wanglab/gogpt-training-data huggingface dataset:
Protein: Histone deacetylase 1 (HD1) (EC 3.5.1.98) (Protein deacetylase HDAC1) (EC 3.5.1.-) (Protein deacylase HDAC1) (EC 3.5.1.-) (O09106)
Organism: Mus musculus (Mouse)
Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity). Also functions as deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3 and TSHZ3 (By similarity). Deacetylates SP proteins, SP1 and SP3, and regulates their function (By similarity). Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons (By similarity). Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation (By similarity). Deacetylates TSHZ3 and regulates its transcriptional repressor activity (By similarity). Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B (By similarity). Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (By similarity). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones.
Subcellular location: Nucleus {ECO:0000269|PubMed:11115394, ECO:0000269|PubMed:21454521}.
Interaction partners:
- Histone-binding protein RBBP7
- Nuclear receptor corepressor 2
- Chromodomain-helicase-DNA-binding protein 4
- Nuclear receptor corepressor 1
- DNA helicase
- DNA
- Lysine-specific histone demethylase 1A
- Paired amphipathic helix protein Sin3a
- Histone-binding protein RBBP4
- Histone deacetylase complex subunit SAP30
Sequence:
MAQTQGTKRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEEDPDKRISICSSDKRIACEEEFSDSDEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA
Protein: Solute carrier family 51 member A (D4AC81)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- SLC51 subunit beta
- Ileal sodium/bile acid cotransporter
- Bile salt export pump
- Hepatic sodium/bile acid cotransporter
- Cytochrome P450 7A1
- Bile acid receptor
- Nuclear receptor subfamily 0 group B member 2
- Gastrotropin
- ATP-binding cassette sub-family C member 2
- Fibroblast growth factor
Sequence:
MEPGRTHIKLDPRYTADLLELLETNYSISPACFSHPPTAAQLLRELGSVEIALTIILTFFTIGSVAIFLEDAIYLYKNTLCPIKKRTLIWSSSAPTVVSVFCCFGLWIPRALTLVEMAITSFYAVCFYLLMMVMVEGFGGKEAVLRTLKDTPMRVHTGPCCCCCPCCPPLILTRKKLQLLMLGPFQYAFFKIVMSIVGLFLIPDGIYDPAEISEKSAALWISNFLAVSTLLALWSLAILFRQAKLHLGEQNMGSKFALFQVLVILTALQPSIFSILANSGQIACSPPYSSKIRSQVMNCHMLILETFLLTVLTRMYYRKKDNKVGYEACLPPDLDSTLKA
Protein: Polypeptide N-acetylgalactosaminyltransferase (EC 2.4.1.-) (Protein-UDP acetylgalactosaminyltransferase) (B0V0U4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU361242}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU361242}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1-B
- EF-hand calcium-binding domain 2.
- alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase
- Protein Z, vitamin K-dependent plasma glycoprotein a
- Hexosyltransferase.
- C1GALT1-specific chaperone 1
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1-A
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3
- Phosphoinositide phospholipase C.
- Golgi phosphoprotein 3-like.
Sequence:
MRRKSRMYLCFAVLWVLGIAYYFYSGTTLSRKDDWSGINSNRIQTHSNADDKDHSLESLPLGKVRWQDYDQDLYVGATVVRPGQDPYARNKFNQVESDKLRMDRNIPDTRHDHCRHKQWRTDLPASSVVITFHNEARSALLRTVISVLKKSPPHLVKEIILVDDYSDNPEDGALLGKIEKVRVLRNDRREGLMRSRVRGADAATASVLTFLDSHCECNEHWLEPLLERVAEDKTRVVSPIIDVINMDNFQYVGASADLKGGFDWNLVFKWDYMTLEQRRARQGNPIAPIKTPMIAGGLFVMDKDYFEELGKYDMMMDVWGGENLEISFRVWQCGGSLEIIPCSRVGHVFRKQHPYTFPGGSGTVFARNTRRAAEVWMDDFKNFYYAAVPSARNVPYGNIQSRLEMKKRLGCKPFKWYLENVYPELRVPDHQDIAFGALQQGQNCLDTLGHFADGVVGVYECHNAGGNQEWALTKDKSVKHMDLCLTVVDRTAGSQIKLQGCRENDTRQKWEQIDNNTKLRHVGSNLCLDSRSARSGGLTVEVCSPSLTQQWKFTLNLQP
Protein: Taste receptor type 2 member 102 (T2R102) (mT2R51) (STC9-7) (Q7M717)
Organism: Mus musculus (Mouse)
Function: Putative taste receptor which may play a role in the perception of bitterness.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MNMESVLHNFATVLIYVEFIFGNLSNGFIVLSNFLDWVIKQKLSLIDKILLTLAISRITLIWEIYAWFKSLYDPSSFLIGIEFQIIYFSWVLSSHFSLWLATTLSVFYLLRIANCSWQIFLYLKWRLKQLIVGMLLGSLVFLLGNLMQSMLEERFYQYGRNTSVNTMSNDLAMWTELIFFNMAMFSVIPFTLALISFLLLIFSLWKHLQKMQLISRRHRDPSTKAHMNALRIMVSFLLLYTMHFLSLLISWIAQKHQSELADIIGMITELMYPSVHSCILILGNSKLKQTSLCMLRHLRCRLKGENITIAYSNQITSFCVFCVANKSMR
Protein: DNA ligase 1 (EC 6.5.1.1) (DNA ligase I) (Polydeoxyribonucleotide synthase [ATP] 1) (P04819)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. The mitochondrial form is required for mitochondrial DNA maintenance but is non-essential while the nuclear form is essential for cell viability.
Subcellular location: [Isoform Mitochondrial]: Mitochondrion.; SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus.
Interaction partners:
- Proliferating cell nuclear antigen
- Flap endonuclease 1
- DNA mismatch repair protein MSH6
- Exodeoxyribonuclease 1
- ATP-dependent DNA helicase II subunit 1
- DNA polymerase alpha catalytic subunit A
- DNA polymerase delta catalytic subunit
- Thymidylate synthase
- DNA replication ATP-dependent helicase/nuclease DNA2
- N-glycosylase/DNA lyase
Sequence:
MRRLLTGCLLSSARPLKSRLPLLMSSSLPSSAGKKPKQATLARFFTSMKNKPTEGTPSPKKSSKHMLEDRMDNVSGEEEYATKKLKQTAVTHTVAAPSSMGSNFSSIPSSAPSSGVADSPQQSQRLVGEVEDALSSNNNDHYSSNIPYSEVCEVFNKIEAISSRLEIIRICSDFFIKIMKQSSKNLIPTTYLFINRLGPDYEAGLELGLGENLLMKTISETCGKSMSQIKLKYKDIGDLGEIAMGARNVQPTMFKPKPLTVGEVFKNLRAIAKTQGKDSQLKKMKLIKRMLTACKGIEAKFLIRSLESKLRIGLAEKTVLISLSKALLLHDENREDSPDKDVPMDVLESAQQKIRDAFCQVPNYEIVINSCLEHGIMNLDKYCTLRPGIPLKPMLAKPTKAINEVLDRFQGETFTSEYKYDGERAQVHLLNDGTMRIYSRNGENMTERYPEINITDFIQDLDTTKNLILDCEAVAWDKDQGKILPFQVLSTRKRKDVELNDVKVKVCLFAFDILCYNDERLINKSLKERREYLTKVTKVVPGEFQYATQITTNNLDELQKFLDESVNHSCEGLMVKMLEGPESHYEPSKRSRNWLKLKKDYLEGVGDSLDLCVLGAYYGRGKRTGTYGGFLLGCYNQDTGEFETCCKIGTGFSDEMLQLLHDRLTPTIIDGPKATFVFDSSAEPDVWFEPTTLFEVLTADLSLSPIYKAGSATFDKGVSLRFPRFLRIREDKGVEDATSSDQIVELYENQSHMQN
Protein: Dynamin associated protein isoform Dap160-1 (O61618)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSAVDAWAVTPRERLKYQEQFRALQPQAGFVTGAQAKGFFLQSQLPPLILGQIWALADTDSDGKMNINEFSIACKLINLKLRGMDVPKVLPPSLLSSLTGDVPSMTPRGSTSSLSPLDPLKGIVPAVAPVVPVVAPPVAVATVISPPGVSVPSGPTPPTSNPPSRHTSISERAPSIESVNQGEWAVQAAQKRKYTQVFNANDRTRSGYLTGSQARGVLVQSKLPQVTLAQIWTLSDIDGDGRLNCDEFILAMFLCEKAMAGEKIPVTLPQEWVPPNLRKIKSRPGSVSGVVSRPGSQPASRHASVSSQSGVGVVDADPTAGLPGQTSFEDKRKENYVKGQAELDRRRKIMEDQQRKEREERERKEREEADKREKARLEAERKQQEELERQLQRQREIEMEKEEQRKRELEAKEAARKELEKQRQQEWEQARIAEMNAQKEREQERVLKQKAHNTQLNVELSTLNEKIKELSQRICDTRAGVTNVKTVIDGMRTQRDTSMSEMSQLKARIKEQNAKLLQLTQERAKWEAKSKASGAALGGENAQQEQLNAAFAHKQLIINQIKDKVENISKEIESKKEDINTNDVQMSELKAELSALITKCEDLYKEYDVQRTSVLELKYNRKNETSVSSAWDTGSSSAWEETGTTVTDPYAVASNDISALAAPAVDLGGPAPEGFVKYQAVYEFNARNAEEITFVPGDIILVPLEQNAEPGWLAGEINGHTGWFPESYVEKLEVGEVAPVAAVEAPVDAQVADTYNDNINTSSIPAASADLTAAGDVEYYIAAYPYESAEEGDLSFSAGEMVMVIKKEGEWWTGTIGSRTGMFPSNYVQKADVGTASTAAAEPVESLDQETTLNGNAAYTAAPVEAQEQVYQPLPVQEPSEQPISSPGVGAEEAHEDLDTEVSQINTQSKTQSSEPAESYSRPMSRTSSMTPGMRAKRSEIAQVIAPYEATSTEQLSLTRGQLIMIRKKTDSGWWEGELQAKGRRRQIGWFPATYVKVLQGGRNSGRNTPVSGSRIEMTEQILDKVIALYPYKAQNDDELSFDKDDIISVLGRDEPEWWRGELNGLSGLFPSNYVGPFVTSGKPAKANGTTKK
Protein: Protein tramtrack, beta isoform (Repressor protein fushi tarazu) (Tramtrack p69) (P17789)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds to a number of sites in the transcriptional regulatory region of ftz. Isoform beta is required to repress inappropriate segmentation gene transcription and repress genes incompatible with development of photoreceptor cell fates. Probable repressor of the transcription of the segmentation genes ftz, eve, h, odd, run, and en. Inhibits Trl-dependent activation of eve. May bind to the region AGGGC/TGG. Degradation of ttk is directed by binding of sinah or sina, via the adapter molecule phyl which binds to the BTB domain of ttk. A second method of degradation exists that is phyl-independent, this is mediated by recognition of motifs in the C-terminus of ttk.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MKMASQRFCLRWNNHQSNLLSVFDQLLHAETFTDVTLAVEGQHLKAHKMVLSACSPYFNTLFVSHPEKHPIVILKDVPYSDMKSLLDFMYRGEVSVDQERLTAFLRVAESLRIKGLTEVNDDKPSPAAAAAGAGATGSESTATTPQLQRIQPYLVPQRNRSQAGGLLASAANAGNTPTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGNGKMCNESYSGNDDGSDDNQPNAGHTDDLNESRDSLPSKRSKNSKDHRVVSHHEDNSTSDGNDSDGEGLDTSYMEPQLMLDEYDEPVEFKYNPLTDNSSPTQDHTDGSHLNEQARQQAFLIAAQRKHQVETAAAAAASGIKLNIIGMAAGGAQVKSMVSIPKLTPIGKVNAASTPLVSPAGSFSTATVKPRVQKRPKLGKQNGDVKPAVFSSQEYLDIYNSNDGFKLKAAGLSGSTPNLSAGLGTPSVKTKLNLSSNVGEGEAEGSVRDYCTKEGEHTYRCKVCSRVYTHISNFCRHYVTSHKRNVKVYPCPFCFKEFTRKDNMTAHVKIIHKIENPSTALATVAAANLAGQPLGVSGASTPPPPDLSGQNSNQSLPATSNALSTSSSSSTSSSSGSLGPLTTSAPPAPAAAAQ
Protein: Calmodulin 1 (G1NK53)
Organism: Meleagris gallopavo (Wild turkey)
Interaction partners:
Sequence:
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Protein: GMP synthase [glutamine-hydrolyzing] (PfGMPS) (EC 6.3.5.2) (Glutamine amidotransferase) (Guanosine monophosphate synthetase) (Q8IJR9)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes the conversion of xanthine monophosphate (XMP) to GMP in the presence of glutamine and ATP through an adenyl-XMP intermediate, which is the final step of de novo synthesis of GMP. The conversion of XMP to GMP involves the coordinated action of the glutamine amidotransferase (GATase) domain that catalyzes the hydrolysis of the amide side chain of glutamine producing ammonia and the ATP pyrophosphatase (ATPPase) domain that catalyzes the synthesis of adenyl-XMP intermediate from ATP. The ammonia produced by the GATase domain is tunnelled to the ATP-PPase domain where it attacks the adenyl-XMP intermediate generating GMP.
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase
- Guanylate kinase
- Hypoxanthine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- Dihydroorotate dehydrogenase
- CTP synthase
- Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase beta
- cGMP-specific 3',5'-cyclic phosphodiesterase alpha
- cGMP-specific 3',5'-cyclic phosphodiesterase delta
- Ubiquitin carboxyl-terminal hydrolase, putative
Sequence:
MEGEEYDKILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILSGGPYSVTEAGSPHLKKEVFEYFLEKKIPIFGICYGMQEIAVQMNGEVKKSKTSEYGCTDVNILRNDNINNITYCRNFGDSSSAMDLYSNYKLMNETCCLFENIKSDITTVWMNHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEVYESLDGELMFYNFAYNICKCKKQFDPIRYHELELKNIEKYKHDHYVIAAMSGGIDSTVAAAYTHKIFKERFFGIFIDNGLLRKNEAENVYTFLKSTFPDMNITKIDASENFLSNLQGVTDPEQKRKIIGKLFIEEFEKAVNNIDIDINKTFLLQGTLYPDIIESKCSKNLSDTIKTHHNVGGLPKNLKFKLFEPFKYLFKDDVKTLSRELNLPEEITNRHPFPGPGLAIRVIGEINKHKLNILREVDDIFINDLKQYGLYNQISQAFAVLLSSKSVGVRGDARSYDYVCVLRAVKTSSFMTANWYQIPYDILDKITTRILSEVKGVNRILYDVSSKPPATIEFE
Protein: CREB/ATF bZIP transcription factor (Host cell factor-binding transcription factor Zhangfei) (HCF-binding transcription factor Zhangfei) (Q9NS37)
Organism: Homo sapiens (Human)
Function: Strongly activates transcription when bound to HCFC1. Suppresses the expression of HSV proteins in cells infected with the virus in a HCFC1-dependent manner. Also suppresses the HCFC1-dependent transcriptional activation by CREB3 and reduces the amount of CREB3 in the cell. Able to down-regulate expression of some cellular genes in CREBZF-expressing cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:15705566}. Note=Colocalizes in promyelocytic leukemia protein nuclear bodies (PML-NB) with CREB3 and HCFC1.
Interaction partners:
- Host cell factor 1
- Host cell factor 2
- Cyclic AMP-responsive element-binding protein 3
- Polynucleotide 5'-hydroxyl-kinase NOL9
- Cyclic AMP-responsive element-binding protein 3-like protein 4
- Cyclic AMP-dependent transcription factor ATF-4
Sequence:
MRHSLTKLLAASGSNSPTRSESPEPAATCSLPSDLTRAAAGEEETAAAGSPGRKQQFGDEGELEAGRGSRGGVAVRAPSPEEMEEEAIASLPGEETEDMDFLSGLELADLLDPRQPDWHLDPGLSSPGPLSSSGGGSDSGGLWRGDDDDEAAAAEMQRFSDLLQRLLNGIGGCSSSSDSGSAEKRRRKSPGGGGGGGSGNDNNQAATKSPRKAAAAAARLNRLKKKEYVMGLESRVRGLAAENQELRAENRELGKRVQALQEESRYLRAVLANETGLARLLSRLSGVGLRLTTSLFRDSPAGDHDYALPVGKQKQDLLEEDDSAGGVCLHVDKDKVSVEFCSACARKASSSLKM
Protein: Podocalyxin (Podocalyxin-like protein 1) (Q5RHU2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004221, ECO:0000256|PIRNR:PIRNR038143}. Cell projection, filopodium {ECO:0000256|ARBA:ARBA00004486}. Cell projection, microvillus {ECO:0000256|ARBA:ARBA00004105, ECO:0000256|PIRNR:PIRNR038143}. Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Membrane raft {ECO:0000256|PIRNR:PIRNR038143}. Cell projection, lamellipodium {ECO:0000256|PIRNR:PIRNR038143}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- NPHS1 adhesion molecule, nephrin.
- NPHS2 stomatin family member, podocin.
- Na
- Moesin a
- Wilms tumor protein homolog
- Ezrin
- Ras-interacting protein 1
- Chloride intracellular channel protein
Sequence:
MTITWTIIVLGAFLHDMAYAQSETTIPTASESHSTSNRSVVTDATVSTTVHKATNAQTTEAQTTSIPAGPTSQATHPPTSAPTTQSDPNNNQGSTALPSTSTLYMQNVSSAQVIPTGVDPNTSFSPTTQYTLTDSPKSVTQPHSSDQASTSNPDNLNTPTSTSERTTQRVSTEQTTAYSPAKQDRPTISDPATPANSTTELITSKPDITTDKKTTTGTTTQLLTTAKPNARSFVSQSLQTTIVPQSTTAPIKTSQPSDLRKNFTHPVYDLSSSSSSTERNIVRETCKKLGQNLKGNCSVEVEINNNQLIATITINANQAIPLENYNPPETNENENSNKEPVQDTIPDTLIAILASCGALVLILCGFAAYCTYHRRSYRKNQQHLTEELQTVENGYHDNPTLEVMEVQPEMQEKKLALNGEFNDSWIVPIDNLLKEDIPDEEDTHL
Protein: Thioredoxin-2, mitochondrial (Trx-2) (O94504)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Disulfide reductase which serves multiple functions in mitochondria, protecting mitochondrial components against thiol-oxidative damage as a thiol-disulfide oxidoreductase, and supporting urea cycle and respiration in mitochondria in a manner independent of active site thiols.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Glutathione reductase
- Peroxiredoxin tpx1
- Probable peptide methionine sulfoxide reductase
- Thioredoxin reductase
- Peroxisomal membrane associated protein 20
- Tryptophan synthase
- SUMO-conjugating enzyme ubc9
Sequence:
MRGFIANSLKPHMRSFALRRSFTSSRILRKVNAVESFGDYNTRISADKVTVVDFYADWCGPCKYLKPFLEKLSEQNQKASFIAVNADKFSDIAQKNGVYALPTMVLFRKGQELDRIVGADVKTLSSLLAKYQE
Protein: Progestin and adipoQ receptor family member 8 (D6RCM7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTTAILERLSTLSVSGQQLRRLPKILEDGLPKMPCTVPETDVPQLFREPYIRTGYRPTGHEWRYYFFSLFQKHNEVVNVWTHLLAALAVLLRFWAFAEAEALPWASTHSLPL
Protein: 2-dehydro-3-deoxygalactonokinase (EC 2.7.1.58) (2-keto-3-deoxy-galactonokinase) (2-oxo-3-deoxygalactonate kinase) (P31459)
Organism: Escherichia coli (strain K12)
Interaction partners:
- 2-dehydro-3-deoxy-6-phosphogalactonate aldolase
- D-galactonate dehydratase
- Galactonate operon transcriptional repressor
- D-galactonate transporter
- Uncharacterized protein YidR
Sequence:
MTARYIAIDWGSTNLRAWLYQGDHCLESRQSEAGVTRLNGKSPAAVLAEVTTDWREEKTPVVMAGMVGSNVGWKVAPYLSVPACFSSIGEQLTSVGDNIWIIPGLCVSHDDNHNVMRGEETQLIGARALAPSSLYVMPGTHCKWVQADSQQINDFRTVMTGELHHLLLNHSLIGAGLPPQENSADAFTAGLERGLNTPAILPQLFEVRASHVLGTLPREQVSEFLSGLLIGAEVASMRDYVAHQHAITLVAGTSLTARYQQAFQAMGCDVTAVAGDTAFQAGIRSIAHAVAN
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) (BCKAD-E2) (BCKADE2) (Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex) (Dihydrolipoamide branched chain transacylase) (Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase) (P53395)
Organism: Mus musculus (Mouse)
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.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P11181}.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Isovaleryl-CoA dehydrogenase, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Isobutyryl-CoA dehydrogenase, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MAAARVLRTWSQNAVRLTCVRYFQTFNSARVLKPKCVCSVGYPLFKYSQPRHSLRTAAVLQGQVVQFKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDIETEALKDSEEDVVETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILSFLEKQTGAILPPSPKSEITPPPPQPKDRTFPTPIAKPPVFTGKDRTEPVTGFQKAMVKTMSAALKIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPRFDQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDLK
Protein: L-lactate dehydrogenase (L-LDH) (EC 1.1.1.27) (P78007)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Catalyzes the conversion of lactate to pyruvate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}.
Interaction partners:
- Pyruvate kinase
- Pyruvate dehydrogenase E1 component subunit beta
- Glucose-6-phosphate isomerase
- Pyruvate dehydrogenase E1 component subunit alpha
- Transketolase
- Fructose-bisphosphate aldolase
- Glyceraldehyde-3-phosphate dehydrogenase
- Enolase
- Glycerol 3-phosphate oxidase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
MKSLKVALIGSGAVGTSFLYAAMSRGLASEYMVIDINEKSQVGNVFDLQDAVPSSPQYSKVIAGDYKQLKDYDFIFIGAGRPQKQGGETRLQLLEGNVEIMKNIAKAVKESGFKGITLIASNPVDIMAYTYLKVTGFEPNKVIGSGTLLDSARLKFAIAEKYGMSSRDVQAYVLGEHGDSSVSIISSAKIAGLPLKHFSKASDIEKEFAEIDHFIRRRAYEIIERKGATFYGIGEATAEVAELILRDTKEVRVVASLINGQYGAKDVMFGTPCVLGRNGVEKILEIELSATEKAGLDKSIQVLKDNIKLAKL
Protein: MRG domain-containing protein (O45625)
Organism: Caenorhabditis elegans
Interaction partners:
- CaeNaCin
- DeHydrogenases, Short chain
- Transmembrane protein
- Serpentine receptor class gamma
- Stomatin-3
- Epoxide hydrolase
- Glucosamine 6-phosphate N-acetyltransferase
- Protein ver-2
- Transmembrane protein
Sequence:
MSILVYDREHNFKKWYIYWIPKTKMLGVKDDKDVVYEKMCTLQERTDILKVSKSLVEEKWSSLFSESGLHIEEVCEKELVLTFALQRNITLERTELSGRFDECLYLEYLRLKTLTNVSPMKRKRTASTVEHVIRSDDIKPILAPKSDPVKKRTTRMAAKASGPEFDDE
Protein: Zyxin (Q9U3F4)
Organism: Caenorhabditis elegans
Function: Functions as both a mechanical stabilizer (via LIM domains) of focal adhesions and as a sensor component for muscle cell damage (via N-terminus). Regulates, stabilizes and maintains posterior lateral mechanosensory (PLM) synaptic branch extension and new synapse formation and growth during larval development.
Subcellular location: Nucleus {ECO:0000269|PubMed:18094057, ECO:0000269|PubMed:23427270, ECO:0000269|PubMed:25252943}. Cytoplasm {ECO:0000269|PubMed:25252943}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:18094057, ECO:0000269|PubMed:23427270}. Cell projection, axon {ECO:0000269|PubMed:23427270}. Cell junction, focal adhesion {ECO:0000269|PubMed:23427270}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23427270}. Note=Shuttles between dense bodies and M lines (PubMed:18094057, PubMed:23427270). Localizes to nucleus in body wall muscle cells. Highly mobile in cytoplasm. Mobility seems to depend on atn-1 (PubMed:23427270). {ECO:0000269|PubMed:18094057, ECO:0000269|PubMed:23427270}.
Interaction partners:
- Vinculin
- Protein unc-112
- Alpha-actinin, sarcomeric
- FERM domain-containing protein
- UNC-34
- Calponin-homology
- Dystrophin-like protein 1
- Actin
- RNA-binding protein 42
- PDZ domain-containing protein
Sequence:
MGPPPPPPPPPLLPSGEILPSRKWKTEDAPRRNNHPAPAPPKPSRPTVDASALQHAAARLRKTGYNEPVRGDVENLSDGRLDRPHQQLPDGDRTYRANLQQLAQPKTRAEIPSPPTYSNQPRPLGDFHRDPNALSQFQQSREALLSSTSPTSNYSPINKFSSSTLTQYANKSPSPPSFGNSNSEATYVSPYSSKHSYPTNFRSYHKDDDYFNNTATTATTTTSSNSLNENNNSNKYGNKETVLQWSEPYDPSKIRRSQSPIRNAREMIHEYSTTNYVTEVQQPPPPPPDLYQRMTQARTFLQNSLAKQLRDEGLTESQKAANRNQTGALSASSSIPFDASQIVKNSYNGDEVDHLVHQMRTKLNQPADTSPSIVQYPRRQAPDSSRANYSATTSTSFSSSTTRKIMNINICVGCGKEITGDQPGCNAMNQIFHVDCFKCGQCSKTLAGASFYNIDDKPTCEGCYQNSLEKCTACNRAISDKLLRACGGVYHVNCFVCFSCKKSLDGIPFTLDKDNNVHCVPCFHDKFAPRCALCSKPIVPQDGEKESVRVVAMDKSFHVDCYKCEDCGMQLSSKLEGQGCYPIDNHLLCKTCNGNRLRVVSST