ACSA_HUMAN
ID ACSA_HUMAN Reviewed; 701 AA.
AC Q9NR19; A6NE90; Q5QPH2; Q5QPH3; Q8N238; Q96EL0; Q9NQP7; Q9UJ15;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Acetyl-coenzyme A synthetase, cytoplasmic;
DE EC=6.2.1.1 {ECO:0000269|PubMed:10843999, ECO:0000269|PubMed:28003429};
DE AltName: Full=Acetate--CoA ligase;
DE AltName: Full=Acetyl-CoA synthetase;
DE Short=ACS;
DE Short=AceCS;
DE AltName: Full=Acetyl-CoA synthetase 1 {ECO:0000250|UniProtKB:Q9QXG4};
DE Short=AceCS1 {ECO:0000250|UniProtKB:Q9QXG4};
DE AltName: Full=Acyl-CoA synthetase short-chain family member 2;
DE AltName: Full=Acyl-activating enzyme;
DE AltName: Full=Propionate--CoA ligase;
DE EC=6.2.1.17 {ECO:0000250|UniProtKB:Q9QXG4};
GN Name=ACSS2; Synonyms=ACAS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=10843999; DOI=10.1074/jbc.m004160200;
RA Luong A., Hannah V.C., Brown M.S., Goldstein J.L.;
RT "Molecular characterization of human acetyl-CoA synthetase, an enzyme
RT regulated by sterol regulatory element-binding proteins.";
RL J. Biol. Chem. 275:26458-26466(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-30 AND SER-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-30; SER-36 AND
RP SER-267, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=28003429; DOI=10.1093/jb/mvw067;
RA Yoshimura Y., Araki A., Maruta H., Takahashi Y., Yamashita H.;
RT "Molecular cloning of rat acss3 and characterization of mammalian
RT propionyl-CoA synthetase in the liver mitochondrial matrix.";
RL J. Biochem. 161:279-289(2017).
CC -!- FUNCTION: Catalyzes the synthesis of acetyl-CoA from short-chain fatty
CC acids (PubMed:10843999, PubMed:28003429). Acetate is the preferred
CC substrate (PubMed:10843999, PubMed:28003429). Can also utilize
CC propionate with a much lower affinity (By similarity).
CC {ECO:0000250|UniProtKB:Q9QXG4, ECO:0000269|PubMed:10843999,
CC ECO:0000269|PubMed:28003429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC Evidence={ECO:0000269|PubMed:10843999, ECO:0000269|PubMed:28003429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC Evidence={ECO:0000305|PubMed:10843999, ECO:0000305|PubMed:28003429};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456215; EC=6.2.1.17;
CC Evidence={ECO:0000250|UniProtKB:Q9QXG4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC Evidence={ECO:0000250|UniProtKB:Q9QXG4};
CC -!- ACTIVITY REGULATION: Inhibited by acetylation at Lys-661 and activated
CC by deacetylation mediated by the deacetylases SIRT1 and SIRT3.
CC {ECO:0000250|UniProtKB:Q9QXG4}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10843999}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10843999,
CC ECO:0000269|PubMed:28003429}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NR19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NR19-2; Sequence=VSP_046376;
CC -!- PTM: Reversibly acetylated at Lys-661 (By similarity). The acetyl-CoA
CC synthase activity is inhibited by acetylation and activated by
CC deacetylation mediated by the deacetylases SIRT1 and SIRT3 (By
CC similarity). {ECO:0000250|UniProtKB:Q9QXG4}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF263614; AAF75064.1; -; mRNA.
DR EMBL; AK092281; BAC03849.1; -; mRNA.
DR EMBL; AL133324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76248.1; -; Genomic_DNA.
DR EMBL; BC012172; AAH12172.1; -; mRNA.
DR CCDS; CCDS13243.1; -. [Q9NR19-1]
DR CCDS; CCDS42868.2; -. [Q9NR19-2]
DR RefSeq; NP_001070020.2; NM_001076552.2. [Q9NR19-2]
DR RefSeq; NP_061147.1; NM_018677.3. [Q9NR19-1]
DR AlphaFoldDB; Q9NR19; -.
DR SMR; Q9NR19; -.
DR BioGRID; 120989; 9.
DR IntAct; Q9NR19; 5.
DR STRING; 9606.ENSP00000253382; -.
DR BindingDB; Q9NR19; -.
DR ChEMBL; CHEMBL4523467; -.
DR DrugBank; DB00131; Adenosine phosphate.
DR DrugBank; DB00171; ATP.
DR DrugBank; DB09395; Sodium acetate.
DR GuidetoPHARMACOLOGY; 3128; -.
DR SwissLipids; SLP:000001167; -.
DR GlyGen; Q9NR19; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NR19; -.
DR PhosphoSitePlus; Q9NR19; -.
DR BioMuta; ACSS2; -.
DR DMDM; 20137525; -.
DR EPD; Q9NR19; -.
DR jPOST; Q9NR19; -.
DR MassIVE; Q9NR19; -.
DR MaxQB; Q9NR19; -.
DR PaxDb; Q9NR19; -.
DR PeptideAtlas; Q9NR19; -.
DR PRIDE; Q9NR19; -.
DR ProteomicsDB; 63659; -.
DR ProteomicsDB; 82253; -. [Q9NR19-1]
DR Antibodypedia; 1332; 450 antibodies from 33 providers.
DR DNASU; 55902; -.
DR Ensembl; ENST00000253382.5; ENSP00000253382.5; ENSG00000131069.20. [Q9NR19-2]
DR Ensembl; ENST00000360596.7; ENSP00000353804.2; ENSG00000131069.20. [Q9NR19-1]
DR GeneID; 55902; -.
DR KEGG; hsa:55902; -.
DR MANE-Select; ENST00000360596.7; ENSP00000353804.2; NM_018677.4; NP_061147.1.
DR UCSC; uc002xbd.3; human. [Q9NR19-1]
DR CTD; 55902; -.
DR DisGeNET; 55902; -.
DR GeneCards; ACSS2; -.
DR HGNC; HGNC:15814; ACSS2.
DR HPA; ENSG00000131069; Tissue enhanced (skeletal).
DR MalaCards; ACSS2; -.
DR MIM; 605832; gene.
DR neXtProt; NX_Q9NR19; -.
DR OpenTargets; ENSG00000131069; -.
DR PharmGKB; PA24429; -.
DR VEuPathDB; HostDB:ENSG00000131069; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000156358; -.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; Q9NR19; -.
DR OMA; DHWWHDL; -.
DR OrthoDB; 288915at2759; -.
DR PhylomeDB; Q9NR19; -.
DR TreeFam; TF300417; -.
DR BioCyc; MetaCyc:HS05484-MON; -.
DR BRENDA; 6.2.1.1; 2681.
DR PathwayCommons; Q9NR19; -.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-71384; Ethanol oxidation.
DR SignaLink; Q9NR19; -.
DR BioGRID-ORCS; 55902; 8 hits in 1083 CRISPR screens.
DR ChiTaRS; ACSS2; human.
DR GeneWiki; ACSS2; -.
DR GenomeRNAi; 55902; -.
DR Pharos; Q9NR19; Tchem.
DR PRO; PR:Q9NR19; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NR19; protein.
DR Bgee; ENSG00000131069; Expressed in ileal mucosa and 178 other tissues.
DR ExpressionAtlas; Q9NR19; baseline and differential.
DR Genevisible; Q9NR19; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0016208; F:AMP binding; IC:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050218; F:propionate-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR GO; GO:0006069; P:ethanol oxidation; TAS:Reactome.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Ligase;
KW Lipid metabolism; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..701
FT /note="Acetyl-coenzyme A synthetase, cytoplasmic"
FT /id="PRO_0000208423"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219..222
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 439..441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 463..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 575
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 636
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXG4"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXG4"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 418
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 661
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXG4"
FT VAR_SEQ 277
FT /note="V -> VQGKLKEKSKRVQP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046376"
FT CONFLICT 79
FT /note="F -> L (in Ref. 2; BAC03849)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="V -> F (in Ref. 5; AAH12172)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="M -> L (in Ref. 2; BAC03849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 78580 MW; 833580B41B73A8B4 CRC64;
MGLPEERVRS GSGSRGQEEA GAGGRARSWS PPPEVSRSAH VPSLQRYREL HRRSVEEPRE
FWGDIAKEFY WKTPCPGPFL RYNFDVTKGK IFIEWMKGAT TNICYNVLDR NVHEKKLGDK
VAFYWEGNEP GETTQITYHQ LLVQVCQFSN VLRKQGIQKG DRVAIYMPMI PELVVAMLAC
ARIGALHSIV FAGFSSESLC ERILDSSCSL LITTDAFYRG EKLVNLKELA DEALQKCQEK
GFPVRCCIVV KHLGRAELGM GDSTSQSPPI KRSCPDVQIS WNQGIDLWWH ELMQEAGDEC
EPEWCDAEDP LFILYTSGST GKPKGVVHTV GGYMLYVATT FKYVFDFHAE DVFWCTADIG
WITGHSYVTY GPLANGATSV LFEGIPTYPD VNRLWSIVDK YKVTKFYTAP TAIRLLMKFG
DEPVTKHSRA SLQVLGTVGE PINPEAWLWY HRVVGAQRCP IVDTFWQTET GGHMLTPLPG
ATPMKPGSAT FPFFGVAPAI LNESGEELEG EAEGYLVFKQ PWPGIMRTVY GNHERFETTY
FKKFPGYYVT GDGCQRDQDG YYWITGRIDD MLNVSGHLLS TAEVESALVE HEAVAEAAVV
GHPHPVKGEC LYCFVTLCDG HTFSPKLTEE LKKQIREKIG PIATPDYIQN APGLPKTRSG
KIMRRVLRKI AQNDHDLGDM STVADPSVIS HLFSHRCLTI Q
