR
Protein: F-box domain-containing protein (O45285)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPAILETNPIAIRACILYEVRQKRPIFESFKNFCNAFGNDFMEYREFERWFYRFYHGNEDLDYDMSREPKTASLSELPIEILFKIVENLNFLDRLLLRNVSPCFRSIAEDHVNEVTNISVTSIPNHVHVCFYHESDYTDIICKRVDDDCVITKMSQYEDSKDWKIEGVSHVTVALNYLSRVLKSPKLKLEKLRLDFLEHNKEDTQCMEELLTVLENSEPHVLNIEFEGLNFHETSSVLKNLKNVEEIQLSMYSIQELSGIEKLVELEQWKTAKTLDISSHEDIEMDIKDLLHFQSIDVRLKSFSVQDAVKVKETLELRTSDFRSGTFRVLNTDTRKIGKVFNPKYTDAANNTFNFKTKNSSFEITMCSKEIYVKRKL
Protein: Mitochondrial-derived peptide MOTS-c (Mitochondrial open reading frame of the 12S rRNA-c) (A0A0C5B5G6)
Organism: Homo sapiens (Human)
Function: Regulates insulin sensitivity and metabolic homeostasis. Inhibits the folate cycle, thereby reducing de novo purine biosynthesis which leads to the accumulation of the de novo purine synthesis intermediate 5-aminoimidazole-4-carboxamide (AICAR) and the activation of the metabolic regulator 5'-AMP-activated protein kinase (AMPK). Protects against age-dependent and diet-induced insulin resistance as well as diet-induced obesity. In response to metabolic stress, translocates to the nucleus where it binds to antioxidant response elements (ARE) present in the promoter regions of a number of genes and plays a role in regulating nuclear gene expression in an NFE2L2-dependent manner and increasing cellular resistance to metabolic stress. Increases mitochondrial respiration and levels of CPT1A and cytokines IL1B, IL6, IL8, IL10 and TNF in senescent cells. Increases activity of the serine/threonine protein kinase complex mTORC2 and reduces activity of the PTEN phosphatase, thus promoting phosphorylation of AKT. This promotes AKT-mediated phosphorylation of transcription factor FOXO1 which reduces FOXO1 activity, leading to reduced levels of MSTN and promotion of skeletal muscle growth. Promotes osteogenic differentiation of bone marrow mesenchymal stem cells via the TGFB/SMAD pathway. Promotes osteoblast proliferation and osteoblast synthesis of type I collagens COL1A1 and COL1A2 via the TGFB/SMAD pathway.
Subcellular location: Secreted {ECO:0000269|PubMed:25738459}. Mitochondrion {ECO:0000269|PubMed:29983246}. Nucleus {ECO:0000269|PubMed:29983246, ECO:0000269|PubMed:33473109}. Note=Translocates to the nucleus in response to metabolic stress in an AMPK-dependent manner. {ECO:0000269|PubMed:29983246}.
Interaction partners:
Sequence:
MRWQEMGYIFYPRKLR
Protein: ALK and LTK ligand 1 (Augmentor beta) (AUG-beta) (Q6UXT8)
Organism: Homo sapiens (Human)
Function: Cytokine that acts as a physiological ligand for receptor tyrosine kinase LTK, leading to its activation. Monomeric ALKAL1 binds to LTK, leading to LTK homodimerization and activation. In contrast to ALKAL2, does not act as a potent physiological ligand for ALK.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q6UX46}. Cell membrane {ECO:0000305|PubMed:34646012}. Note=Following interaction with receptor tyrosine kinase LTK, associates with the cell membrane, membrane-binding is required to activate LTK. {ECO:0000250|UniProtKB:Q6UX46}.
Interaction partners:
- Leukocyte tyrosine kinase receptor
Sequence:
MRPLKPGAPLPALFLLALALSPHGAHGRPRGRRGARVTDKEPKPLLFLPAAGAGRTPSGSRSAEIFPRDSNLKDKFIKHFTGPVTFSPECSKHFHRLYYNTRECSTPAYYKRCARLLTRLAVSPLCSQT
Protein: Acetate kinase EutQ (EC 2.7.2.1) (Ethanolamine utilization protein EutQ) (P76555)
Organism: Escherichia coli (strain K12)
Function: A bidirectional acetate kinase that may drive flux through the ethanolamine degradation pathway under anoxic conditions. It may generate ATP that can be used by other enzymes (EutA and EutT) in the eut pathway. Might serve as an assembly hub for bacterial microcompartment (BMC) shell proteins.
Subcellular location: Bacterial microcompartment {ECO:0000250|UniProtKB:Q9ZFV5}. Note=May be found on the cytoplasmic face of the BMC. {ECO:0000250|UniProtKB:Q9ZFV5}.
Interaction partners:
- Corrinoid adenosyltransferase EutT
- Probable acetate kinase EutP
- Ethanolamine ammonia-lyase reactivase EutA
- Bacterial microcompartment shell protein EutS
- Ethanolamine utilization protein EutJ
- Ethanolamine ammonia-lyase small subunit
- Bacterial microcompartment shell protein EutL
- Bacterial microcompartment shell vertex protein EutN
- Probable ethanolamine permease EutH
- Bacterial microcompartment shell protein EutM
Sequence:
MKKLITANDIREAHARGEQAMSVVLRASIITPEAREVADLLGFTITECDESIPVTASVPASVPADKTESQRIRETIIAQLPEGQFTESLVAQLMEKVMKEKQSLEQGAMQPSFKSVTGKGGIKVIDGSSVKFGRFDGAEPHCVGLTDLVTGDDGSSMAAGFMQWENAFFPWTLNYDEIDMVLEGELHVRHEGQTMIAKAGDVMFIPKGSSIEFGTTSSVKFLYVAWPANWQSL
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (F1N329)
Organism: Bos taurus (Bovine)
Interaction partners:
- Small ubiquitin-related modifier 1
- Kelch-like protein 7
Sequence:
MGSQQPPGSPLSREEGEAPRPTPAPEGRRRSRRVRLRGSCRHRPSLLGRRELATSAPVRPAPASSEIMASAAKEFKMDNFSPKAGTSKLQQTVPADASPDSKCPICLDRFDNVSYLDRCLHKFCFRCVQEWSKNKAECPLCKQPFDSIFHSVRAEDDFKEYVLRPSYNGSFATPEVRRFRYRTTMTRERSASVHSPSSTVNRRTTTPPDSGVLFEGLSISARPRDGEIPPFMRQISVRRPTTTDERSLRKIQEQDIINFRRTLYRAGARVRNIEDGGRYRDISAEFFRRNPACLHRLVPWLKRELTVLFGAHGSLVNIVQHIIMSNVTRYDLESQAFVSDLRPFLLNRTEHFIHEFISFARSPFNMAAFDQHANYDCPAPSYEEGSHSDSSVITISPDEAETQELDVNVATVSQAPWDDETPGPSYSSSEQVHAAMSSLLNTSDSSDEELVTARATSQIQGVQTNEDLNNDSDSSSDNCVIVGFVKPLAERTPELVELSSDSEVELGSYEKMETMKTQEQEQSYSSGDSDVSRCSSPRSVVGKDEQINKGRCDSGTKINSKKEEKRSISLSSLRDLSSSLRGDRVYSPYTRRHRKRGRSRSSDSYSQSRSGHDQKNRRKHHGKKRMKGKRSRSRESSRPRGRRDKKRSRTRDSSWSRRSQTLSLSSESSSRSRSRSSDHGKRRSRSRNRDRYYLRNNYGSRYKWEYTYYSRNKDRDGYESSYRRRTLSRAHYSRQSSSPELRIQSFSERTNARKKNNHSERKYYYYERHRSRSLSSNRSKTASTGPDRVRNEKPGGKRKYKTRHLEGTNDVAQPCHEFASKVKEGHYSKSSSKLDGGYKNESDSFSDSRSSDRETKHKRRKRRTRSLSVEIVYEGKATDTTRHHKKKKKKHKRKHKRHHGDNASHSPVVITIDSDSDKDCEVKEDIECDPSGPQGPLQSEVLAPFESKDVVTIEDEFGVLSKECDITILNNNLNNANKTVDNISPQAASIGQTLDVREESTLASDLENQPSTVSFQTEPSRTSSLMSVSLGRDHDVS
Protein: E3 ubiquitin-protein ligase TRIM50 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM50) (Tripartite motif-containing protein 50) (Q810I2)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that ubiquitinates Beclin-1/BECN1 in a 'Lys-63'-dependent manner enhancing its binding to ULK1. In turn, promotes starvation-induced autophagy activation. Interacts also with p62/SQSTM1 protein and thereby induces the formation and the autophagy clearance of aggresome-associated polyubiquitinated proteins through HDAC6 interaction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22792322, ECO:0000269|PubMed:24308962, ECO:0000269|PubMed:29604308, ECO:0000269|PubMed:36178239}. Note=Localizes mainly into discrete cytoplasmic punctuate structures heterogeneous in size and shape containing polyubiquitinated proteins. {ECO:0000269|PubMed:22792322}.
Interaction partners:
Sequence:
MAWRLTVPELQDQLQCPICLEVFKEPLMLQCGHSYCKDCLDNLSQHLDSELCCPVCRQSVDCSSSPPNVSLARVIDALRLPGDIEPTVCVHHRNPLSLFCEKDQEFICGLCGLLGSHQHHRVTPVSTVYSRMKEELAGRISELKEEHRNVEEHIGKLVNNRTRIINESDVFSWVIRREFQELHHLVDEEKARCLEGLEGHTRGLVASLDMQLEQAQGTQERLAQAEQVLEQFGNESHHEFIRFHSVASRAEVQQARPLEGVFSPISFKPALHQADIKLTVWKRLFRKVLPAPASLKLDPATAHPLLELSKGNTVVHCGLLAQRRASQPERFDYSTCVLASKGFSWGRHYWEVVVGSKSDWRLGVIKGTASRKGKLNKSPEHGVWLIGLKEGRVYEAFGCPRLPLPVAGHPHRIGVYLHYEQGELTFFDADRPDDLRTLYTFQADFQGKLYPILDTCWHERGSNSLPMVLPPPSGPGHFTLGQV
Protein: TRAF2 and NCK interacting kinase a isoform X4 (TRAF2 and NCK-interacting kinase a) (A0A0R4IEP9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASDSPARSLDEIDLSTLRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKCMDVTGEEEEEIKAEINMLKKYSHHRNIATYYGAFIKKNPPGVDDQLWLVMEFCGAGSVTDLIKNTKGNSLKEDWTAYISREILRGLTHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVSRRNTFIGTPYWMAPEVIACDENPDATYDYKSDLWSLGITALEMAEGAPPLCELHPMRALFLIPRNAPPRLKSKKWTKRFHSFIESCLVKNHNMRPGTDQLLKHPFIRDMANERTIRIQLKDHIDRTRKKRGERDETEYEYSGSEEEEEAMLEIGEPSSIINIPGESTLRRDFLRLQVANKERSDALRRQQLEQQQNEGHKHQLLAERQKRIEEQKEQRRRLEEQQRREREARKQQEQRHRYEELRREEERRQAEREQEYIRRQLEEEQRQLEILQQQLLQEQALLLEYKRKQVEEQRQADRLQRQLQQERAYLVSLQQQQQQQQQDSRPEEKKQLYHYKDAVNPSDKPAWAKKVEERSKLNRQSSPALQHKVANRISDPSLPPRSESFSSGGMQPARTPPMHRPVEPQMAHLVPVRSHSSSMSVSQSLHDQSAKGVSAFQESLVSNRPEMPRQNSDPTSEMPPPAPRMASHEEKPDRSSPWLREDAVPPKLSGTTQVPQRTTSISPALARKNSPGNGESSGGGRSASQLIRTSNPDLRRTELSLDVALQRTSSNSSSSSSTPSSQGGSQPGSSERNQPRGSGKSEGSPVALQETSKPIQEEGRELSKPSRPADLTALAKELRELRIDEVSRPPLKLTDYSSSSEDSDSSEDEDGTVGHDGTVSVSDIPRIMPSVQGNNESFTSSHDDSLTDSYNDESKDGTLRMRENNERQRLGHGESNGFAGHGNLPDLLQQSHSPSGTPTGLNSQDLDSMDEFGLGGGSKASFTPFVDPRVYQTSPTDDNDESSAAAMFANELLRQEQAKLNEARKISVVNVNPTNIRPHSDTPEIRKYKKRFNSEILCAALWGVNLLVGTENGLMLLDRSGQGKVYNLITRRRFQQMDVLEGLNVLVTISGKKNKLRVYYLSWLRNRILHNDPEVEKKQGWITVGELEGCIHYKVVKYERIKFLVIALKNSVEIYAWAPKPYHKFMAFKSFTELQHRPQLVDLTVEEGQRLKVIYGSSVGFHVIDVDSGSPYDIYIPSHIQSTVTPHAIVVLPKTDGMEMLLCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIHSNQIMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVFFMTLNRNSLMNW
Protein: Ribosomal RNA small subunit methyltransferase J (EC 2.1.1.242) (16S rRNA m2G1516 methyltransferase) (rRNA (guanine-N(2)-)-methyltransferase) (P68567)
Organism: Escherichia coli (strain K12)
Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01523}.
Interaction partners:
- Oligopeptidase A
- Putative membrane protein insertion efficiency factor
Sequence:
MKICLIDETGTGDGALSVLAARWGLEHDEDNLMALVLTPEHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAKAVGIKGDYLPDVVDATAGLGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADAEIGGWLQERLQLIHASSLTALTDITPRPQVVYLDPMFPHKQKSALVKKEMRVFQSLVGPDLDADGLLEPARLLATKRVVVKRPDYAPPLANVATPNAVVTKGHRFDIYAGTPV
Protein: Cellular retinoic acid-binding protein 1 (Cellular retinoic acid-binding protein I) (CRABP-I) (P40220)
Organism: Gallus gallus (Chicken)
Function: Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 26A1
- Cytochrome P450 26B1
Sequence:
MPNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKIGESFEEETVDGRKCRSLATWENENKIYCKQTLIEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE
Protein: Meiotic expression up-regulated protein 29 (O13980)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein C2A9.02
- U6 small nuclear RNA
Sequence:
MFVVKTAVLLFFALFIGNTYAYTYSLDRIQALKFSSESSNVDDGPRLHCKGPACSSHSNDLAICQHNQLNVAPHLLKWTCVWPNQSSHVEVIDYNIECKKTVALSMDSITKTCILNYKLEWTYSGVLLHRPWKLFSLKPFTAAFVLLLAASYLATACFRMLGYLGTPRSRFHDNRRWNEQKFMELAVSAVEEQLSNGIQLFSNVKQRVPVPVLDESV
Protein: Autophagy-related protein 27 (Enhancer of VPS34 missorting protein 1) (P46989)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Effector of VPS34 phosphatidylinositol 3-phosphate kinase signaling. Regulates the cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a role in ATG protein retrieval from the pre-autophagosomal structure (PAS) and is especially required for autophagy-dependent cycling of ATG9.
Subcellular location: Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Mitochondrion membrane; Single-pass membrane protein. Preautophagosomal structure membrane; Single-pass type I membrane protein. Note=Cycles among the pre-autophagosomal structure (PAS), mitochondria and Golgi.
Interaction partners:
- Autophagy-related protein 9
- Autophagy-related protein 23
- Serine/threonine-protein kinase ATG1
- Autophagy-related protein 13
- Autophagy-related protein 18
- Autophagy-related protein 11
- Sorting nexin-4
- Autophagy-related protein 8
- Autophagy-related protein 19
- Autophagy-related protein 2
Sequence:
MVSKTWICGFISIITVVQALSCEKHDVLKKYQVGKFSSLTSTERDTPPSTTIEKWWINVCEEHNVEPPEECKKNDMLCGLTDVILPGKDAITTQIIDFDKNIGFNVEETESALTLTLKGATWGANSFDAKLEFQCNDNMKQDELTSHTWADKSIQLTLKGPSGCLKSKDDDKKNGDGDNGKDGDSEGKKPAKKAGGTSWFTWLFLYALLFTLIYLMVVSFLNTRGGSFQDFRAEFIQRSTQFLTSLPEFCKEVVSRILGRSTAQRGGYSAV
Protein: Protein PELPK1 (Proline-rich protein 10) (Protein Pro-Glu-Leu|Ile|Val-Pro-Lys 1) (Q9LXB8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Positive regulator of germination and plant growth.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:25850299}.
Interaction partners:
- Non-specific lipid transfer protein GPI-anchored 20
- Leucine-rich repeat extensin-like protein 6
- Transmembrane protein, putative
- C2 domain-containing protein At1g53590
- Filament-like protein
- Haloacid dehalogenase-like hydrolase
- Glycine-rich cell wall protein-like protein
- Protein NETWORKED 2D
- At1g64330
- At3g45160
Sequence:
MALMKKSLSAALLSSPLLIICLIALLADPFSVGARRLLEDPKPEIPKLPELPKFEVPKLPEFPKPELPKLPEFPKPELPKIPEIPKPELPKVPEIPKPEETKLPDIPKLELPKFPEIPKPELPKMPEIPKPELPKVPEIQKPELPKMPEIPKPELPKFPEIPKPDLPKFPENSKPEVPKLMETEKPEAPKVPEIPKPELPKLPEVPKLEAPKVPEIQKPELPKMPELPKMPEIQKPELPKLPEVPKLEAPKVPEIQKPELPKMPELPKMPEIQKPELPKMPEIQKPELPKVPEVPKPELPTVPEVPKSEAPKFPEIPKPELPKIPEVPKPELPKVPEITKPAVPEIPKPELPTMPQLPKLPEFPKVPGTP
Protein: Calpastatin (Calpain inhibitor) (F8W7E0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSQPGQKPAASPRPRRAAAARRTHEHVSEKTSESPSKPGEKKGSDEKKAASLGSSQSSRTYAGGTASATKVSASSGATSKSSSMNPTETKAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAISGKPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPAT
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (A0A060X010)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein RACK1
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
Sequence:
MGVEIETISPGDGEFFCYILAVCVIPLPGMLQNGKKFDSSRDRNKPFKFKIGRQEVIKGWEEGIAQMSVGQRAKITCTPDMAYGATGHPGVIPPNATLIFDVELLKLE