wanglab/gogpt-training-data huggingface dataset:
Protein: Cystinosin homolog (Q09500)
Organism: Caenorhabditis elegans
Function: Cystine/H(+) symporter that mediates export of cystine, the oxidized dimer of cysteine, from lysosomes (By similarity). May play a role in the degradation of engulfed apoptotic cells.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:18351800}; Multi-pass membrane protein {ECO:0000269|PubMed:18351800}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:18351800}. Note=During degradation of apoptotic cells when lysosomes fuse to phagosomes, located to phagosomal surfaces until the cell corpse is fully degraded. {ECO:0000269|PubMed:18351800}.
Interaction partners:
- Lysosomal amino acid transporter 1
- Hepatocyte growth factor-regulated tyrosine kinase substrate
Sequence:
MSFPVAFLLVLFLVPFTFATNNLVVRQKELEIVIGGEVSVNFQIKNHTSQSLNATRISLSQSPYISHPDAILVDNWNANVTVLGSQLVSGAILEALNCTTDGSITCPLDLEDAFARITVIRSHFLAILIQIVGWTYFFAWSISFYPQMYLNFKRKSVVGLNFDFLSLNLVGFCAYAIFNLLMYYNSHVKNEYNIVNPRSPPPVLLNDVVFAVHAFLACFITILQCLFYERDNQSVSSKCIALMIVLISFGFCSAAATVLRKIQLLSFVTSLSYIKMAVTCCKYFPQAYFNYTRKSTVGWSIGNIMLDFTGGTLDILQMILQAVNVNDWSAFYANPVKFGLGFVSIFFDIIFMVQHYVLYPNAEVPHNEYHGVDNPNPDNIARDAEQYAGDSESMESTEPIIVHD
Protein: Amino-acid acetyltransferase (EC 2.3.1.1) (N-acetylglutamate synthase) (AGS) (NAGS) (O33289)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of L-glutamate to alpha-N-acetyl-L-glutamate. L-glutamine is a significantly better substrate compared to L-glutamate.
Interaction partners:
- Arginine biosynthesis bifunctional protein ArgJ
- Acetylglutamate kinase
- Probable histone acetyltransferase Rv0428c
- Alanine aminotransferase
- NAD-specific glutamate dehydrogenase
- Glutamate synthase large chain
- Probable phosphatidylglycerophosphate synthase
Sequence:
MTERPRDCRPVVRRARTSDVPAIKQLVDTYAGKILLEKNLVTLYEAVQEFWVAEHPDLYGKVVGCGALHVLWSDLGEIRTVAVDPAMTGHGIGHAIVDRLLQVARDLQLQRVFVLTFETEFFARHGFTEIEGTPVTAEVFDEMCRSYDIGVAEFLDLSYVKPNILGNSRMLLVL
Protein: Glutamate receptor 4 (GluR-4) (GluR4) (AMPA-selective glutamate receptor 4) (GluR-D) (Glutamate receptor ionotropic, AMPA 4) (P48058)
Organism: Homo sapiens (Human)
Function: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P19493}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19493}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P19493}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19493}. Cell projection, dendrite {ECO:0000250|UniProtKB:P19493}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P42262}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P42262}.
Interaction partners:
- Glutamate receptor 2
- Glutamate receptor 3
- Glutamate receptor 1
- Voltage-dependent calcium channel gamma-2 subunit
- cAMP-dependent protein kinase catalytic subunit alpha
- Protein cornichon homolog 2
- Voltage-dependent calcium channel gamma-8 subunit
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- Protein cornichon homolog 3
Sequence:
MRIISRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVIKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDVPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGVLDKLKNKWWYDKGECGPKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEAIRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASDLP
Protein: Ribonucleoside-diphosphate reductase small chain (EC 1.17.4.1) (Q382Q2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribonucleoside-diphosphate reductase
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
- dTMP kinase
- dTMP kinase
- Nucleoside diphosphate kinase
- Nucleoside diphosphate kinase, putative
- Nucleoside diphosphate kinase, putative
- Guanylate kinase, putative
- Guanylate kinase, putative
Sequence:
MPPKSHKRSRKEGEVEEPLLTENPDRYVIFPIKYPDIWQKYKEAESSIWTVEEIDLGNDMTDWEKLDDGERHFIKHVLAFFAASDGIVLENLAERFMCEVQVPEVRCFYGFQIAMENIHSETYSVLIDTYVVDPDEKQRLLHAIRTIPCIEKKAKWAIEWIGSQTSFPTRLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYEKYIVNKLPRDRVLEIICNAVSIEREFICDALPVRLIGMNSQLMTQYIEFVADRLLVSLGYDRHYNSKNPFDFMDMISLQGKTNFFEKKVGEYQKAGVMSSERSSKVFSLDADF
Protein: Transcriptional activator protein Pur-alpha (Purine-rich single-stranded DNA-binding protein alpha) (Q00577)
Organism: Homo sapiens (Human)
Function: This is a probable transcription activator that specifically binds the purine-rich single strand of the PUR element located upstream of the MYC gene. May play a role in the initiation of DNA replication and in recombination.
Subcellular location: Nucleus.
Interaction partners:
- Fragile X messenger ribonucleoprotein 1
- Y-box-binding protein 1
- RNA-binding protein FXR2
- RNA-binding protein FXR1
- N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
- Nucleolin
- Adenosine kinase
- DNA helicase MCM8
- Cardiolipin synthase
- Heterogeneous nuclear ribonucleoproteins A2/B1
Sequence:
MADRDSGSEQGGAALGSGGSLGHPGSGSGSGGGGGGGGGGGGSGGGGGGAPGGLQHETQELASKRVDIQNKRFYLDVKQNAKGRFLKIAEVGAGGNKSRLTLSMSVAVEFRDYLGDFIEHYAQLGPSQPPDLAQAQDEPRRALKSEFLVRENRKYYMDLKENQRGRFLRIRQTVNRGPGLGSTQGQTIALPAQGLIEFRDALAKLIDDYGVEEEPAELPEGTSLTVDNKRFFFDVGSNKYGVFMRVSEVKPTYRNSITVPYKVWAKFGHTFCKYSEEMKKIQEKQREKRAACEQLHQQQQQQQEETAAATLLLQGEEEGEED
Protein: 60S acidic ribosomal protein P0 (F8VWS0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILVFDNGSIYNPEVLDITEETLHSRFLEGVRNVASVCLQIGYPTVASVPHSIINGYKRVLALSVETDYTFPLAEKVKAFLADPSAFVAAAPVAAATTAAPAAAAAPAKVEAKEESEESDEDMGFGLFD
Protein: Uncharacterized protein P22H7.03 (O13619)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- 1,3-beta-glucan synthase component bgs1
- Cell division control protein 15
- LIM domain-containing protein C4F6.12
- Uncharacterized beta-glucan synthesis-associated protein C17G6.11c
- Uncharacterized beta-glucan synthesis-associated protein C23H3.11c
- Probable Rho-GTPase-activating protein 7
- Cell wall alpha-1,3-glucan synthase ags1
- 1,3-beta-glucan synthase component bgs4
- Septation protein imp2
Sequence:
MSQSPIDYNESLRPDDMLDNELNYELANEVSAGDEEPYDDDIWESEDLEPVGHDIQPMDSVSDFHVKDFSEKKYSPYTDEIASAQLTGPSESAFGSASSLGTVESPVTMQSATLLWDPSVKEVDDILHNEDFYDGRDLNIFTLRGFVNILTLILLSCGLLMLFIGYPILSAVEVEKQRKKN
Protein: Chaperone protein dnaJ 2 (AtDjA2) (P42825)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a continuous role in plant development probably in the structural organization of compartments.
Subcellular location: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 17
- Heat shock 70 kDa protein 1
- Heat shock 70 kDa protein 3
- Heat shock 70 kDa protein 8
- Heat shock 70 kDa protein 2
- Heat shock protein 90-2
- Heat shock 70 kDa protein 10, mitochondrial
- Chaperone protein dnaJ 8, chloroplastic
- Heat shock 70 kDa protein 5
Sequence:
MFGRGPSRKSDNTKFYEILGVPKTAAPEDLKKAYKKAAIKNHPDKGGDPEKFKELAQAYEVLSDPEKREIYDQYGEDALKEGMGGGGGGHDPFDIFSSFFGSGGHPFGSHSRGRRQRRGEDVVHPLKVSLEDVYLGTTKKLSLSRKALCSKCNGKGSKSGASMKCGGCQGSGMKISIRQFGPGMMQQVQHACNDCKGTGETINDRDRCPQCKGEKVVSEKKVLEVNVEKGMQHNQKITFSGQADEAPDTVTGDIVFVIQQKEHPKFKRKGEDLFVEHTISLTEALCGFQFVLTHLDKRQLLIKSKPGEVVKPDSYKAISDEGMPIYQRPFMKGKLYIHFTVEFPESLSPDQTKAIEAVLPKPTKAAISDMEIDDCEETTLHDVNIEDEMKRKAQAQREAYDDDEEDHPGGAQRVQCAQQ
Protein: Purinergic receptor P2X, ligand-gated ion channel, 5 (B1AUD6)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MGQAAWKGFVLSLFDYKTAKFVVAKSKKVGLLYRVLQLTILLYLLIWVFLIKKSYQDIDTSLQSAVVTKVKGVAYTNTTMLGERLWDVADFVIPSQREGIPDGECSEDTDCHAGESVVAGHGLKTGRCLRVGNSTRGTCEIFAWCPVETKSMPTDPLLKDAEGFTIFIKNFIRFPKFNFSKANVLETGNKHFLKTCHFSSTNLYCPIFRLGSIVRWAGADFQDIALKGGVIGIHIEWDCDLDKAASHCNPHYYFNRLDNKHTQSISSGYNFRFARYYRDPHGVEFRDLMKAYGIRFDVIVNGKGAFFCDLVLIYLIRKSEFYRDKKFEKV
Protein: Bud site selection protein 27 (P43573)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in gene expression controlled by TOR kinase and nutrient signaling. May also be involved in positioning the proximal bud pole signal.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- Prefoldin subunit 6
- DNA-directed RNA polymerase III subunit RPC1
- RNA polymerase II nuclear localization protein IWR1
- GPN-loop GTPase 3
- Prefoldin subunit 2
- DNA-directed RNA polymerase II subunit RPB1
- Prefoldin subunit 5
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- GPN-loop GTPase 2
Sequence:
MDLLAASVESTLKNLQDKRNFLSEQREHYIDIRSRLVRFINDNDDGEEEGEGQGMVFGDIIISTSKIYLSLGYEYYVEKTKEEAITFVDDKLKLMEDAIEQFNLKIEEAKKTLDNLNHMEDGNGIEEDEANNDEDFLPSMEIREELDDEGNVISSSVTPTTKQPSQSNSKKEQTPAVGPKEKGLAKEKKSKSFEENLKGKLLKRNDEVKKKVQPSKVDTENVYTFADLVQQMDQQDELEDGYIETDEINYDYDAFENSNFKVNDNYEEDDEDEDEEEYLNHSIIPGFEAQSSFLQQIQRLRAQKQSQDHEREEGDVNKSLKPILKKSSFAENSDKKQKKKQVGFASSLEIHEVENLKEENKRQMQSFAVPMYETQESTGIANKMTSDEFDGDLFAKMLGVQEADEVHEKYKEELINQERLEGEASRSNRRTRVSRFRKDRASKKENTLSTFKQETTRSVENEVVEKEPVVGDIIEKEPVVGDVIEKEPVVGDVIEKEPAVTDIVEREPAVNDIVERKPVVGDIIEKEPTINDIVEKEPEINSKSEFETPFKKKKLKSLQKPRSSKSMKKKFDPKILENISDDDYDDDDDGNKKLLSNKSKNNTDEQDKFPSKIQEVSRSMAKTGATVGSEPVRITNVDYHALGGNLDDMVKAYSLGLYDDDLEEDPGTIVEKLEDFKEYNKQVELLRDEIRDFQLENKPVTMEEEENDGNVMNDIIEHEFPESYTNDEDEVALHPGRLQEEVAIEYRRLKEATASKWQSSSPAAHTEGELEPIDKFGNPVKTSRFRSQRLHMDSKP
Protein: Restriction of telomere capping protein 5 (Q12108)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in a process influencing telomere capping.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Glutamyl-tRNA
- Aspartate--tRNA ligase, mitochondrial
Sequence:
MGQSSSISSSNEEGSSHSKKFTNSKDILAYFNNKAQQQVTIPELVSFKGNLQIEDLNTPISHKALCNSLYFPQNHAMIVGIVTNMLRVLSNFPLMKSSYEPITGYGLLKCILLLNRARCAKFLKTKSYDQLKLLFISLSLQKTDKEELSEESENDGNKELTIKQIITGFDDVDTEMLCIPADFMLQFLTWLLILTVDCPTTNSKLDNTETHDQWGNFKVSALNLLRTMNPDVVGDIESHSITFQQFSTAIRTVMPNLLKPLENLMEHFFYLQHDLVDHDTNLSSIQDSKVMTPALLAQLSTGLPKELFIHKLQSLYIGRKSGFSMRSLQAKVFKWMAPSILVVSGMRITNSEEYAAEKNPRYRHFLEEFPKLKESDQMMDASHLNKRKTTFAVYIDDPWKVTNKDYFGDLNTRIIEISPRQDIYKVNQKGTIYFNTIGGGIGIGDKQPLIKPASKRYIPGNVSLTFDSTLEFAVFRNTGYGGSLDPGLLSMERKEENSPYELHFLIQDVEVWGCGGEKELEEQIKQLEWEEAESKRRQQINLRSLGEDRALLEMAGLVGQHQGGGSM
Protein: Carnitine O-acetyltransferase (Carnitine acetylase) (EC 2.3.1.137) (EC 2.3.1.7) (Carnitine acetyltransferase) (CAT) (CrAT) (P47934)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible transfer of acyl groups from carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio. Also plays a crucial role in the transport of fatty acids for beta-oxidation. Responsible for the synthesis of short- and branched-chain acylcarnitines. Active towards some branched-chain amino acid oxidation pathway (BCAAO) intermediates. Trans-2-enoyl-CoAs and 2-methylacyl-CoAs are poor substrates.
Subcellular location: Endoplasmic reticulum {ECO:0000305}. Peroxisome {ECO:0000305}. Mitochondrion inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- Mitochondrial carnitine/acylcarnitine carrier protein
- Vesicular acetylcholine transporter
- Ribonuclease P protein subunit p14
- Peroxisomal acyl-coenzyme A oxidase 1
- Trifunctional enzyme subunit beta, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MLAFAARTVVKPLGLLKPSSLMKVSGRFKAHQDALPRLPVPPLQQSLDYYLKALQPIVSEEEWAHTKQLVDEFQTSGGVGERLQKGLERRAKKMENWLSEWWLKTAYLQFRQPVVIYSSPGVILPKQDFVDLQGQLRFAAKLIEGVLDFKSMIDNETLPVEFLGGQPLCMNQYYQILSSCRVPGPKQDSVVNFLKSKRPPTHITVVHNYQFFELDVYHSDGTPLTSDQIFVQLEKIWNSSLQSNKEPVGILTSNHRNTWAKAYNNLIKDKVNRESVNSIQKSIFTVCLDKQVPRVSDDVYRNHVAGQMLHGGGSKFNSGNRWFDKTLQFIVAEDGSCGMVYEHAAAEGPPIVALVDHVMEYTKKPELVRSPMVPLPMPKKLRFNITPEIKNDIEKAKQNLSIMIQDLDIMMLTFHHFGKDFPKSEKLSPDAFIQVALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASIDSLAFVKGMGDSTVPEQQKVELLRKAVQAHRAYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMDTSYAIAMHFNLSTSQVPAKTDCVMFFGPVVPDGYGICYNPMEAHINFSVSAYNSCAETNAARMAHYLEKALLDMRTLLQNHPRAKL
Protein: Allophagy receptor allo-1 (Q9U389)
Organism: Caenorhabditis elegans
Function: Autophagy receptor, which is required for allophagy, an autophagic process in which paternal organelles, including mitochondria and membranous organelles, are degraded in early embryos. After fertilization, recruited to ubiquitin-modified paternal organelles and is required for the formation of autophagosomes around the paternal organelles. Also plays a role in the regulation of autophagy in germ cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29255173}. Note=Localizes to cytoplasmic puncta in oocytes and to paternal organelles in 1-stage embryos. After fertilization, localizes around paternal mitochondria and ubiquitinated membranous organelles at metaphase phase of meiosis I, before lgg-1 is recruited. Also, localizes to paternal organelles during meiosis II. Co-localizes with ikke-1 in embryos and oocytes. {ECO:0000269|PubMed:29255173}.
Interaction partners:
- Inhibitor of nuclear factor kappa-B kinase epsilon subunit homolog 1
- Protein lgg-1
- Ubiquitin-conjugating enzyme E2 W
- FUN14 domain-containing protein fndc-1
- Golgin subfamily A conserved domain-containing protein
Sequence:
MNDPLDSLSNDEFEIIETFDPETEDREDQWSIQQSIRIEPISIQMPNTLQSQRAPSPVGSKAPESLKDEDPDRTPEASIVETPLLTETLKEDRTPMSTPLASLVNSSQSPEFTLQNMSIVSESECSNNSSLVNVADVESTEIALRTSLLLVSELKSQLQAAKMSESTLLKSNSNHEIEENKKLSEKMEVMKNEFELKMQESAASVEKVIQEKDSAIEQLKVQLAQSQQVAELWKQGAEKNSNAQYSDSKTTIDRLLEENSKLRNLVDEEVARRLEESERRKLAEDQLKHARGGSVFDPPASFVASQLAERTTYSLNLEHELITLRKELEETKEALKKSVEESSNKDEIVSALHELAGPTGEHPHARFERAGDQQSEAEMSSTWSAGRLLELSRQIVHFISHQ
Protein: E3 ubiquitin-protein ligase SIAH2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH2) (Seven in absentia homolog 2) (Siah-2) (mSiah2) (Q06986)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia. Promotes monoubiquitination of SNCA (By similarity). Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (GPS2, POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP). It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes. Has some overlapping function with SIAH1. Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 does not. Regulates cellular clock function via ubiquitination of the circadian transcriptional repressors NR1D1 and NR1D2 leading to their proteasomal degradation (By similarity). Plays an important role in mediating the rhythmic degradation/clearance of NR1D1 and NR1D2 contributing to their circadian profile of protein abundance. Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4. Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O43255}. Nucleus {ECO:0000250|UniProtKB:O43255}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000250|UniProtKB:O43255}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 13
- Serine/threonine-protein kinase LATS2
- Calcyclin-binding protein
- Prolyl hydroxylase EGLN3
- Prolyl hydroxylase EGLN2
- Protein sprouty homolog 2
- Nuclear receptor corepressor 1
- Hypoxia-inducible factor 1-alpha
- A-kinase anchor protein 1, mitochondrial
Sequence:
MSRPSSTGPSANKPCSKQPPPPQTPHAPSPAAPPAAATISAAGPGSSAVPAAAAVISGPGAGGGADPVSPQHHELTSLFECPVCFDYVLPPILQCQAGHLVCNQCRQKLSCCPTCRGALTPSIRNLAMEKVASAVLFPCKYATTGCSLTLHHTEKPEHEDICEYRPYSCPCPGASCKWQGSLEAVMSHLMHAHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGHHFMLVLEKQEKYEGHQQFFAIVLLIGTRKQAENFAYRLELNGNRRRLTWEATPRSIHDGVAAAIMNSDCLVFDTAIAHLFADNGNLGINVTISTCCQ
Protein: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (PP2A subunit A isoform PR65-beta) (PP2A subunit A isoform R1-beta) (Q7TNP2)
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.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform
Sequence:
MAGAAGPGSGPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRTELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLESLATVEETVVRDKAVESLRQISQEHTPVALEAHFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQHFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKTEIVPLFTNLASDEQDSVRLLAVEACVSIAQLLSQEDLEALVMPTLRQAAEDKSWRVRYMVADKFSELQKAVGPKIALSDLIPAFQSLLRDCEAEVRAAAAHKVRELCENLPAEGRETVIMNQILPYIKELVSDTNQHVKSALASVIMGLSTVLGKENTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATNNLMKLVQKFGTEWAQNTIVPKVLVMANDPNYLHRMTTLFCINALSEACGKEITTKQMLPIVLKMAGDQVANVRFNVAKSLQKIGPILDTNALQGEVKPVLQKLGQDEDMDVKYFAQEAISVLALA
Protein: DoxX family protein (Q8VK13)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSGLTSPKTYAVLAALQAGDAVACAIPLPPIARLLDDLDVPVSVRPVLPVVKAASAVGLLSVTRFPALARLTTAMLTLYFILAVGAHVRVRDRVVNAIPAASFLTLFALMTAKGPERT
Protein: Solute carrier family 52, riboflavin transporter, member 2 (Porcine endogenous retrovirus A receptor 2) (Protein GPR172B) (Riboflavin transporter 1) (rRFT1) (B5MEV3)
Organism: Rattus norvegicus (Rat)
Function: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism. May also act as a receptor for 4-hydroxybutyrate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18632736, ECO:0000269|PubMed:19122205}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAAPPLGRLVLTHLLVALFGMGSWIAVNGIWVELPVVVKELPEGWSLPSYLSVLVALGNLGLLLVTLWRRLAPGKSERIPIQVVQGLSIVGTGLLAPLWSNMALVAGQLHSVAFLTLAFVLALSCCASNVTFLPFLSHLPPPFLRSFFLGQGLSALLPCVLALAQGVGRLECLHVPANGTTGPPIKVSPINFPERFSAGTFFWVLTALLGTSAAAFQGLLLLLPSPPPEATMGTGLRVETPGTEEEEEEEEASPLQEPPGQVASIVSSPDPKAHRLFSSRSACLLGLLAITNALTNGVLPAVQSFSCLPYGRLAYHLAVVLGSSANPLACFLAMAVLCRSLAGLYGLCLLGMFFGTYLMTLAVLSPCPPLVGTSAGVVLVVLSWVLCAGVFSYIKVATSSMLHSGGRPALLAAGVAIQVGSLLGAIAMFPPTSVYPVFRSGEDCVDQCGP
Protein: Thymidine kinase, cytosolic (EC 2.7.1.21) (P04047)
Organism: Gallus gallus (Chicken)
Function: Cell-cycle-regulated enzyme of importance in nucleotide metabolism. Catalyzes the first enzymatic step in the salvage pathway converting thymidine into thymidine monophosphate. Transcriptional regulation limits expression to the S phase of the cell cycle and transient expression coincides with the oscillation in the intracellular dTTP concentration.
Subcellular location: Cytoplasm.
Interaction partners:
- Thymidylat_synt domain-containing protein.
- Cytidine deaminase
- Thymidylate kinase
- Deoxycytidylate deaminase
- dNK domain-containing protein.
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Dihydrofolate reductase
- Uridine phosphorylase
- Thymidylat_synt domain-containing protein.
- Uridine phosphorylase
Sequence:
MNCLTVPGVHPGSPGRPRGQIQVIFGPMFSGKSTELMRRVRRFQLAQYRCLLVKYAKDTRYCTTGVSTHDRNTMEARPACALQDVYQEALGSAVIGIDEGQFFPDIVEFCEKMANTGKTVIVAALDGTFQRKAFGSILNLVPLAESVVKLNAVCMECYREASYTKRLGAEREVEVIGGADKYHSVCRACYFQKRPQQLGSENKENVPMGVKQLDMPASRKIFAS
Protein: E-box binding protein 1 (Transcription factor 12 isoform X2) (Q6QR58)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Stem cell protein
- Myogenic factor
- Myogenic factor
- Rhombotin-2
- Myogenin
Sequence:
MNPQQRIAAIGTDKELSDLLDFSAMFSPPVNSGKNRPTTLGSSQFSASGIDERTTEAPWAAGGQSSPSYDESSRGFSDSPHYGDHLSDSRLVSHEGLSPTPFMSSSIMGKSERPPFSAYGREPGVSGCQSSLRSDMGLSSPGPVTTTGKSPAPFYSFTGSNPRRRSLQDPSPLDPLQAKKVRKVPPGLPSSVYAPSPNSDDFNRESPSYPSSKPPSSMFASTFFDATHNSSDPWNSSNGISQPAYGGMLGGSSSHMPQSGNYSSLHSHDRLNYPPHSVSPTDINASLPPMSSFHRSTASSSPFVTASHTPPVNTTEGVMAAANRGNATGSSQTGDALGKALASIYSPDHTSSSFPSNPSTPVGSPSPLTAQAGAASAGTVVTASGPPGRAGTTQWPRAAGQTPSSPSYENSLHSLSRMEDRLDRLDDAIHVLRNHAVGSTASLPSDIHSLLGQTHNGPITAIGTNFPTSGLVTSRTASMGPAHREETASLNANHTGLQSTPGPASSAELNHQADTFRGSQSFALKCLSGSLASQVASALELKIENQDKDDMHDNHSSDDIKSDDESDKRDIKTPRGGTRTSSINEDEDLNPEQKAERERERRMANNARERLRVRDINEAFKELGRMCQLHLKSEKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSGVSGEPQQTHPSVHPGLTDTSNPMGHL