wanglab/gogpt-training-data huggingface dataset:
Protein: NEDD8-conjugating enzyme UBE2F (EC 2.3.2.34) (NEDD8 carrier protein UBE2F) (NEDD8 protein ligase UBE2F) (NEDD8-conjugating enzyme 2) (RING-type E3 NEDD8 transferase UBE2F) (Ubiquitin-conjugating enzyme E2 F) (Q9CY34)
Organism: Mus musculus (Mouse)
Function: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5.
Interaction partners:
- Ubiquitin-like protein NEDD8
- NEDD8-activating enzyme E1 catalytic subunit
- RING-box protein 2
- NEDD8-activating enzyme E1 regulatory subunit
- Cullin-5
- E3 ubiquitin-protein ligase RBX1
- DCN1-like protein 3
- Cullin-1
- DCN1-like protein 1
- DCN1-like protein 2
Sequence:
MLTLASKLKRDDGLKGSRTSASTSDSTRRVSVRDKLLVKEVAELEANLPCTCKVHFPDPNKLHCFQLTVSPDEGYYQGGKFQFETEVPDAYNMVPPKVKCLTKIWHPNITETGEICLSLLREHSIDGTGWAPTRTLKDVVWGLNSLFTDLLNFDDPLNIEAAEHHLRDKEDFRDKVDEYIKRYAR
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.26) (A0A0B4LHQ4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MAESVKSQSLSALTEGQHDDGGSTATSATLANKTSGTNTTSASNHSSQRRRNNNTNSNRNKSHHKNEKRNAPATSGPAVSSSVDVVPATSTASATSTRRSRSQGRHSSAAALSSKESQIPKRSVGAIRSPSSPAFNSIPVVSDQSLSPGSRKRQLNQHNNSNNKASSSHQSAPGGDQLVCAPLKKRRLQQSLGSGICEGAVEINLGAASFDHTPRQASGDCVAQRTRSKTISPEELPSTSSAAAARHHQIRPSASSTSFSSSHRNKRKASIGGSIAAVETTPHRGTAAARAGRSGNLLNYYRKTRKVSHTRSSQKSEKQSIPAEDTTANRNGSAGSGSSSKSGVIPKNRKSLRHSQQNLLDTEAAEVESAAAETGGEQQSEHGNLDVIDQLPTPEAGPNQSEASGIHNQSQLEADRQPVVQDEDDEEDDEEEEEEEEEEVGFYGIVNSAGSSYEEDTQIVAEEDEITTEEEVDDEDDDEIEEEDLSESEFAQQLIGELGGANSANLSIVAAALSAARDVGGGSDGGGSAGGATPATGASASSVGNTSAVGASSSSNSSAGQAASSNSNNVTATGSGSAPGGGPTSTGTTSGTQHGSGSGAAAAVDSESDDSEVGRLQALLEARGLPPHLFGALGPRVTHILHRTIGNSSSSKANQLLQGLQSHDESQQLQAAIEMCQMLVMGNEDTLAGFPIKQVVPALIQLLRMEHNFDIMNNACRALAYMLEALPRSSGTVVEAVPVFLEKLQVIQCMDVAEQSLSALEILSRRHNKAILQANGISACLTYLDFFSIVAQRAALAIAANCCLNMHPEEFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASPDLLKNCQQLLLVTPAILNTGTFTAVVRMLSLMCCSCPDLAISLLRNDIAATLLYLLTGNAEPAAASATHVELISRSPSELYELTCLIGELMPRLPLDGIFAVDSLLDRPTLNTQDQVHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVAPMSAGQDLTTTSAGSAAAGGASTSAAAAAASSNNNNNNNNNPPGNSVNLNQVKRRPSLDARIACLKEERGLAADFIKHIFNVLYEVYSSSAGPNVRYKCLRALLRMVYYATPELLRQVLKYQLVSSHIAGMLGSNDLRIVVGALQMAEILMRQLPDVFGTHFRREGVIYQFTQLTDPNNPICANPSPKPLSATATPTANAGGSQSAPASANSLQVNPFFMDSAPGLSSASTTPSSSKHQSYSVKSFSHAMNALTASAKGTPSGALDATSSSTTAGGYNYSSSAPSSSSGAPAAYFVTQQGDPRQYVHFQQPAVPAPPPQQELLPSGVQQQGQQVPQVIYQPHHQQPAHLVLASTSSGAASSSSSSSSSSSASALQHKMTDMLKRKAPPKRKSQSGGRAKSRQEDAAVAPAGSGPGGAPPSSSGSAMHELLSRATSLGSGNGGRSTPNSGGGSGSSKSRFNAGNSSNAGSSKSSFLASLNPARWGRQTHQNHHHHHQQSQQQHHGLSKDSGNSNSTGSGSGAGLAYTVSQHGAGSGAGGLNAAAVAASISKSISHANLLAAANRERARQWVREQAVDFVKRYTEQEAKRSKAASESGATQSGSSGVGLSSTGNTPLSTAGSTNVLERLSSILFKLNGSYHDCLDALLELKTILLESDISPFEVNHSGLIKAMLNYMTSETGLVERDARLRSFMHVFAGLPLEPLLQNVGQMPTIEPIAFGAFVAKLNGCVTQLEQFPVKVHDFPAGPGGRSNQSALRFFNTHQLKCNLQRHPQCNNLRQWKGGTVKIDPLAMVQAIERYLVVRGYGGIRADSDDDSEEDMDDNVAAVVLSQASFRHKLQFTIGDHVLPYNMTVYQAVKQFSPLVSEQPETDNESETLLGNASIWVQQHTIHYRPVEEEVTSGAAAGAASSSSSCSSGVQKQQSSSSSASSCVNATSSCSSSSGVASGGGSLTKKAHKSSSKFMRKKTELWHEGIAPVVISALKPFLSSSLPADVVTVQDASLDALCMLRVIHALNRHWDHLYGCVVRQNIIPQSDFIHPKIMAKANRQLQDPLVIMTGNLPQWLPQIGMACPFLFPFETRHLLFYATSFDRDRALQRLLDTTPDLNAAESSERVAPRLDRRKRAISRTEILKQAEHILQDFGHSKALLEIQYENEVGTGLGPTLEFYALVSAELQRTDLGLWNGSDSYKQNSVTIVDVVKANSAVLHIEDALEATTTDQNTPAVAGASLVSSSTTTTTTTAQQHQHPPTRSSSRSHVLRSGAGQQPVEHSSSSAGANENALNMVIAQQFSDTNSANPAAIDNPSSTTTATTVVQHNTTTNNSSIITTTTTTSYVHAVHGLFPLPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEHSIGLADLMRVAPEVQNTLVRLQDLVRQREYILSDPNIDAMEKTEKIEQLDLDGCPIADLGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSEQQHSRWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHLS
Protein: Tensin 1 (A0A2R8Y4T1)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}.
Interaction partners:
Sequence:
MTRLSWCFSCVIRWGKYLFSCLLPLRFCLRSQPEDLEAPKTHRFKVKTFKKVKPCGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPCVPPSNHELVPITTENAPKNVVDKGEGASRGGNTRKSLEDNGSTRVTPSVQPHLQPIRNMSVSRTMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPVYTSGIYNIPGDSQTSVCITIEPGLLLKGDILLKCYHKKFRSPARDVIFRVQFHTCAIHDLGVVFGKEDLDDAFKDDRFPEYGKVEFVFSYGPEKIQGMEHLENGPSVSVDYNTSDPLIRWDSYDNFSGHRDDGMEEVVGHTQGPLDGSLYAKVKKKDSLHGSTGAVNATRPTLSATPNHVEHTLSVSSDSGNSTASTKTDKTDEPVPGASSATAALSPQEKRELDRLLSGFGLEREKQGAMYHTQHLRSRPAGGSAVPSSGRHVVPAQVHVNGGALASERETDILDDELPNQDGHSAGSMGTLSSLDGVTNTSEGGYPEALSPLTNGLDKSYPMEPMVNGGGYPYESASRAGPAHAGHTAPMRPSYSAQEGLAGYQREGPHPAWPQPVTTSHYAHDPSGMFRSQSFSEAEPQLPPAPVRGGSSREAVQRGLNSWQQQQQQQQQPRPPPRQQERAHLESLVASRPSPQPLAETPIPSLPEFPRAASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSRQSHPLTQSRSGYIPSGHSLGTPEPAPRASLESVPPGRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPPASLPGLTAQPLLSPKEATSDPSRTPEEEPLNLEGLVAHRVAGVQAREKQPAEPPAPLRRRAASDGQYENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLHSYKEAFEEMEGTSPSSPPPSGVRSPPGLAKTPLSALGLKPHNPADILLHPTGEPRSYVESVARTAVAGPRAQDSEPKSFSAPATQAYGHEIPLRNGTLGGSFVSPSPLSTSSPILSADSTSVGSFPSGESSDQGPRTPTQPLLESGFRSGSLGQPSPSAQRNYQSSSPLPTVGSSYSSPDYSLQHFSSSPESQARAQFSVAGVHTVPGSPQARHRTVGTNTPPSPGFGWRAINPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSPQSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSLGRHPGAHQGNLASGLHSNAIASPGSPSLGRHLGGSGSVVPGSPCLDRHVAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGSLPNYATINGKVSSPVASGMSSPSGGSTVSFSHTLPDFSKYSMPDNSPETRAKVKFVQDTSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTIMQQNKKGDMTHELVRHFLIETGPRGVKLKGCPNEPNFGSLSALVYQHSIIPLALPCKLVIPNRDPTDESKDSSGPANSTADLLKQGAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQERKWMKTEGGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVMLNAGQKR
Protein: Protein monoglycylase TTLL8 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 8) (A4Q9F1)
Organism: Mus musculus (Mouse)
Function: Monoglycylase which modifies both tubulin and non-tubulin proteins, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of target proteins. Not involved in elongation step of the polyglycylation reaction. Preferentially monoglycylates alpha-tubulin over beta-tubulin. Together with TTLL3, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance. Together with TTLL3, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility. Monoglycylates non-tubulin proteins such as ANP32A, ANP32B, SET, NCL and NAP1.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:33414192}. Cell projection, cilium {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:33414192}.
Interaction partners:
- Leucine-rich repeat-containing protein 63
Sequence:
MSCPPTPNPPFRPPSHTRVLRTPPLPPWVCLNSKSLSTGVGGQKNQLREASMENGERKKLSSTLSDGDHKEENKLKQGIPQDLSSSPKLDRYKIARQLTEKAIKERKIFSIYGHYPVIRATLRRKGWVEKKFNFFPKALQNLGSEDKSAETKENQEIALERFDDIHDVMSRLVKNEIPYLLWTIKRDVVDYHSLTCDQMLNHYGKTASFTTKIGLCLNMRSLPWYVQANPNTFFPRCYGLCTESEKQEFLDDFRRTVAASILKWVVLHQNYCSKVKGKSKKEEAKNSDPSPKKDPENPDLKLPSLSGQVVDTACKVCQAYLGQLEHEDIDVSEASTEALSEEEWNDLTQQYYLLVHGNASITDSKSYFAQCQALLSKISSVNPQTEIDGIRNIWIIKPAAKSRGRDIVCMDRVENILSLVAADSQTTKDNKWVVQKYIETPMLIYDTKFDIRQWFLVTDWNPLTIWFYKESYLRFSTQRFSLDKLDSAIHLCNNSIQRRLKNDKERSPLLPCHNMWTSTRFQEYLQKRGRGGTWGSIIYPSMKRAVTNAMRVAQDHVEARKNSFELYGADFILGRDFKPWLIEINSSPTMHPSTPVTAQLCAQVQEDTIKVVVDRKLDRNCDIGNFELLWRQPAVELPPFNGSDLCVEGISVKKAKKQMPPIASVGLSESLLDAPPKVRSARALMETVIRPPRTTVRQDWKREEAKVLSTTWSMPVMDAEVRGRAKPIYAFEVNDYQHVDNKSHKSGYTRVQSSKVPGVTLTSAQHPALFAQTMKPTQMTSSPPPTASGNHRDSSPFCPIVFEELWLHPNSQRRPSSCILQSRAQGWIRGIP
Protein: Damage-control phosphatase At2g17340 (EC 3.1.3.-) (Sugar phosphates phosphatase At2g17340) (Q949P3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Metal-dependent phosphatase with probable damage-control functions. Shows phosphatase activity against several substrates, including sugar phosphates and p-nitrophenyl phosphate(pNPP). Prefers sugar phosphate substrates, including the extremely potent glycating agents ribose-5-phosphate and erythrose-4-phosphate.
Interaction partners:
- Pantothenate kinase 1
- Cysteine proteinase inhibitor 7
Sequence:
MESDSEMVPFPQLPMPIENNYRACTIPYRFPSDDPKKATPNEISWINVFANSIPSFKKRAESDITVPDAPARAEKFAERYAGILEDLKKDPESHGGPPDGILLCRLREQVLRELGFRDIFKKVKDEENAKAISLFPQVVSLSDAIEDDGKRLENLVRGIFAGNIFDLGSAQLAEVFSRDGMSFLASCQNLVPRPWVIDDLENFQAKWINKSWKKAVIFVDNSGADIILGILPFARELLRRGAQVVLAANELPSINDITCTELTEILSQLKDENGQLLGVDTSKLLIANSGNDLPVIDLSRVSQELAYLSSDADLVIVEGMGRGIETNLYAQFKCDSLKIGMVKHLEVAEFLGGRLYDCVFKFNEVQS
Protein: U6 snRNA-associated Sm-like protein LSm2 (Protein G7b) (snRNP core Sm-like protein Sm-x5) (O35900)
Organism: Mus musculus (Mouse)
Function: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y333}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm5
- Small nuclear ribonucleoprotein Sm D2
- U6 snRNA-associated Sm-like protein LSm8
- Small nuclear ribonucleoprotein F
- U6 snRNA-associated Sm-like protein LSm3
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm6
- U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm1
- Small nuclear ribonucleoprotein E
Sequence:
MLFYSFFKSLVGKDVVVELKNDLSICGTLHSVDQYLNIKLTDISVTDPEKYPHMLSVKNCFIRGSVVRYVQLPADEVDTQLLQDAARKEALQQKQ
Protein: Nicotinamide N-methyltransferase (A0A8I6A6E7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MESGFTSKDTYLSHFNPRDYLEKYYSFGSRHCAENEILRHLLKNLFKIFCLDGVKGELLIDIGSGPTIYQLLSACESFTEIIVTDYTDQNLWELQKWLKKEPGAFDWSPVVTYVCDLEGNRTKGPEKEEKLRRAIKQEPGQPAQARGLPGDGGRSE
Protein: E3 SUMO-protein ligase PIAS3 (EC 2.3.2.-) (E3 SUMO-protein transferase PIAS3) (Protein inhibitor of activated STAT protein 3) (O54714)
Organism: Mus musculus (Mouse)
Function: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pathway. Repressor of STAT3 signaling via inhibiting STAT3 DNA-binding and suppressing cell growth. Repressor of MITF transcriptional activity. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Sumoylates CCAR2 which promotes its interaction with SIRT1 (By similarity). Diminishes the sumoylation of ZFHX3 by preventing the colocalization of ZFHX3 with SUMO1 in the nucleus (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556}. Nucleus {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:14596924}. Nucleus speckle {ECO:0000269|PubMed:12077349}. Note=Colocalizes with MITF in the nucleus (PubMed:11709556). Colocalizes with GFI1 in nuclear dots (PubMed:11060035). Colocalizes with SUMO1 in nuclear granules (PubMed:12077349). {ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:12077349}.
Interaction partners:
- Signal transducer and activator of transcription 3
- SUMO-conjugating enzyme UBC9
- Small ubiquitin-related modifier 1
- Signal transducer and activator of transcription 1
- Signal transducer and activator of transcription
- Small ubiquitin-related modifier 2
- Small ubiquitin-related modifier 3
- Transcription factor p65
- Sentrin-specific protease 1
- Signal transducer and activator of transcription 5B
Sequence:
MAELGELKHMVMSFRVSELQVLLGFAGRNKSGRKHELLAKALHLLKSSCAPSVQMKIKELYRRRFPRKTLGPSDLSLLSLPPGTSPVGSPGPLAPIPPTLLTPGTLLGPKREVDMHPPLPQPVHPDVTMKPLPFYEVYGELIRPTTLASTSSQRFEEAHFTFALTPQQLQQILTSREVLPGAKCDYTIQVQLRFCLCETSCPQEDYFPPNLFVKVNGKLCPLPGYLPPTKNGAEPKRPSRPINITPLARLSATVPNTIVVNWSSEFGRNYSLSVYLVRQLTAGTLLQKLRAKGIRNPDHSRALIKEKLTADPDSEVATTSLRVSLMCPLGKMRLTVPCRALTCAHLQSFDAALYLQMNEKKPTWTCPVCDKKAPYESLIIDGLFMEILNSCSDCDEIQFMEDGSWCPMKPKKEASEVCPPPGYGLDGLQYSAVQEGIQPESKKRVEVIDLTIESSSDEEDLPPTKKHCPVTSAAIPALPGSKGALTSGHQPSSVLRSPAMGTLGSDFLSSLPLHEYPPAFPLGADIQGLDLFSFLQTESQHYGPSVITSLDEQDTLGHFFQYRGTPSHFLGPLAPTLGSSHRSSTPAPPPGRVSSIVAPGSSLREGHGGPLPSGPSLTGCRSDVISLD
Protein: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein (A8MRQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- GDSL esterase/lipase At5g03810
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Tubulin beta-1 chain
- Polygalacturonase ADPG2
- E3 ubiquitin-protein ligase ATL76
Sequence:
MAPKGSTKTLALFLTLISILLLGQTQAQNRPYLRPPPPRIPPPPCPVCTCPEPSPPPPPTVTPQIPPTLPPTIPPETPPTGPPATPPTEVLPTGPPTLPPQTPPTIPPEIPPNTPPQTPPTLPPNTPPETPPTTPPETPPNTPPESPPNTPPEIPPNTPPGTPPNTPPETPPTTPPETPPTTPPETSPNTPPETSPTTPPEIPPNTPPQSPPNTPPETPPNTPPGTPPNTPPETLPNTPPGTPPNTPPETPPTTPPETPPITPPETPPNTPPQSPPNTPPETPPNTPPGTPPNTPPETLPNTPPGTPPNTPPETPPTTPPETPPITPPETPPNTPPQSPPNTPPETPPNTPPGTPPNTPKTPPTTPPETPPNTPPETPPTTQPETPPNTPPQSPPNTPPETPPNTPPETLPNTPPGTPPNQSPQIPPTLPPNTPPETPPQTPPNSPPETLPTLPPNTPPEALPNTPPQSPPTLPPNTPPQIPPTLPPNTPPQTPPNTPPETPPNTPPQTPPTVPPNTPPVTPPVRPPTTPPSPPPTTTLPPSSPTSPPNNSPSPPPPKSQPPPPPPRFQPPPPPRGTCPRNANQIRTCSNVLRFFGNFLDFRLAQPCCTLIRNLSDAEAAACLCDLVRARRSTLSPNIIILCRACGRRIPRGFTCP
Protein: Receptor-like protein EIX2 (EIX receptor 2) (Q6JN46)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Involved in plant defense. Confers resistance to the fungal pathogen T.viride through recognition of the EIX elicitor protein.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Ethylene-inducing xylanase
- Receptor-like protein EIX1
Sequence:
MGKRTNPRHFLVTWSLLLLETAFGLTSREVNKTLCIEKERDALLEFKRGLNDDFGRLSTWGDEEECCNWKGIECDKRTGHVIVLDLHSEVTCPGHACFAPILTGKVSPSLLELEYLNFLDLSVNGFENSEIPRFIGSLKRLEYLNLSSSDFSGEIPAQFQNLTSLRILDLGNNNLIVKDLVWLSHLSSLEFLRLGGNDFQARNWFREITKVPSLKELDLSVCGLSKFVPSPADVANSSLISLSVLHLCCNEFSTSSEYSWLFNFSTSLTSIDLSHNQLSRQIDDRFGSLMYLEHLNLANNFGAEGGVPSSFGNLTRLHYLDMSNTQTYQWLPELFLRLSGSRKSLEVLGLNDNSLFGSIVNVTRFSSLKKLYLQKNMLNGFFMERVGQVSSLEYLDLSDNQMRGPLPDLALFPSLRELHLGSNQFQGRIPQGIGKLSQLRIFDVSSNRLEGLPESMGQLSNLERFDASYNVLKGTITESHFSNLSSLVDLDLSFNLLSLNTRFDWVPPFQLQFIRLPSCNMGPSFPKWLQTQNNYTLLDISLANISDMLPSWFSNLPPELKILNLSNNHISGRVSEFIVSKQDYMIIDLSSNNFSGHLPLVPANIQIFYLHKNHFSGSISSICRNTIGAATSIDLSRNQFSGEVPDCWMNMSNLAVLNLAYNNFSGKVPQSLGSLTNLEALYIRQNSFRGMLPSFSQCQLLQILDIGGNKLTGRIPAWIGTDLLQLRILSLRSNKFDGSIPSLICQLQFLQILDLSENGLSGKIPQCLNNFTILRQENGSGESMDFKVRYDYIPGSYLYIGDLLIQWKNQESEYKNALLYLKIIDLSSNKLVGGIPKEIAEMRGLRSLNLSRNDLNGTVVEGIGQMKLLESLDLSRNQLSGMIPQGLSNLTFLSVLDLSNNHLSGRIPSSTQLQSFDRSSYSGNAQLCGPPLEECPGYAPPIDRGSNTNPQEHDDDDEFSSLEFYVSMVLGFFVTFWGILGCLIVNRSWRNAYFTFLTDMKSWLHMTSRVCFARLKGKLRN
Protein: Ras-interacting protein 1 (E7F6P4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Rho GTPase-activating protein 29
- Krev interaction trapped protein 1
- Protein HEG
- Podocalyxin
Sequence:
MEESGSPRFRKLHFPVGLWINSPRKHFAKLGARWPSAASVKSTTSSDAASVHEAPSSVPSSLSHSTPSLAPPSPSPSPAFLRPRPANQQSRAKRLSHLFLRGRSNSDRDRAIGEREREIWAHSATPSSHHYLPPASSNAPGLVKIYGDALSSGANYRSLLANMHSTARQLIQQVITRYTERERENESEDTALQKYFPEDFLLCDVIGKPIHQADGAVKWQTECRRGVASWECPLQLVDMWRPKDGFERRFEIQRLDEYEREEKEKEKERERDGESYQGVRWRRSRMSSGGGAEEERGHRGRNSELRRSISDMNLSLRRRQGNTGNDPRRSGCAQNNGQDRKNIVSMIATEGGEVSGSRGGVSESDRRTRVAEEDKDTCDLEVMSQSLILPPTDRPYFLLLQGYDQSKDFVLYIMAGHTHVFGRKPTFREREMDREREKKGKRPLKVDTYLSAPDLLARHLLIRRDTAVPEQPHGQALARPFRGGQATLNGAPLYREAVLKPGDLLGLGSHFLFLYRDPRVTPVPPLALPPPWQGDMPTSFGPGGMTDRQEMLRLYLGSTESLLRYQAKHADALLQEIILKNTSPDSGGGALAPAYLLSLMIDYASKHLDPELTPQLLLKAANQIKGIVWDKIKEFGDKHPTQNSADAEVDLPPPSAQKLSSDLRPLMFWMSNATELLNFFQVKVEALEKEWEFEAPGDPVLSADMDTCSEALAQLDDVIMHTFQQCVYHLTKTLYSLLPALLDTNPFSSEERKKAKAGVKDKTGSGGEGDEEEDGSALPPTVAGLVEVYRCSLQLSREACLSPPLTSQTFGYLFFFTNTSLLNTLLERDNLFSWSRAVQIRTNLDLVLDWLQGAGLGDIASEFLKKLSVTVNFLCIPKTRLIQSSWSSLQEEHPLLSPSQLHHLLTHYKLGPTRAPPSSWAPPLGTELGGDIFESFLDHPPLILPNETPRLDLTQPIPSPELQKEVTRLRTFLWGLDQDELPANQRTRL
Protein: Putative actin-fragmin kinase DDB_G0279609 (Q54WK1)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNKIKVFKKNFFFEKIKNKKNNIEIKKSTNDSTSNTCTDIKNNIIIENKINEENIENNNNINIGNNSVNNNNINNNNNSINNNNNNNNKNKNKNNNSYIPMIQYSNIHCIDWSSLISVDKLDLGSSNIFLIATFLNNKCEYNQVLLKSSTTIVQEVYASVLESILKLPIPEMRLLEYSNDEYIQMSRSLLTISSKTNKSLYDYIKLELLKSFFLIMEYAPNGKSFKDLDYKEYFSGYGGEKKLNQLGQVIAFDIFCNNSDRLPLIWDNVSSHFSNILFYDIPNRNGWYISLMNSNVTCINNSSFTIGYRKYITRVKSILYALFKRPNIESNQIKKMRESISKSYKINLSSSCGISIQRGIIQGVQLIISRISISILSDTKEKLRHLVKVDSTTNAWKKGLDSIHLPFLSDLLDTMVLFY
Protein: DNA dC->dU-editing enzyme APOBEC-3C (A3C) (EC 3.5.4.38) (APOBEC1-like) (Phorbolin I) (Q9NRW3)
Organism: Homo sapiens (Human)
Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV), herpes simplex virus 1 (HHV-1) and Epstein-Barr virus (EBV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22977230}. Cytoplasm {ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22977230}.
Interaction partners:
- Cullin-5
- Putative C->U-editing enzyme APOBEC-4
- Cytidine deaminase
- Elongin-B
- Cytochrome c oxidase subunit 5A, mitochondrial
- Apolipoprotein B-100
- Elongin-C
- Cytochrome c1, heme protein, mitochondrial
- RING-box protein 2
- Cytochrome c oxidase subunit 7C, mitochondrial
Sequence:
MNPQIRNPMKAMYPGTFYFQFKNLWEANDRNETWLCFTVEGIKRRSVVSWKTGVFRNQVDSETHCHAERCFLSWFCDDILSPNTKYQVTWYTSWSPCPDCAGEVAEFLARHSNVNLTIFTARLYYFQYPCYQEGLRSLSQEGVAVEIMDYEDFKYCWENFVYNDNEPFKPWKGLKTNFRLLKRRLRESLQ
Protein: DNA repair and recombination protein RadA (O73948)
Organism: Methanococcus voltae
Function: Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity).
Interaction partners:
Sequence:
MSDNLTDLPGVGPSTAEKLVEAGYIDFMKIATATVGELTDIEGISEKAAAKMIMGARDLCDLGFKSGIDLLKQRSTVWKLSTSSSELDSVLGGGLESQSVTEFAGVFGSGKTQIMHQSCVNLQNPEFLFYDEEAVSKGEVAQPKAVYIDTEGTFRPERIMQMAEHAGIDGQTVLDNTFVARAYNSDMQMLFAEKIEDLIQEGNNIKLVVIDSLTSTFRNEYTGRGKLAERQQKLGRHMATLNKLADLFNCVVLVTNQVSAKPDAFFGMAEQAIGGHIVGHAATFRFFVRKGKGDKRVAKLYDSPHLPDAEAIFRITEKGIQD
Protein: ATP-dependent zinc metalloprotease FTSH 9, chloroplastic (AtFTSH9) (EC 3.4.24.-) (Q9FIM2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable ATP-dependent zinc metallopeptidase.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:14630971}; Multi-pass membrane protein {ECO:0000269|PubMed:14630971}; Stromal side {ECO:0000269|PubMed:14630971}.
Interaction partners:
- Non-canonical heme oxygenase HOZ, chloroplastic
Sequence:
MTSIELLSPLIHDKFRFSTCCSTSSLLYLHASSFFRDRSFGFRQNPNRFVSNSSIQLPQSVPGSINQERFNLWQGFSRKKSTSSSRTIVNCQEGDQKASSSEGEGKTNKDKGRKQGKNELWWSKGKKWQWKPIIQAQEIGVMLLQLGIVMFVVRLLRPGIPLPGSEPRTQTTFMSVPYSDFLSKVNNDEVQKVEVDGFHVLFKLKDDGNLQESETSSSSIKLSESSETMLRSVAPTKRVVYSTTRPRDIKTPYEKMLENNVEFGSPDKRSGGFFNSGLIVLFYIAVLAGLLHRFPVNFSQSTTGQLRTRKSGGPGGGKVSGDGETITFADVAGVDEAKEELEEIVEFLKNPDRYVRLGARPPRGVLLVGLPGTGKTLLAKAVAGESDVPFISCSASEFVELYVGMGASRVRDLFARAKKEAPSIIFIDEIDAVAKSRDGKFRMVSNDEREQTLNQLLTEMDGFDSSSAVIVLGATNRADVLDPALRRPGRFDRVVTVESPDKVGRESILKVHVSKKELPLGDDVNLASIASMTTGFTGADLANLVNEAALLAGRKSKMTVDKIDFIHAVERSIAGIEKKTARLKGSEKAVVARHEAGHAVVGTAVASLLSGQSRVEKLSILPRSGGALGFTYIPPTHEDRYLLFIDELHGRLVTLLGGRAAEEVVYSGRISTGALDDIRRATDMAYKAVAEYGLNEKIGPVSVATLSAGGIDDSGGSPWGRDQGHLVDLVQREVTNLLQSALDVALTVVRANPDVLEGLGAQLEDEEKVEGEELQKWLNRVVPSEELAVFIKGKQTALLPAQASSS
Protein: RNA-binding protein, putative (Q57WI8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cleavage stimulation factor 50 kDa subunit
- C3H1-type domain-containing protein
- Cleavage and polyadenylation specificity factor subunit, putative
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor-like protein, putative
- Suppressor of forked domain-containing protein
- Uncharacterized protein
- RNA-binding protein RBP14, putative
- Cleavage and polyadenylation specificity factor subunit 5
Sequence:
METHQDPRNLIVNYIPTPVTEEDLEELFRPFGPLVSVRIICDRENGNHPKGYGFVRYKFVESAMNAMSRMNGYSINNKRLRVTQATGPRKYSQAAGSTSVRQPGPRAPPGSAPPKVSGPCFGDGAVEQISLTTSSLVPCPIVHPFDSRNSVLTAMARPQETTVHHPATFALVDRGRMHMIQAAPGIMAAPVGNQQFVQTVPASWAPALSTIQPPVVLSEGDTGGIVTGNIKTCGSSSPMELSVLSMTTQPVPAMTIPRVQQSNSATQPEQYHPSSKTMEPLCFQSYMPLNPVRDGILQGSVSSFFTPLGASDPTTGSLCGAALSSPTTRMIGTTNFMSPN
Protein: Pro-epidermal growth factor (EGF) [Cleaved into: Epidermal growth factor] (P07522)
Organism: Rattus norvegicus (Rat)
Function: EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Receptor protein-tyrosine kinase
- Protransforming growth factor alpha
- Receptor tyrosine-protein kinase erbB-4
- Receptor tyrosine-protein kinase erbB-2
- Receptor tyrosine-protein kinase erbB-3
- Insulin-2
- Insulin-like growth factor 1 receptor
- Insulin-1
- Insulin-like growth factor 1
- Amphiregulin
Sequence:
MLFSLTFLSVFLKITVLSVTAQQTRNCQSGPLERSGTTTYAAAGPPRFLIFLQGNSIFRINTDGTNHQQLVVDAGVSVVMDFHYKEERLYWVDLERQLLQRVFFNGSGQETVCKVDKNVSGLAINWIDGEILRTDRWKGVITVTDMNGNNSRVLLSSLKRPANILVDPTERLIFWSSVVTGNLHRADLGGMDVKTLLEAPERISVLILDILDKRLFWAQDGREGSHGYIHSCDYNGGSIHHIRHQARHDLLTMAIFGDKILYSALKEKAIWIADKHTGKNVVRVNLDPASVPPRELRVVHLHAQPGTENRAQASDSERCKQRRGQCLYSLSERDPNSDSSACAEGYTLSRDRKYCEDVNECALQNHGCTLGCENIPGSYYCTCPTGFVLLPDGKRCHELVACPGNRSECSHDCILTSDGPLCICPAGSVLGKDGKTCTGCSFSDNGGCSQICLPLSLASWECDCFPGYDLQLDRKSCAASMGPQPFLLFANSQDIRHMHFDGTDYKTLLSRQMGMVFALDYDPVESKIYFAQTALKWIERANLDGSQRERRITEGVDTPEGLAVDWIGRRIYWTDSGKSVIEGSDLSGKHHQIIIKESISRPRGIAVHPKARRLFWTDTGMSPRIESSSLQGSDRTLIASSNLLEPSGIAIDYLTDTLYWCDTKLSVIEMADLDGSKRRRLTQNDVGHPFSLAVFEDHVWFSDWAIPSVIRVNKRTGQNRVRLRGSMLKPSSLVVVHPLAKPGADPCLHRNGGCEHICQESLGTAQCLCREGFVKAPDGKMCLTRKDDQILAGDNADLSKEVASLDNSPKAYVPDDDRTESSTLVAEIMVSGLNYEDDCGPGGCGSHAHCISEGEAAVCQCLKGFAGDGNLCSDIDECELGSSDCPPTSSRCINTEGGYVCQCSEGYEGDGIYCLDVDECQQGSHGCSENATCTNTEGGYNCTCAGCPSAPGLPCPDSTSPSLLGKDGCHWVRNSNTGCPPSYDGYCLNGGVCMYVESVDRYVCNCVIGYIGERCQHRDLRWWKLRHADYGQRHDITVVSVCVVALALLLLLGMWGTYYYRTRKQLSESSKKPSEESSSNVSSNGPDSSGAGVSSGPQPWFVVLEEHQQPKNGRLPAAGTNGAVVEAGLSSSL