wanglab/gogpt-training-data huggingface dataset:
Protein: Protein pangolin, isoform J (dTCF) (Q8IMA8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Segment polarity protein. Functions together with arm to transduce the Wingless (Wg) signal in embryos and in developing adult tissues. Acts as a transcriptional activator, but in the absence of arm, it binds to gro and acts as a transcriptional repressor of wg-responsive genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:9783586}.
Interaction partners:
- Armadillo segment polarity protein
- Protein groucho
- Mitogen-activated protein kinase
- Protein wingless
- Protein BCL9 homolog
- Protein pygopus
- histone acetyltransferase
- Mothers against decapentaplegic homolog
- C-terminal-binding protein
- Axin
Sequence:
MPHCGTTNSEINLNSNELISYQKKKSNEDLQKKHDKKCSINLKTSQVPDGGFNNQYTQLTANKIEQYNCNDLDKVCIVPSSRSDGMEASFSELLLSPNKLISQPWQTAEEIENWQNDSFRQRNEMFSCIYTNSMLNQQPCSQQQLLATQLLYARLLRSQLAEREFHSNKFNMVHYSGSKKTMLREDELLSTPSSQDNNNNIKLIKDIENSISCVDPPLFEFSNVHQRAEQKNKQDDKNCYSPKLKSNKEALDGYDLQHTCDFIREQKNILIDIKKKLDNLSDSSGKFRKRLSVRQSHIEVNNGSNSALEESVRRQLNGNRKSIENLLEEVKRLYNQWSSAELYYVRSLQRLGLPSEEDGEYTSTPTHTIMALAAIALSNESILPQKTNAVHSKIPDVESESDFFLTSAKPKTLVEIEDIILQLASSVNMHQSSSASTPHESYSDSVKSDCEESNSAPTCIWHSTRQTFRHKKDVEPCSTAAEIILEYASLSSSSNIETSRLLTSASNLTDVTENYNVTTQLPIVFNYNRESSAESIVTDPLLVPEFSTAPSTPSTGSNSGCSTGMVSGIFGLSQNRRKQRLARHIETLTTNSFKSNAIRGNVDNEITNQLKTSPSIRALPTENVSHLITKTLSSANASLTAQELSITNLFKERLCALQGNAGSMKTEIFPMIDAPYDLSIGSKTKHMNLEAKHTSNAQSNESKETTNDKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHELSREEQSKYYEKARQERQLHMELYPGWSARDNYGYVSKKKKRKKDRSTTDSGGNNMKKCRARFGLDQQSQWCKPCRRKKKCIRYMEALNGNGPAEDGSCFDEHGSQLSDDDEDDYDDDKLGGSCGSADETNKIEDEDSESLNQSMPSPGCLSGLSSLQSPSTTMSLASPLNMNANSATNVIFPASSNALLIVGADQPTAQQRPTLVSTSGSSSGSTSSISTTPNTSSTVSPVTCMTGPCLGSSQERAMMLGNRFSHLGMGLSPPVVSTSTSKSEPFFKPHPTVCNNPIFALPSIGNCSLNISSMPNTSRNPIGANPRDINNPLSINQLTKRREYKNVELIEASESKTIVAHAATSIIQHVAVNGYHANHSLLNSNLGHLHHQLNNRTENPNRSEQTMLSVSNHSVNSSECHKESDSQAIVSSNPPNAGSSDNGVISVS
Protein: Replication protein A1, large subunit (Q9U0J0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 3'-5' exonuclease
- Replication factor A protein 3, putative
- Spindle assembly abnormal protein 6, putative
- DNA repair protein RAD51 homolog
- DNA repair endonuclease XPF, putative
- DNA topoisomerase
- Double-strand break repair protein MRE11
- Telomerase reverse transcriptase
- DNA polymerase
- DNA polymerase
Sequence:
MMSKNEEILSKATPNFIYKFFTEPNSQESLKWLNGEINLICFSQMNAGANQTFLKVIDGSIPPQYYAIVHLGIEENNSTISYVKKIISIENFSITNYYGKLFILAKKVTVYLNIDHFDIEDLFKKYHLQSISYFLLNSKNENNSRENYSRIVKDSNNNMNNVNNVNNVNNMNNMNSMNSVNNMNSMNSMNNSTHNVGSSNGGAGGYNNRDDNKLRENYTHSNDDNINHTNIKDNYYYSRDNNYHNNNNINNSSSSRGEKWEQVRDNYKSNEYFNNNGKAYNHNVHNRQNSEHIMKENNNKNFTTPIHMNEDNRIDKQQNYMDNNNNNNMDKPNRGKFVYKENPNIPNYTNVNDYESKNNLHKPFPVQKSASAYKGPSEYSEYNRNNMCYENNSPGNEAYNKNSRAYINKNNYDNNNNNNNNYYYYHHHNNMNTNSRQATNNQPYDYNNHNRDYDNKNVNKYSDGIKDNSCYNKNEESSKMYMNSNCLPHTTSIVKLNRCDESLHERYFSIDNNNNMNNMSNVNNMSNVNNVNNVNNVNNVNNVNNVNNVNNVNNVSNNNSVIMDHPSGNYNHENDPNNHHNYNNHNNYHTYDRHVNPSNNHQHYNNKDEYTYTNNEDCHLKIRKDDMGSNQESRDYNYYDENSMDNIMKKDEKILKDKTLNRNNRKITPYQSNAVIKMNDGILMQINKLSQYSSKWIIKARVQSKDNIRRYTSGSKEGKVFNIELCDEDGEIKANFFGKAVDKWFDFIEVGKIYKISKGMIKVANKKFNTLNHDYEITLDENSLIEILDEENENIPKYNYNFISIDNIKNMNTGSFVDIIAVVLNYQEKMQIFVKKTGQYKDKRDVTLIDESFDTIQVTLWEKNATIIDEMNLRDNCIVCFKYLKIGEWQGKKLESHARTKIEINPDNIEKAYILKNWWIHNKKMICNSINLSSNYINIETQKTIQEIKKNVNLVNEEALSGKGIMFTTYGFIDQIYNNMPVYSACPDCNKKMISNSVDDNEYEPSSNLLEETMYCAKCNKNNIPVYNYYINLKITDSTDSIRASAFANCAKIIMNGLSAEEYMKLRQEYIMQENIENFDIIEKIKLNEFFFRIKVYMTSHMDELKKNYTIIDIAPVGKLLIDNCRYLIKSIKNLTSKRDTDHDE
Protein: Probable cyclic nucleotide-gated ion channel 14 (Cyclic nucleotide- and calmodulin-regulated ion channel 14) (Q9SJA4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable cyclic nucleotide-gated ion channel.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Chloroplastic calcium uniporter protein
Sequence:
MEFKRDNTVRFYGDEKQTIEVGEKRVPLFKSTTAPFMKQEVLPKKSKTRLKIPRFGRFKVFPENFEIERDKILDPGGDAVLQWNRVFLFWCLVALYVDPLFFFLSSVKRIGRSSCMTTDLKLGIVITFFRTLADLFYVLHIVIKFRTAYVSRTSRVFGRGELVKDPKLIARRYLRSDFIVDLIACLPLPQIVSWFILPSIRSSHSDHTTNALVLIVLVQYIPRLYLIFPLSAEIIKATGVVTTTAWAGAAYNLLQYMLASHILGSAWYLLSIERQATCWKAECHKESVPLQCVTDFFDCGTLHRDDRNNWQNTTVVFSNCDPSNNIQFTFGIFADALTKNVVSSPFLEKYLYCLWFGLQNLSSYGQNLSTSTSVLETMFAILVAIFGLVLFALLIGNMQTYLQSITVRLEEWRLKRRDTEEWMGHRLLPQNLRERVRRFVQYKWLATRGVDEETILHSLPADLRRDIQRHLCLDLVRRVPLFAQMDDQLLDAICERLASSLSTQGNYIVREGDPVTEMLFIIRGKLESSTTNGGRTGFFNSITLRPGDFCGEELLAWALLPKSTVNLPSSTRTVRALEEVEAFALQAGDLKFVANQFRRLHSKKLQHTFRYYSHQWRTWAACFVQVAWRRYKRKKLAKSLSLAESFSSYDEEEAVAVAATEEMSHEGEAQSGAKARHHTSNVKPHFAATILASRFAKNTRRTAHKLKDVEIPMLPKPDEPDFSVDD
Protein: PAB1-binding protein 1 (Ataxin-2 homolog) (Poly(A)-binding protein-binding protein) (Q57UZ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Involved in post-transcriptional regulation of gene expression. Promotes mRNA stabilization by bridging poly(A)-binding protein to mRNAs.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24470144}. Cytoplasm, Stress granule {ECO:0000269|PubMed:24470144}. Note=Localizes to polysomes (PubMed:24470144). Localizes to starvation-induced stress granules but not heat shock-induced stress granules (PubMed:24470144). {ECO:0000269|PubMed:24470144}.
Interaction partners:
- Sm protein B
- Probable eukaryotic initiation factor 4A
- Post-transcriptional regulator MKT1
- F-box domain-containing protein
- Polyadenylate-binding protein
- RNA-binding protein, putative
- Polyadenylate-binding protein
- RNA-binding protein, putative
Sequence:
MEGSHSSNMERLEYLYLNLVGQVVQVRLVDDMCVEGLFVACTDVDAETDAGIMICCTRNLASAKRSPLSPSCVNFTDDLFIPYQSIVMIEVQNAKIRTETPGRPDTGRADFSATKFDWADDGVSELLESEPHQTGTWNQFEANEKSFGVKTTYKEEFYTTRLDHSKITEEQRAQADRLAREIESSSTRGIAHRMEREECLHDDEGLDEGQLYSDVHRPQEKKPPYVPPSTGGRKLVNEPPPVPAAAAPATAPTTAPAAAPAPAAAPPAAAPAAAAPPPPPAATSMADDGSMRHKRMNEDPHHMQYDANQTAAGFNPAAAPYTPMKPGAAVPVVDFLASLADAISNNDMCYDCEPHWPGMCNLFYDQDDSSYSQQNYEAAAMPPSHSMNMHMYVNSQPNIPNAHRGYQGPLGRVPHNQSMPMHHMQGQGFHHEMHHHQAFHGMGNYSSQHHNPPIQEYAPHKGQQGVVSRPGMRQGKGGGASRVEPQQPVSANTASSPPPVPTVDSAPNEVKPPAKLQRGRGMAAFTKGDMDGDSGATTNATGGPKKRVGK
Protein: MIF4G domain-containing protein (B5BM23)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPYQPAQPAQQQMTHTAPQEPKRQRKALEIVDPTTKKAIEVTPHLAPAAPAPAAPAAPIAPEEEKKKQNITLEFLNQVKNELHHEDRRHDNPPAVPAAVPAAVQAAVLPNFSVPPPALGQTPPAASIAPQVVPSVPKTPEAPAKADYEVKQAETLVTPVSSPHASDTTTTTPASGTAESASTVADVRVTPTLTKEESKEETDDDKFEENDERESTPDVADSSTEKTPEELEIEKAQKEAEEIEKKKLREEALEKRIEELILAGSAVISDGTFGRDFMVTIREIEKVFSRTPCPLSPAQLADFGLDIKTMRVSDNKKPNFTPNWANKGGNRQQVPYRGRTTTDGTGRGGQQQRDRMHNKRPPVVRPSIERVQRVTLPSSKDAWKPDRQKTAEAVASEEAAVIEVCKKVRSLMNKVTPTSQRPLTEEFISYNVSSNDAQLAQVVEIVFDKAVEEPKFCALYAEMCKAQANHELSQTGGKSAFRNKVLTRTQMTFQDKKDIDADKLAIIEKEEDPVKKELMLAEEKQKFRRRKFGVMTFMGYLYRNQLLSTKIVQTCTFELFNSIKDQDIKKEDVDEESIHCGLQLIETVGVMLDKSKDSTTVFLDQWFQKLEAAKPYCSNKIRFMIMNLMELRKDKWIPRKSTESGPKKIDEIHKDIRQEKIENEKARDQYDRDRDRRHGGVRPNSNSLRKSVPVSRNSLDRNRGMQHPEQKRAAAAANTKLASSSVQPKNISLSSMDNNTLGKSKKEWHSGASGGGNTSSESAVPVKSAWGRRDSNDQRKKSTVDEKQAALAAAKEISAMSISSRRSTSQNSNTDKTDDELTEEEKAVRAKIMNTVKSDLLEMSSGELSQKELVDSITDYVGKEKYGSPSLTVVYEMIIRAVIEKGLKDDDRKKLAIALRMSLVSKTEKQAFIEGATRFCKFANDVELQQDYPKLWTVTGEVLVNTSHAPHDEIGEVESFSLADMKPIFSAAKGEGNKKFDLLVQVLKQLIELELEVTGAAEGISWEFSDMKLKTEMEEGLSAEMEAVTFKNGKTLSSYLTGN
Protein: 13 kDa ribonucleoprotein-associated protein (Small nuclear ribonucleoprotein-associated protein 1) (P39990)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Common component of the spliceosome and rRNA processing machinery. In association with the spliceosomal U4/U6.U5 tri-snRNP particle, required for splicing of pre-mRNA. In association with box C/D snoRNPs, required for processing of pre-ribosomal RNA (rRNA) and site-specific 2'-O-methylation of substrate RNAs. Essential for the accumulation and stability of U4 snRNA, U6 snRNA, and box C/D snoRNAs.
Subcellular location: Nucleus, nucleolus.
Interaction partners:
- Small ribosomal subunit protein eS6A
- KRR1 small subunit processome component
- Small ribosomal subunit protein uS11A
- Pre-mRNA-processing factor 31
- NET1-associated nuclear protein 1
- Small ribosomal subunit protein uS4A
- Small ribosomal subunit protein eS7A
- U3 small nucleolar RNA-associated protein MPP10
- Ribosomal RNA small subunit methyltransferase NEP1
- Pre-mRNA-splicing factor 6
Sequence:
MSAPNPKAFPLADAALTQQILDVVQQAANLRQLKKGANEATKTLNRGISEFIIMAADCEPIEILLHLPLLCEDKNVPYVFVPSRVALGRACGVSRPVIAASITTNDASAIKTQIYAVKDKIETLLI
Protein: Phenylacetate-coenzyme A ligase (EC 6.2.1.30) (Phenylacetyl-CoA ligase) (PA-CoA ligase) (P76085)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA).
Interaction partners:
- Acyl-coenzyme A thioesterase PaaI
- 1,2-phenylacetyl-CoA epoxidase, subunit B
- 1,2-phenylacetyl-CoA epoxidase, subunit A
- 1,2-phenylacetyl-CoA epoxidase, subunit C
- Putative 1,2-phenylacetyl-CoA epoxidase, subunit D
- 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase
- 1,2-phenylacetyl-CoA epoxidase, subunit E
- 1,2-epoxyphenylacetyl-CoA isomerase
- Bifunctional protein PaaZ
- Transcriptional repressor PaaX
Sequence:
MITNTKLDPIETASVDELQALQTQRLKWTLKHAYENVPMYRRKFDAAGVHPDDFRELSDLRKFPCTTKQDLRDNYPFDTFAVPMEQVVRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGSPKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSGGQTEKQAQLIRDFQPDMIMVTPSYCLNLIEELERQLGGDASGCSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEVMGPGVAMECLETTDGPTIWEDHFYPEIVNPHDGTPLADGEHGELLFTTLTKEALPVIRYRTRDLTRLLPGTARTMRRMDRISGRSDDMLIIRGVNVFPSQLEEEIVKFEHLSPHYQLEVNRRGHLDSLSVKVELKESSLTLTHEQRCQVCHQLRHRIKSMVGISTDVMIVNCGSIPRSEGKACRVFDLRNIVGA
Protein: Caspase-8 (CASP-8) (EC 3.4.22.61) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10] (O89110)
Organism: Mus musculus (Mouse)
Function: Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood. Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (By similarity). Binding to the adapter molecule FADD recruits it to either receptor TNFRSF6/FAS mediated or TNFRSF1A. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (By similarity). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (By similarity). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (By similarity). In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-325', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response. Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-D (GSDMD): GSDMD cleavage promoting release of the N-terminal moiety (Gasdermin-D, N-terminal) that binds to membranes and forms pores, triggering pyroptosis. Initiates pyroptosis following inactivation of MAP3K7/TAK1. Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production. May participate in the Granzyme B (GZMB) cell death pathways (By similarity). Cleaves PARP1 and PARP2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12065591}. Nucleus {ECO:0000269|PubMed:12065591}. Note=Translocates into the nucleus during apoptosis. {ECO:0000269|PubMed:12065591}.
Interaction partners:
- FAS-associated death domain protein
- Receptor-interacting serine/threonine-protein kinase 3
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- CASP8 and FADD-like apoptosis regulator
- Receptor-interacting serine/threonine-protein kinase 1
- Tumor necrosis factor receptor superfamily member 6
- B-cell lymphoma/leukemia 10
- Caspase-1
- Caspase recruitment domain-containing protein 9
- Caspase-3
Sequence:
MDFQSCLYAIAEELGSEDLAALKFLCLDYIPHKKQETIEDAQKLFLRLREKGMLEEGNLSFLKELLFHISRWDLLVNFLDCNREEMVRELRDPDNAQISPYRVMLFKLSEEVSELELRSFKFLLNNEIPKCKLEDDLSLLEIFVEMEKRTMLAENNLETLKSICDQVNKSLLGKIEDYERSSTERRMSLEGREELPPSVLDEMSLKMAELCDSPREQDSESRTSDKVYQMKNKPRGYCLIINNHDFSKAREDITQLRKMKDRKGTDCDKEALSKTFKELHFEIVSYDDCTANEIHEILEGYQSADHKNKDCFICCILSHGDKGVVYGTDGKEASIYDLTSYFTGSKCPSLSGKPKIFFIQACQGSNFQKGVPDEAGFEQQNHTLEVDSSSHKNYIPDEADFLLGMATVKNCVSYRDPVNGTWYIQSLCQSLRERCPQGDDILSILTGVNYDVSNKDDRRNKGKQMPQPTFTLRKKLFFPP
Protein: Zinc finger BED domain-containing protein 4 (O75132)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator that binds to poly-guanine tracts in gene promoters and activates transcription (By similarity). Able to bind single- and double-stranded DNA and RNA (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:19369242, ECO:0000269|PubMed:22693546}. Cytoplasm {ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:22693546}. Photoreceptor inner segment {ECO:0000269|PubMed:19369242}.
Interaction partners:
Sequence:
MENNLKTCPKEDGDFVSDKIKFKIEEEDDDGIPPDSLERMDFKSEQEDMKQTDSGGERAGLGGTGCSCKPPGKYLSAESEDDYGALFSQYSSTLYDVAMEAVTQSLLSSRNMSSRKKSPAWKHFFISPRDSTKAICMYCVKEFSRGKNEKDLSTSCLMRHVRRAHPTVLIQENGSVSAVSSFPSPSLLLPPQPADAGDLSTILSPIKLVQKVASKIPSPDRITEESVSVVSSEEISSDMSVSEKCGREEALVGSSPHLPALHYDEPAENLAEKSLPLPKSTSGSRRRSAVWKHFYLSPLDNSKAVCIHCMNEFSRGKNGKDLGTSCLIRHMWRAHRAIVLQENGGTGIPPLYSTPPTLLPSLLPPEGELSSVSSSPVKPVRESPSASSSPDRLTEDLQSHLNPGDGLMEDVAAFSSSDDIGEASASSPEKQQADGLSPRLFESGAIFQQNKKVMKRLKSEVWHHFSLAPMDSLKAECRYCGCAISRGKKGDVGTSCLMRHLYRRHPEVVGSQKGFLGASLANSPYATLASAESSSSKLTDLPTVVTKNNQVMFPVNSKKTSKLWNHFSICSADSTKVVCLHCGRTISRGKKPTNLGTSCLLRHLQRFHSNVLKTEVSETARPSSPDTRVPRGTELSGASSFDDTNEKFYDSHPVAKKITSLIAEMIALDLQPYSFVDNVGFNRLLEYLKPQYSLPAPSYFSRTAIPGMYDNVKQIIMSHLKEAESGVIHFTSGIWMSNQTREYLTLTAHWVSFESPARPRCDDHHCSALLDVSQVDCDYSGNSIQKQLECWWEAWVTSTGLQVGITVTDNASIGKTLNEGEHSSVQCFSHTVNLIVSEAIKSQRMVQNLLSLARKICERVHRSPKAKEKLAELQREYALPQHHLIQDVPSKWSTSFHMLERLIEQKRAINEMSVECNFRELISCDQWEVMQSVCRALKPFEAASREMSTQMSTLSQVIPMVHILNRKVEMLFEETMGIDTMLRSLKEAMVSRLSATLHDPRYVFATLLDPRYKASLFTEEEAEQYKQDLIRELELMNSTSEDVAASHRCDAGSPSKDSAAEENLWSLVAKVKKKDPREKLPEAMVLAYLEEEVLEHSCDPLTYWNLKKASWPGLSALAVRFLGCPPSIVPSEKLFNTPTENGSLGQSRLMMEHFEKLIFLKVNLPLIYFQY
Protein: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (PP2Aa) (PP2A subunit A isoform PR65-alpha) (PP2A subunit A isoform R1-alpha) (Q76MZ3)
Organism: Mus musculus (Mouse)
Function: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (By similarity). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q32PI5}. Nucleus {ECO:0000250|UniProtKB:P30153}. Chromosome {ECO:0000250|UniProtKB:P30153}. Chromosome, centromere {ECO:0000250|UniProtKB:P30153}. Lateral cell membrane {ECO:0000250|UniProtKB:P30153}. Cell projection, dendrite {ECO:0000250|UniProtKB:P30153}. Note=Centromeric localization requires the presence of BUB1. Recruited to chromatin and transcription pause-release checkpoint via its association with the Integrator complex. {ECO:0000250|UniProtKB:P30153}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform
Sequence:
MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCRENVIMTQILPCIKELVSDANQHVKSALASVIMGLSPILGKDNTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4 (Hormone-regulated proliferation-associated protein of 20 kDa) (Q9P032)
Organism: Homo sapiens (Human)
Function: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). May be involved in cell proliferation and survival of hormone-dependent tumor cells. May be a regulator of breast tumor cell invasion.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18179882}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Complex I assembly factor TIMMDC1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Complex I intermediate-associated protein 30, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex assembly factor 2
Sequence:
MGALVIRGIRNFNLENRAEREISKMKPSVAPRHPSTNSLLREQISLYPEVKGEIARKDEKLLSFLKDVYVDSKDPVSSLQVKAAETCQEPKEFRLPKDHHFDMINIKSIPKGKISIVEALTLLNNHKLFPETWTAEKIMQEYQLEQKDVNSLLKYFVTFEVEIFPPEDKKAIRSK
Protein: Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (EC 2.3.1.168) (Branched-chain alpha-keto acid dehydrogenase complex component E2) (BCE2) (BCKAD-E2) (BCKADE2) (Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex) (Dihydrolipoamide branched chain transacylase) (Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase) (Protein DARK INDUCIBLE 3) (Q9M7Z1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component (By similarity). Required during sugar starvation and acts under the control of a sugar-sensing mechanism involving Ser/Thr kinases and phosphatases.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:14764908}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha 1, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta 2, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta 1, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha 2, mitochondrial
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- Putative 2-dehydropantoate 2-reductase
- Isovaleryl-CoA dehydrogenase, mitochondrial
Sequence:
MIARRIWRSHRFLRPFSSSSVCSPPFRVPEYLSQSSSSPASRPFFVHPPTLMKWGGGSRSWFSNEAMATDSNSGLIDVPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLAVEDSQDSLLTTDSSEIVTLGGSKQGTENLLGALSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQKGFVTDSVSSEHAVIGGDSVSTKASSNFEDKTVPLRGFSRAMVKTMTMATSVPHFHFVEEINCDSLVELKQFFKENNTDSTIKHTFLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPKFSKEGTVYPASIMMVNIAADHRVLDGATVARFCCQWKEYVEKPELLMLQMR
Protein: RRM domain-containing protein (Q387L6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEEKESDSSFVYVNGEKFNLLEDGRLALYPRLPEGTLLFDPGNVPPQEVPLSTDATERGVTACRLLPYAHYEAYVPDPATGDLVPVTGGYVCAYVSNLPPNTTAEMLGRFFEAFDMVAEADIFTDPTGACTGRGWVVLQDPAKLLLVPPVMEFFPRNFIHVALSDIIPTPAMFRSITESLLQPPSSVADLGPQLKACIDQCGNGKHVNNTEVRKGDGLATMPILHAPLDTSVVNLDAYYFVVVMSREDAERSVEAGFFRTEPENQRAFYKVMDRGPVIIIVVLQRCSAVFGFGQLLSPVDDGTGDSLCFIQWMKHGVFLEETDLRGPQSVPLSKMRDGIPLKPEIGEGICYLASGYLPTAAVQDMSKRDARHGRQRPAVGLTPRQTGGRQMVRPPLLPVPRGQMIAAQNYVKGPPVGRNGGYGGGKAVLNPRRQF
Protein: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3 (EC 2.4.1.149) (Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase) (EC 2.4.1.146) (Beta-1,3-galactosyltransferase 8) (Beta-1,3-GalTase 8) (Beta3Gal-T8) (Beta3GalT8) (b3Gal-T8) (Beta-3-Gx-T8) (Core 1 extending beta-1,3-N-acetylglucosaminyltransferase) (Core1-beta3GlcNAcT) (Transmembrane protein 3) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 8) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3) (BGnT-3) (Beta-1,3-Gn-T3) (Beta-1,3-N-acetylglucosaminyltransferase 3) (Beta3Gn-T3) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 8) (Q9Y2A9)
Organism: Homo sapiens (Human)
Function: Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Has activity for type 2 oligosaccharides. Also acts as a core1-1,3-N-acetylglucosaminyltransferase (Core1-beta3GlcNAcT) to form the 6-sulfo sialyl Lewis x on extended core1 O-glycans.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
- Type 2 lactosamine alpha-2,3-sialyltransferase
- Beta-1,4-galactosyltransferase 4
- N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
- Galactoside alpha-
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6
- Galactoside alpha-
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 3
Sequence:
MKYLRHRRPNATLILAIGAFTLLLFSLLVSPPTCKVQEQPPAIPEALAWPTPPTRPAPAPCHANTSMVTHPDFATQPQHVQNFLLYRHCRHFPLLQDVPPSKCAQPVFLLLVIKSSPSNYVRRELLRRTWGRERKVRGLQLRLLFLVGTASNPHEARKVNRLLELEAQTHGDILQWDFHDSFFNLTLKQVLFLQWQETRCANASFVLNGDDDVFAHTDNMVFYLQDHDPGRHLFVGQLIQNVGPIRAFWSKYYVPEVVTQNERYPPYCGGGGFLLSRFTAAALRRAAHVLDIFPIDDVFLGMCLELEGLKPASHSGIRTSGVRAPSQRLSSFDPCFYRDLLLVHRFLPYEMLLMWDALNQPNLTCGNQTQIY
Protein: GH03002p (Q86NV1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
PFLLNVLENQKFLHGVLDTYFIDEHPQLFKFKPSLNRAQKLLNYMGEVLVNGPQTPLATTLKPALVSPHVPEVPLDLSPEAIEREERGEAKVTEPPKGLREVLVCEGPEAFAKEVRNRKELLLMDTTFRDAHQSLLATRVRSHDLLKISPYVTHKFNNLYSLENWGGATFDVALRFLHECPWERLEEMRKRIPNIPFQMLLRGANAVGYTSYPDNVVYKFCELAVQTGMDIFRVFDSLNYLPNLILGMEAAGKAGGVVEAAISYTGDVSDPKRTKYDLKYYTNLADELVKAGTHVLCIKDMAGLLKPESARLLITAIRDKHPDIPIHIHTHDTSGAGVASMLACANAGADVVDVAVDSMSGMTSQPSMGAVVASLQGTPLDTNLDLRTVSEYSAYWEQTRTLYAPFECTTTMRSGNADVYLNEIPGGQYTNLQFQAFSLGLGDFFEDVKKAYREANLLLGDIIKVTPSSKVVGDLAQFMVQNDLTADQVLERAEELSFPKSVVEYLQGSIGIPHGGFPEPLRSRVLKDMPRIEGRPGAELKDLDFDKLKKELQESHTCVTNRDVMSAALYPQVTNDFLNFREKYGPVDKLDTRIFLTGPKVGEEFDVPLERGKTLSVKALAVSADLKPNGIREVFFELNGQLRAVHILDKEAVKEIHVHPKANKSNKSEVGAPMPGTVIDIRVKVGDKVEKGQPLVVLSAMKMEMVVQSPLAGVVKKLEIANGTKLEGEDLIMIIE