wanglab/gogpt-training-data huggingface dataset:
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FK93)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSSSISDREAVKVDSGKQEIYEVSSSLDIDELRSDFDPEQNIREDLTRALSPRHINMISIAGIIGTGLYLSTAKSLHNGGPASLFMNYTIIGGVVYLTMLCLGEMSTFMPISGSFCSYARKFGSESFACALMWNYWFNDAVSVASDLTALQLVLDYWHTADHHFPYWGASLIFWFFVLFLNVIHVRIYGEAEYWLAMLKVIAIVIFFIMSIIVNVGKNPQHEYIGFKNWTHGEAPFVNGFKGFASLFVSACFAYGGTESITLTGGEASNPVRNTPKIVKTVFWRILIFYVLSTFFIGMNIPYDYPGLSTKSVMTSPFTLVFQMAGTRGAGSFMNAVILTSVISACNHALFAGSRIMYNMALDGYLPKKIVGRTNRYKAPYVAVLITWAVGGLCLGASFIGAGTLWTWLQNIVGVSNQIAWLCIGITSIRFRKGLEVQGKTDLLQFKNWTYPFGPYFLVIFTVFIILIQGWQAFDPWSVTDFFSVYLELFVFPFVYIIWWLWKRDWFVKYEDMDFVTDRYIPTKEIVELNERLDNLKGWKKVRQIFSDYIA
Protein: Opt3p (A0A1D8PS61)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDEKNPTTELSVPNIEAVGSHLQVQDHEINLQAIISNPLSIGEVATTLTESQKWFVLKRLHFDALVSLDELPPQASFIFEKIEQMTTEEAVEILEKNIEEHETDVNIPENDLVLWKELVENSHKFTKVQLQEKLGSNSSSSVEGEKTADVEKGHEIVDWDLQVRLEAVLVAYWSPYPEVRAVTFPYDDPTIPAETFRVYLIAIIWTAIGAVINQFFVERQPAITLAMSVVQVFLYPSGLLCEWILPKWKFKIWKLSIDLNPGPYTYKEQMLATIFCGVTGGGTSYVSSNILMQKSEIFYDNKWVDFGYQVLLILSTNFLGIGLAGIMRKFAVYPTKAVWPSILPGLALNKTLLTPAKKEVINGWKISGYNFFFIAFVASFLYFWVPDYLFQALSTFNWMTWIKPDNQNLAVVTGSVGGLGLNPITTFDWNYFSSMLQPLQVPFFYPVNNIIGMAIAFFCIIGVWYSNYKWTGYLPINDNGLYTNTGEPYSVRSVVDANSLFDQAKYAEMGPPFYTAANLVVYGAFFAIYPFHFVYELGMNYDQMWDAFKSFWRVIKDYKKSTYDGFDDPHSTMMRAYPEVPEWAYLIIVVISLVLAILCVKVYPAETPVWGIFFALGINFVFLIPLTTIYARTGFAFGLNVLVELIVGYAIPGNGLALAFIKALGYNIDGQAQNFVNDLKQGHYAKLPPRAVYRVQLLSIFISSFIQLGILNFQINGGIKDYCEPGNTQKFTCPSSRTFYSASVLWGVIGPKRVFNGLYPILRWCFLIGFLIAFPCIAIKKWGPRKYVKYFEPSIIIGGFLNYAPYNLSYYIPGLYVSFTFMSYIKRKYEAWWQKYTYVLSTGLNAGIAFSSIIIFFAVMYHEKDINWWGNTVMYSGVDYAMTGWLNATVDAPDGYFGPRVGHFP
Protein: EKC/KEOPS complex subunit bud32 (EC 3.6.-.-) (Atypical serine/threonine protein kinase bud32) (EC 2.7.11.1) (Q5BAB7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P53323}. Nucleus {ECO:0000250|UniProtKB:P53323}. Chromosome, telomere {ECO:0000250|UniProtKB:P53323}.
Interaction partners:
- tRNA N6-adenosine threonylcarbamoyltransferase
- Uncharacterized protein
- N
- Uncharacterized protein
- Serine/threonine-protein kinase bur1
- Serine/threonine-protein kinase cbk1
- Kinase
Sequence:
MPPTNRPPPFSTILSSASLPSYSSTDELTPIYQGAEAHLYKTTFLSPSQPAALKIRPSKPYRHPILDRRLTRARILQEARCLQKLVKEGVSVPALLGVDWEPSAGDGSSWLVMEWIEGEPVRVILEEWEAYLKGIEREKRLGLGEGVQGSEEEKVRGLMRRIGRAVGGLHRAGVIHGDLTTSNLMLRPLGSADTTETIEERDQSPSMAGEVVMIDFGLAMQSSQDEDRAVDLYVLERAFGSSHPRTERFFEEVLVGYRESYKGAVSALKRLEDVRMRGRKRSMIG
Protein: Elastin (Tropoelastin) (P15502)
Organism: Homo sapiens (Human)
Function: Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17035250}. Note=Extracellular matrix of elastic fibers. {ECO:0000269|PubMed:17035250}.
Interaction partners:
- Fibulin-5
- Fibrillin-1
- Fibronectin
- Microfibrillar-associated protein 2
- Decorin
- Protein-lysine 6-oxidase
- Vitronectin
- Microfibril-associated glycoprotein 4
- Biglycan
- Beta-galactosidase
Sequence:
MAGLTAAAPRPGVLLLLLSILHPSRPGGVPGAIPGGVPGGVFYPGAGLGALGGGALGPGGKPLKPVPGGLAGAGLGAGLGAFPAVTFPGALVPGGVADAAAAYKAAKAGAGLGGVPGVGGLGVSAGAVVPQPGAGVKPGKVPGVGLPGVYPGGVLPGARFPGVGVLPGVPTGAGVKPKAPGVGGAFAGIPGVGPFGGPQPGVPLGYPIKAPKLPGGYGLPYTTGKLPYGYGPGGVAGAAGKAGYPTGTGVGPQAAAAAAAKAAAKFGAGAAGVLPGVGGAGVPGVPGAIPGIGGIAGVGTPAAAAAAAAAAKAAKYGAAAGLVPGGPGFGPGVVGVPGAGVPGVGVPGAGIPVVPGAGIPGAAVPGVVSPEAAAKAAAKAAKYGARPGVGVGGIPTYGVGAGGFPGFGVGVGGIPGVAGVPGVGGVPGVGGVPGVGISPEAQAAAAAKAAKYGAAGAGVLGGLVPGAPGAVPGVPGTGGVPGVGTPAAAAAKAAAKAAQFGLVPGVGVAPGVGVAPGVGVAPGVGLAPGVGVAPGVGVAPGVGVAPGIGPGGVAAAAKSAAKVAAKAQLRAAAGLGAGIPGLGVGVGVPGLGVGAGVPGLGVGAGVPGFGAGADEGVRRSLSPELREGDPSSSQHLPSTPSSPRVPGALAAAKAAKYGAAVPGVLGGLGALGGVGIPGGVVGAGPAAAAAAAKAAAKAAQFGLVGAAGLGGLGVGGLGVPGVGGLGGIPPAAAAKAAKYGAAGLGGVLGGAGQFPLGGVAARPGFGLSPIFPGGACLGKACGRKRK
Protein: Rfx, isoform I (A8JQX0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTTRLAPQRQFILSTRSAIVDATSPPEDSAEEQQQLTVEVESATNGVITNSTTSPPPHAEQFEFCTEDGVVVSATLEDVMTQNCQLLQKKLVDEDDDSTGVGATDADQLEVISVVLPMDAEDSTSDAHLHGHVVNSSSDTMGTITTTEPNGTTVTHSIPIHSMADLAAIKDGVDLAQQVANGQVTVVQTTEDDDGTPFITVTVSGQEQNYQVQYVDSELYHSNSSQTQMTYPFCPVGDYQGNGQTAYYSTTGQYGTTSSAGGSSNGAHSTTLPYLVPVEEGILLNGSAHSLSQSQSQSHGRDSPHSLTEVAYIQEAQSTPQTPTSTTTTHSASGGSLGTGGGGASPDSDQSALGSSNKIASATIKWLSRNYETADGVSLPRSTLYNHYMQHCSEHKLEPVNAASFGKLIRSVFSGLRTRRLGTRGNSKYHYYGIRIKPGSLLNSQAMDDKQMLAAGYGPSSDGTGGPGSGPMVSVTSSTAGQLTGSNGLGGGHGQRHSNGTKKHTFKPETYEACIQYIGDGTSALPSFPPIELNHSFNSELTLEDVDTFRGLYREHCESFLDAVLNLEFNTVEFLLRDFWRASDNNNLDECEEEKYLSKTKLYLLCHCAEVQKFVREVDYQFYQNTVDVIIPDVLRSIPNALTQAIRNFAKNLEIWLCESMLGVPEQLAQIKTSAVSAFCQTLRRYTSLNHLAQAARAVLQNGAQISQMLSDLNRVDFHNVQEQAAWVSQCAPAVVQRLESDFKAALQQQSSLEQWASWLQLVVESAMEEYNGKPTYARAARQFLLKWSFYSSMIIRDLTLRSASSFGSFHLIRLLFDEYMFYLVEHKIAEAQDKTAIAVICERMKKDMDFEFECQFAYITSDTEHQTTPSSASSGGDVGNEAKRLKQE
Protein: Ras-related protein R-Ras2 (EC 3.6.5.-) (P62071)
Organism: Mus musculus (Mouse)
Function: GTP-binding protein with GTPase activity involved in the regulation of MAPK signaling pathway, thereby controlling multiple cellular processes. Involved in the regulation of MAPK signaling pathway. Regulation of craniofacial development.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P62070}; Lipid-anchor {ECO:0000250|UniProtKB:P62070}; Cytoplasmic side {ECO:0000250|UniProtKB:P62070}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P62070}; Lipid-anchor {ECO:0000250|UniProtKB:P62070}.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Neurofibromin
- Ras and Rab interactor 1
- Serine/threonine-protein kinase A-Raf
- Son of sevenless homolog 1
- Ral guanine nucleotide dissociation stimulator
- Serine/threonine-protein kinase B-raf
- Leucine-rich repeat protein SHOC-2
Sequence:
MAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCVIDDRAARLDILDTAGQEEFGAMREQYMRTGEGFLLVFSVTDRGSFEEIYKFQRQILRVKDRDEFPMILIGNKADLDHQRQVTQEEGQQLARQLKVTYMEASAKIRMNVDQAFHELVRVIRKFQEQECPPSPEPTRKEKDKKGCHCVIF
Protein: POU domain protein (A0A0G2K3R5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- POU domain, class 2, transcription factor 1
- POU domain, class 2, transcription factor 3
- POU class 2 homeobox associating factor 1
- Transcription factor Sp1
Sequence:
MVHSSMGAPEIRMSKPLEAEKQSLDSPSEHTDTERNGPDINHQNPQNKASPFSVSPTGPSTKVGILSGLHLTFWGPGPCLSPPQIKAEDPSGDSAPAAPPPPQPAQPHLPQAQLMLTGSQLAGDIQQLLQLQQLVLVPGHHLQPPAQFLLPQAQQSQPGLLPTPNLFQLPQQTQGALLTSQPRAGLPTQPSKCLEPPSHPEEPSDLEELEQFARTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAETMSVDSSLPSPNQLSSPSLGFDGLPGRRRKKRTSIETNVRFALEKSFLANQKPTSEEILLIAEQLHMEKEVIRVWFCNRRQKEKRINPCSAAPMLPSPGKPTSYSPHLVTPQGGAGTLPLSQASSSLSTTVTTLSSAVGTLHPSRTAGGGGGGGGAAPPLNSIPSVTPPPPATTNSTNPSPQGSHSAIGLTGLNPSAGSTMVGLSSGLSPALMGNNPLATIQALASGGTLPLTSLDSSGNLVLGAAGAAPGSPSLVTSPLFLNHTGLPLLSAPPGVGLVSAAAAAVAATISSKSPGLSSSSSSSSSSSTCSEVAAQTSGGPGGPEAGSKAE
Protein: Cation-transporting P-type ATPase N-terminal domain-containing protein (F5GUA7)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MRMVPCTFEAAEYIYIIDNHNVSELQPVLRKSNATIPTENGEMRKVPELRWFVYRKLEYVWIDDLNSDESVDEISDNDNCWKTSFEIANRIPCRSLLAVSESNFGLTLSEISRRLEFYGRNEIVVQLRPILYLLVMEVITPFYVFQIFSVTVWYNDEYAYYASLIVILSLGSIVMDVYQIRTQEIRLRSMVHSTESVEVIREGTEMTIGSDQLVPGDILLIPPHGCLMQCDSVLMNGTVIVNESVLTGESVPITKVALTDETNDSVFNIEKNSKNVLFCGTQVLQTRFYRGKKVKAIVLRTAYSTLKGQLVRSIMYPKPVDFRFTKDLFKFILFLACISGCGFIYTIIVMIMRGNTLRRIIVRSLDIITITVPPALPAAMSVGIINAQLRLKKKEIFCISPSTINTCGAINVVCFDKTGTLTEDGLDFHVVRPVMSAVNQEIQKVKLEKSNRTEFMGEMTELTSRNGLPFDGDLVKAIATCHSLTRINGVLHGDPLDLILFQKTGWTMEEGIEGDIEEETQRFDNVQPSIIKPTDDKSAEYSVIRQFTFSSSLQRMSVIVFDPREDRPDNMMLYSKGSPEMILSLCDPNTVPEDYLLQVNSYAQHGFRLIAVARRPLDLNFNKASKVKRDAVECDLEMLGLIVMENRVKPVTLGVINQLNRANIRTVMVTGDNLLTGLSVARECGIIRPSKRAFLVEHVPGELDEYGRTKIFVKQSVSSSDEVIEDDASVSISMCSSTWKGSSEGDGFSPTNTEVETPNPVTADSLGHLIASSYHLAISGPTFAVIVHEYPELVDQLCSVCDVFARMAPDQKQSLVEQLQQIDYTVAMCGDGANDCAALKAAHAGISLSDAEASIAAPFTSKVPDIRCVPTVISEGRAALVTSFGIFKYMAGYSLTQFVTVMHLYWISNILTDGQFMYIDMFLITMFALLFGNTPAFYRLAHTPPPTRLLSIASMTSVVGQLIIIGVVQFIVFFSTSQQPWFTPYQPPVDDEVEDKRSMQGTALFCVSMFQYIILALVYSKGPPFRGNLWSNKPMCALTIFATLLCLFIVIWPTELVLKTLGNVELPSLTFRIFIVIVGAVNAAVSYGFETLFVDFFLLGYWERYKKKRSIEAIIDYVPTTNSDHIRRPSINGVTSSRTESTLLSAEGQQLHMTTSKNGKGGENPHSSALFERLISRIGGEPTWLTNPIPPHSLSEPEEPEKLERTY
Protein: Patulin cluster transcription factor patL (Patulin biosynthesis cluster protein L) (A0A075TXZ8)
Organism: Penicillium expansum (Blue mold rot fungus)
Function: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria.
Subcellular location: Nucleus {ECO:0000255, ECO:0000269|PubMed:25625822}.
Interaction partners:
Sequence:
MYSTFSANFDTTIDASRDRSATPVTAPRPKRNQVARACDWCRLNRVRCDDKQPCQNCQNRGGSCSNTKPQEATSLPAANREMQRLRNKVKDLQDQIAKLKEGAEIQAQTGFATPPLSDAAHTSFDFAELTNTTEGWQGLQQTGQIHYGPLSSSYFVSRISRYLSQALNEPIEDAKLEACMARFHYIAPSHQPSRWDASPASQADQPQDGTEEAEDLTRSQEEHFLNLLWQSFHCVYPILDEREFQQYYESLWSSSPDGMSTRKPSALVDVLLAVCMQYSSTFFVSDDNQQGDTDSEWQAKHANLASRTYYQRAQRLLQSELENPTIMVVQSHIYSIVYLYNTSLLNTAHINLGATLRIAHALRLHIRPLDGTSPEQQELQRRIWWALYRIDSQLSMTLGRPPLIQLSHVSCGLPGDDREHARLSGTVLLTNHEDISWLSFHVQCTKLIFLVQGVQTAFNRKCSQLLNGDKVKDLYEDPRLLETLAEFLGQEMTAIHNWVQNVPQSLCNPRKGGSDPFSTNRDALNLSAYSPLWLQRQRLLLELHYHHLVISTLRPFIRFPPVSSSMTPLTDGYNISCLNHAMAITSILNQVLSETDLLRGWSPIFQYQWDAILCTLGFVLANSVCPPTPSARKSLQTAIRTLDLVSDHFLAAKNAAQVVREVSCQADRLVKNVQQGLTRRQAPRASQALSTRAQNPRQASNQTSFVAPAQPGVRSNSLKRALPPTTLEVSQHQPMPNFEARMQLMDMMPIGSLSELSPSLGTTESMSMPSVTSADMVIGTEAQWLHASAMILDSWTTNS
Protein: 1-phosphofructokinase (EC 2.7.1.56) (Fructose 1-phosphate kinase) (Fru1PK) (P0AEW9)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate. Is specific for fructose-l-phosphate (Ref.6). GTP, UTP and CTP can also function as phosphoryl donors showing 60%, 20% and 10% of the activity of ATP (Ref.6).
Interaction partners:
- Multiphosphoryl transfer protein
- PTS system fructose-specific EIIB'BC component
- PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component
- Fructose-like PTS system EIIBC component
- ATP-dependent 6-phosphofructokinase isozyme 1
- Fructose-bisphosphate aldolase class 2
- Fructose-1,6-bisphosphatase class 1
- ATP-dependent 6-phosphofructokinase isozyme 2
- Fructose-bisphosphate aldolase class 1
- Fructose-1,6-bisphosphatase 2 class 2
Sequence:
MSRRVATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQCPCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPEMKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPSVDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVAALAVSQSNVGITDRPQLAAMMARVDLQPFN
Protein: RAB GTPase Vps21/Ypt51, putative (AFU_orthologue AFUA_3G10740) (Q5B3G5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Phosphatidylinositol 3-kinase VPS34
- RAB GTPase Ypt5, putative
- Vacuolar segregation protein
- Rab GDP dissociation inhibitor
- AvaB protein
- Vacuolar protein sorting protein
- TGF beta receptor associated protein 1, putative
- Vacuolar sorting protein
- Guanine nucleotide exchange factor Vps9, putative
- Pep3/Vps18/deep orange beta-propeller domain-containing protein
Sequence:
MSESTPANAPKPSSSVKLVLLGEAAVGKSSLVLRFVNNDFQENKEPTIGAAFLTQKCSLPSRTIKFEIWDTAGQERFASLAPMYYRNAQAALVVYDVTKPSSLTKAKHWVAELQRQASPGIVIALVGNKLDLTNDGGETPAETEREAGTEGDDADDNQEEQEDNTPGDARKVPTREASTYADEEGLLFFETSAKTGLNVTDVFTAIANAIPESSLKSGRGAGAGTGQTTLGGGGRSTDDSRVNLGDRGAATAKEGCAC
Protein: Glutathione S-transferase theta-2 (EC 2.5.1.18) (GST class-theta-2) (Q61133)
Organism: Mus musculus (Mouse)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:8761485}. Nucleus {ECO:0000269|PubMed:8761485}.
Interaction partners:
- Glutathione S-transferase omega-1
- Glutathione S-transferase A3
- Glutathione S-transferase kappa 1
- Glutathione S-transferase omega-2
- Glutathione S-transferase P 1
- Glutathione S-transferase Mu 1
- Glutathione S-transferase Mu 2
- Hematopoietic prostaglandin D synthase
- Glutathione S-transferase A4
- Glutathione S-transferase Mu 5
Sequence:
MGLELYLDLLSQPSRAVYIFAKKNGIPFQTRTVDILKGQHMSEQFSQVNCLNKVPVLKDGSFVLTESTAILIYLSSKYQVADHWYPADLQARAQVHEYLGWHADNIRGTFGVLLWTKVLGPLIGVQVPQEKVERNRDRMVLVLQQLEDKFLRDRAFLVGQQVTLADLMSLEELMQPVALGYNLFEGRPQLTAWRERVEAFLGAELCQEAHSTILSILGQAAKKMLPVPPPEVHASMQLRIARIP
Protein: E3 ubiquitin-protein ligase Topors (EC 2.3.2.27) (RING-type E3 ubiquitin transferase Topors) (SUMO1-protein E3 ligase Topors) (Topoisomerase I-binding RING finger protein) (Topoisomerase I-binding arginine/serine-rich protein) (Tumor suppressor p53-binding protein 3) (p53-binding protein 3) (p53BP3) (Q80Z37)
Organism: Mus musculus (Mouse)
Function: Functions as an E3 ubiquitin-protein ligase and as a E3 SUMO1-protein ligase. Probable tumor suppressor involved in cell growth, cell proliferation and apoptosis that regulates p53/TP53 stability through ubiquitin-dependent degradation. May regulate chromatin modification through sumoylation of several chromatin modification-associated proteins. May be involved in DNA-damage-induced cell death through IKBKE sumoylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:15703819, ECO:0000269|PubMed:15735665}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9NS56}. Note=Localizes to discrete nuclear foci which partly overlap with PML nuclear bodies. Targeted to PML nuclear bodies upon DNA damage. {ECO:0000250|UniProtKB:Q9NS56}.
Interaction partners:
- SUMO-conjugating enzyme UBC9
- Cellular tumor antigen p53
- Small ubiquitin-related modifier 1
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Protein NEDD1
- Paired amphipathic helix protein Sin3a
- CDK5 regulatory subunit-associated protein 2
- Phosphodiesterase
- Mitotic-spindle organizing protein 1
- Gamma-tubulin complex component 5
Sequence:
MGSQPPPPGSPLSREEGEAPPLVPAEEGRRRSRRVRLRGSCRHRPSLLSRRELASNGPAVPATASSEIMASAAKEFKMDNFSPKAGTSKLQQTVPADASPDSKCPICLDRFDNVSYLDRCLHKFCFRCVQEWSKNKAECPLCKQPFDSIFHSVRAEDDFKEYVLRPSYNGSFTNPEVRRFRYRTTMTRERSASLYSPSSTVSRRTTTPPDSGVLFEGLGISTRPRDVDIPQFMRQMALRGPTTTDERSLRKIQEQDIINFRRTLYRAGVRVRSIEDGGRYRDISAEFFRRNPACLHRLVPWLKRELTVLFGAHGSLVNIVQHIIMSNVTRYDLESQAFVSDLRPFLLNRTEHFIHEFISFARSPFNMAAFDQHANYDCPPSSEEGSRSDSSVITISPDEAETQELDMNASTVRQAPWDDETPGPSYSSSEQVHVGVSSLLNSSDSSDEELVSGGTTSQIQGVQTNDDVNNDSDSSSDNCVIVGFVKPLAERTPELVELSSDSEELGPYEKVETVKTQEQEQSYSSGDSDVSRASSPRSVLGKDEQMSKSHCDSDTRISSKKEEKRSTSLPAPRDSSSTRGDRVCSPYNHRHRKGGRSRSSDSRSQSRSGHDPRNHRKHGKKRLRNKRSRSRESSSRPRARKDKKRSRTRDSSWSRRSQTLSLSSGSTSRSRSRSSDHGKRRSRSRNRDRYYLRNNYGSKYKWEYTYYSRNKDRDGYESSYRRRTLSRAHYSRQSSSPEFRIQSFSERTNARKKNHSERKYYYYERRRSRSVSSNRSRTTSAGPDRVRNEKPGGKRKYKTRHLEGTSEEAQPAREFTSKGKDSHYQKSKLDGSYKNESDSFSDSRSSDRETKHKRRRRRTRSLSVEIVYEGKATDTSKHHKKKKKKHKKKHKKHHGDNTSRSPVVITIDSDSDGESEVKAGIECSNGSLPQPIQDGAFETKDVVTIEDELGVLDKDCDVTALADDLSTSQTVENCDSPAVPVEQTLDVREESTFASDLESQSSNVSIQAEPSRPVPSPRTSLSSVSPGRDCDVS
Protein: Alanine--glyoxylate aminotransferase 2 homolog 3, mitochondrial (EC 2.6.1.44) (Beta-alanine-pyruvate aminotransferase 3) (Q9SR86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Serine--glyoxylate aminotransferase
- Glutamate--glyoxylate aminotransferase 2
- Alanine aminotransferase 1, mitochondrial
- Glutamate--glyoxylate aminotransferase 1
- Alanine aminotransferase 2, mitochondrial
- Beta-ureidopropionase
- Aldehyde dehydrogenase family 7 member B4
- Aldehyde dehydrogenase family 3 member H1
- Aldehyde dehydrogenase family 2 member B4, mitochondrial
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
Sequence:
MRKLTAVNSLLKRNNYLLPRHGSSQTAAQRTSSVRETETETKLPKMPPFNYSPPPYDGPSTAEIIAKRREFLSPALFHFYNTPLNIVEAKMQYVFDENGRRYLDAFGGIATVSCGHCHPEVVNSVVKQLKLINHSTILYLNHTISDFAEALVSTLPGDLKVVFFTNSGTEANELAMMMARLYTGCNDIVSLRNSYHGNAAATMGATAQSNWKFNVVQSGVHHAINPDPYRGIFGSDGEKYASDVHDLIQFGTSGQVAGFIGESIQGVGGIVELAPGYLPAAYDIVRKAGGVCIADEVQSGFARTGTHFWGFQSHGVIPDIVTMAKGIGNGIPLGAVVTTPEIAGVLSRRSYFNTFGGNPMCTAAGHAVLRVLHEEKLQENANLVGSHLKRRLTLLKNKYELIGDVRGRGLMLGVEFVKDRDLKTPAKAETLHLMDQMKEMGVLVGKGGFYGNVFRITPPLCFTLSDADFLVDVMDHAMSKM
Protein: b(0,+)-type amino acid transporter 1 (b(0,+)AT1) (Glycoprotein-associated amino acid transporter b0,+AT1) (Solute carrier family 7 member 9) (Q9QXA6)
Organism: Mus musculus (Mouse)
Function: Involved in the high-affinity, sodium-independent transport of cystine and neutral and dibasic amino acids (system B(0,+)-like activity). Thought to be responsible for the high-affinity reabsorption of cystine in the kidney proximal tubule.
Subcellular location: Apical cell membrane {ECO:0000305|PubMed:12167606}; Multi-pass membrane protein {ECO:0000305|PubMed:12167606}.
Interaction partners:
- Amino acid transporter heavy chain SLC3A1
- Aromatic-preferring amino acid transporter, member 15)
- Amino acid transporter heavy chain SLC3A2
- Sodium-dependent neutral amino acid transporter B
- Sodium- and chloride-dependent neutral and basic amino acid transporter B
Sequence:
MEETSLRRRREDEKSTHSTELKTTSLQKEVGLLSGICIIVGTIIGSGIFISPKSVLANTESVGPCLIIWAACGILATLGALCFAELGTMITKSGGEYPYLMEAFGPIPAYLFSWTSLIVMKPSSFAIICLSFSEYVCAAFYSGCKPPAVVVKLLAAAAILFITTVNALSVRLGSYVQNVFTAAKMVIVAIIIISGLVFLAQGNVKNFQNSFEGTQTSVGAISLAFYNGLWAYDGWNQLNYITEELRNPYRNLPMAIVIGIPLVTVCYILMNIAYFTVMTPTELLQSQAVAVTFGDRVLYPASWVVPLFVAFSTIGAANGTCFTAGRLIYVAGREGHMLKVLSYISVKRLTPAPALIFYGIIAIIYIIPGDINSLVNYFSFAAWLFYGMTILGLVVMRFTRKDLERPIKVPLFIPIIVILVSLFLILAPIISEPAWEYLYCVLFILSGLIFYFLFVYYKFGWAQRISRPVTKHLQMLMEVVPPEKDPE
Protein: Heterochromatin protein 1 (HP1) (Non-histone chromosomal protein C1A9 antigen) (P05205)
Organism: Drosophila melanogaster (Fruit fly)
Function: Structural component of heterochromatin, involved in gene repression and the modification of position-effect-variegation. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression.
Subcellular location: Nucleus {ECO:0000269|PubMed:17875665, ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:26389589, ECO:0000269|PubMed:9378752}. Nucleus, nucleoplasm {ECO:0000269|PubMed:9378752}. Chromosome {ECO:0000269|PubMed:12826664, ECO:0000269|PubMed:17875665, ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:26389589, ECO:0000269|PubMed:9378752}. Chromosome, telomere {ECO:0000269|PubMed:12826664, ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:19240120, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638}. Note=Colocalizes with Arp6 on pericentric heterochromatin (PubMed:12826664, PubMed:9378752). Telomere localization is not dependent on peo/pendolino, ver/verrocchio or moi/modigliani (PubMed:19181850, PubMed:19240120, PubMed:20679394, PubMed:26110638). {ECO:0000269|PubMed:12826664, ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:19240120, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:9378752}.
Interaction partners:
- Histone H3.3A
- Histone H3
- Histone-lysine N-methyltransferase Su
- Lamin-B receptor
- Protein piwi
- Telomere-binding protein cav
- G9a, isoform B
- Histone-lysine N-methyltransferase eggless
- Histone H2A.v
- Signal transducer and transcription activator
Sequence:
MGKKIDNPESSAKVSDAEEEEEEYAVEKIIDRRVRKGKVEYYLKWKGYPETENTWEPENNLDCQDLIQQYEASRKDEEKSAASKKDRPSSSAKAKETQGRASSSTSTASKRKSEEPTAPSGNKSKRTTDAEQDTIPVSGSTGFDRGLEAEKILGASDNNGRLTFLIQFKGVDQAEMVPSSVANEKIPRMVIHFYEERLSWYSDNED
Protein: TATA box-binding protein-associated factor RNA polymerase I subunit A (RNA polymerase I-specific TBP-associated factor 48 kDa) (TAFI48) (TATA box-binding protein-associated factor 1A) (TBP-associated factor 1A) (Transcription factor SL1) (Transcription initiation factor SL1/TIF-IB subunit A) (Q15573)
Organism: Homo sapiens (Human)
Function: Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (pre-initiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits.
Subcellular location: Nucleus, nucleolus {ECO:0000305|PubMed:11250903, ECO:0000305|PubMed:11283244}.
Interaction partners:
- TATA box-binding protein-associated factor RNA polymerase I subunit B
- TATA box-binding protein-associated factor RNA polymerase I subunit C
- TATA box-binding protein-associated factor RNA polymerase I subunit D
- TATA-box-binding protein
- DNA-directed RNA polymerase I subunit RPA49
- Nucleolar transcription factor 1
- DNA-directed RNA polymerase I subunit RPA34
- RNA polymerase I-specific transcription initiation factor RRN3
- DNA polymerase iota
- DNA-directed RNA polymerase I subunit RPA1
Sequence:
MSDFSEELKGPVTDDEEVETSVLSGAGMHFPWLQTYVETVAIGGKRRKDFAQTTSACLSFIQEALLKHQWQQAAEYMYSYFQTLEDSDSYKRQAAPEIIWKLGSEILFYHPKSNMESFNTFANRMKNIGVMNYLKISLQHALYLLHHGMLKDAKRNLSEAETWRHGENTSSREILINLIQAYKGLLQYYTWSEKKMELSKLDKDDYAYNAVAQDVFNHSWKTSANISALIKIPGVWDPFVKSYVEMLEFYGDRDGAQEVLTNYAYDEKFPSNPNAHIYLYNFLKRQKAPRSKLISVLKILYQIVPSHKLMLEFHTLLRKSEKEEHRKLGLEVLFGVLDFAGCTKNITAWKYLAKYLKNILMGNHLAWVQEEWNSRKNWWPGFHFSYFWAKSDWKEDTALACEKAFVAGLLLGKGCRYFRYILKQDHQILGKKIKRMKRSVKKYSIVNPRL