wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor E2F7 (E2F-7) (Q6S7F2)
Organism: Mus musculus (Mouse)
Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Also involved in DNA damage response: up-regulated by p53/TP53 following genotoxic stress and acts as a downstream effector of p53/TP53-dependent repression by mediating repression of indirect p53/TP53 target genes involved in DNA replication. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. Acts as a negative regulator of keratinocyte differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:12893818}.
Interaction partners:
- Transcription factor E2F8
- Cell division control protein 6 homolog
- Cyclin-A2
Sequence:
MEVNCLTLKDLISPRQTRLDFAIEDAENAQKENIFVDRSRMTPKTPMKNEPIDLSKQRIFTPDRNPITPVKPVDRQPQVEPWTPTANLKMLISAASPDIRDREKKKELFRPIENKEDAFVNSLQLDVAGDGAVDEYEKQRPSRKQKSLGLLCQKFLARYPSYPLSTEKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYGWHGRHSLPKTLRTLQRLGEEQKYEEQMACLQQKELDLMGYRFGERRKDGSPDPRDPHLLDFSEADYPSSSANSRKDKSLRIMSQKFVMLFLVSKTKIVTLDVAAKILIEESQDTPDHSKFKTKVRRLYDIANVLTSLALIKKVHVTEERGRKPAFKWIGPVDFSSIDEELLDVSASILPELKKEAYGQIRVCAKERLVRYGSFNTVHTSEKIQRKVSSEPSSPQGERQGSAYSLEIGSLAAIYRQKVEDNSQEEAFVSNTAVPPASILDPALSMDSEYCVKPLAQPVFSVAQTDLPAFSAQNGPSGQVGVPVPSAASDTENLKPALLAGQPLVYVPSTQLFMLYGSVQEGLSPESRSEEDGGGSDVPADLSVTPSAQKRLCEERDPQEEEDEPAMKRQSQEFEDSPLSLVMPKKPSSSTDLACPVTMGNGSSPPLEDACVKGQLPAAEEVTGKAAPNCYVASECGNPARNPDTEKPSNENEITKDPSLMQYLYVQSPAGLNGFNMVLPGTQTPHTVAPSPAQLPSFGVPCMFLQSPGLGPFPVLYSPAIPGPISSAPGTHPNPGPMNFGLSTLASASHLLISPAAMVNPKPSTLPCTDPQLRCQPSLNLNPVMPGSHGVIHPESPCYVRHPVSMVKAEQSPAPATPKSIQRRHRETFFKTPGSLGDPVFRRKERNQSRNTSSAQRRLEISSSGPD
Protein: Matrix protein (D7F419)
Organism: Avian paramyxovirus 1 (NDV) (Avian orthoavulavirus 1)
Subcellular location: Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MDSSRTIRLYFDSALPSSSLLAFPIVLQGTGDGKKRITPQYRIQRLDSWTDSKEDSVFITTYGFIFQIGNEEVNVGTINDNPRHELLSSAMLCLGSVPNDGDLVELARACLTMVITCKKSATNTERIVFSVVQAPRVLQSCMVVANKYSSVNAVKHVKAPKKIPGSGTLEYKVNFVSLTVVPRKDVYRIPTAALRISGSSLYNLALNVTIDVEVDPKSPLVKSLSKSDSGYHANLFLHIGLMSTVDKRGRKVTFDKIEEKIRRLNLSVGLSDVLGPSVLVKARGARTKLLAPFFSSSGTACYPIANASPQVAKILWSQTAHLRSVKVIIQAGTQRAVAVTADHEVTSTKIEKRHTIAKYNPFKK
Protein: JAZF zinc finger 1 (H0Y403)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XYFVLGSLIYSDAKSKKNRNCVFITDTDPRVLEKQELQQPTYVALSYINRFMTDAARREQESLKKKIQPKLSLTLSSSVSRGNVSTPPRHSSGSLTPPVTPPITPSSSFRSSTPTGSEYDEEEVDYEESDSDESWTTESAISSEAILSSMCMNGGEEKPFACPVPGCKKRYKNVNGIKYHAKNGHRTQIRVRKPFKCRCGKSYKTAQGLRHHTINFHPPVSAEIIRKMQQ
Protein: Cytochrome c oxidase subunit 9, mitochondrial (Cytochrome c oxidase polypeptide VIIA) (P07255)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome c oxidase subunit 8, mitochondrial
- Cytochrome c oxidase subunit 7, mitochondrial
Sequence:
MTIAPITGTIKRRVIMDIVLGFSLGGVMASYWWWGFHMDKINKREKFYAELAERKKQEN
Protein: Protein TAB2 homolog, chloroplastic (Zm-TAB2) (B4FTR7)
Organism: Zea mays (Maize)
Function: Nuclear genome-encoded factor involved in the biogenesis of photosystem I (PSI). Required for the accumulation of PSI during plant development. Does not seem to be required for the translation of mRNAs of the PSI subunits.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- DCD
Sequence:
MTTATAIVAGHGLALRRSLPLPNPPGRATTSVSLSARPVTPARRMIVPASPSPRSPRRCRSISSESSTEASAAADIADEEVEAENKVDPQAEVCYLDPDVDPESIREWELDFCSRPILDARGKKVWELVVCDATLSLQFTRYFPNNAINSVTLRDALASVSEALGVPMPDRVRFFRSQMQTIITRACGDLGVKAVPSRRCVSLLLWLEERYEVVYSRHPGFQAGTRPLLALDNPFPTTLPENLFGDKWAFVQLPFSAVREEVESLERRYAFGAGLDLELLGFELDDTTLVPGVAVESSRAKPLAAWMNGLEICAMEADTGRASLILSAGVSTRYVYSGYQKTAASTQEAEAWEAAKKACGGLHFLAIQENLNSDGCVGFWLLLDLPPPPV
Protein: C-terminal-binding protein 2 (CtBP2) (Q0VCQ1)
Organism: Bos taurus (Bovine)
Function: Corepressor targeting diverse transcription regulators. Functions in brown adipose tissue (BAT) differentiation (By similarity). Isoform 2 probably acts as a scaffold for specialized synapses.
Subcellular location: Nucleus {ECO:0000305}. Synapse {ECO:0000250}.
Interaction partners:
- DNA endonuclease RBBP8
- Transcription factor 7 like 1
- Lymphoid enhancer-binding factor 1
- C-terminal-binding protein 1
- Phosphoserine aminotransferase
- Histone deacetylase 1
- Recombining binding protein suppressor of hairless
- MDS1 and EVI1 complex locus
- Runt-related transcription factor
- Recombining binding protein suppressor of hairless-like protein
Sequence:
MALVDKHKVKRQRLDRICEGIRPQIMNGPLHPRPLVALLDGRDCTVEMPILKDLATVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVLFYDPYLQDGTERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPESLRNCVNKEFFVTTAPWSVIDQQAIHPELNGATYRYPPGIVGVAPGGLPAAMEGIIPGGIPVTHNLPTVAHPSQAPSPNQPTKHGDNREHPNEQ
Protein: CCT-beta (Q386W9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- T-complex protein 1 subunit eta
- T-complex protein 1, zeta subunit, putative
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit delta
- CCT-theta
- Phosducin domain-containing protein
- GST N-terminal domain-containing protein
- Elongation initiation factor 2 alpha subunit, putative
Sequence:
MLFANQAQQVLRDGASEEKGERARLMNIMGAVSVADIVKTTLGPKGMDKILQGMDRSQGVRVTNDGATILKSLFMDNPAGKILIDMSKTQDDEVGDGTTSVTVLAGELLRNAEKLLDQSIHPQTIIEGYRLATQVAREALVASAEDHGSDEKLFYDDLIRIAKTTLSSKIITVEKEHFAKLCVDAVLRLKGSGNLEMINIMKKLGGTLRDSYLEPGFLLDKKIGVGQPRFLEDAKILVANTPMDTDKIKIFGAKVRVESVSQLAEVEASEKEKMKNKCMKIIKHNINCFINRQLIYNYPEEIFAQHGIMAIEHADFEGIERLAKALGADVLSQFDESQNVKYGFAKRIDEIMIGESTVIRFSGLPKGEACTIVVRGMSQHILDEAERSIHDALCVISQTIGETRTVLGAGCSEFVMARAVEERAKTTPGKKQLAMIAFANALRMIPSIIADNAGLDSNDLITRLQAEHYQGRNTFGIDVVKGDVADVKALGITESFKVKSSVLGYAAEAAEMILRVDDILRAVPRKRTQ
Protein: Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Cell adhesion kinase) (Discoidin receptor tyrosine kinase) (Protein-tyrosine kinase 3) (Tyrosine kinase DDR) (Tyrosine-protein kinase CAK) (CD antigen CD167a) (Q63474)
Organism: Rattus norvegicus (Rat)
Function: Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MGTGTLSSLLLLLLLVTIGDADMKGHFDPAKCRYALGMQDRTIPDSDISVSSSWSDSTAARHSRLESSDGDGAWCPAGPVFPKEEEYLQVDLRRLHLVALVGTQGRHAGGLGKEFSRSYRLRYSRDGRRWMDWKDRWGQEVISGNEDPGGVVLKDLGPPMVARLVRFYPRADRVMSVCLRVELYGCLWRDGLLSYTAPVGQTMQLSEMVYLNDSTYDGYTAGGLQYGGLGQLADGVVGLDDFRQSQELRVWPGYDYVGWSNHSFPSGYVEMEFEFDRLRSFQTMQVHCNNMHTLGARLPGGVECRFKRGPAMAWEGEPVHHALGGSLGDPRARAISVPLGGHVGRFLQCRFLFAGPWLLFSEISFISDVVNDSSDTFPPAPWWPPGPPPTNFSSLELEPRGQQPVAKAEGSPTAILIGCLVAIILLLLLIIALMLWRLHWRRLLSKAERRVLEEELTVHLSVPGDTILINNRPGPREPPPYQEPRPRGTPTHSAPCVPNGSALLLSNPAYRLLLATYARPPRGPGPPTPAWAKPTNTQACSGDYMEPEKPGAPLLPPPPQNSVPHYAEADIVTLQGVTGGNTYAVPALPPGAVGDGPPRVDFPRSRLRFKEKLGEGQFGEVHLCEVEDPQDLVTSDFPISVQKGHPLLVAVKILRPDATKNARNDFLKEVKIMSRLKDLNIIRLLGVCVQDDPLCMITDYMENGDLNQFLSAHQLENKVTQGLPGDRESDQGPTISYPMLLHVGAQIASGMRYLATLNFVHRDLATRNCLVGENFTIKIADFGMSRNLYAGDYYRVQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEVLMLCRSQPFGQLTDEQVIENAGEFFRDQGRQVYLSRPPACPQTLYELMLRCWSREPEQRPPFSQLHRFLADDALNTV
Protein: XK-related protein 7 (Q5GH64)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000269|PubMed:25231987}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Spermatogenesis associated glutamate
Sequence:
MAAKSDGAAAVAGPGPEGPAGADRGGAGGRGEAAAGIAGPGPVEAGCPGPRYELRDCCWVLCALLVFFSDGATDLWLAASYYLQGQSTYFGLTLLFVLLPSLVVQLLSFRWFVYDYSEPAGTPGPAVSTKDSDIVGAAISTKDSAVAFRTKEGSAELVPRPAPSSAGTYRRRCCRLCVWLLQTLVHLLQLGQVWRYLRALYLGLQSRWRGERLRRHFYWQMLFESADVSMLRLLETFLRSAPQLVLQLSLLVHRGREPELLTALSISASLVSLAWTLASYQKVLRDSRDDKRPLSYKGAVVQVLWHLFTIAARTLAFALFASVYKLYFGIFIVAHWCIMTFWVIQGETDFCMSKWEEIIYNMVVGIIYIFCWFNVKEGRSRRRVTLYYCIVLLENAALTGFWYSSRNFSTDFYSLILVCVVASSFALGIFFMCVYYCLLHPNGPMLGPQAPGCIFPEAPGPCGPPADAITSPPRSLPRTTGTERDGVAVGGERAGTPTLPVFQVRPGLPPTPVARPLRTEGPVIRIDLPRKKYPAWDAHFIDRRLRKTILALEYSSPATPRLQYRSMGTSQELLEYETTV
Protein: Ceroid-lipofuscinosis, neuronal 6 (F6SXC2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XGASIHLVGDSVNHRLLFSGYQHHLSVRENPIIKNLKPETLIDSFELLYYYDEYLGHCMWAEKAGSRAVCMTCQHGDTLGPVGRWWGQPLARRVKLLPLCHRYLVTEGQIFILFIFTFFAMLALVLHQKRRRLFLDSNGLFLLYSFALTLSLVALWVAWLWNDPVLRKKYPGVIYVPEPWAFYTLHVSSQQ
Protein: PH domain-containing protein (Q38A08)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Coatomer subunit gamma
Sequence:
MEQAQRPPDNVMGVMRCAVERGRKSFVAYKKRFWVVDETQGRLEVYKNDQEPVPLDRFCASEVRGVIISGDRQNKFYGLVLQLRRGQNIKLRLSSLAERDRWYAAITRLIERCSTYNRDYNLLRVAQRRTLVAGRLLGVNITLAVARLSDIPDDLLQYLVEAVDVAIDTISAAVHAYGGDVEVPRRYTITVEAGQDRIDTGPQYDPTTGSLLLNVWISRDVTGNVRFNVADSAEVMKMTQSHVWREPRIEGWITTNPSCVAVCREIGEMLGSRNFSFSFQWGQNLRDTERVEQYLHQYVHEDFLRAIHRNIVEVVEDFRRSDTDADDSCYLKYIGDFVSGIAIVLDESTVNAGKPPLLRVTTTVEYQRRCRHAVVLKSKYFEVYRTQRVLTKSLRLQLVEVILLADLSKRLSDSKTALTQAIGGNECVRIIWVNLFRSFASVGAQLPQFKLSDVVTSITNTYLTRLESLQQLGSLELPYAGVKPLYASLFSNVTTLVVDFVPFKEDDVSQLPEPKVHDGILTDYIVCCTAAQQRAMMNFICSRRGVPQIDRAYVLLNGLFAFPSMPATTFKEWCEKQAFNGVEGYSGANDDDSSSRSSGGSDDLGDAVAFERNAEAQVLDLHRVVSTIYDSQGAAVHLKIGADSIRDAIEALEQAFDGRQIRKHDLVRVLTANLRRLRAIYSHAVGGEVMTRLDLDAAGRLLRSLCEYKESEQGLDELLQRCAQQRQQAVRLGSSDSVPQERRSLSCSASESIYDFQCVSQVALNYVLPREVKLARKAWRVGLVAGLQDVGKTLILNSLHGVIQPTFPTIGLSQRVIAFEEWVFAMHELGGRESFRENWRYYVERMEEVDFLFFVVDSMNKRAFKYASNYLREITNYFVNTPLVVLFNNVRVGVRGVSLLDHLSGAVKLDKIKKRQPERFIIVGTCDITVVSSSHRTIPPTLLETMQRLGEYLRQVSPPERTPSEPKKGSGVEYTTT
Protein: Fgfr1op N-terminal like (LisH domain-containing protein FOPNL) (I3ITH9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
- Pre-mRNA-splicing factor ISY1 homolog
- Homeobox protein goosecoid
- Serine/threonine-protein kinase PLK
- KIAA0669-like protein
Sequence:
MATITELKSALRETLEARGVLGQLKARVRAEVFSALDDPNTPRPPLSHDNLLINELIREYLEFNKYRYTASVLTAESGQPEVPLDRDFLAKELNVAEDSSARSVPLLYGLFHHFLSSKEEHKGQIFLKGSATVTSQEPHGHRDAES
Protein: Phosphodiesterase YfcE (EC 3.1.4.-) (P67095)
Organism: Escherichia coli (strain K12)
Function: Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). The physiological substrate is unknown.
Interaction partners:
- Uncharacterized Nudix hydrolase YfcD
- dITP/XTP pyrophosphatase
Sequence:
MMKLMFASDIHGSLPATERVLELFAQSGAQWLVILGDVLNHGPRNALPEGYAPAKVAERLNEVAHKVIAVRGNCDSEVDQMLLHFPITAPWQQVLLEKQRLFLTHGHLFGPENLPALNQNDVLVYGHTHLPVAEQRGEIFHFNPGSVSIPKGGNPASYGMLDNDVLSVIALNDQSIIAQVAINP
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (A0A0B4K638)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
Sequence:
MGTKTQPQLAKENERRIRANDKEFNAQFKYHNNYIKTSKYSLFTFLPFNLLEQFQRLANFYFLCLLVLQLIPAISSLTPVTTAIPLIGVLTLTAVKDAYDDIQRHISDSQVNNRKSKTLRNGKLVEAKWSEVQVGDVIRLDNNQFVAADTLLLSTSEPNGLCFIETAELDGETNLKAKQCLTETIELGDRHDSLWNFNGEIICERPNNLLNKFDGTLIWRGQRFALDNEKILLRGCVLRNTQWCYGVVVFAGVDTKLMQNSGKTQFKSTGVDRLLNFIIIGIVLFLVSICALFAIGCAIWEGLIGQHFQLYLPWEHIIPKDYIPTGATVIGLLVFFSYAIVLNTVVPISLYVSVEVIRFVQSFLINWDEEMYYPTTNTYAKARTTTLNEELGQIQYIFSDKTGTLTQNIMTFNKCSINGRSYGDVIDLRTGELVEITEQQTIFQNSNTNNRPSPLSGAIVAPPAAPPPIILVHKAEVHAKKTSMVVTSSGEAQVLPDRPRSDIERSAPPMDASEKRPGLKHVRYSAPSRSQDADAGRLSPRLDGSGGLSPPVGNEERRISGGFKRSGAGCMQRQLSRTSSCDKVKILHDSQQTETHNMHHSSHNRKRLVKIRFKKAPSTATLGVVISQLEHHLDEEPQSTSTLSTTKHHHHRSKAFATNWSSSPHRVHALQSVDFSANPHHESDFRWYDRTLLDAVRSDEEHSHVFFRLLALCHTVMAETVDGKLEYQAQSPDEAALVSAARNFGFVFRTRTPNSITIEVMGQTEEYELLNILDFNNVRKRMSVILRRGDSMVLYCKGADNVIYDRLHGGQEDLKARTQDHLNKFAGEGLRTLALAERRLTEQYYNDWRSRQQEAALSMDSREQKLNAIYEEIESEMQLVGVTAIEDKLQDGVPKSIANLQNAGIKIWVLTGDKQETAINIGYSCQLLTDELADVFIVDGNSVEEVEKQLRQFKESIKIYNRFRPGGFDPFDRLNSDSNMDPLSVTMTQTSAFMQETNLPPTPPPPPAISVVTFRWDEKNKDNKGGPDSAECNNLFGDEKGSEDGGTASIVVDENTGFALVVNGHSLVHCLSPELENKFLDIASQCKAVICCRVTPLQKALVVELIKRAKNAVTLAIGDGANDVSMIKAAHIGVGISGQEGLQAVLSSDYSIAQFRYLERLLLVHGRWSYYRMCKFLRYFFYKNFAFTLCHCWYSLFCGFSAQTVFDPMFISVYNLFYTSLPVLALGVFEQDVSDKNSLEFPRLYTPGLKSELFNIREFIYSVLHGAFTSLVLFLIPYGVYKDGVSANGFVVSDHMTLGAVVATILIVDNTAQISLYTSYWTVVNHVTIWGSLVWYFVLDYFYNYVIGGPYVGSLTQAMKDLTFWVTMLITVMALVAPVLAYKFYLLDVHPSLSDKIRQKSLKKIHSRASSDVRRTASSRRGRRSVRSGYAFAHQEGFGRLITSGKIMHKLPQDFAFPLGLGTKKTQVLHNNLNSADGPNSKGNNVTGHHMVNNNTNMRHNQNQNHSSMADITADGRGNGGDDGRGSGGSDDMSPRAPCQDLDTINL
Protein: Ubiquitin-conjugating enzyme E2 D3 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D3) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D3) (Ubiquitin carrier protein D3) (Ubiquitin-conjugating enzyme E2(17)KB 3) (Ubiquitin-conjugating enzyme E2-17 kDa 3) (Ubiquitin-protein ligase D3) (P61079)
Organism: Mus musculus (Mouse)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction. Together with RNF135, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P61077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P61077}. Endosome membrane {ECO:0000250|UniProtKB:P61077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P61077}.
Interaction partners:
- Polyubiquitin-B
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- E3 ubiquitin-protein ligase RING2
- Polycomb complex protein BMI-1
- Ubiquitin-like modifier-activating enzyme 1
- Breast cancer type 1 susceptibility protein homolog
- Histone H2B type 2-B
- Histone H2B type 1-C/E/G
Sequence:
MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM
Protein: DYNC1H1 protein (Q6P2H7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKRTVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVSDFSERIKQLQNISLAAASGGAKELKVKALLTSLGWSAAVLGWGGSGSGEKHRAQV
Protein: Acyl-coenzyme A diphosphatase SCS3 (EC 3.6.1.-) (FIT family protein SCS3) (P53012)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (By similarity). May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (By similarity). May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Involved in phospholipid biosynthesis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03231, ECO:0000269|PubMed:26504167, ECO:0000269|PubMed:29417057, ECO:0000269|PubMed:29526591}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03231}. Note=Enriched at sites of lipid droplet (LD) biogenesis. {ECO:0000269|PubMed:29526591}.
Interaction partners:
- Acyl-coenzyme A diphosphatase YFT2
- Protein SEY1
- Seipin
- Protein PET10
- CTP-dependent diacylglycerol kinase 1
- Protein ICE2
Sequence:
MSSKWFNAIHLLVCPLTVLVGYLMNAYGYGAALQATLNKDGLVNAMLVKKGWFWTSLVGWWCIIRYRAVPGATGRDRRHIVQSFKRYAILTVWWYVFTQGIWFGVGPIMDLVFVYTGGHCHYDVFDDAGHVNEDFQGSVTRTNRALALIHNVLTLHGHHQEHRQQQLWDRSIGSIQGALQATQPKTPKNVTASAAAAINTFIHDQMHRWQGPLTTSAQCRRFGGHWAGGHDPSGHVFLATLMCMFLLGELRVFGRRALAHLYAQKWQLVRLVTRLFDTGPLWTWRRCGGGSMTCGARLWRAIVEPPVTCAAALLRLTRCIACDHPVIILLTLLVTWLWQLLLTAVASRFHTVREHMSGLLAAYIVTGLVYARDAAALRPV
Protein: Uncharacterized protein C1919.07 (O94475)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MVVQDKWKRKATLAYKKKHDIHDAPVKPRKKNLGNNEWRFKNAGEYFDEDNNEEEYPSLESLKTVGNGDTIQDEEEDFEYSKLQARPLTGLGISNQKPKSKVRTIQREEVADMLESVEHEKSIQEFRKRYNVQKPKVNISHAEAEEDIDSFLESMDQSAPPSITEDKGENYISSNHSSMHISRNDSRNYMSEKPNKDQSWLDELLR
Protein: Uncharacterized transcriptional regulatory protein C530.08 (O59744)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDNESHSQETESKILEGAKVATRRRRVTRACDMCRRKKIKCDGLRPCKNCKAGKLECTYHMPSSRKSSFSPEYVENLESRVRYLETLLKKNTNFDLSSNSPSFLFFLREQKFQATNELENMSPERKVIFTSMINYGNLFVDAKHGTRYFRGGSSIHVLIQHLIRRLPGDFEICEPYSAYPLGNKNIQFDDNDPEYQFFTPTPRFSIDFMVSSVDPREIQLPGIEEALCITKAAVSYVSGIVFYTTYADFPKKIRLLYSGNYQGNFFPLFLSILCVGYYHHLLNNPSNTELQSLIKKYSFYSERLVKSADNFTIESIQCLLILSIYRYCRTEISAAWYYMKLGLNCCLRLGLHRNITEGFTEEQIDSRRRIFWAIYCYDRQLCTLFGFPLGVRDEDIDQCLPVTPKFPSVTEIEANARLFFFHGVKLYKISSRILTKLYSPNSRNVTKKHISYAVIQDLEQLLDGFYNSLPRVFRAEQPGEFQANHFFYNLQLVYYSFRMLIYRPLLHYLEADSPAMQALKVPDRQTAFTLACKCVDSAIVCVQNLSHLSKGLKRTLDRYYWTTVYCGFSTIVTLIFAALLTKNTNLLIHISVARESIEALAHECVTRRLLPLIDKMRESLMKILESNADGYKQMSPTKAPQVFESESNVPINNGPQQSIDKESNSNTQLPQVETEGQQQSVFDGNIGTIPYQAYNMNEDSFIDINTLSSMLNYHTQAVSIHHPSFYISRSDVPLEEEFQIPNELLAVDPVAESMQENSDIINEAFGLVDPDVSDGKSRESSSLNNSTPFNPTVNIDPASILEHFSQNVMKDSQNS