wanglab/gogpt-training-data huggingface dataset:
Protein: COMM domain-containing protein 8 (Q9NX08)
Organism: Homo sapiens (Human)
Function: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21778237}. Nucleus {ECO:0000269|PubMed:21778237}.
Interaction partners:
- Coiled-coil domain-containing protein 22
- COMM domain-containing protein 2
- COMM domain-containing protein 10
- COMM domain-containing protein 4
- COMM domain-containing protein 5
- COMM domain-containing protein 1
- COMM domain-containing protein 9
- COMM domain-containing protein 6
- COMM domain-containing protein 3
- COMM domain-containing protein 7
Sequence:
MEPEEGTPLWRLQKLPAELGPQLLHKIIDGICGRAYPVYQDYHTVWESEEWMHVLEDIAKFFKAIVGKNLPDEEIFQQLNQLNSLHQETIMKCVKSRKDEIKQALSREIVAISSAQLQDFDWQVKLALSSDKIAALRMPLLSLHLDVKENGEVKPYSIEMSREELQNLIQSLEAANKVVLQLK
Protein: Zinc finger HIT domain-containing protein 2 (Protein FON) (Q9UHR6)
Organism: Homo sapiens (Human)
Function: May act as a bridging factor mediating the interaction between the R2TP/Prefoldin-like (R2TP/PFDL) complex and U5 small nuclear ribonucleoprotein (U5 snRNP). Required for the interaction of R2TP complex subunit RPAP3 and prefoldin-like subunit URI1 with U5 snRNP proteins EFTUD2 and PRPF8. May play a role in regulating the composition of the U5 snRNP complex.
Interaction partners:
- Protein AAR2 homolog
- Delta
- U5 small nuclear ribonucleoprotein TSSC4
- 116 kDa U5 small nuclear ribonucleoprotein component
- Protein ecdysoneless homolog
- Cytoskeleton-associated protein 5
- RuvB-like 2
- RuvB-like 1
- U5 small nuclear ribonucleoprotein 40 kDa protein
- Pre-mRNA-processing-splicing factor 8
Sequence:
MEPAGPCGFCPAGEVQPARYTCPRCNAPYCSLRCYRTHGTCAENFYRDQVLGELRGCSAPPSRLASALRRLRQQRETEDEPGEAGLSSGPAPGGLSGLWERLAPGEKAAFERLLSRGEAGRLLPPWRPWWWNRGAGPQLLEELDNAPGSDAAELELAPARTPPDSVKDASAAEPAAAERVLGDVPGACTPVVPTRIPAIVSLSRGPVSPLVRFQLPNVLFAYAHTLALYHGGDDALLSDFCATLLGVSGALGAQQVFASAEEALQAAAHVLEAGEHPPGPLGTRGAMHEVARILLGEGPTNQKGYTLAALGDLAQTLGRARKQAVAREERDHLYRARKKCQFLLAWTNENEAALTPLALDCARAHQAHAVVAEEVAALTGELERLWGGPVPPAPRTLIEELPS
Protein: Protein Rv1269c (P9WM45)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Putative thiosulfate sulfurtransferase SseA
Sequence:
MTTMITLRRRFAVAVAGVATAAATTVTLAPAPANAADVYGAIAYSGNGSWGRSWDYPTRAAAEATAVKSCGYSDCKVLTSFTACGAVAANDRAYQGGVGPTLAAAMKDALTKLGGGYIDTWACN
Protein: Cruciform cutting endonuclease 1, mitochondrial (EC 3.1.21.10) (Protein ydc2) (Q10423)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Capable of resolving Holliday junctions. Specific for 4-way junctions. Seems to be important for the maintenance of mitochondrial DNA. Cleaves fixed junctions at the point of strand exchange. Cleaves after 5'-CT-3' and 5'-TT-3' sequences.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10954073}.
Interaction partners:
- Flap endonuclease 1
Sequence:
MATVKLSFLQHICKLTGLSRSGRKDELLRRIVDSPIYPTSRVLGIDLGIKNFSYCFASQNEDSKVIIHNWSVENLTEKNGLDIQWTEDFQPSSMADLSIQLFNTLHEKFNPHVILMERQRYRSGIATIPEWTLRVNMLESMLYALHYAEKRNSIEQKIQYPFLLSLSPKSTYSYWASVLNTKASFSKKKSRVQMVKELIDGQKILFENEEALYKWNNGSRVEFKKDDMADSALIASGWMRWQAQLKHYRNFCKQFLKQ
Protein: Nuclear import protein MOG1 (Multicopy suppressor of GSP1) (P47123)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the Ran-GTPase system for nuclear protein import and poly(A)+ mRNA export.
Subcellular location: Nucleus {ECO:0000269|PubMed:11509570, ECO:0000269|PubMed:9860978}.
Interaction partners:
- GTP-binding nuclear protein GSP1/CNR1
- GTP-binding nuclear protein GSP2/CNR2
- Nuclear transport factor 2
- Nucleoporin NUP2
- Ran-specific GTPase-activating protein 1
Sequence:
MKIEKASHISQPVQLSTCTLIDTYPGHQGSMNNKEVELYGGAITTVVPPGFIDASTLREVPDTQEVYVNSRRDEEEFEDGLATNESIIVDLLETVDKSDLKEAWQFHVEDLTELNGTTKWEALQEDTVQQGTKFTGLVMEVANKWGKPDLAQTVVIGVALIRLTQFDTDVVISINVPLTKEEASQASNKELPARCHAVYQLLQEMVRKFHVVDTSLFA
Protein: Aspartic proteinase 39 (EC 3.4.23.-) (Q9S9K4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Displays aspartic proteolytic activity. Together with A36, contributes to pollen and ovule development, including the apical cell wall constitution of the growing pollen tubes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27872247}; Lipid-anchor, GPI-anchor {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:27872247}. Note=Displays punctate cytosolic localization and colocalizes with the GPI-anchored protein COBL10 at the plasma membrane and in the cytosol (PubMed:27872247). In pollen grains, mainly present at the plasma membrane and in reticular structures in the cytosol (PubMed:27872247). In pollen tubes, exhibits a punctate localization in the cytosol and occurs weakly at the plasma membrane (PubMed:27872247). {ECO:0000269|PubMed:27872247}.
Interaction partners:
- UDP-galactose/UDP-glucose transporter 5B
- D111/G-patch domain-containing protein
- Remorin family protein
- Protein trichome birefringence-like 6
- Probable protein phosphatase 2C 33
- Remorin family protein
- Receptor-like protein 11
- Polyadenylate-binding protein RBP45C
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Protein FATTY ACID EXPORT 5
Sequence:
MELRRKLCIVVAVFVIVIEFASANFVFKAQHKFAGKKKNLEHFKSHDTRRHSRMLASIDLPLGGDSRVDSVGLYFTKIKLGSPPKEYHVQVDTGSDILWINCKPCPKCPTKTNLNFRLSLFDMNASSTSKKVGCDDDFCSFISQSDSCQPALGCSYHIVYADESTSDGKFIRDMLTLEQVTGDLKTGPLGQEVVFGCGSDQSGQLGNGDSAVDGVMGFGQSNTSVLSQLAATGDAKRVFSHCLDNVKGGGIFAVGVVDSPKVKTTPMVPNQMHYNVMLMGMDVDGTSLDLPRSIVRNGGTIVDSGTTLAYFPKVLYDSLIETILARQPVKLHIVEETFQCFSFSTNVDEAFPPVSFEFEDSVKLTVYPHDYLFTLEEELYCFGWQAGGLTTDERSEVILLGDLVLSNKLVVYDLDNEVIGWADHNCSSSIKIKDGSGGVYSVGADNLSSAPRLLMITKLLTILSPLIVMAFTSLA
Protein: G-protein coupled receptor 22 (D4A3U0)
Organism: Rattus norvegicus (Rat)
Function: Orphan G-protein coupled receptor. Seems to act through a G(i)/G(o) mediated pathway (By similarity). May be involved in ciliogenesis (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:18539757}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- tRNA-dihydrouridine synthase
Sequence:
MCFSPVLEINMQSESNVTVRDDIEDIDTNMYQPLSYPLSFQVSLTGFLMLEIVLGLGSNLTVLVLYCMKSNLISSVSNIITMNLHVLDVIICVGCIPLTIVILLLSLERNTALICCFHEACVSFASVSTAINVFAITLDRYDISVKPANRILTMGRAVMLMTSIWIFSFFSFLIPFIEVNFFSLQSGNAWENKTLLCVSTSEYYTELGMYYHLLVQIPIFFFTVIVMLITYTKILQALNIRIGTRFSTGQKKKARKKKTISLTTHETTDMSQSSGGRNVVFGVRTSVSVIIALRRAVKRHRERRERQKRVFKMSLLIISTFLLCWTPISVLNTTILCLGPSDLLVKLRLCFLVMAYGTTIFHPLLYAFTRQKFQKVLKSKMKKRVVSIVEADPMPNNAVIHNSWIDPKRNKKVTYEDSEIREKCLVPQVVTD
Protein: Cytochrome P450, family 3, subfamily c, polypeptide 1 (Q7ZTW6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MFDLSSLSVTWTLVVLVITLLLIYGVWPHGFFKKLGIPGPRPLPFVGTALSYSKGICNFDIECSKKYGKVWGIYDGRLPLLLVTDLEMIKTILVKDCYSTFTNRRNMNPDLVGPFADGITLVKDERWRRIRSSLSPYFTSGRLKEIFPIAMTHADRFIKNMEKKDPNLPLKIKDVVAPYSLDVVASSSFSVDFDSINNPDDPFVTSIKSFFNINPLSPLFLLLAFCPSAANLLAKMGISVFSRSTTDFYYKALRKIKDEHNESNGRVDFLKLMIQNQIPDDQVKDTASEQPVKGLTDHEILSQSFIFILGGYETTSTTLSYLLYNLATNPDCLEKLVEEIDKNFPLDIPITYDALMRMDYLEMAIHESMRVFPAGPRLERVCKKTVEINGITIPKNTLVGIPLYVLSRDPDLWESPNEFKPERFSPESKTEINQCAFMPFGLGPRNCIGMRFALMMMKLLVVKLLQKYTVETCKETQIPVQLNFFFQPKVPITLKLIPRSHKEKQ
Protein: Histidine ammonia-lyase (Histidase) (EC 4.3.1.3) (Q20502)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable urocanate hydratase
- Probable imidazolonepropionase
- Arginase
- Amidohydrolase-related domain-containing protein
- Cation diffusion facilitator family protein 1
- FIP
- Zinc transporter 2
- SUppressor of activated let-60 Ras
- Protein MAK10 homolog
- Glycine cleavage system P protein
Sequence:
MRLQVQIGTECVVVPCKPDDTIHAVAKKSVEKLRRLRPKLPLADDYFEVRRTVGNSLLDPEDLVSDVLKDSDFIIVAASVEETEDAKEAKKQEEIDNARAEIEKIDNRRRKVSFADSLAPMVLAPPTKLLILDGNSLLPEDLVRCEKGECAIQLSMESEDRIRKARTFLEKIASEHRAVYGVTTGFGTFSNVTIPPEKLKKLQLNLIRSHATGYGEPLAPNRARMLLALRINILAKGHSGISVENIKKMIAAFNAFCVSYVPQQGTVGCSGDLCPLAHLALGLLGEGKMWSPTTGWQPADVVLKKNNLEPLELGPKEGLALINGTQMVTALGAYTLERAHNIARQADVIAALSLDVLKGTTRAYDPDIHRIRPHRGQNLSALRLRALLHSEANPSQIAESHRNCTKVQDAYTLRCVPQVHGVVHDTIEFVREIITTEMNSATDNPLVFADREEIISGGNFHGEYPAKALDFLAIAVAELAQMSERRLERLVNKELSGLPTFLTPDGGLNSGFMTVQLCAASLVSENKVLCHPSSVDSIPTSCNQEDHVSMGGFAARKALTVVEHVEAVLAMELLAACQGIEFLKPLISTAPLHKIYQLVRSVAPPLNEDRYMKPEIDAVLEMIRENRIWEAVLPHLETLEAMEELDPDALRQFTKTPTGIVQDRSMIPISDDEESIE
Protein: Glutathione S-transferase U28 (AtGSTU28) (EC 2.5.1.18) (GST class-tau member 28) (Q9C8M3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19174456}.
Interaction partners:
- Glutathione S-transferase DHAR2
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase L2, chloroplastic
- Glutathione S-transferase DHAR3, chloroplastic
- Glutathione S-transferase Z1
- Glutathione S-transferase F10
- Glutathione S-transferase F5
- Glutathione S-transferase F8, chloroplastic
- Glutathione S-transferase T2
- Glutathione S-transferase TCHQD
Sequence:
MGKENSKVVVLDFWASPYAMRTKVALREKGVEFEVQEEDLWNKSELLLKSNPVHKKVPVLIHNNTPISESLIQVQYIDETWTDAASFLPSDPQSRATARFWADYADKTISFEGGRKIWGNKKGEEQEKGKKEFLESLKVLEAELGDKSYFGGETFGYVDITLVPFYSWFYALEKCGDFSVEAECPKIVAWGKRCVERNSVAATLPESEKVYQQVLKLRQIFGVE
Protein: Probable histone-binding protein lin-53 (Abnormal cell lineage protein 53) (Synthetic multivulva protein p48) (P90916)
Organism: Caenorhabditis elegans
Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA (By similarity). Required for hcp-3 and his-1 stabilization, localization of hcp-3 to centromeres and for proper chromosome segregation. Synthetic multivulva class B (synMuvB) protein. SynMuvB proteins are required to repress the induction of vulval development by Ras signaling and probably act by forming the multiprotein DRM complex that represses transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:9875852}. Chromosome, centromere {ECO:0000269|PubMed:26904949}. Note=Localizes to centromeres during metaphase. Requires hcp-3 and knl-2 for nuclear and centromere localization. {ECO:0000269|PubMed:26904949}.
Interaction partners:
- Histone acetyltransferase type B catalytic subunit
- DIOX_N domain-containing protein
- Protein lin-9
- Protein let-418
- Protein lin-54
- Protein lin-52
- Polycomb protein mes-6
- Histone-lysine N-methyltransferase mes-2
- Uncharacterized protein
- Retinoblastoma-like protein homolog lin-35
Sequence:
MATLEDGTSEDRVANDEYKIWKKNTPFLYDLVMTHALEWPSLSVQWLPDVAKDNSDHTIHRLILGTHTSDEQNHLLISKICMPTDDAQFDASRYDTERSEYGGFGAVNGKVEPDIRINHEGEVNRARYMPQKSNIIATKSPHADVYIFDYLKHSAVPRDNTFNPLIRLKGHTKEGYGLSWNPNKEGLILSASDDQTVCHWDINANQNVAGELQAKDVFKGHESVVEDVAWHVLHDGVFGSVGDDKKLLIWDVRTSTPGHCIDAHSAEVNCLAFNPYSEFILATGSADKTVALWDLRNLRMKLHSFESHRDEIFQVQWSPHNETILASSGTDKRLHVWDLSKIGEDQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVVCSVSEDNILQVWQMADNIYNEVDEETPADVVERQQ
Protein: Tryptophan synthase beta chain 1, chloroplastic (EC 4.2.1.20) (P14671)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Tryptophan synthase alpha chain, chloroplastic
- Tryptophan synthase alpha chain
- Indole-3-glycerol phosphate synthase, chloroplastic
- indole-3-glycerol-phosphate synthase
- Anthranilate phosphoribosyltransferase, chloroplastic
- N-
- Anthranilate synthase beta subunit 1, chloroplastic
- Tryptophan N-monooxygenase 1
- N-
- Threonine dehydratase biosynthetic, chloroplastic
Sequence:
MAASGTSATFRASVSSAPSSSSQLTHLKSPFKAVKYTPLPSSRSKSSSFSVSCTIAKDPPVLMAAGSDPALWQRPDSFGRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRRENGEGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGAEVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGGSNAMGLFHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFFKDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTVAKYLDV
Protein: ATP-dependent DNA helicase PriA (EC 5.6.2.4) (DNA 3'-5' helicase PriA) (DNA replication initiation factor PriA) (Primosomal protein n') (Replication factor Y) (Replication restart primosome protein PriA) (P17888)
Organism: Escherichia coli (strain K12)
Function: Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA. Is also involved in initiation of normal DNA replication in various plasmids and phages. Binds to branched DNA structures that resemble D-loops or to the primosome assembly site (PAS). Binds to DNA in two distinct modes, either dependent on or independent of the 3' terminus recognition.
Interaction partners:
- Single-stranded DNA-binding protein
- Replicative DNA helicase DnaB
- Replication restart protein DnaT
- Replicative helicase loader DnaC
- DNA primase
- Replication restart protein PriB
- Methionyl-tRNA formyltransferase
- Disulfide bond formation protein B
- Beta sliding clamp
- Thiol:disulfide interchange protein DsbA
Sequence:
MPVAHVALPVPLPRTFDYLLPEGMTVKAGCRVRVPFGKQQERIGIVVSVSDASELPLNELKAVVEVLDSEPVFTHSVWRLLLWAADYYHHPIGDVLFHALPILLRQGRPAANAPMWYWFATEQGQAVDLNSLKRSPKQQQALAALRQGKIWRDQVATLEFNDAALQALRKKGLCDLASETPEFSDWRTNYAVSGERLRLNTEQATAVGAIHSAADTFSAWLLAGVTGSGKTEVYLSVLENVLAQGKQALVMVPEIGLTPQTIARFRERFNAPVEVLHSGLNDSERLSAWLKAKNGEAAIVIGTRSALFTPFKNLGVIVIDEEHDSSYKQQEGWRYHARDLAVYRAHSEQIPIILGSATPALETLCNVQQKKYRLLRLTRRAGNARPAIQHVLDLKGQKVQAGLAPALITRMRQHLQADNQVILFLNRRGFAPALLCHDCGWIAECPRCDHYYTLHQAQHHLRCHHCDSQRPVPRQCPSCGSTHLVPVGLGTEQLEQTLAPLFPGVPISRIDRDTTSRKGALEQQLAEVHRGGARILIGTQMLAKGHHFPDVTLVALLDVDGALFSADFRSAERFAQLYTQVAGRAGRAGKQGEVVLQTHHPEHPLLQTLLYKGYDAFAEQALAERRMMQLPPWTSHVIVRAEDHNNQHAPLFLQQLRNLILSSPLADEKLWVLGPVPALAPKRGGRWRWQILLQHPSRVRLQHIINGTLALINTIPDSRKVKWVLDVDPIEG
Protein: Mitochondrial import receptor subunit TOM40 homolog (Mitochondrial outer membrane protein of 35 kDa) (MOM35) (Protein Haymaker) (Translocase of outer membrane 40 kDa subunit homolog) (Q9QYA2)
Organism: Mus musculus (Mouse)
Function: Channel-forming protein essential for import of protein precursors into mitochondria. Plays a role in the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) by forming a complex with BCAP31 and mediating the translocation of Complex I components from the cytosol to the mitochondria.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:O96008}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with the mitochondria-associated ER membrane via interaction with BCAP31. {ECO:0000250|UniProtKB:O96008}.
Interaction partners:
- Mitochondrial import receptor subunit TOM20 homolog
- Mitochondrial import receptor subunit TOM6 homolog
- Mitochondrial import receptor subunit TOM5 homolog
- Mitochondrial import receptor subunit TOM22 homolog
- Mitochondrial import receptor subunit TOM70
- Mitochondrial import receptor subunit TOM7 homolog
- Sorting and assembly machinery component 50 homolog
- Metaxin-1
- Mitochondrial import inner membrane translocase subunit TIM50
- Superoxide dismutase
Sequence:
MGNVLAASSPPAGPPPPPTPSLVGLPPPPPSPPGFTLPPLGGGLGTGSSTGRGSERTPGAAASGAAAASEDGSCGCLPNPGTFEECHRKCKELFPVQMEGVKLTVNKGLSNRFQVTHTVALGTIGESNYHFGVTYVGTKQLSPTEAFPVLVGDMDNSGSLNAQVIHQLSPGLRSKMAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVGSGILVAHYLQSITPCLALGGELVYHRRPGEEGTVMSLAGKYTLNNWLATVTLGQAGMHATYYHKASDQLQVGVEFEASTRMQDTSASFGYQLDLPKANFLFKGSVNSNWIVGATLEKKLPPLPLTLSLCAFLNHRKNKFLCGFGLTIG
Protein: Ubiquitin-like modifier-activating enzyme 7 (Ubiquitin-activating enzyme 7) (EC 6.2.1.-) (D8) (Ubiquitin-activating enzyme E1 homolog) (P41226)
Organism: Homo sapiens (Human)
Function: Activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Catalyzes the ISGylation of influenza A virus NS1 protein.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29743376}. Nucleus {ECO:0000269|PubMed:29743376}.
Interaction partners:
- Ubiquitin-like protein ISG15
- Ubiquitin/ISG15-conjugating enzyme E2 L6
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- E3 ISG15--protein ligase HERC5
- Polyubiquitin-C
- Polyubiquitin-B
- Ubiquitin-conjugating enzyme E2 N
- Ubiquitin-conjugating enzyme E2 E2
- Ubiquitin-conjugating enzyme E2 B
Sequence:
MDALDASKLLDEELYSRQLYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLTLHDPHPTCWSDLAAQFLLSEQDLERSRAEASQELLAQLNRAVQVVVHTGDITEDLLLDFQVVVLTAAKLEEQLKVGTLCHKHGVCFLAADTRGLVGQLFCDFGEDFTVQDPTEAEPLTAAIQHISQGSPGILTLRKGANTHYFRDGDLVTFSGIEGMVELNDCDPRSIHVREDGSLEIGDTTTFSRYLRGGAITEVKRPKTVRHKSLDTALLQPHVVAQSSQEVHHAHCLHQAFCALHKFQHLHGRPPQPWDPVDAETVVGLARDLEPLKRTEEEPLEEPLDEALVRTVALSSAGVLSPMVAMLGAVAAQEVLKAISRKFMPLDQWLYFDALDCLPEDGELLPSPEDCALRGSRYDGQIAVFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAGNSGGLTVVDMDHIERSNLSRQFLFRSQDVGRPKAEVAAAAARGLNPDLQVIPLTYPLDPTTEHIYGDNFFSRVDGVAAALDSFQARRYVAARCTHYLKPLLEAGTSGTWGSATVFMPHVTEAYRAPASAAASEDAPYPVCTVRYFPSTAEHTLQWARHEFEELFRLSAETINHHQQAHTSLADMDEPQTLTLLKPVLGVLRVRPQNWQDCVAWALGHWKLCFHYGIKQLLRHFPPNKVLEDGTPFWSGPKQCPQPLEFDTNQDTHLLYVLAAANLYAQMHGLPGSQDWTALRELLKLLPQPDPQQMAPIFASNLELASASAEFGPEQQKELNKALEVWSVGPPLKPLMFEKDDDSNFHVDFVVAAASLRCQNYGIPPVNRAQSKRIVGQIIPAIATTTAAVAGLLGLELYKVVSGPRPRSAFRHSYLHLAENYLIRYMPFAPAIQTFHHLKWTSWDRLKVPAGQPERTLESLLAHLQEQHGLRVRILLHGSALLYAAGWSPEKQAQHLPLRVTELVQQLTGQAPAPGQRVLVLELSCEGDDEDTAFPPLHYEL
Protein: Homeodomain-like superfamily protein (A0A178VFA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVHSYSLELFPIRHPRPRPRFYSPYTRTLASPPSHPSHSIPRRKNCFEFLEEVFKLESVSEQISRIDERIQELEVKQMKRDAVIANVSRMITELQMRTMEERRNIDEDERITTEARSHLFLIRHPRPGYFKKRSWKDCNEFEQEISKIESFPEIISRIDEYVAQLKEEVAYLKIAKAIVEERARIRSIKRAEARKLQAMTNLDEFLEELSSIESHSQKIVKIDEHLKKLDEETKEDEDEDAAKIIQDRSTAREAEIALLMDLRQNFLPPPSMSSSSLQPPSSSTLAPSSSSSLQPPAPLIDFFRSSVSYSHQPPSSSTLATSSSPSLQPPSMSSSSLQPPASLREFFTSSVSYSHQPSSSSTLATSSFFPSSMPYSVRPPDSSDRPSLREFFPSSPSSSIQPPESSSSKRARLSNIFPSPLSSSPSPFVNPFLRPQAQEPTIPNFINPIPQISPGLPALFPNPNPNPNPNPIPNPIRNPDLVWTNRLQLVFDDAVVRLGGLFSATPKAINELISEEGLTGDQIRSHLQVLRDRQKAIADKLALE
Protein: Heavy metal transport/detoxification superfamily protein (A0A178W6S0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAEKVVMMKLKVDLNCSKCYKKVKKAIRKFPQITDELFDEKSNTIIIKVVCYDPERLMNKLCYKGDGSIKSIVILEPPKPPQPQPQPPQKPTAPAPAPAQAQAPALVRPAPVPVLVSSSAPQPMPMWQPYHCGPYYEAQQYQCYGRPVYESWGGGRQCCHEDMNSQGCSIM
Protein: Membrane-spanning 4-domains subfamily A member 13 (Testis-expressed transmembrane protein 4) (Q5J8X5)
Organism: Homo sapiens (Human)
Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MIGIFHIFMWYFLLVLYMGQIKGAFGTYEPVTYKTGCTLWGIFFIIAGVFLIRVTKYPTRSGIISTLIINIICIITTITAVTLTIIELSHFNSVSYRNYGQAKLGREVSRILLFFYGLEFSIALTHSIYSCSNLFRRQNDLTSVTEEAESTP
Protein: Uncharacterized protein YEL025C (P39991)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein FMP27, mitochondrial
Sequence:
MARQDETDCKKLDSNSAFLPLCITSYRSKDEAEKLVSCLHHEGSYFLCFSYGLYTGTSNELKAKVEFALDGPFVVNYATVPMFMSASFCHLLMFNDGSIKGFKCENNKFEIIYDSNVAPKLDTISLLTSSWLNASFEGVLYTCNKNISYDSDLHTLCTTIYSFDFREGIVERFYATDGEEIISFDFISREDLLDDATCTGKSHVYFLCLLKSCYSENLFLKEYNLAGKHGSRKFDLNEYRQYNLLPICDNEFCYMKVVCGHTIVVLTTNYTQIINIKASGLTNGAFFNNKGLPNVENYQFLKDSYDVIYERSVILLTISDVYANKYTAKIHTRSLHRDHVLKELQWTKERVFKPPKHDLCDVILQLPREKYIAVTRINGVNFISKDHRGSKLEKVKSGPAYTNKVYLASQVIGNKGTDIDSLLLGGSFNSRRGFLEKKILVYDKTLFKLVTSSKALVENVTDFWVTDLALNGGDEFAYESGGLIYKNGIFLMDEPYDYGLFVSRTGKVLKAGMDGSTGEFRQVDFLQSNHNSSTMFCYPVQNSKLRISILEAKSGFLRKKEEFFIHGLNSKESIVSCFSDGAEKYLFVIYLDGVFSVWNANQKKVATSHPDYSFIAYDQLIKISWLSKKHKHDSIYVIASSYTGCVRVYKSESNFLRVDLEIHSLYDQKLELLDTIPSLPLVFLYNDKEIILLNLQNMSYGCIQLGLVPRRMRIRPGKALFSLCVLDYDSRISIFEFGSTFYREGFTKQMTSLKPQLENHIFYLPSIPVELYTVPNNLNQAVVCLVDSNSRQYKLMLFNYASMKAVSTFSFSDEKYLHAVVKPLWPEQNSIYLSQRPFYGNKFVVCLGVGEKRTKFWLFEIRNNNITQLYANYLEDCIFSVFIYYECNLVLFSGDSGIAAYKINMLKEGAEILEAYSFPALSSINHIGLPAYMSGDYLVQFEILRDFLRTRFPIRTSIVYPSEYPECPYLGFKRLGSITQVATKIIPKKLREPKNDCLASDKNYLLGRLSDLSCATLKYSNRSYVATIGIDNTLTIYEDSKLSVDKGGLAMPYLKIRLPNKIISLAAIPDGFQNLQICPNFNSQRLEGVIPLFLLCGTEGQIYIISEFIGELWMRTLHDYKKIKLECKRAFRRSEKSMRNVTKQYSVSKETGINESGFDELARNSKRRHIDHSPYKTIDFFDPVKLKR
Protein: Forkhead box protein L2 (D4A0S1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Muellerian-inhibiting factor
- Mothers against decapentaplegic homolog 3
- Transcription factor SOX-9
- Steroidogenic factor 1
- Doublesex and mab-3 related transcription factor 1
- Mothers against decapentaplegic homolog 4
- Aromatase
- Protein Wnt-4
- Growth/differentiation factor 9
- Sex-determining region Y protein
Sequence:
MMASYPEPEDTAGTLLSPESGRAVKEAEASPPSPGKGGGTAPEKPDPAQKPPYSYVALIAMAIRESAEKRLTLSGIYQYIIAKFPFYEKNKKGWQNSIRHNLSLNECFIKVPREGGGERKGNYWTLDPACEDMFEKGNYRRRRRMKRPFRPPPAHFQPGKGLFGSGGGAGGCGVPGAGADGYGYLAPPKYLQSGFLNNSWPLPQPPSPMPYASCQMAAAAAAAAAAAAAAGPGSPGAAAVVKGLAGPAASYGPYSRVQSMALPPGVVNSYNGLGGPPAAPPPPPPPHPHPHPHAHHLHAAAAPPPAPPHHGAAAPPPGQLSPASPATAAPPAPAPTSAPGLQFACARQPELAMMHCSYWDHDSKTGALHSRLDL
Protein: At4g35360/F23E12_80 (Pantothenate kinase) (Q8W4Q1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pantothenate kinase 1
Sequence:
MESDSEMVALPLLPTPIESNYRACTIPYRFPSDNPRKATPTEISWIDLFSNSIPSFKERAESDTTVPDAPVRAEKFAKRYAEILEDLKKDPESHGGPPDCILLCRIRELILRELGFRDIFKKVKDEENAKAISLFPEVVRLSDAINDEGKRIENLVRGIFAGNIFDLGSAQLAEVFSKDGMSFLASCQNLVSRPWVIDDLDNFQARWLKKPWKKAVIFVDNSGADIILGILPFAREMLRLGMQVVLAANELPSINDVTYIELAEILSKLNDENGQLMGVDTSNLLIANSGNDLPVIDLARVSQEVAYLSSDADLVILEGMGRGIETNLYAQFKCDSLKIGMVKHPEVAQFLGGRLYDCVIKYNEVQI
Protein: Exo-beta-D-glucosaminidase (EC 3.2.1.165) (Q4R1C4)
Organism: Hypocrea jecorina (Trichoderma reesei)
Function: Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has no activity against beta-D-galactoside, beta-D-glucuronide, beta-D-mannoside, chitin, glycol chitosan, cellulose, N,N'-diacetylchitibiose and pNP-GlcNAc.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:16349528}.
Interaction partners:
Sequence:
MLANAIAALLLGSGIASAAGHGSPLTSKAGHRAVIPDWDLKSSSDVSKDLGGLSKPGVDTSSWYHAGTSRCTIMGCLINAGVYNDEELWYSDNLNHVNWGQFSVPWVYRHEFALSPAKGKHFLLQTNGITSKADLFFNGKQIADKEYQSGAYAGRTYDITNLAAKKNALLVQVYPTDYLYDFALGYVDWNPYPSDNGSGIWRDITIKETGSVSMGPVSVLVDIDVPVEKNPARVTVRAEAQNLESHAVEFNAAAVISGNSCSGEALKQTIKLAPGEKKLVQFTQTIKTPSIWWPKQWGDQPLYTAEVTFSVKGAVSDTAQTKFGVRKVTSFVNQFNDTQYSVNGHPFQVIGGGYGADMFLRWDSERFTRIVEYMLDMHQNTIRLEGKMEHPELYEICDEYGLMVMPGWECCDKWEAWAYNDELAIFPPPVWDANDYETANYSMIHEAAMMQPHPSVLTFLVGSDFWPNDEAVVLYANALKNAGWQTPIIASASKRGFPALLGPGGMKMDGPYDWVPPNYWYDVEPSEDRLGAAFGFGSELGAGVGTPELSSLRRFLNQSDLDDLWKNPNKNLFHMSTNASSFYNRKIYNQGLWKRYGAPTSLDDYLLKAQMMDYEATRAQYEGFGALWTASRPATGVIYWMLNNAWPSLHWNQFDYYLHPAGSYFGTKVGSRIEHVAYNYQKKEIWVINHSLYQTGSRNIKVELIDMNGKQIAKKLVQVRTKANSGFKAMDISSDINKLSSVAFLRLVLSDEKGSVLSRNVYWVTKTIDELNWDESTWYYTPVSKFVDYTPLNTLATAQVSVTTSGGKHLPGIPGSQTRTVTLENKSSVPAVFIRLTLVDSKGNDVNPVSWSDNYVTLWPHEKLQLEVGGWDGSGDKIQISGKNIKATTVKL