wanglab/gogpt-training-data huggingface dataset:
Protein: Receptor-type tyrosine-protein phosphatase H (R-PTP-H) (EC 3.1.3.48) (Stomach cancer-associated protein tyrosine phosphatase 1) (SAP-1) (Transmembrane-type protein-tyrosine phosphatase type H) (Q9HD43)
Organism: Homo sapiens (Human)
Function: Protein phosphatase that may contribute to contact inhibition of cell growth and motility by mediating the dephosphorylation of focal adhesion-associated substrates and thus negatively regulating integrin-promoted signaling processes. Induces apoptotic cell death by at least two distinct mechanisms: inhibition of cell survival signaling mediated by PI 3-kinase, Akt, and ILK and activation of a caspase-dependent proapoptotic pathway. Inhibits the basal activity of LCK and its activation in response to TCR stimulation and TCR-induced activation of MAP kinase and surface expression of CD69. Inhibits TCR-induced tyrosine phosphorylation of LAT and ZAP70. Inhibits both basal activity of DOK1 and its CD2-induced tyrosine phosphorylation. Induces dephosphorylation of BCAR1, focal adhesion kinase and SRC. Reduces migratory activity of activity of Jurkat cells. Reduces tyrosine phosphorylation of CEACAM20 and thereby contributes to suppress the intestinal immune response CEACAM20 (By similarity).
Subcellular location: Cell projection, microvillus membrane {ECO:0000250|UniProtKB:E9Q0N2}; Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:E9Q0N2}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:12879010}. Note=Colocalizes with CEACAM20 at the apical brush border of intestinal cells. {ECO:0000250|UniProtKB:E9Q0N2}.
Interaction partners:
- 6-pyruvoyl tetrahydrobiopterin synthase
Sequence:
MAGAGGGLGVWGNLVLLGLCSWTGARAPAPNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTTETRNTTATNVTVDGLGPGSLYTCSVWVEKDGVNSSVGTVTTATAPNPVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGGRAGTRSTAHTNITVDGLEPGCLYAFSMWVGKNGINSSRETRNATTAHNPVRNLRVEAQTTSSISLSWEVPDGTDPQNSTYCVQCTGDGGRTETRNTTDTRVTVDGLGPGSLYTCSVWVEKDGVNSSVEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGGRAGTRSTAHTNITVDRLEPGCLYVFSVWVGKNGINSSRETRNATTAPNPVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGTETRNTTNTSVTAERLEPGTLYTFSVWAEKNGARGSRQNVSISTVPNAVTSLSKQDWTNSTIALRWTAPQGPGQSSYSYWVSWVREGMTDPRTQSTSGTDITLKELEAGSLYHLTVWAERNEVRGYNSTLTAATAPNEVTDLQNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRRGQDPQANWVNQTSRTNETWYKVEALEPGTLYNFTVWAERNDVASSTQSLCASTYPDTVTITSCVSTSAGYGVNLIWSCPQGGYEAFELEVGGQRGSQDRSSCGEAVSVLGLGPARSYPATITTIWDGMKVVSHSVVCHTESAGVIAGAFVGILLFLILVGLLIFFLKRRNKKKQQKPELRDLVFSSPGDIPAEDFADHVRKNERDSNCGFADEYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQQSAQAPAEKEVPYEDVENLIYENVAAIQAHKLEV
Protein: Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (HGPRTase) (EC 2.4.2.8) (Bypass of repression by adenine protein 6) (Q04178)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Xanthine phosphoribosyltransferase 1
- Adenine phosphoribosyltransferase 1
- Adenylosuccinate synthetase
- Adenine phosphoribosyltransferase 2
- Purine nucleoside phosphorylase
- Guanylate kinase
- Bifunctional purine biosynthesis protein ADE17
- Inosine-5'-monophosphate dehydrogenase 2
- AMP deaminase
- GMP synthase
Sequence:
MSANDKQYISYNNVHQLCQVSAERIKNFKPDLIIAIGGGGFIPARILRTFLKEPGVPTIRIFAIILSLYEDLNSVGSEVEEVGVKVSRTQWIDYEQCKLDLVGKNVLIVDEVDDTRTTLHYALSELEKDAAEQAKAKGIDTEKSPEMKTNFGIFVLHDKQKPKKADLPAEMLNDKNRYFAAKTVPDKWYAYPWESTDIVFHTRMAIEQGNDIFIPEQEHKQ
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (G1T7Z6)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- phosphoglycerate mutase
- Phosphoglycerate mutase
- Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
- Bisphosphoglycerate mutase
- Enolase
- Beta-enolase
- Beta-enolase
- Glucose-6-phosphate isomerase
Sequence:
MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDHGAKSVVLMSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIETFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDEHAKTGQATVASGIPAGWMGLDCGPESSKKYAEAVGRAKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNV
Protein: Type II secretion system core protein G (Q7BSV8)
Organism: Escherichia coli O157:H7
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004377}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004377}.
Interaction partners:
Sequence:
MRKQHQRGFTLLEIMVVIVILGVLASLVVPNLMGNKDKADRQKVMSDLVALESTLDMYRLDNNRYPTTEQGLRALVSKPTVQPEPRNYRQDGYIRRLPQDPWGGDYQLLNPGQYSDIDIFSPGPDGVPNTEDDIGNWTLGNAQP
Protein: Glutamine synthetase family protein (Q9A3S2)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
- Glutamate synthase large chain
- Glutamine--fructose-6-phosphate aminotransferase
- Bifunctional protein PutA
- FAD dependent oxidoreductase domain-containing protein
- Glutamine synthetase
- Glutamate synthase, small subunit
- Uncharacterized protein
- Glutamine synthetase family protein
- Carbamoyl phosphate synthase small chain
- SIS domain protein
Sequence:
MKPKHNKAKRDQILDRGVSTIEEAKDWFARQHIEEIECVVPDLAGVARGKIMPVRKFLGSPSMNLPLAVFYQTITGDFPEFEGAVNAVQSDTDIFLTPDFATLAAVPWAQDPTAQVIHDAFHPDGRPVEEAPRQVLRRVLALYADKGWHPIVAPEIEFYLVDRNTDPDYPLKPPIGRSGRPETGRQGYSISAVNEFDALFEDMYEYSERQGLEIDTLIHESGVAQMEINLQHGHPLELADQVFMMKRTIREAALEHEIYATFMAKPMANEPGSAMHIHQSIVDKKGRNLFSDEDGAESAMFHGFIAGQQTYLPAIMAILAPYVNSYRRISRDSGAPVNTQWGYDNRTCGLRVPPSGPNNRRVENRIPSSDANPYLAIAASLAAGYLGMVQGLKPSEPVSIDAGARGIELPRSLSDSLRLFVACQPLVEILGPTFCAAYDRVKQAEYETFMRTISPWEREFLLLNV
Protein: Transcription factor bHLH137 (Basic helix-loop-helix protein 137) (AtbHLH137) (bHLH 137) (Transcription factor EN 89) (bHLH transcription factor bHLH137) (Q93W88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor bHLH153
- Transcription factor bHLH123
- RING-type E3 ubiquitin transferase
- Transcription factor bHLH36
- Transcription factor bHLH168
- L-type lectin-domain containing receptor kinase I.7
Sequence:
MATFSYFQNYPHSLLDPLLFPTPHSSINLTSFIDQNHLYPLPNISTVEDISFLEYNVDKTENSGSEKLANTTKTATTGSSSCDQLSHGPSAITNTGKTRGRKARNSNNSKEGVEGRKSKKQKRGSKEEPPTDYIHVRARRGQATDSHSLAERVRREKISERMRTLQNLVPGCDKVTGKALMLDEIINYVQTLQTQVEFLSMKLTSISPVVYDFGSDLDGLILQSEMGSPEVGTSFTNAMPTTTPIFPSLLDNSVVPTHAQVQEEGEERENFVDRSGFNNNNFCSFP
Protein: Zgc:153721 (Q05AK7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAVPFSNTHLRIPRGFGNLLEGLTREVLREQPEDIATFAAVYFTELLKAREESGLDPAEWGAKLEDRFYNNHSFKGTSLQGNIISPKINTRINAESSSETLGNNETQLSALKDLDTDNSVGSEVNLDKKFDEESGEKERGHAEDILPAETADGDKCAEELKDTNEIPGETSEVAKEEVDVDICRSELEPTPLPSFGGHANVDVCAEEINLQSESSKSKEELVSPKPLFLNKDQSESQDEIHSHTEQDASKQANEMSDHGDDDDDDDDDEDDEHDDNDAEDPEEEVSEIADNLLEDIDPEEKSTEQVYAEESTESTIEKYITESVAGQESEDAINEDQEETNYEYTSTNDFVEDAGDSTSDINSRSLMEMKDTHVDYSDEIHDSKSEVVDVLDKVHHQCDTRTGEEEAENSSDEENTSKILDALNEEDFLETPKPVSQMNDSEAEASNEILNADAFEKDLNTENVNEGSDLDSDGFEAEEMDLDISNVLQPNEEKTEDDGNHDPEPEEDAFSEAEQANPEPLENETVVVNEELFESQEQTENTENDVDQEAQLEEQRDKIQEMTLESENLENTDISEPKEESSQPQEEEDIMDIPLDDPEANKAAAKIQAGFRGHMTRKKMKPGEKPGEEVSSSGEALNGSQGDSGGTDGVETDGTSGPEQ
Protein: Probable DNA-directed RNA polymerase catalytic subunit (EC 2.7.7.6) (Late expression factor 8) (P41452)
Organism: Autographa californica nuclear polyhedrosis virus (AcMNPV)
Function: Component of the viral DNA-dependent RNA polymerase which is composed of four equimolar subunits of LEF-4, LEF-8, LEF-9, and p47. Plays an essential role in late and very late gene expression.
Interaction partners:
Sequence:
MTDVVQDFNELYDRIENKYKLKYTFDCATNSNERMLFCAIQERKSYLCCALNEQLSCVMHKCVPVIFGTRLDKQFRETDDVDANNNINGTFMLDGRFLSFPNIMMNNNVLVHNFYDKLYAKHCKRMFLYGNVDQEKHINRAIQLVYDKQDDVLFARDVYASDYVVTEDLNSVLETYLANSGKWKPLDFLFEYNTLHKQQLVEHIKIIMNHDINYSIDSLANKIVYKHAYLIELLLTSTILQNYQRVLDKTADDDAYTVANKRRKIQSVLYNKESKKIVDCIVNGRLIYCVSKTFSKQRKVFPNQQDNSSNNNIEISLPVLKYRVGNEVARITNDSMRQKMLKQKKDFVKFIGSFFHGEMTVAGKKFFLCRNACLPNVDYEMVAQKFQYLLKHNLVAFVDDLNDVQDDSLLIAFNDRPTNLKCLKSNTSFIVYTMKRNMAPIELKITDRILYVNHHEGMICIKKKLRVNNEADINVLLTPYEYHYKHSIYYNPIIQCTIVENDDVKSLMSKLEQYYYRNFIHLFHTTPVPKLIVSLTNLKNAMPVFEYKEENCVSGLPNGYSVAVNKSILLNNKMFKLWTLVRDNKLMTAEDPYIPHIALPICLYNNKVNKLKGKLVVGPKQSCLVKFTNSSDKNYVALDDGLVLYMAGVLVSNAKINWVYDGRRYKIETCTNGNFNVYKVYVYFRQIKNQKIEKLDASMVVNGDNVMLKIVIVTSTNDLEGIKICGIHGQKGVFNRSEDLTEWMAEDGTHAQICLSPVSFLSRQSNFDKIERKYVVRGGNHDDPHAKRYPIFNIPYMLFNNTPDNIFKEFIKTSHTGHEKVEGTRFDQWTKNQSFVGNRMSESLHWMRGGSNLPQNCGEFNVVSSLLMCNNTIMKN
Protein: Inactive heparanase-2 (Hpa2) (B2RY83)
Organism: Mus musculus (Mouse)
Function: Binds heparin and heparan sulfate with high affinity, but lacks heparanase activity. Inhibits HPSE, possibly by competing for its substrates (in vitro) (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Syndecan-1
- Heparanase
- Iduronate 2-sulfatase
- Leucine-rich repeats and immunoglobulin-like domains protein 2
Sequence:
MRVLCAFPEAMASSSSRPPSCLALVALFLALLLHLSLSFHAGNRRPLPVDRATGLKEKTLILLDVSTKNPVRTVNENFLSLQLDPSIIHDGWLDFLSSKRLVTLARGLSPAFLRFGGKRTDFLQFQNLRNPAKSRGGPGPDYYLKNYEDDIVRSDVALDKQKGCKIAQHPDVMLELQREKASQMHLVLLKEQYSNTYSNLILTARSLDKLYNFADCSGLHLIFALNALRRNPNNSWNSSSALSLLKYSASKKYNISWELGNEPNNYRSIHGRAVNGSQLGKDYIQLKSLLQPIRVYSRASLYGPNIGRPRKNVIALLDGFMKVAGSTVDAVTWQHCYIDGRVVKVMDFLKTRLLDTLSDQIRKIQKVVNTYTPGKKIWLEGVVTTSAGGTNNLSDSYAAGFLWLNTLGMLANQGIDVVIRHSFFDHGYNHLVDQNFNPLPDYWLSLLYKRLIGPKVLAVHVAGLQRKPRPGRVIRDKLRIYAHCTNHHNHNYVRGSITLFIINLHRSRKKIKLAGTLRDKLVHQYLLQPYGQEGLKSKSVQLNGQPLVMVDDGTLPELKPRPLRAGRTLVIPPVTMGFYVVKNVNALACRYR
Protein: Mitochondrial carnitine/acylcarnitine carrier protein (Carnitine/acylcarnitine translocase) (CAC) (CACT) (Solute carrier family 25 member 20) (P97521)
Organism: Rattus norvegicus (Rat)
Function: Mediates the electroneutral exchange of acylcarnitines (O-acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-carnitines) with free carnitine ((R)-carnitine or L-carnitine) across the mitochondrial inner membrane, via a ping-pong mechanism. Key player in the mitochondrial oxidation pathway, it translocates the fatty acids in the form of acylcarnitines into the mitochondrial matrix, where the carnitine palmitoyltransferase 2 (CPT-2) activates them to undergo fatty acid beta-oxidation (Probable). Catalyzes the unidirectional transport (uniport) of carnitine at lower rates than the antiport (exchange).
Subcellular location: Mitochondrion inner membrane; Multi-pass membrane protein.
Interaction partners:
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Carnitine O-acetyltransferase
- Mitochondrial basic amino acids transporter
- Carnitine O-palmitoyltransferase 1, liver isoform
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
- Palmitoyl thioesterase CPT1C
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Organic cation/carnitine transporter 2
Sequence:
MAEEPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTIDCFRKTLFREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKRLQQKSPEDELTYPQLFTAGMLSGVFTTGIMTPGERIKCLLQIQASSGKNKYSGTLDCAKKLYQEFGIRGFYKGTALTLMRDVPASGMYFMTYEWLKNLFTPQGKSVHDLSVPRVLVAGGFRGIFNWVVAIPPDVLKSRFQTAPPGKYPNGFRDVLRELIREEGVTSLYKGFNAVMIRAFPANAACFLGFEIPMKILNWIAPNL
Protein: Zinc finger protein 490 (Q9ULM2)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MRRNSSLSFQMERPLEEQVQSKWSSSQGRTGTGGSDVLQMQNSEHHGQSIKTQTDSISLEDVAVNFTLEEWALLDPGQRNIYRDVMRATFKNLACIGEKWKDQDIEDEHKNQGRNLRSPMVEALCENKEDCPCGKSTSQIPDLNTNLETPTGLKPCDCSVCGEVFMHQVSLNRHMRSHTEQKPNECHEYGEKPHKCKECGKTFTRSSSIRTHERIHTGEKPYECKECGKAFAFLFSFRNHIRIHTGETPYECKECGKAFRYLTALRRHEKNHTGEKPYKCKQCGKAFIYYQPFLTHERTHTGEKPYECKQCGKAFSCPTYLRSHEKTHTGEKPFVCRECGRAFFSHSSLRKHVKTHTGVQPYTCKKCGEAFKSSSSCEVHERTHFGEKPYECKQCGKAFNSSSYLQLHERVHTGEKTYECKECGKAFLYSTHFRIHERTHTREKPYECKQCGRVFIYFSHLRRHERSHTGVKPCECKQCGKAFTCLNSLKVHKRIHTGERPFQCRQCGKAFSYSKSLHVHERTHSRQKP
Protein: Mitochondrial carrier protein, putative (Q388H4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLKQRLQAGQHRNLRSALVHITHGVTPGVATDTAPTSMRVRGIPNLLSGIPVMLLRDVPFAVIQMLCYEALKVALHTDRRPHYLPLCGALGGATAAFITTPLDLLKTRIMLGQVSSPRAGRPKKLSVVCGALQELLHEVPRPTDRWGPMQRFFRGAVPRVTWISIGGSVFFTTYEVVRRYCSCYRFHEK
Protein: Insulinoma-associated protein 1 (Zinc finger protein IA-1) (A7UKY7)
Organism: Xenopus laevis (African clawed frog)
Function: May act as a transcriptional regulator (By similarity). Plays a role in noradrenergic neuron, pancreatic and gastrointestinal endocrine cells differentiation during embryonic development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q63ZV0}.
Interaction partners:
Sequence:
MPKGFLVKRNRKSPPVSYRVREDEENRGESLPGWMLLATMCPTGGAPPPSSPERLASAAPSCNNPRPPPAGQFGNPEAVPQTLYSPTRPVSREQRERKYLGSPVSAESFPGLGSSSEALLFPPTSTANGHHGLALLPPVSSSSSISRTHGKRPAPEPDVKAGAAPGTACKPPAAKKTKAIRKLTFEDEVTTSPVLGLKIKEGPVEPPRPRAPSSGPRPLGEFICQLCKEEYSDPFSLAQHKCSRIVRVEYRCPECHKVFSCPANLASHRRWHKPRPPAVPAVQPKEEALSDRDTPSPESGSEDGLYECPRCARKFRRQAYLRKHLLSHQVTKEPEEAGHMMYQSDEQRPQAKSPPSLNVPQECHPCPVCGETFPGKSSQERHIRLLHSSQLYPCKYCPATFYSSPGLTRHINKCHPSENRQVILLQVPVRPAC
Protein: Secretagogin (O76038)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm. Secreted {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Predominantly cytoplasmic. A small proportion is associated with secretory granules and membrane fractions (By similarity). Detectable in human serum after ischemic neuronal damage. {ECO:0000250}.
Interaction partners:
- Synaptosomal-associated protein 25
- Synaptosomal-associated protein 23
- Double C2-like domain-containing protein alpha
- Rootletin
- Myeloid leukemia factor 2
- Putative hydrolase DDAH2
- Protachykinin-1
Sequence:
MDSSREPTLGRLDAAGFWQVWQRFDADEKGYIEEKELDAFFLHMLMKLGTDDTVMKANLHKVKQQFMTTQDASKDGRIRMKELAGMFLSEDENFLLLFRRENPLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHHKKAISEAKLEEYTGTMMKIFDRNKDGRLDLNDLARILALQENFLLQFKMDACSTEERKRDFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVNKDGKIQKSELALCLGLKINP
Protein: Protein LDOC1 (Leucine zipper protein down-regulated in cancer cells) (O95751)
Organism: Homo sapiens (Human)
Function: May have an important role in the development and/or progression of some cancers.
Subcellular location: Nucleus {ECO:0000269|PubMed:10403563}.
Interaction partners:
- Retrotransposon-derived protein PEG10
Sequence:
MVDELVLLLHALLMRHRALSIENSQLMEQLRLLVCERASLLRQVRPPSCPVPFPETFNGESSRLPEFIVQTASYMLVNENRFCNDAMKVAFLISLLTGEAEEWVVPYIEMDSPILGDYRAFLDEMKQCFGWDDDEDDDDEEEEDDY
Protein: Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein homolog) (GRP-78 homolog) (Binding-immunoglobulin protein homolog) (BiP) (Heat shock 70 kDa protein cognate 3) (Heat shock protein cognate 72) (P29844)
Organism: Drosophila melanogaster (Fruit fly)
Function: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins (By similarity). Acts as a key repressor of the unfolded protein response (UPR) (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P11021}.
Interaction partners:
- Heat shock protein 83
- Hypoxia up-regulated protein 1
- Mesencephalic astrocyte-derived neurotrophic factor homolog
- Heat shock protein 83
- Nucleotide exchange factor Sil1
- Calreticulin
- non-specific serine/threonine protein kinase
- DnaJ homolog shv
- RE14391p
- Derlin-1
Sequence:
MKLCILLAVVAFVGLSLGEEKKEKDKELGTVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQHDIKFFPFKVVEKNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVIAGLQVMRIINEPTAAAIAYGLDKKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGGKEPSRGINPDEAVAYGAAVQAGVLSGEQDTDAIVLLDVNPLTMGIETVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFEIDANGILQVSAEDKGTGNKEKIVITNDQNRLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIGDKDKLGAKLSDDEKNKLESAIDESIKWLEQNPDADPEEYKKQKKDLEAIVQPVIAKLYQGAGGAPPPEGGDDADLKDEL
Protein: FAD synthase (EC 2.7.7.2) (FAD pyrophosphorylase) (FMN adenylyltransferase) (Flavin adenine dinucleotide synthase) [Includes: Molybdenum cofactor biosynthesis protein-like region; FAD synthase region] (Q8NFF5)
Organism: Homo sapiens (Human)
Function: Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.
Subcellular location: [Isoform 1]: Mitochondrion matrix {ECO:0000269|PubMed:20060505}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
Interaction partners:
- Riboflavin kinase
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Tartrate-resistant acid phosphatase type 5
- Low molecular weight phosphotyrosine protein phosphatase
- Elongation factor Tu, mitochondrial
- Probable gluconokinase
Sequence:
MGWDLGTRLFQRQEQRSRLSRIWLEKTRVFLEGSTRTPALPHCLFWLLQVPSTQDPLFPGYGPQCPVDLAGPPCLRPLFGGLGGYWRALQRGREGRTMTSRASELSPGRSVTAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVAQAFGDELKPHPKLEAATKALGGEGWEKLSLVPSSARLHYGTDPCTGQPFRFPLVSVRNVYLFPGIPELLRRVLEGMKGLFQNPAVQFHSKELYVAADEASIAPILAEAQAHFGRRLGLGSYPDWGSNYYQVKLTLDSEEEGPLEECLAYLTARLPQGSLVPYMPNAVEQASEAVYKLAESGSSLGKKVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNLQMLEAEGSMKQALGELQARHPQLEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLGSRENTVRNPALKCLSPGGHPTYRPAYLLENEEEERNSRT
Protein: Zinc finger CCHC domain-containing protein 12 (Smad-interacting zinc finger protein 1) (Q6PEW1)
Organism: Homo sapiens (Human)
Function: Transcriptional coactivator in the bone morphogenetic protein (BMP)-signaling pathway. It positively modulates BMP signaling by interacting with SMAD1 and associating with CBP in the transcription complex. It contributes to the BMP-induced enhancement of cholinergic-neuron-specific gene expression (By similarity).
Interaction partners:
- Cerebellar degeneration-related protein 2-like
- Paraneoplastic antigen Ma1
- Small ubiquitin-related modifier 1
Sequence:
MASIIARVGNSRRLNAPLPPWAHSMLRSLGRSLGPIMASMADRNMKLFSGRVVPAQGEETFENWLTQVNGVLPDWNMSEEEKLKRLMKTLRGPAREVMRVLQATNPNLSVADFLRAMKLVFGESESSVTAHGKFFNTLQAQGEKASLYVIRLEVQLQNAIQAGIIAEKDANRTRLQQLLLGGELSRDLRLRLKDFLRMYANEQERLPNFLELIRMVREEEDWDDAFIKRKRPKRSESMVERAVSPVAFQGSPPIVIGSADCNVIEIDDTLDDSDEDVILVESQDPPLPSWGAPPLRDRARPQDEVLVIDSPHNSRAQFPSTSGGSGYKNNGPGEMRRARKRKHTIRCSYCGEEGHSKETCDNESDKAQVFENLIITLQELTHTEMERSRVAPGEYNDFSEPL
Protein: 116 kDa U5 small nuclear ribonucleoprotein component (Elongation factor Tu GTP-binding domain-containing protein 2) (U5 snRNP-specific protein, 116 kDa) (U5-116 kDa) (O08810)
Organism: Mus musculus (Mouse)
Function: Required for pre-mRNA splicing as component of the spliceosome, including pre-catalytic, catalytic and post-catalytic spliceosomal complexes (By similarity). Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex, a building block of the spliceosome (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15029}.
Interaction partners:
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-processing factor 6
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D1
- U4/U6 small nuclear ribonucleoprotein Prp4
- Pre-mRNA-processing factor 19
- U4/U6 small nuclear ribonucleoprotein Prp31
- Small nuclear ribonucleoprotein Sm D3
- Protein BUD31 homolog
Sequence:
MDTDLYDEFGNYIGPELDSDEDDDELGRETKDLDEDEDEDEDDVGEHEDDHPGMEVVLHEDKKYYPTAEEVYGPEVETIVQEEDTQPLTEPIIKPVKTKKFTLMEQTLPVTVYEMDFLADLMDNSELIRNVTLCGHLHHGKTCFVDCLIEQTHPEIRKRYDQDLCYTDILFTEQERGVGIKSTPVTVVLPDTKGKSYLFNIMDTPGHVNFSDEVTAGLRISDGVVLFIDAAEGVMLNTERLIKHAVQERLAVTVCINKIDRLILELKLPPTDAYYKLRHIVDEVNGLISMYSTDENLILSPLLGNVCFSSSQYSICFTLGSFAKIYADTFGDINYQEFAKRLWGDIYFNPKTRKFTKKAPSSSSQRSFVEFILEPLYKILAQVVGDVDTSLPRTLDELGIHLTKEELKLNIRPLLRLVCKKFFGEFTGFVDMCVQHIPSPKVGAKPKIEHTYTGGVDSDLGEAMSDCDPDGPLMCHTTKMYSTDDGVQFHAFGRVLSGTIHAGQPVKVLGENYTLEDEEDSQICTVGRLWISVARYHIEVNRVPAGNWVLIEGVDQPIVKTATITEPRGNEEAQIFRPLKFNTTSVIKIAVEPVNPSELPKMLDGLRKVNKSYPSLTTKVEESGEHVILGTGELYLDCVMHDLRKMYSEIDIKVADPVVTFCETVVETSSLKCFAETPNKKNKITMIAEPLEKGLAEDIENEVVQITWNRKKLGEFFQTKYDWDLLAARSIWAFGPDATGPNILVDDTLPSEVDKALLGSVKDSIVQGFQWGTREGPLCDELIRNVKFKILDAVVAQEPLHRGGGQIIPTARRVVYSAFLMATPRLMEPYYFVEVQAPADCVSAVYTVLARRRGHVTQDAPIPGSPLYTIKAFIPAIDSFGFETDLRTHTQGQAFSLSVFHHWQIVPGDPLDKSIVIRPLEPQPAPHLAREFMIKTRRRKGLSEDVSISKFFDDPMLLELAKQDVVLNYPM
Protein: Dimethylglycine dehydrogenase, mitochondrial (EC 1.5.8.4) (ME2GLYDH) (Q9UI17)
Organism: Homo sapiens (Human)
Function: Catalyzes the demethylation of N,N-dimethylglycine to sarcosine. Also has activity with sarcosine in vitro.
Subcellular location: Mitochondrion.
Interaction partners:
- Betaine--homocysteine S-methyltransferase 1
- Glycine N-methyltransferase
- Peroxisomal sarcosine oxidase
- Sarcosine dehydrogenase, mitochondrial
- Glycine dehydrogenase
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
- Serine hydroxymethyltransferase, cytosolic
- Glycine cleavage system H protein, mitochondrial
- Serine hydroxymethyltransferase, mitochondrial
- Glycine cleavage system H protein
Sequence:
MLRPGAQLLRGLLLRSCPLQGSPGRPRSVCGREGEEKPPLSAETQWKDRAETVIIGGGCVGVSLAYHLAKAGMKDVVLLEKSELTAGSTWHAAGLTTYFHPGINLKKIHYDSIKLYEKLEEETGQVVGFHQPGSIRLATTPVRVDEFKYQMTRTGWHATEQYLIEPEKIQEMFPLLNMNKVLAGLYNPGDGHIDPYSLTMALAAGARKCGALLKYPAPVTSLKARSDGTWDVETPQGSMRANRIVNAAGFWAREVGKMIGLEHPLIPVQHQYVVTSTISEVKALKRELPVLRDLEGSYYLRQERDGLLFGPYESQEKMKVQDSWVTNGVPPGFGKELFESDLDRIMEHIKAAMEMVPVLKKADIINVVNGPITYSPDILPMVGPHQGVRNYWVAIGFGYGIIHAGGVGKYLSDWILHGEPPFDLIELDPNRYGKWTTTQYTEAKARESYGFNNIVGYPKEERFAGRPTQRVSGLYQRLESKCSMGFHAGWEQPHWFYKPGQDTQYRPSFRRTNWFEPVGSEYKQVMQRVAVTDLSPFGKFNIKGQDSIRLLDHLFANVIPKVGFTNISHMLTPKGRVYAELTVSHQSPGEFLLITGSGSELHDLRWIEEEAVKGGYDVEIKNITDELGVLGVAGPQARKVLQKLTSEDLSDDVFKFLQTKSLKVSNIPVTAIRISYTGELGWELYHRREDSVALYDAIMNAGQEEGIDNFGTYAMNALRLEKAFRAWGLEMNCDTNPLEAGLEYFVKLNKPADFIGKQALKQIKAKGLKRRLVCLTLATDDVDPEGNESIWYNGKVVGNTTSGSYSYSIQKSLAFAYVPVQLSEVGQQVEVELLGKNYPAVIIQEPLVLTEPTRNRLQKKGGKDKT