wanglab/gogpt-training-data huggingface dataset:
Protein: GA-binding protein subunit beta-2 (GABP subunit beta-2) (GABPB-2) (GA-binding protein beta-2-1) (GABP subunit beta-2-1) (GABPB2-1) (P81069)
Organism: Mus musculus (Mouse)
Function: Transcription factor capable of interacting with purine rich repeats (GA repeats). Must associate with GABP-alpha to bind DNA.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MSLVDLGKRLLEAARKGQDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTNHERANPVANPVTVTAPFIFTSGEVINLASFVSSANTKATSAHLEEMEEGNSLDSSTQQVVGSGGQRVITIVTDGVPLGNIQTSLPAGGIGQPFIVTMQDGQQVLTVPAGQVAEETIIEDEEEEEEKLPLVKRPRMAEMTNRVEEMKEGSERELLQQQLQEANRRAQEYRHQLLKKEQEAEQYRLRLEAMAQQQTNGVEVDVTVVEEVAEVDAVVVTEGDEVERATQVMKSGRTTEPHTNVSIETISS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (B7ZB17)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDEPMGEEEINPQTEEVSIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGFSFVAITSDDESQAMQTVGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQRRGIKKITSTAL
Protein: Adenylylsulfate reductase subunit beta (AdoPSO(4) reductase subunit B) (Adenosine 5'-phosphosulfate reductase subunit beta) (APSR subunit B) (T2G899)
Organism: Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759) (Desulfovibrio gigas)
Function: Iron-sulfur cluster subunit of the adenylylsulfate reductase which catalyzes reversibly the reduction of adenosine 5'-phosphosulfate (APS) to sulfite and AMP during dissimilatory sulfate reduction. The iron-sulfur cluster 2 is thought to accept electrons from a still unknown electron donor and transfer electrons to the iron-sulfur cluster 1 of this protein and then onto the FAD of AprA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7240092}.
Interaction partners:
- Adenylylsulfate reductase subunit alpha
- sulfate adenylyltransferase
- Sulfite reductase, dissimilatory-type subunit alpha
- Sulfite reductase, dissimilatory-type subunit beta
- Putative phosphoadenosine phosphosulfate reductase
- Putative adenylylsulfate kinase
- 3'
- Putative methyl-viologen-reducing hydrogenase subunit delta
- Putative phosphoesterase RecJ domain protein
- Pyruvate:ferredoxin oxidoreductase
Sequence:
MPTFVDPSKCDGCKGGEKTACMYICPNDLMILDPEEMKAFNQEPEACWECYSCIKICPQGAITARPYADFAPMGGTCIPLRGSEDIMWTIKFRNGSVKRFKFPIRTTPEGSIKPFEGKPEAGDLENELLFTETALTVPQVALGQKAQIADAETSQCWFDLPCEGGNR
Protein: ADP-ribosylhydrolase ARH1 (EC 3.2.2.19) (ADP-ribose-L-arginine cleaving enzyme) ([Protein ADP-ribosylarginine] hydrolase) (ADP-ribosylarginine hydrolase) (P54923)
Organism: Mus musculus (Mouse)
Function: Specifically acts as an arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins.
Interaction partners:
Sequence:
MGGGLIERYVAAMVLSAAGDTLGYFNGKWEFIRDGETIHQQLAQMGDLEAIDVARWRVSDDTVMHLATAEALMEAGQSPDLPRLYSLLAKHYRDCMGDMDGRAPGGACMQNAMLLQPNRADGYRIPFNSHEGGCGAAMRAMCIGLRFPHPSQLDLLIQVSIESGRMTHHHPTGYLGSLASALFTAYAVNGKSPWQWGKGLMEVLPEAKKYITQSGYFVKENLQHWSYFEKEWEKYLELRGILDGNSAPVFPQPFGVKERDQFYIDVSYSGWGGSSGHDAPMIAYDALLAAGDSWKELAHRAFFHGGDSDSTAAIAGCWWGVMYGFKGVNPANYEKLEYRQRLEEAGRALYSLGSKEDPVLDP
Protein: Spore wall maturation protein DIT1 (P21623)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in spore wall maturation. Catalyzes a two step reaction that leads to the LL-dityrosine containing precursor of the spore wall.
Interaction partners:
- Cytochrome P450-DIT2
- Sporulation-specific wall maturation protein
- GLC7-interacting protein 1
- pH-response transcription factor pacC/RIM101
- Putative uncharacterized protein YJR037W
- Meiosis-specific protein ISC10
- Outer spore wall protein 2
- Outer spore wall protein 1
Sequence:
MTFTSNLPSSSEQSISPPASSFSSSTDTLKDIDIPHNGADLSTYSKFLALYCRSDKCDDFYSLEEKQNCKFGDQWLDFINTIHNLDFSESEVSGRVSERILPASLANKFTNNLGVAIKISEYTRDDERQIRGCVTTVENENSFNNWFVYHILDQSQLSLSEHPIVTKEVKYHELFADFFEKNLKNTIVNDQWNFGGRDYFIERSRYFTDRYLRIECILPAFPCKSSNEQKVYGSVPDKGEELALKRLIKATQDLVKIYPPGMKIWIVSDGHVFSDCIGVDDDVVSTYTTKLHELYKRVAIPGVDAIGFCGLNDLFFSGAASKVFDPKWVSDVEVAHYTGTQICPKSDLSRQILMKGCDTDAGRLRKQIAIEGHPRLHLYRGFSRFMMEDLSLLEHFQSYSRKKFKKIISMIAFNMIKRNDAYSNLVELIFPHHLRISIHAHTNSGPKFGIKVISNEQCSIVSSLEDLDEPKFEDFLHIPTPWHNCVVKVEDEKEKYFLTKSKVVKEALEKGMYDGVWKDTRFDIGEGGHFVIKKIS
Protein: Uncharacterized protein (Q387Q6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Kinteoplast poly
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Small ribosomal subunit protein mS41
- Enoyl-CoA hydratase/isomerase domain-containing protein
- Uncharacterized protein
- 30S ribosomal protein S8, putative
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MRRSGRGSAVRWSSLCKCQCCLYRTPLGGTYFEQALPRSLGARQGKGVLSTVNTALSRKALKRRQSLPRKKLNVPLTAEGLKERLKQLSAEERELSIKNNTEECDEPSPNEFTTTHEARVALARVLHHGENAGEREEVAMRIPSFCRSPAVSETQSIVVDDKEGDITNAAVHVGCSVLGSDLDHLERDMIRDYHQRGKKLPTFDNIYRTLGCGRKGTSVSDTEPENENSSGAIQSESGLGDAGRRGTVVVAPSHLHHSRPPTKGRSGKEEEEGGYFDTNTLPADANPHFPPGACDNEVLAPLSGGCAASEQSEITDTASFIPSNSRLSTAVYDAYRQRPADDRLVVLRGTDFWDNEENRARLQELTDYAEEDFAREMLMEGAMDTSEVGYSTNKVRKETLLYFQAHPINEMIQEPFARVRSILPSDGGPEVHFPADDPDTDVDIPTAQARTMARELGLALIRVGTLYTPINDRRVVAVCTIADHREHMRDMIRFKIKKLGVQRPPTKEGIEVPFRGGTHPHAVRFKSIGIAKHLLLGHVVRINLTDFGTVREGFPVFGSILDEVARQALQLRAYHTAGVVRANYNEVYCYLYPSTGRSPKSTVLHPTQEQLATVRDRCLLEREREVYFDGLYDKKTPRERLTYMRKLQDGTAWADRDDGLSLQRQRDMKVMLGYLPKGNHELYAARGDVNVPAPFRASHPTSVDRWTHPQESNLEQAARGSAVLAKRLSMTVSEMHDRQETAENPATLDRFYYRIQGPALEAGELKEALGLKGNRKRLPRRAPGWATLGMEKVSPQEPGHAAK
Protein: RELA proto-oncogene, NF-kB subunit (A0A087X0W8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFSGPTDPRPPPRRIAVPSRSSASVPKPAPQPYPFTSSLSTINYDEFPTMVFPSGQISQASALAPAPPQVLPQAPAPAPAPAMVSALAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS
Protein: AP-1 complex subunit gamma (Q8WQB3)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029433}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
- AP complex subunit beta
- MHD domain-containing protein
- AP complex subunit sigma
- AP-1 complex subunit mu-1-I
- Probable clathrin heavy chain 1
- ADP-ribosylation factor 1-like 1
- AP complex mu/sigma subunit domain-containing protein
- ADP-ribosylation factor
- RAP domain-containing protein
- AP-2 complex subunit mu
Sequence:
MATAVELAIEKIDEYKSKIGRTLGTPMRLRDLIRQVRAARTMAEERAVVDRESANIRESFRDDDSPWKCRNIAKLLYIHMLGYPAHFGQMECMKLVAHPRFTDKRIGYLGAMLLLDERSEVHMLVTNSLKNDLTCSTQFVSGLALCTLGSICSAEMCRDLANEVEKIIKQNNAYLKKKAALCAFRIVRKVPELMEVFIPCTRSLLGEKNHGVLMGATTLVTEMCEKSPDVLNHFKKLVPNLVRILKNLLMSGYSPEHDVTGISDPFLQVKILRLLRVLGKDDVRVTEEMNDILAQVATNTETAKNVGNAILYETVLTIMEIKSESGLRILAVNILGRFLLNTDKNIRYVALNTLLKTVHVDYQAVQRHRNVVVECLKDPDISIRKRAMELCFALMNRTNIAIMTKEVLIFLETADAEFKSECASRMYIATERYSPNHEWHLDTMITVLRLAGKYVPDEVVSCMIQMISANEQLQSYAVSQLYHAAQKDAINAQPLLQVAFWTIGEFGDLLLQPTDVDSTPISENDVVGVFESVLPSALTSLWTKCYGVTALAKLGTRFQSTGDRIGALVRMNQAHIQLELQQRSVEFNVILNLGDLRDGLLERMPVITHNSLNAAAPSMIDEEVSAESGAPVVTNGDLLGDLNLGGGGSTNPSNDYSSDLLGVGVGSGAASAQAPPPPPPPTSNSNILDIFGDTPSSNAAGGFDFGMAAPAKEPTYQPVIAINKGGIEVQLQVIETWKNEKARLRMTAYNYTPRTLSNYNFFAAVTKTFEIALEPASSPNIDPNEHTTQFMTITRKAPNTTARMRTKISYIVDGTEQVGEGVVNEFPGL
Protein: INO80 complex subunit E (Coiled-coil domain-containing protein 95) (Q8NBZ0)
Organism: Homo sapiens (Human)
Function: Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:18922472}.
Interaction partners:
- Actin-related protein 5
- Nuclear factor related to kappa-B-binding protein
- Chromatin-remodeling ATPase INO80
- TCF3 fusion partner
- INO80 complex subunit B
- INO80 complex subunit D
- INO80 complex subunit C
- Actin-related protein 8
- RuvB-like 1
- RuvB-like 2
Sequence:
MNGPADGEVDYKKKYRNLKRKLKFLIYEHECFQEELRKAQRKLLKVSRDKSFLLDRLLQYENVDEDSSDSDATASSDNSETEGTPKLSDTPAPKRKRSPPLGGAPSPSSLSLPPSTGFPLQASGVPSPYLSSLASSRYPPFPSDYLALQLPEPSPLRPKREKRPRLPRKLKMAVGPPDCPVGGPLTFPGRGSGAGVGTTLTPLPPPKMPPPTILSTVPRQMFSDAGSGDDALDGDDDLVIDIPE
Protein: Non-reducing polyketide synthase aoiG (EC 2.3.1.-) (Q2TXQ8)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
Sequence:
MVNIYIFGDQTVRVDDAVHKLLHVKNNPILKSFLDGSFAAIRKQIFLLPANERTSLPDAHTLPLLLEAVRRGRRHVALESALVCLCEIGQYIALLQTTDLCHPPTGSILVGFCTGSLAAAAVSCVRTSIDLLTLGIEAVVVAFRVGMHVARRANALGGDGGSQWKPWSLAVTDGSESETEKILEEFTRDEVSGVHVANRHDAYILAKGLPAIMKPYVSAAGSNTLTISGTPRVLEALKASPHLRGTKSLPVSIYAPYHAAHLYNEADVESIFACKPVESALFHRELRTPLISCATGTVLKEKTFGDLLRALVMEILTCQIRFDKVEESIVQHTPGATAQLIPIHTNIAPRMKTSLTQVGLQVECFKAIANQEPAAEALSESPSNDSSKIAIIGFSGRFPEADGLNEFWELLQQGLDVHKPIPADRFDLEAHYDATLREKNTSRIKHGCWIRSPGSFDARFFQMSPREACQTDPAQRLALLTAYEAMEMAGFVPDRTPSSQRDRVGVYYGMTSDDWREVNSSQDIDTYFIPGGIRAFVPGRINYFFKFSGPSITVDTACSSSLAAIHTACNALLNSDCDTALAGGTNILTNPDNFAGLDRGHFLSSTGNCKTFDDDADGYCRADGVGTVILKRLQDAIADNDPIFGVIVGARTSHSAEAVSITRPLADAQAHLFRKLLAESGIHPHEISYIEMHGTGTQAGDAVEMKSVLDSFARDDSRAPDRPLHLGSVKANVGHGESASGVTALIKVLLMMQKNRIPPHCGIKGRINRHFPTDMEYRNVHIPFMETDWTRPQEGKRRSFINNFSAAGGNTAVLVEDAPLLEQSRAISSPDPQRYHVITLSARSVRSLSKNMRALGEFIGSETSPGLLARIAYTTTARRMHHSYRVAFVGNDLQEVKRRFLDTDVTEAIKPCPTKSPGVGFLFTGQGAQQTAMARELYDRFTSFRADILEFEAVGRGHGFPSILPLITGAVDVEELSPMIVQLGTVVIQIAMARLWQTWGLTPEYALGHSLGEYAALQIAGVLSISDTIYLAGSRAALLEKRCTAGSHGMLAVKASVAHLEEALKGMQVEVSCINGFDDTVLSGTNDEIDRASKELSELKVTFKRLILPFAFHSSQVDPILEELEHIASQLSFQPPRIPIVSPTVGHIITDEGTIGAQYIRRHCREPVNFLGAIQAAQGSGICNSGALAVEIGAHPILTRMMKAAVGSSVTVCSTLSHREDMFKTLTESLSVLHLAGVRLNWDEYHRDFNNQVVMLPAYSWDYQDYWIQYQNNFCLTKGSPERSESVDAIQPMSTRLSPSVQKILEEEMTAAQASIIIESDITDPELLPVALDHKVNGVTLCPSSLYADIGHTLGTYLLGKKEDVTDYKIDVSNMAVEKALVVKGTGPQLFRASLDMDWNMLRGMMKVYSVNNMGTLTTHHAQCTIELQRPHQWQEGWNRQLYLIQRSIEQLKKGVEEGWTHKMRRGVAYRLFSSMMQYGPSYQAMEEVIFDSSGLEATAQVRLQSTTGRYSFNPVWSDSLGHITGFVTNCNDSIDLTENLFVNHGWGFMRCVEPFSPDTVYQTHVKMQPVDGNNGFYVGDVYVLNDHRIIAQYGAVTFQKVARRVLEMLLPATTSKGRSSNIRPRNVGTAQSAKIVQSKRRTQTPHVEDAWQQVLEMIARELGVDPGQLTEDVNFTDMGVDSLMSLTIIGNFREFLSLDVPWSLFEDCPSVQSLRIYLNMSSLSESDSIETSSYPTPDESTTTTITSPSGSDRNVGRNSGIDGVGTTVGLVLSILAEEIGVNVRDLSNADGLSELGLDSLLSITALGRVRDETDLDLPSDFFLEHSSVAAITAALHAIFGSTEQGPEQSLITSHPPAMSINLQGDEGCPQTLFLFPDGSGSSTSYSALPTISKDVRVYAMDCPYLKRPNELAKCQLQDLTPVYVAEIRRRQLRGPYSLGGWSAGGIAAYEAAQYLVDQGERVERLILIDSPNPMGLGKCPPHFYRFLEEAGVFGVHGGRKPPAWLLQHFQAFNDVLSQYTLEPFRPADATPNTTLIYAQDGVCKSPRDPRPERHPGDPEVFSWLLENRVDMSCNGWDQLLGEDNIHLGTVFDANHFTIVRTPAVVRLSEIVRMAMSRKFQ
Protein: Cilia- and flagella-associated protein 45 (A0A480NP79)
Organism: Sus scrofa (Pig)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity). It is an AMP-binding protein that may facilitate dynein ATPase-dependent ciliary and flagellar beating via adenine nucleotide homeostasis. May function as a donor of AMP to AK8 and hence promote ADP production (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:33139725}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:33139725}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9UL16}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q9UL16}. Note=Located in the proximal region of respiratory cilia. {ECO:0000250|UniProtKB:Q9UL16}.
Interaction partners:
Sequence:
MPLSPAGVLSSTSTASNRSRNRPRYRTKALSSEVDESLFGGIKPLNQSDSPIVLLRDKHAIRKTLTALGLDHKPETIQLITRDMVRELIIPTKDPSGESLIMSPEEFERIRWASHVPTREELEAKEQACKKEKEAIVDAVTTRKKIMKQKEMVSRNNQKLSDLEEVAKERAQNLLQRASQLRMEQEEELKDMKKIILNAKCHAIRDAQILEKQLIQKELDAEEKRLDQMMEVERQKSIQRQEELDKKRREERIRGRRHIVEQMEKNQEERSLLAEQREQEKEQMLEYMEQLQEEDLRDLERRHQQKLKMQAEIKRINDENQKQKAELLAQEKLADQMVMEFTKKKMAREAEFEAEQERIRREKEKEISRLRALQEKVQDYQAEQDALRAKRNQEVADREWRRKEKENAQKKMETEAQLRKSRLEQVAFKEHSLAVQVQRDRDEFERILRAQREQIEKEQQEEEKKAMERLQHANELRRQVRENQQKQVQDRIAIFEEGQRLKEEAQKRRERIEGIKKKKIEELRATGLPEKYCIEAERKANIPTNTSVN
Protein: 7SK snRNA methylphosphate capping enzyme (MePCE) (EC 2.1.1.-) (Bicoid-interacting protein 3 homolog) (Bin3 homolog) (Q7L2J0)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA (7SK RNA), leading to stabilize it. Also has a non-enzymatic function as part of the 7SK RNP complex: the 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC). In the 7SK RNP complex, MEPCE is required to stabilize 7SK RNA and facilitate the assembly of 7SK RNP complex. MEPCE has a non-enzymatic function in the 7SK RNP complex; interaction with LARP7 within the 7SK RNP complex occluding its catalytic center.
Subcellular location: Nucleus {ECO:0000269|PubMed:19906723}.
Interaction partners:
- La-related protein 7
- Protein HEXIM1
- Protein HEXIM2
- Cyclin-dependent kinase 9
- Cyclin-T1
- Spliceosome associated factor 3, U4/U6 recycling protein
- Bridging integrator 3
- Cyclin-T2
- U4/U6 small nuclear ribonucleoprotein Prp3
- U4/U6 small nuclear ribonucleoprotein Prp31
Sequence:
MIEMAAEKEPFLVPAPPPPLKDESGGGGGPTVPPHQEAASGELRGGTERGPGRCAPSAGSPAAAVGRESPGAAATSSSGPQAQQHRGGGPQAQSHGEARLSDPPGRAAPPDVGEERRGGGGTELGPPAPPRPRNGYQPHRPPGGGGGKRRNSCNVGGGGGGFKHPAFKRRRRVNSDCDSVLPSNFLLGGNIFDPLNLNSLLDEEVSRTLNAETPKSSPLPAKGRDPVEILIPKDITDPLSLNTCTDEGHVVLASPLKTGRKRHRHRGQHHQQQQAAGGSESHPVPPTAPLTPLLHGEGASQQPRHRGQNRDAPQPYELNTAINCRDEVVSPLPSALQGPSGSLSAPPAASVISAPPSSSSRHRKRRRTSSKSEAGARGGGQGSKEKGRGSWGGRHHHHHPLPAAGFKKQQRKFQYGNYCKYYGYRNPSCEDGRLRVLKPEWFRGRDVLDLGCNVGHLTLSIACKWGPSRMVGLDIDSRLIHSARQNIRHYLSEELRLPPQTLEGDPGAEGEEGTTTVRKRSCFPASLTASRGPIAAPQVPLDGADTSVFPNNVVFVTGNYVLDRDDLVEAQTPEYDVVLCLSLTKWVHLNWGDEGLKRMFRRIYRHLRPGGILVLEPQPWSSYGKRKTLTETIYKNYYRIQLKPEQFSSYLTSPDVGFSSYELVATPHNTSKGFQRPVYLFHKARSPSH
Protein: Branched-chain-amino-acid aminotransferase, mitochondrial (BCAT) (EC 2.6.1.42) (Protein ECA39) (Protein TWT1) (P38891)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the biosynthesis of the branched chain amino acids leucine, isoleucine, and valine. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using branched chain amino acids (leucine, isoleucine, and valine) as the amino donors. Appears to be involved in the regulation of the transition from G1 to S phase in the cell cycle. High copy suppressor of a temperature-sensitive mutation in the ABC transporter, ATM1.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:21267457, ECO:0000269|PubMed:8798704}.
Interaction partners:
- Dihydroxy-acid dehydratase, mitochondrial
- 2-isopropylmalate synthase
- Branched-chain-amino-acid aminotransferase, cytosolic
- 2-isopropylmalate synthase 2, mitochondrial
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Threonine dehydratase, mitochondrial
- Homocysteine/cysteine synthase
- Putative cystathionine gamma-synthase YML082W
- 3-isopropylmalate dehydratase
- Cystathionine gamma-synthase
Sequence:
MLQRHSLKLGKFSIRTLATGAPLDASKLKITRNPNPSKPRPNEELVFGQTFTDHMLTIPWSAKEGWGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSAARICLPTFESEELIKLTGKLIEQDKHLVPQGNGYSLYIRPTMIGTSKGLGVGTPSEALLYVITSPVGPYYKTGFKAVRLEATDYATRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNLWLFGPEKNITEVGTMNVFFVFLNKVTGKKELVTAPLDGTILEGVTRDSVLTLARDKLDPQEWDINERYYTITEVATRAKQGELLEAFGSGTAAVVSPIKEIGWNNEDIHVPLLPGEQCGALTKQVAQWIADIQYGRVNYGNWSKTVADLN
Protein: Transcription regulatory protein motB (Q01437)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Compacts the host nucleoid. Probably dysregulates hundreds of host genes including derepression of most of the H-NS regulon. Plays a role in the transcriptional regulation of middle promoters.
Interaction partners:
Sequence:
MIINIGELARVSDKSRSKAAGKLVEVVSIQLKHGVKDEDSEVKVRIIPKDGKSKPQFGYVRAKFLESAFLKAVPAKGIETIDTSHVGVDFKWKLGQAIKFIAPCEFNFIKDDGRVVYTRAMCGYITDQWVEDGVKLYNVVFLGTYKVIPESWIKHYSNALYA
Protein: Regulatory protein E2 (P06422)
Organism: Human papillomavirus type 8
Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001}.
Interaction partners:
Sequence:
MENLSERFNVLQDQLMNIYEAAEQTLEAQIAHWLLLRKEAVLLYFARQKGITRIGYQPVPPLAVSEAKAKQAIGIMLQLQSLQKSEFADEPWTLVDTSIETYKNAPENHFKKGATPVEVIYDKQPDNANVYTMWKHIYYTDADDKWHKTTSGVNQTGIYYMQGSFRHYYVVFADDARRYSATGEWEVKINKDTVFAPVTSSTPPGSPPGQADTDTAAKTPTTSADSTSRQQRSPAKQPQQTETKGRRYGRRPSSRTRPQKEQRRSRSRHRTRSRSRSLSRVRAVGSTTVSRSRSSSLTKAVRPRSRSRSRGRATATSRRRAGRGSPRRRRSTSRSPSTNTFKRSQRGGGRRGRGRGSRGRRERSSSTSPTPTKRSRGESSRLRGVSPSEVGRSVQSVSAKHTGRLGRLLDEAIDPPVILVRGEANTLKCFRNRARVRYRGLFKYFSTTWSWVAGDSTERLGRSRMLILFTSAGQRKDFDETVKYPKGVDTSYGNLDSL
Protein: Histone deacetylase HDT4 (HD-tuins protein 4) (Histone deacetylase 2d) (Q9M4T3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably mediates the deacetylation of lysine residues lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Subcellular location: Nucleus, nucleolus {ECO:0000305}.
Interaction partners:
- Histone deacetylase 6
- Histone deacetylase 19
- Telomere repeat-binding factor 2
- Histone deacetylase 7
- Histone deacetylase 5
- Histone deacetylase 14, chloroplastic
- Histone deacetylase 2
- Histone deacetylase 15
- Histone deacetylase 8
- NAD-dependent protein deacylase SRT2
Sequence:
MEFWGIEIKPGKPFKVIQKDGFMVHASQVTLGDVEKVKKDETFAVYVKIGDDENGFMIGNLSQKFPQFSIDLYLGHEFEISHNSTSSVYLIGYRTFDAFDELDEEIDSDSELDEYMEQQIAALPQNEINPEEDDESDSDEMGLDEDDDSSDEEDVEAEAPLKVAPPSKKMPNGAFEIAKGGKKNKSSGGKKRCPFPCGPSCKK
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (Q9VMT1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Protein decapentaplegic
- Protein mothers against dpp
- Protein 60A
- Protein screw
- Serine/threonine-protein kinase receptor
- Inhibin beta chain
- receptor protein serine/threonine kinase
- receptor protein serine/threonine kinase
- Schnurri, isoform F
- Mothers against decapentaplegic homolog
Sequence:
MRLQLVALELQATSGTADGLFEEIALEALTRSEFSANVQPDVEAMAAAALSGMEMGSGPGSEGYEDADNEKSKTVENARSLTCYCDGSCPDNVSNGTCETRPGGSCFSAVQQLYDETTGMYEEERTYGCMPPEDNGGFLMCKVAAVPHLHGKNIVCCDKEDFCNRDLYPTYTPKLTTPAPDLPVSSESLHTLAVFGSIIISLSVFMLIVASLCFTYKRREKLRKQPRLINSMCNSQLSPLSQLVEQSSGSGSGLPLLVQRTIAKQIQMVRLVGKGRYGEVWLAKWRDERVAVKTFFTTEEASWFRETEIYQTVLMRHDNILGFIAADIKGNGSWTQMLLITDYHEMGSLHDYLSMSVINPQKLQLLAFSLASGLAHLHDEIFGTPGKPAIAHRDIKSKNILVKRNGQCAIADFGLAVKYNSELDVIHIAQNPRVGTRRYMAPEVLSQQLDPKQFEEFKRADMYSVGLVLWEMTRRCYTPVSGTKTTTCEDYALPYHDVVPSDPTFEDMHAVVCVKGFRPPIPSRWQEDDVLATVSKIMQECWHPNPTVRLTALRVKKTLGRLETDCLIDVPIKIV
Protein: E3 ubiquitin-protein ligase CBL-B (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene b) (RING finger protein 56) (RING-type E3 ubiquitin transferase CBL-B) (SH3-binding protein CBL-B) (Signal transduction protein CBL-B) (Q13191)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. Slightly promotes SRC ubiquitination. May be involved in EGFR ubiquitination and internalization. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBL, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12177062}. Note=Upon EGF stimulation, associates with endocytic vesicles.
Interaction partners:
- Tyrosine-protein kinase ZAP-70
- Epidermal growth factor receptor
- SH3 domain-containing kinase-binding protein 1
- Polyubiquitin-C
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Growth factor receptor-bound protein 2
- Ubiquitin-conjugating enzyme E2 D2
- Tyrosine-protein kinase SYK
- E3 ubiquitin-protein ligase CBL
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFGMPMLDLDDDDDREESLMMNRLANVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPPERPPPIPPDNRLSRHIHHVESVPSRDPPMPLEAWCPRDVFGTNQLVGCRLLGEGSPKPGITASSNVNGRHSRVGSDPVLMRKHRRHDLPLEGAKVFSNGHLGSEEYDVPPRLSPPPPVTTLLPSIKCTGPLANSLSEKTRDPVEEDDDEYKIPSSHPVSLNSQPSHCHNVKPPVRSCDNGHCMLNGTHGPSSEKKSNIPDLSIYLKGDVFDSASDPVPLPPARPPTRDNPKHGSSLNRTPSDYDLLIPPLGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFVDLASGQVPLPPARRLPGENVKTNRTSQDYDQLPSCSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFPPPVSPRLNL
Protein: Ufm1-specific protease 1 (UfSP1) (EC 3.4.22.-) (Q6NVU6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:35926457}.
Interaction partners:
- Ubiquitin-fold modifier 1
- Ubiquitin-fold modifier-conjugating enzyme 1
- Ubiquitin-like modifier-activating enzyme 5
- E3 UFM1-protein ligase 1
- DDRGK domain-containing protein 1
Sequence:
MEPLRDVHVGLSPPSRGPVRLALLSGHYLYYHYGCDGLDDRGWGCGYRTLQTLCSWPEGQPAGVPGLAAVQAALEDMGDKPPGFRGSRDWIGCVEASLCLAHFGGPQGRLCHVPRGVGLHGELERLYSHFAGGGGPVMVGGDADARSKALLGVCVGSGTEAYVLVLDPHYWGTPKSPSELQAAGWVGWQEVSAAFDPNSFYNLCLTSLSSQQQQRTLD