HMCS1_HUMAN
ID HMCS1_HUMAN Reviewed; 520 AA.
AC Q01581; B2RDL8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Hydroxymethylglutaryl-CoA synthase, cytoplasmic {ECO:0000305};
DE Short=HMG-CoA synthase {ECO:0000303|PubMed:20346956};
DE EC=2.3.3.10 {ECO:0000269|PubMed:7913309};
DE AltName: Full=3-hydroxy-3-methylglutaryl coenzyme A synthase;
GN Name=HMGCS1 {ECO:0000312|HGNC:HGNC:5007}; Synonyms=HMGCS;
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], AND SUBCELLULAR LOCATION.
RC TISSUE=Fibroblast;
RX PubMed=1358203; DOI=10.1016/0167-4781(92)90172-v;
RA Russ A.P., Ruzicka V., Maerz W., Appelhans H., Gross W.;
RT "Amplification and direct sequencing of a cDNA encoding human cytosolic 3-
RT hydroxy-3-methylglutaryl-coenzyme A synthase.";
RL Biochim. Biophys. Acta 1132:329-331(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-129, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Fetal adrenal gland;
RX PubMed=7913309; DOI=10.1006/abbi.1994.1273;
RA Rokosz L.L., Boulton D.A., Butkiewicz E.A., Sanyal G., Cueto M.A.,
RA Lachance P.A., Hermes J.D.;
RT "Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase:
RT expression, purification, and characterization of recombinant wild-type and
RT Cys129 mutant enzymes.";
RL Arch. Biochem. Biophys. 312:1-13(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-476 AND SER-495, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46 AND LYS-273, AND
RP IDENTIFICATION BY MASS 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-495, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-495 AND SER-516, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP 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 [16] {ECO:0007744|PDB:2P8U}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 16-470 OF HOMODIMER IN COMPLEX
RP WITH COENZYME A, SUBSTRATE-BINDING SITES, REGION, AND SUBUNIT.
RX PubMed=20346956; DOI=10.1016/j.jmb.2010.03.034;
RA Shafqat N., Turnbull A., Zschocke J., Oppermann U., Yue W.W.;
RT "Crystal structures of human HMG-CoA synthase isoforms provide insights
RT into inherited ketogenesis disorders and inhibitor design.";
RL J. Mol. Biol. 398:497-506(2010).
CC -!- FUNCTION: Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA
CC to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into
CC mevalonate, a precursor for cholesterol synthesis.
CC {ECO:0000269|PubMed:7913309}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-
CC methylglutaryl-CoA + CoA + H(+); Xref=Rhea:RHEA:10188,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.10;
CC Evidence={ECO:0000269|PubMed:7913309};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10189;
CC Evidence={ECO:0000305|PubMed:7913309};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29 uM for acetyl-CoA {ECO:0000269|PubMed:7913309};
CC Vmax=0.7 umol/min/mg enzyme for acetyl-CoA as substrate
CC {ECO:0000269|PubMed:7913309};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20346956}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:1358203}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00297.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X66435; CAA47061.1; -; mRNA.
DR EMBL; L25798; AAA62411.1; -; mRNA.
DR EMBL; BT007302; AAP35966.1; -; mRNA.
DR EMBL; AK315593; BAG37965.1; -; mRNA.
DR EMBL; CH471119; EAW56054.1; -; Genomic_DNA.
DR EMBL; BC000297; AAH00297.2; ALT_INIT; mRNA.
DR CCDS; CCDS34154.1; -.
DR PIR; S27197; S27197.
DR PIR; S45497; S45497.
DR RefSeq; NP_001091742.1; NM_001098272.2.
DR RefSeq; NP_001311148.1; NM_001324219.1.
DR RefSeq; NP_001311149.1; NM_001324220.1.
DR RefSeq; NP_001311151.1; NM_001324222.1.
DR RefSeq; NP_001311152.1; NM_001324223.1.
DR RefSeq; NP_001311153.1; NM_001324224.1.
DR RefSeq; NP_001317592.1; NM_001330663.1.
DR RefSeq; NP_002121.4; NM_002130.7.
DR PDB; 2P8U; X-ray; 2.00 A; A/B=16-470.
DR PDBsum; 2P8U; -.
DR AlphaFoldDB; Q01581; -.
DR SMR; Q01581; -.
DR BioGRID; 109400; 87.
DR IntAct; Q01581; 18.
DR MINT; Q01581; -.
DR STRING; 9606.ENSP00000322706; -.
DR DrugBank; DB07740; (7R,12R,13R)-13-formyl-12,14-dihydroxy-3,5,7-trimethyltetradeca-2,4-dienoic acid.
DR GuidetoPHARMACOLOGY; 638; -.
DR SwissLipids; SLP:000000724; -.
DR GlyGen; Q01581; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q01581; -.
DR MetOSite; Q01581; -.
DR PhosphoSitePlus; Q01581; -.
DR SwissPalm; Q01581; -.
DR BioMuta; HMGCS1; -.
DR DMDM; 1708239; -.
DR EPD; Q01581; -.
DR jPOST; Q01581; -.
DR MassIVE; Q01581; -.
DR MaxQB; Q01581; -.
DR PaxDb; Q01581; -.
DR PeptideAtlas; Q01581; -.
DR PRIDE; Q01581; -.
DR ProteomicsDB; 57972; -.
DR Antibodypedia; 23240; 252 antibodies from 32 providers.
DR DNASU; 3157; -.
DR Ensembl; ENST00000325110.11; ENSP00000322706.6; ENSG00000112972.15.
DR Ensembl; ENST00000433297.2; ENSP00000399402.2; ENSG00000112972.15.
DR GeneID; 3157; -.
DR KEGG; hsa:3157; -.
DR MANE-Select; ENST00000325110.11; ENSP00000322706.6; NM_001098272.3; NP_001091742.1.
DR UCSC; uc003jnq.6; human.
DR CTD; 3157; -.
DR DisGeNET; 3157; -.
DR GeneCards; HMGCS1; -.
DR HGNC; HGNC:5007; HMGCS1.
DR HPA; ENSG00000112972; Tissue enhanced (liver).
DR MIM; 142940; gene.
DR neXtProt; NX_Q01581; -.
DR OpenTargets; ENSG00000112972; -.
DR PharmGKB; PA29337; -.
DR VEuPathDB; HostDB:ENSG00000112972; -.
DR eggNOG; KOG1393; Eukaryota.
DR GeneTree; ENSGT00390000006096; -.
DR HOGENOM; CLU_008065_0_1_1; -.
DR InParanoid; Q01581; -.
DR OMA; DDAYNWI; -.
DR OrthoDB; 495111at2759; -.
DR PhylomeDB; Q01581; -.
DR TreeFam; TF105361; -.
DR BioCyc; MetaCyc:ENSG00000112972-MON; -.
DR BRENDA; 2.3.3.10; 2681.
DR PathwayCommons; Q01581; -.
DR Reactome; R-HSA-191273; Cholesterol biosynthesis.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR SignaLink; Q01581; -.
DR UniPathway; UPA00058; UER00102.
DR BioGRID-ORCS; 3157; 750 hits in 1099 CRISPR screens.
DR ChiTaRS; HMGCS1; human.
DR EvolutionaryTrace; Q01581; -.
DR GenomeRNAi; 3157; -.
DR Pharos; Q01581; Tchem.
DR PRO; PR:Q01581; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q01581; protein.
DR Bgee; ENSG00000112972; Expressed in adrenal tissue and 202 other tissues.
DR ExpressionAtlas; Q01581; baseline and differential.
DR Genevisible; Q01581; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome.
DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR000590; HMG_CoA_synt_AS.
DR InterPro; IPR013746; HMG_CoA_synt_C_dom.
DR InterPro; IPR013528; HMG_CoA_synth_N.
DR InterPro; IPR010122; HMG_CoA_synthase_euk.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08540; HMG_CoA_synt_C; 1.
DR Pfam; PF01154; HMG_CoA_synt_N; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01833; HMG-CoA-S_euk; 1.
DR PROSITE; PS01226; HMG_COA_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cholesterol biosynthesis;
KW Cholesterol metabolism; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW Phosphoprotein; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..520
FT /note="Hydroxymethylglutaryl-CoA synthase, cytoplasmic"
FT /id="PRO_0000213747"
FT REGION 492..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 95
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT ACT_SITE 129
FT /note="Acyl-thioester intermediate"
FT ACT_SITE 264
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT BINDING 44..46
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:20346956,
FT ECO:0007744|PDB:2P8U"
FT BINDING 167
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:20346956,
FT ECO:0007744|PDB:2P8U"
FT BINDING 221
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:20346956,
FT ECO:0007744|PDB:2P8U"
FT BINDING 269
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:20346956,
FT ECO:0007744|PDB:2P8U"
FT BINDING 273
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:20346956,
FT ECO:0007744|PDB:2P8U"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 273
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 476
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 129
FT /note="C->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7913309"
FT CONFLICT 248
FT /note="G -> A (in Ref. 1; CAA47061)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="K -> N (in Ref. 1; CAA47061)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="E -> K (in Ref. 1; CAA47061)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="Q -> H (in Ref. 1; CAA47061)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="P -> Q (in Ref. 1; CAA47061)"
FT /evidence="ECO:0000305"
FT CONFLICT 519..520
FT /note="EH -> VW (in Ref. 1; CAA47061)"
FT /evidence="ECO:0000305"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2P8U"
FT TURN 112..116
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 173..184
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 218..247
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 268..285
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 324..330
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 348..359
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:2P8U"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 380..388
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 397..403
FT /evidence="ECO:0007829|PDB:2P8U"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 408..413
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:2P8U"
FT HELIX 420..433
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 453..458
FT /evidence="ECO:0007829|PDB:2P8U"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:2P8U"
SQ SEQUENCE 520 AA; 57294 MW; C669212BF86CFF9B CRC64;
MPGSLPLNAE ACWPKDVGIV ALEIYFPSQY VDQAELEKYD GVDAGKYTIG LGQAKMGFCT
DREDINSLCM TVVQNLMERN NLSYDCIGRL EVGTETIIDK SKSVKTNLMQ LFEESGNTDI
EGIDTTNACY GGTAAVFNAV NWIESSSWDG RYALVVAGDI AVYATGNARP TGGVGAVALL
IGPNAPLIFE RGLRGTHMQH AYDFYKPDML SEYPIVDGKL SIQCYLSALD RCYSVYCKKI
HAQWQKEGND KDFTLNDFGF MIFHSPYCKL VQKSLARMLL NDFLNDQNRD KNSIYSGLEA
FGDVKLEDTY FDRDVEKAFM KASSELFSQK TKASLLVSNQ NGNMYTSSVY GSLASVLAQY
SPQQLAGKRI GVFSYGSGLA ATLYSLKVTQ DATPGSALDK ITASLCDLKS RLDSRTGVAP
DVFAENMKLR EDTHHLVNYI PQGSIDSLFE GTWYLVRVDE KHRRTYARRP TPNDDTLDEG
VGLVHSNIAT EHIPSPAKKV PRLPATAAEP EAAVISNGEH
