wanglab/gogpt-training-data huggingface dataset:
Protein: GTP binding protein (Bud4), putative (AFU_orthologue AFUA_2G08470) (C8V2A5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Riboflavin synthase
- Flavoprotein, putative
- 6,7-dimethyl-8-ribityllumazine synthase
- Phosphomannomutase
- Septin-type G domain-containing protein
Sequence:
MGNGTGHRPLSEVSPMAHRRNSPVWNQSNRSTKSIDSSPYESPSSTRRFWQGRESGSPFQKNSENQAPYDPDVTFTTSKRPSLENLKRASRVKGNSMFRDYNHEYDPTSVYVPQRPLAINRGSHEKQSQVVATARPPSPDKTQMGPRPPSPSKDQAPPAKSSLSRASRFGTKDMTFDPENEIWSDADGTRYTKSVTFDAAPPQVNEYEMTTPDPSSVASGSRDGSYDSEEDEGDISFDRGSLDRDDSFDASLEDLEKTPVVMPEDWRFMSPDTANDELAEKNEDPFTSEGSESPEPRSVSTQQVPARRSRVESLDSNGERRPLPPLPAIQGLSFSPRASDKLAAAFELASGNQRVLPAPPAAATYSKSDITGLSHSSMSLEDRLRLMMIQREERENANGKQETKPENKEDESKAETAEKSKGQEPAEGPANPTEADEADVFSPPRISRDSILRDLRRGDDYLDVSYENSSQGSASPRQYSHYDPDIPIPSLESDHDNSYEDDDDETSSVIIKPELEDDSNNLYDIPDYYGTVPSKDSSYKDLKDQEDGDNKSHHSNHSMEDVFCKSNGSVPSEATPVPADRAEEGLNDKTPASPAEHQDNEVAAPKMTAMLESLRRPVTPENAEQISPPSTPDSVIRHPVDDEISDLEDSVDESVPEPIATVKAHGSSLKIRPSLTRADVEQMAATRRKISGQIPPTTQATQEPEESEQLEPDSQEKTLQPEPSAAAAPRKPSFMKLDIPFSIQEDESLGFGLDKEFDRVIESQKRGYLMRHNTKVIVASSRPEEEPVPSSNGESSGDMRSTKAGASPQRKVSQQTWTTVPWNSGARRASIRTPSGAIRKKPVNGPVPPLPGQPSIAQDPPTPVEEIDPTFNALEDGEERGRLFVKVVGLKYLDLPLPKGERTYFSLTLDNGLHCVTTAWLELGKSAPIGQEFELIVQNDLEFQLTLQMKMDEEKFRIQEPAPSASPSRQKHSAFSKMFASPRKRKELDMKQQLASQQHKKQDPNAPIWERLRTLVASDGSFARAYTALSDHEKHAYGRPYTVDVACFNEWAVDEQPSSVKSKKSTASGMSQRRPPYKIGKLELQLLFVPKPKGAKDEDMPKSMNACIREMREAETASTRSWEGFLSQQGGDCPYWRRRFFKLQGSKLTAYHETTRQPRATINLAKAVKLIDDRSTLTQKETTARGGKRRKSAFAEEEEGYMFVEEGFRIRFGNGEVIDFYADSAADKEGWMKVLSETVGKGPTGANQAKPWTELVLKRERSMKATRRETADRFSQFGAAPPPPVKKDVPKPPPAQAPTSQAAPSQRPRHKHTQSQPEVRSAESRRQKARSLIF
Protein: Basic helix-loop-helix (BHLH) family protein-like (Q6YW41)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MKAAVGLHHIELGTVCGLEGFKRTLPSVARSSAAIARSDASVADLAKRLAVVMAWMLAKATGGCGQASWLANVSLQQSWRPCGDRGRCMDTIFVLGQESRQRILHRAAARLPGCAYVCAWAPLPLVAAAGLHHQRPSSGGAAGAARLLYCVDGWLSGGEDGGGCVRALFDAYRGSVCGAVTGCVPGWAYVGGGGGVFMELSELELVASASLPVQQSFYQEAGIKMAAFMGCESGEIEVGFSTAPAENYGGGGGGGSLQASVEQVFSEDFFQQSLLEELLQLPPTRPSSSSSSLVGSPADGAASTSLLRTMTPMMASSSATPSPRELAAQVATTTTTTTTPSSSSRLHPRPPAPHHVHVSPFSRHGGVGGSGVLHFPSAEADDAAMAQAMLDVISSPSTSSSAAALHAPWSSVKHRAQIIRSPRRGTPTTTAFRAYNAALAPRAAASRRPPGAPGQRMIKMGFSILRRMHMVRCSQERAAAAAAAASAAAAQRSGGGDDEDATAAPPPPTSSQLHHMISERRRRERLNESFEHLRGLLPPGSKKDKATVLAKTLEYMNLLIAQISELEAKNRALQTQIHQRANGSSSSRSSMIRTVNEVHHHHNHQWLAVAAAAGGSPERVQVHVIGGGDHDGGASASSSSSAPEVTVRVAVRAPERGGADVSELVLRVLALLKAMGGFTVVAVDARQPGGGGGNGVAQASLTLRATVRMLTLLKPNSLSRASSGNCTKSAELLEELHLAIGGGTR
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q380X8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MHQWIALILLLCAAATRDQVKGTNDKALTKNGLEHVCDIAAEVRAKEHVHADGLTAAADKLAANQAVLAKVRILIAAASTAQEALQLQAISAALHRTAAEEEAKFTKATAMTAIEAIRHSSYLLGGLYEYLHIAGQAKDGTNNGCFADDENAGSFYTTEQLKNQVQNCKAVDLDEKAGWADKQVHKPDGYKRKTDKNNLWSTNAKGCKIHGGGNNNGPVESATYGANNHVAMGLISLSSTDAQLTDLSSLAGAEGDSKKRHAAKAFNTLSKPALKVNTIELPDKNALKNLANFDATLAAAVGASKPFSGQEKEQAMEKLYGSKDPDPTTMFWQKLKGLKLSTDSHGVTKGTKLDEIRNLPLLTELETNYTISKAIQRNSLAAADACNCPTAHPKPEEKLCNDATGDEGKCETLKEKGCIFDRNTKKCELNKDVKAQLEKANQETGGNDGKDTNTTGSNSIVIYKVSLLLAFILL
Protein: Gamma-aminobutyric acid receptor subunit delta (GABA(A) receptor subunit delta) (GABAAR subunit delta) (O14764)
Organism: Homo sapiens (Human)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P18506}; Multi-pass membrane protein {ECO:0000269|PubMed:35355020}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit alpha-4
- Gamma-aminobutyric acid receptor subunit beta-3
- Huntingtin-associated protein 1
- Sodium- and chloride-dependent GABA transporter 1
- Trafficking kinesin-binding protein 2
- Inactive phospholipase C-like protein 1
- Vesicle-fusing ATPase
- Gamma-aminobutyric acid type B receptor subunit 1
- Cilia- and flagella-associated protein 74
- EF-hand domain-containing protein 1
Sequence:
MDAPARLLAPLLLLCAQQLRGTRAMNDIGDYVGSNLEISWLPNLDGLIAGYARNFRPGIGGPPVNVALALEVASIDHISEANMEYTMTVFLHQSWRDSRLSYNHTNETLGLDSRFVDKLWLPDTFIVNAKSAWFHDVTVENKLIRLQPDGVILYSIRITSTVACDMDLAKYPMDEQECMLDLESYGYSSEDIVYYWSESQEHIHGLDKLQLAQFTITSYRFTTELMNFKSAGQFPRLSLHFHLRRNRGVYIIQSYMPSVLLVAMSWVSFWISQAAVPARVSLGITTVLTMTTLMVSARSSLPRASAIKALDVYFWICYVFVFAALVEYAFAHFNADYRKKQKAKVKVSRPRAEMDVRNAIVLFSLSAAGVTQELAISRRQRRVPGNLMGSYRSVGVETGETKKEGAARSGGQGGIRARLRPIDADTIDIYARAVFPAAFAAVNVIYWAAYAM
Protein: Resuscitation-promoting factor RpfA (EC 3.-.-.-) (P9WG31)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Active in the pM concentration range. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endogenous Rpf, resulting in low molecular weight products with resuscitation activity. Stimulates growth of stationary phase M.bovis (a slow-growing Mycobacterium), reduces the lag phase of diluted fast-growers M.smegmatis and Micrococcus luteus.
Interaction partners:
- Uncharacterized protein Rv1954A
- CRP-like cAMP-activated global transcriptional regulator
Sequence:
MSGRHRKPTTSNVSVAKIAFTGAVLGGGGIAMAAQATAATDGEWDQVARCESGGNWSINTGNGYLGGLQFTQSTWAAHGGGEFAPSAQLASREQQIAVGERVLATQGRGAWPVCGRGLSNATPREVLPASAAMDAPLDAAAVNGEPAPLAPPPADPAPPVELAANDLPAPLGEPLPAAPADPAPPADLAPPAPADVAPPVELAVNDLPAPLGEPLPAAPADPAPPADLAPPAPADLAPPAPADLAPPAPADLAPPVELAVNDLPAPLGEPLPAAPAELAPPADLAPASADLAPPAPADLAPPAPAELAPPAPADLAPPAAVNEQTAPGDQPATAPGGPVGLATDLELPEPDPQPADAPPPGDVTEAPAETPQVSNIAYTKKLWQAIRAQDVCGNDALDSLAQPYVIG
Protein: Casein kinase I homolog 3 (EC 2.7.11.1) (O74135)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
Subcellular location: Cytoplasm.
Interaction partners:
- Casein kinase I homolog 1
- Pheromone P-factor receptor
- Casein kinase I homolog 2
- Pheromone M-factor receptor
- Meiotic recombination protein rec8
- Meiotic recombination protein rec11
- Separin
- Linear element protein rec10
Sequence:
MSTTSSHSNVVGVHYRVGKKIGEGSFGMLFQGVNLINNQPIALKFESRKSEVPQLRDEYLTYKLLMGLPGIPSVYYYGQEGMYNLLVMDLLGPSLEDLFDYCGRRFSPKTVAMIAKQMITRIQSVHERHFIYRDIKPDNFLIGFPGSKTENVIYAVDFGMAKQYRDPKTHVHRPYNEHKSLSGTARYMSINTHLGREQSRRDDLESMGHVFMYFLRGSLPWQGLKAATNKQKYEKIGEKKQVTPLKELCEGYPKEFLQYMIYARNLGYEEAPDYDYLRSLFDSLLLRINETDDGKYDWTLLNNGKGWQYSAAKQHVVQRRHTQGTNNRRQSTIPPYARTRQNLLSSPSKQTPVNNVVDASVATQKDGIPGKAASPQVQQQQQTSSAQQQQPQRVEQPAPQTTQPTQVDTQQAAKPAPSKEKSRKKFHLRLLSCCISKQE
Protein: Stromal interaction molecule 1 (H0YDB2)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MDVCVRLALWLLWGLLLHQGQSLSHSHSEKATGTSSGANSEESTAAEFCRIDKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNIDPSWMGSTRPNPAHFIMTDDVDDMDEEIVSPLSMQYAAWLMGRRFSDRSLCSTSAGSDDQSLWKYPAPSLQSSVRQRLTEPQHGLGSQRDLTHSDSESSLHMSDRQRVAPKPPQMSRAADEALNAMTSNGSHRLIEGVHPGSLVEKLPDSPALAKKALLALNHGLDKAHSLMELSPSAPPGGSPHLDSSRSHSPSSPDPDTPSPVGDSRALQASRNTRIPHLAGKKAVAEEDNGSIGEETDSSPGRKKFPLKIFKKPLKK
Protein: 5-aminolevulinate synthase (EC 2.3.1.37) (5-aminolevulinic acid synthase) (Delta-ALA synthase) (Delta-aminolevulinate synthase) (A2R9H8)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Mitochondrion matrix {ECO:0000256|RuleBase:RU910713}.
Interaction partners:
Sequence:
MESLLQQSRAMCPFLKRTSPTTLRSLSTATRPSTSPGGGTMSNLQVLARRCPVMSKALAVQSARLAHTKRFTSYTAGVAGLNPKQFRPTVGKRALHSTAGNGADVTPNVYKESQRVHPGLTGVPKQQLEPSAATVPGPRPHAPNAAPFNYNAFYQGELEKKHKDKSYRYFNNINRLAKEFPRAHTASPEERVTVWCSNDYLGMGRNPEVLKSMHKTLDNYGAGAGGTRNISGHNQHAVALESTLAKLHNKEAALVFSSCFVANDATLATLGSKMPDCVILSDSLNHASMIQGIRHSGAKKMVFKHNDLVDLETKLASLPLNVPKIIAFESVYSMCGSIAPIEKICDLADKYGAITFLDEVHAVGMYGPHGAGVAEHLDYDIYASQDTANPRDTKGTVMDRIDIITGTLGKAYGCVGGYIAGSAAMVDTIRSLAPGFIFTTSLPPATMAGADTAIQYQAQHQRDRVLQQLHTRAVKESLKELDIPVIPNPSHIIPLLVGDAEVAKQASDKLLEEHGIYVQAINYPTVPRGEERLRITPTPGHVKEHRDHLVQALQTVWNDLGIKRASDWEAQGGFVGVGVEGAEAANQPIWEDAQLGLQPNETVEAAVTREFQTAAAEALSQAASRMQTATPVRPAAAAAASIPVGVAAA
Protein: Uncharacterized alpha-1,2-galactosyltransferase C637.06 (EC 2.4.1.-) (P78817)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Mannan polymerase complex subunit mnn9
- Mannan polymerase II complex anp1 subunit
- Uncharacterized alpha-1,2-galactosyltransferase C8D2.17
- tRNA
- Meiotically up-regulated gene 190 protein
- UDP-galactose transporter
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
Sequence:
MWNPKKKSEALAKFKSFPYPKPGTSNVLDSKEGDTRRKYFTKTHLHRLFVFVVLLLCSGYFLKHTLLTRPKESNVVMIFVNNIGGGVLDVKSPRQWELEKISTENKKKYAERHGYHFFVKSTGLKRRYAHEWRESWEKADYIMEAMKKYPHAEWFWWVDLTTFIMEPQYSLEKLIINRLDHIATRNITDSMEFNPKNFHEIPFVDYSEDINFILGQDCNGFSLGSFLVRRSDWTSRLMDFLWDPVVYGQKHMDWPHDEQNAIEYFYENNAWLRSGMGFVPLRLFNSYPPGACAGEGENPRFFYNQKEGDFLVNLAGCNYGRDCLDEINHYKGLAQRKRGWRKLVPFL
Protein: DNA polymerase catalytic subunit (EC 2.7.7.7) (Q6SW77)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Replicates viral genomic DNA in the late phase of lytic infection, producing long concatemeric DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein (By similarity).
Subcellular location: Host nucleus {ECO:0000250}. Note=the protein is present at discrete sites in nuclei, called replication compartments where viral DNA replication occurs. {ECO:0000250}.
Interaction partners:
Sequence:
MFFNPYLSGGVTGGAVAGGRRQRSQPGSAQGSGKRPPQKQFLQIVPRGVMFDGQTGLIKHKTGRLPLMFYREIKHLLSHDMVWPCPWRETLVGRVVGPIRFHTYDQTDAVLFFDSPENVSPRYRQHLVPSGNVLRFFGATEHGYSICVNVFGQRSYFYCEYSDTDRLREVIASVGELVPEPRTPYAVSVTPATKTSIYGYGTRPVPDLQCVSISNWTMARKIGEYLLEQGFPVYEVRVDPLTRLVIDRRITTFGWCSVNRYDWRQQGRASTCDIEVDCDVSDLVAVPDDSSWPRYRCLSFDIECMSGEGGFPCAEKSDDIVIQISCVCYETGGNTAVDQGIPNGNDGRGCTSEGVIFGHSGLHLFTIGTCGQVGPDVDVYEFPSEYELLLGFMLFFQRYAPAFVTGYNINSFDLKYILTRLEYLYKVDSQRFCKLPTAQGGRFFLHSPAVGFKRQYAAAFPSASHNNPASTAATKVYIAGSVVIDMYPVCMAKTNSPNYKLNTMAELYLRQRKDDLSYKDIPRCFVANAEGRAQVGRYCLQDAVLVRDLFNTINFHYEAGAIARLAKIPLRRVIFDGQQIRIYTSLLDECACRDFILPNHYSKGTTVPETNSVAVSPNAAIISTAAVPGDAGSVAAMFQMSPPLQSAPSSQDGVSPGSGSNSSSSVGVFSVGSGSSGGVGVSNDNHGAGGTAAVSYQGATVFEPEVGYYNDPVAVFDFASLYPSIIMAHNLCYSTLLVPGGEYPVDPADVYSVTLENGVTHRFVRASVRVSVLSELLNKWVSQRRAVRECMRECQDPVRRMLLDKEQMALKVTCNAFYGFTGVVNGMMPCLPIAASITRIGRDMLERTARFIKDNFSEPCFLHNFFNQEDYVVGTREGDSEESSTLPEGLETSSGGLNERRVEARVIYGDTDSVFVRFRGLTPQALVARGPSLAHYVTACLFVEPVKLEFEKVFVSLMMICKKRYIGKVEGASGLSMKGVDLVRKTACEFVKGVTRDVLSLLFEDREVSEAAVRLSRLSLDEVKKYGVPRGFWRILRRLVQARDDLYLHRVRVEDLVLSSVLSKDISLYRQSNLPHIAVIKRLAARSEELPSVGDRVFYVLTAPGVRAAPQGSSDNGDSVTTGVVSRSDAIDGTDDDADGGGVEESNRRGGEPAKKRARKPPSAVCNYEVAEDPSYVREHGVPIHADKYFEQVLKAVTNVLSPVFPGGETARKDKFLHMVLPRRLHLEPAFLPYSVKAHECC
Protein: BMP-2-inducible protein kinase (BIKe) (EC 2.7.11.1) (Q91Z96)
Organism: Mus musculus (Mouse)
Function: May be involved in osteoblast differentiation.
Subcellular location: Nucleus {ECO:0000305|PubMed:11500515}.
Interaction partners:
- Protein numb homolog
- Numb-like protein
Sequence:
MKKFSRMPKSEGSGGGAAAGGAAGGGLGGGFASSSMGVRVFAVGRYQVTLEESLAEGGFSTVFLVRTHSGIRCALKRMYVNNTPDLNICKREITIMKELSGHKNIVGYLDCAVNSISDNVWEVLILMEYCRAGQVVNQMNKKLQTGFTESEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDAGNYVLCDFGSATNKFLNPQKDGVNVVEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQVAICDGSFTIPDNSRYSHNVHCLIRFMLEPDPECRPDIFQVSYFAFKFAKKDCPVSNINNSFLPSTLPEPMTATEAAARKSQMKARITDTIGPTETSIAPRQRPKANSTAATSSVLTIQSSATPVKVPAPGEFSNHKPKGALRPGNGSEVLMVQGPPQQPPQQHRVLQQLQQGDWRLQQLHLHRHPHHHHQQQQQQQQQQQQQQLQQQQQQQQQLLQNAYLQQYQHAMHQQHILQQQFLMHSVYQPQPPASQYPAMMQQYQQAFLQQQMLARHQQPAQQVSPEYLTSPQEFSPALVSYASSLPAQVGTIVDSSYGANRSVAEKEAVANFTNQKTISHPPDMSGWNPFGEDNFSKLTEEELLDREFDLLRSNRLGASTPSDKTVDLPPAPHSRPPEEPFASVPFISHSGSPEKKTTEHSPNQKSITANLTKNGGSSPLCKDQRAGKKTSENPVIRGQVQKGHDDSESDFESDPPSPKSSEEEQEDEDAQGEHGDFNDDDTEPENLGHRPLLMDSEDEEEDDKHSSDSECEQAKTKRGDTSSLRRDKPGVAPDTALLTPARSPADALTPSQEFDVFGAVPFFAAPAPQSLQHRGDGKNLSQHAFPEQEDFDVFTKAPFNKKVSVQDWPAVGPDARPLPARPRSVDIFGSTPFQPFSVSASKSESKEDVFGLVPFEEITGSQQQQKVKQRSLQKLSSRQRRTKQDVSKSNGKRHHGTPTSAKKTLKPPYRTPERARRHKKVGRRDSQSSNEFLTISDSKENISVALTDGKDRASVLPSDESLLDPFGAKPFHPPDLWHQPHQGLSDICVDHTTILPGRPRQNSVHGSFHSAETLRMDDFGAVPFTELVVQSVTPQQSQPVELDPFGAAPFPSKQ
Protein: RNA-binding protein 8A (Binder of OVCA1-1) (BOV-1) (RNA-binding motif protein 8A) (RNA-binding protein Y14) (Ribonucleoprotein RBM8A) (Q9Y5S9)
Organism: Homo sapiens (Human)
Function: Required for pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Its removal from cytoplasmic mRNAs requires translation initiation from EJC-bearing spliced mRNAs. Associates preferentially with mRNAs produced by splicing. Does not interact with pre-mRNAs, introns, or mRNAs produced from intronless cDNAs. Associates with both nuclear mRNAs and newly exported cytoplasmic mRNAs. The MAGOH-RBM8A heterodimer is a component of the nonsense mediated decay (NMD) pathway. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:11030346, ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}. Nucleus speckle {ECO:0000269|PubMed:11030346, ECO:0000269|PubMed:19324961}. Cytoplasm {ECO:0000269|PubMed:11030346, ECO:0000269|PubMed:19324961}. Note=Nucleocytoplasmic shuttling protein (PubMed:11030346). Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (PubMed:19324961). {ECO:0000269|PubMed:11030346, ECO:0000269|PubMed:19324961}.
Interaction partners:
- RNA-binding protein with serine-rich domain 1
- Regulator of nonsense transcripts 3B
- Partner of Y14 and mago
- Regulator of nonsense transcripts 1
- Regulator of nonsense transcripts 2
- Regulator of nonsense transcripts 3A
- Eukaryotic initiation factor 4A-III
- Protein mago nashi homolog
- Protein mago nashi homolog 2
- Protein CASC3
Sequence:
MADVLDLHEAGGEDFAMDEDGDESIHKLKEKAKKRKGRGFGSEEGSRARMREDYDSVEQDGDEPGPQRSVEGWILFVTGVHEEATEEDIHDKFAEYGEIKNIHLNLDRRTGYLKGYTLVEYETYKEAQAAMEGLNGQDLMGQPISVDWCFVRGPPKGKRRGGRRRSRSPDRRRR
Protein: Probable electron transfer flavoprotein subunit alpha, mitochondrial (Alpha-ETF) (Q93615)
Organism: Caenorhabditis elegans
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Electron transfer flavoprotein subunit beta
- Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial
- medium-chain acyl-CoA dehydrogenase
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Isobutyryl-CoA dehydrogenase, mitochondrial
- Fatty acid synthase
- Succinate--CoA ligase subunit alpha, mitochondrial
- 3-ketoacyl-CoA thiolase
Sequence:
MLSARTVLSRAGLISNASRLNSTLVVAEHDETKLAPITLNAITAASKLGNEVSVLVTGANATKVAEQVAKVNGVKRVLVAQDEKLKNNLPERVAPVILASQKQFNFTAITAGSSAFGRGVIPRVAAKLDVSSISDVTEVHSADSFTRTLYAGNAVKKVKSTAPIKLLTFRGTSFEPAKEGGSGAVENAPSADIKTDLSEFLGQELSKSERPDLATAKVVVSGGRGLKSGDNFKLIYDLADKLGAGVGASRAAVDAGYVPNDMQVGQTGKIVAPELYIAIGISGAIQHLAGMKDSKVIVAINKDPDAPIFQVADIGLKADLFKAVPELTAALP
Protein: Nematode cuticle collagen N-terminal domain-containing protein (Q21556)
Organism: Caenorhabditis elegans
Interaction partners:
- Nematode cuticle collagen N-terminal domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
- PH domain-containing protein
- PERMeable eggshell
- CYtochrome P450 family
- Putative cytochrome P450 cyp-13B1
Sequence:
MSTARYLVSIAAAASTFAVLASIVSLVYLVNDVNNYYDDVTRNIENFKDDANTVWHQMMTVVPQGGKQRQVYESLFGRTKRQAAQCNCGANSAASNCPAGPPGPPGAPGEDGDHGLVGEDGTPGADGNLGVPLSANGCIVCPAGPPGPPGQPGQNGQRGSDGQPGQDAMGGGQGAPGPQGPAGDNGQPGRPGNDGRPGAPGAPGTRSVGRPGTAGSPGPQGPPGQNGNDGQPGNDGAPGQPGQPGPDGHPGQPGNAGPPGTPGAAGQPGGDAAYCPCPSRSSVVRAQAAVARNRHVAARHRSVSRRKAVAARRSKARRVVAAKHRAVAKRHRAVQKA
Protein: Methyl-CpG-binding domain protein 1 (Methyl-CpG-binding protein MBD1) (Q9Z2E2)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor that binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binding is abolished by the presence of 7-mG that is produced by DNA damage by methylmethanesulfonate (MMS). Acts as transcriptional repressor and plays a role in gene silencing by recruiting ATF7IP, which in turn recruits factors such as the histone methyltransferase SETDB1. Probably forms a complex with SETDB1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Isoform 1 can also repress transcription from unmethylated promoters.
Subcellular location: Nucleus. Nucleus matrix. Nucleus speckle. Chromosome. Note=Nuclear, in a punctate pattern. Associated with euchromatic regions of the chromosomes. Colocalizes with the Ten-1 ICD form of TENM1 in foci associated with the nuclear matrix.
Interaction partners:
- DNA
- Histone-lysine N-methyltransferase SETDB1
Sequence:
MAESWQDCPALGPGWKRRESFRKSGASFGRSDIYYQSPTGEKIRSKVELTRYLGPACDLTLFDFRQGTLCHPIPKTHPLAVPSKKKKKPSKPAKTKKQQVGLQRSEVRIETPQGEYKAPTATALASLSVSASASSSASASASASSHAPVCCENCGIHFSWDGVKRQRLKTLCKDCRAQRIAFNREQRMFKRVGCGDCAACLVKEDCGVCSTCRLQLPSDVASGLYCKCERRRCLRIMEKSRGCGVCRGCQTQEDCGHCCICLRSPRPGLKRQWRCLQRRCFWGKRDSSKRGSKVASQRHSQAPPLPPHPASQYTEPTELHISDIAPTSPAEFIYYCVDEDEDELQPYTNQRQNRKCGACAACLRRMDCGRCDFCCDKPKFGGGNQKRQKCRWRQCLQFAMKRLLPSAGSGSGEGAGLRPYQTHQTHQKRPASARQLQLSSPLKAPWAVVTAPPGPVRDSRKQQAGRGSVLPQPDTDFVFLQEGTSSAMQMPGTAAASTEVPVQAAQCSAPSWVVALPQVKQETADAPEEWTAVTTFLTSSTLQSGFPSKAADPDLSPVKQEPPGPEEDGEEKKDDVSETTPAEEIGGVGTPVITEIFSLGGTRLRDAEAWLPRLHKLLAVNEKEYFTELQLKEEVL
Protein: Mechanosensitive ion channel protein Msy2 (O14050)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulates intracellular calcium levels and cell volume for survival in response to hypo-osmotic shock. Involved in maintaining vacuole integrity and protecting the nuclear envelope upon hypo-osmotic shock.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22910366}; Multi-pass membrane protein {ECO:0000305}. Note=Cortical endoplasmic reticulum. {ECO:0000269|PubMed:22910366}.
Interaction partners:
- Mechanosensitive ion channel protein Msy1
Sequence:
MNEHRREPHRRSGYQDDSAFTNTEKLVDELDHNVEPEQLLEKNRTDFKLMYVIVKFYRWFNNLSFITRWITIWFPLAGALVIPLAVGVSPYPNAKLGGVRIFWIFVWLEVAWGGFWVSRVIARLLPYILYPLMGILPFTMYKYTVILTALEMPLAIFFCSIVCVCTFSPIMIGKGNFTSTTVTTTTSATATPTASASSNAVESVFVTKTAASVPSWIKVITKILGAAVVTSIVLLLEKIFLHFIGFHYHEVQYQYRITDNKRNTAVLAKLLTAALDAPYHDSPRVRRQDYLLGLIDTRSMSESKGSGNGKLRKVKKISKNAKRIFSKTRNAISTAFTDMLGKHAKDLTPEQEFILETIRSKKKCLALARKIWYSLVPEGEDCFQKEDLIGLIPDDEINDIFHILDNDYSRTVTLDEMEQFTREISIEFRSISSSLRDVDLALGKLDRVGLGVVGIIAVLTFISFLDTSFATILAAFGTTLLSLSFVFSTSAQELMSSIIFLFSKHPFDISDVVIVNNIKYEVVSLSLLFTVFRTMGGSTVQAPNSLLNTLFIENLRRSQPQSETITIVSPFATDFKQLERLRDLLLTFVKENERDFRPIIDLNVSDFSTLDSLKFTVTYYYKSNWQNVSLQCVRRNKFMCALKNAIATTNLPAVADPVRGSPDYPFVIEQYNLERPEYSKTASRPQFSDISSTASSNSLSNKPGFAHSESRNYHTHDEDNSSDDNHKREDRGHLPAQYLRQSVATWQIPNLISAIEAYDSQNESSQENATYTVVESNGNANGDNTATNSQGATDNGQTTTNTTQNNVDNTQATTDNTQANTDNMQVAIDYSQNMDGQIQY
Protein: Isocitrate dehydrogenase [NADP] (EC 1.1.1.42) (Q7KUB1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFALRRTAAMMTSVHRQPHLSQAVFRANFAISAADPKTHKISMDNERMSAVSEMAQKIKAGPVVDVLGDEMTRIIWDSIKSQLILPFLDIELHTYDLGIENRDKTEDQVTIDCAEAIKKYNVGIKCATITPDEKRVEEFNLKKMWKSPNGTIRNILGGTVFREAIICKNVPRLVTGWQKPIVIGRHAHADQYKAVDYVVPGPGKLTLTWKGTDGQVIDEVINDFKGPGIALGMFNTDDSIVDFAHASFKYALDRKLPLYMSTKNTILKKYDGRFKDIFEDLYNKQYKKEYEAAGIWYEHRLIDDMVAYAMKSEGGFVWACKNYDGDVQSDSVAQGYGSLGLMTSVLLCPDGKTVEAEAAHGTVTRHFRFYQQGKETSTNPIASIFAWTRGLLHRAKLDNNEPLKQFADTLEQVCIDTIESGAMTKDLAICIKGNINAVTRRDYQETFEFINTLAKNLEGALAKNAVAAK
Protein: Intermediate conductance calcium-activated potassium channel protein 4 (SKCa 4) (SKCa4) (rSK4) (KCa3.1) (KCa4) (Smooth muscle intermediate-conductance KCa channel) (SMIK) (rIK1) (Q9QYW1)
Organism: Rattus norvegicus (Rat)
Function: Forms a voltage-independent potassium channel that is activated by intracellular calcium. Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells. The channel is blocked by clotrimazole and charybdotoxin but is insensitive to apamin.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O15554}; Multi-pass membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O15554}. Note=Targeted to membrane ruffles after EGF stimulation. {ECO:0000250|UniProtKB:O15554}.
Interaction partners:
- Calcium-activated potassium channel subunit alpha-1
- Calcium-activated potassium channel subunit beta-1
- Calcium-activated potassium channel subunit beta-4
- Potassium two pore domain channel subfamily K member 5
- Small conductance calcium-activated potassium channel protein 1
- Potassium voltage-gated channel subfamily E member 3
- Potassium voltage-gated channel subfamily KQT member 1
- Calcium-activated potassium channel subunit beta-2
- Inward rectifier potassium channel 13
- Small conductance calcium-activated potassium channel protein 2
Sequence:
MGGELVTGLGALRRRKRLLEQEKRVAGWALVLAGTGIGLMVLHAEMLWFLGCKWVLYLLLVKCLITLSTAFLLCLIVVFHAKEVQLFMTDNGLRDWRVALTRRQVAQILLELLVCGVHPVPLRSPHCTLAGEATDSQAWPGFLGEGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQVRFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLTDTLWLIPITFLTIGYGDVVPGTLWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIHYAKEMKESAARLLQEAWMYYKHTRRKDSRAARRHQRKMLAAIHTFRQVRLKHRKLREQVNSMVDISKMHMILCDLQLGLSASHLALEKRIDGLAGKLDALTELLSTALQQQQPPEPIQEAT