PGAM1_HUMAN
ID PGAM1_HUMAN Reviewed; 254 AA.
AC P18669; Q9BWC0;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 239.
DE RecName: Full=Phosphoglycerate mutase 1 {ECO:0000305};
DE EC=5.4.2.11 {ECO:0000269|PubMed:23653202};
DE EC=5.4.2.4 {ECO:0000269|PubMed:23653202};
DE AltName: Full=BPG-dependent PGAM 1;
DE AltName: Full=Phosphoglycerate mutase isozyme B;
DE Short=PGAM-B;
GN Name=PGAM1 {ECO:0000312|HGNC:HGNC:8888}; Synonyms=PGAMA;
GN ORFNames=CDABP0006;
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 TISSUE SPECIFICITY.
RX PubMed=2846553; DOI=10.1016/s0021-9258(18)37476-3;
RA Sakoda S., Shanske S., Dimauro S., Schon E.A.;
RT "Isolation of a cDNA encoding the B isozyme of human phosphoglycerate
RT mutase (PGAM) and characterization of the PGAM gene family.";
RL J. Biol. Chem. 263:16899-16905(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Leukemia;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RT "Pediatric leukemia cDNA sequencing project.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Liver, Lymph, Skin, and Uterus;
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 [4]
RP PROTEIN SEQUENCE OF 2-254, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=2846554; DOI=10.1016/s0021-9258(18)37477-5;
RA Blouquit Y., Calvin M.C., Rosa R., Prome D., Prome J.-C., Pratbernou F.,
RA Cohen-Solal M., Rosa J.;
RT "Sequence of the human erythrocyte phosphoglycerate mutase by
RT microsequencer and mass spectrometry.";
RL J. Biol. Chem. 263:16906-16910(1988).
RN [5]
RP PROTEIN SEQUENCE OF 11-39; 47-61; 91-100; 118-138; 142-157; 163-176;
RP 181-191 AND 223-240, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 91-100.
RC TISSUE=Mammary carcinoma;
RX PubMed=9150946; DOI=10.1002/elps.1150180342;
RA Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J.,
RA Dorow D.S.;
RT "Two-dimensional electrophoretic analysis of human breast carcinoma
RT proteins: mapping of proteins that bind to the SH3 domain of mixed lineage
RT kinase MLK2.";
RL Electrophoresis 18:588-598(1997).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP 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 [12]
RP ACETYLATION AT LYS-251; LYS-253 AND LYS-254, AND DEACETYLATION BY SIRT1.
RX PubMed=22157007; DOI=10.1074/jbc.m111.317404;
RA Hallows W.C., Yu W., Denu J.M.;
RT "Regulation of glycolytic enzyme phosphoglycerate mutase-1 by Sirt1
RT protein-mediated deacetylation.";
RL J. Biol. Chem. 287:3850-3858(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-31, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-23, AND
RP 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH CITRATE, SUBUNIT, AND
RP ACTIVE SITE.
RX PubMed=15883004; DOI=10.1016/j.bbrc.2005.03.243;
RA Wang Y., Wei Z., Liu L., Cheng Z., Lin Y., Ji F., Gong W.;
RT "Crystal structure of human B-type phosphoglycerate mutase bound with
RT citrate.";
RL Biochem. Biophys. Res. Commun. 331:1207-1215(2005).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-254 IN COMPLEX WITH SUBSTRATE
RP ANALOG, PHOSPHORYLATION AT TYR-26, ACTIVE SITE, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=23653202; DOI=10.1038/ncomms2759;
RA Hitosugi T., Zhou L., Fan J., Elf S., Zhang L., Xie J., Wang Y., Gu T.L.,
RA Aleckovic M., LeRoy G., Kang Y., Kang H.B., Seo J.H., Shan C., Jin P.,
RA Gong W., Lonial S., Arellano M.L., Khoury H.J., Chen G.Z., Shin D.M.,
RA Khuri F.R., Boggon T.J., Kang S., He C., Chen J.;
RT "Tyr26 phosphorylation of PGAM1 provides a metabolic advantage to tumours
RT by stabilizing the active conformation.";
RL Nat. Commun. 4:1790-1790(2013).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglyceratea crucial step in glycolysis, by using 2,3-
CC bisphosphoglycerate (PubMed:23653202). Also catalyzes the
CC interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-
CC glyceroyl phosphate (PubMed:23653202). {ECO:0000269|PubMed:23653202}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000269|PubMed:23653202};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15903;
CC Evidence={ECO:0000305|PubMed:23653202};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC Evidence={ECO:0000269|PubMed:23653202};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15883004}.
CC -!- INTERACTION:
CC P18669; P05067: APP; NbExp=4; IntAct=EBI-717905, EBI-77613;
CC P18669; P12004: PCNA; NbExp=2; IntAct=EBI-717905, EBI-358311;
CC P18669; Q8IV45: UNC5CL; NbExp=3; IntAct=EBI-717905, EBI-12238241;
CC -!- TISSUE SPECIFICITY: Expressed in the liver and brain. Not found in the
CC muscle. {ECO:0000269|PubMed:2846553}.
CC -!- PTM: Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose
CC condition. Acetylation increases catalytic activity. Under glucose
CC restriction SIRT1 levels dramatically increase and it deacetylates the
CC enzyme. {ECO:0000269|PubMed:22157007}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; J04173; AAA60071.1; -; mRNA.
DR EMBL; AY007118; AAG01990.1; -; mRNA.
DR EMBL; BC010038; AAH10038.1; -; mRNA.
DR EMBL; BC011678; AAH11678.1; -; mRNA.
DR EMBL; BC053356; AAH53356.1; -; mRNA.
DR EMBL; BC066959; AAH66959.1; -; mRNA.
DR EMBL; BC073742; AAH73742.1; -; mRNA.
DR CCDS; CCDS7458.1; -.
DR PIR; A31782; PMHUYB.
DR RefSeq; NP_002620.1; NM_002629.3.
DR PDB; 1YFK; X-ray; 2.70 A; A/B=1-254.
DR PDB; 1YJX; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-254.
DR PDB; 4GPI; X-ray; 2.08 A; B/C=1-254.
DR PDB; 4GPZ; X-ray; 1.65 A; A/B=1-254.
DR PDB; 5Y2I; X-ray; 1.92 A; B/C=1-254.
DR PDB; 5Y2U; X-ray; 1.98 A; B/C=1-254.
DR PDB; 5Y35; X-ray; 1.99 A; B/C=1-254.
DR PDB; 5Y64; X-ray; 2.15 A; B/C=1-254.
DR PDB; 5Y65; X-ray; 2.55 A; B/C=1-254.
DR PDB; 5ZRM; X-ray; 2.28 A; B/C=2-235.
DR PDB; 5ZS8; X-ray; 2.20 A; B=2-235, C=2-241.
DR PDB; 6ISN; X-ray; 1.98 A; B/C=2-235.
DR PDBsum; 1YFK; -.
DR PDBsum; 1YJX; -.
DR PDBsum; 4GPI; -.
DR PDBsum; 4GPZ; -.
DR PDBsum; 5Y2I; -.
DR PDBsum; 5Y2U; -.
DR PDBsum; 5Y35; -.
DR PDBsum; 5Y64; -.
DR PDBsum; 5Y65; -.
DR PDBsum; 5ZRM; -.
DR PDBsum; 5ZS8; -.
DR PDBsum; 6ISN; -.
DR AlphaFoldDB; P18669; -.
DR SMR; P18669; -.
DR BioGRID; 111244; 111.
DR IntAct; P18669; 30.
DR MINT; P18669; -.
DR STRING; 9606.ENSP00000359991; -.
DR BindingDB; P18669; -.
DR ChEMBL; CHEMBL3334418; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09130; Copper.
DR DEPOD; PGAM1; -.
DR GlyGen; P18669; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P18669; -.
DR MetOSite; P18669; -.
DR PhosphoSitePlus; P18669; -.
DR SwissPalm; P18669; -.
DR BioMuta; PGAM1; -.
DR DMDM; 130348; -.
DR DOSAC-COBS-2DPAGE; P18669; -.
DR OGP; P18669; -.
DR SWISS-2DPAGE; P18669; -.
DR UCD-2DPAGE; P18669; -.
DR EPD; P18669; -.
DR jPOST; P18669; -.
DR MassIVE; P18669; -.
DR PaxDb; P18669; -.
DR PeptideAtlas; P18669; -.
DR PRIDE; P18669; -.
DR ProteomicsDB; 53605; -.
DR TopDownProteomics; P18669; -.
DR Antibodypedia; 30878; 299 antibodies from 36 providers.
DR DNASU; 5223; -.
DR Ensembl; ENST00000334828.6; ENSP00000359991.4; ENSG00000171314.9.
DR GeneID; 5223; -.
DR KEGG; hsa:5223; -.
DR MANE-Select; ENST00000334828.6; ENSP00000359991.4; NM_002629.4; NP_002620.1.
DR CTD; 5223; -.
DR DisGeNET; 5223; -.
DR GeneCards; PGAM1; -.
DR HGNC; HGNC:8888; PGAM1.
DR HPA; ENSG00000171314; Low tissue specificity.
DR MIM; 172250; gene.
DR neXtProt; NX_P18669; -.
DR OpenTargets; ENSG00000171314; -.
DR PharmGKB; PA33225; -.
DR VEuPathDB; HostDB:ENSG00000171314; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; P18669; -.
DR OMA; RMLPYWY; -.
DR OrthoDB; 804949at2759; -.
DR PhylomeDB; P18669; -.
DR TreeFam; TF300007; -.
DR BioCyc; MetaCyc:HS10286-MON; -.
DR BRENDA; 5.4.2.11; 2681.
DR PathwayCommons; P18669; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SABIO-RK; P18669; -.
DR SignaLink; P18669; -.
DR SIGNOR; P18669; -.
DR BioGRID-ORCS; 5223; 549 hits in 1018 CRISPR screens.
DR ChiTaRS; PGAM1; human.
DR EvolutionaryTrace; P18669; -.
DR GenomeRNAi; 5223; -.
DR Pharos; P18669; Tchem.
DR PRO; PR:P18669; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P18669; protein.
DR Bgee; ENSG00000171314; Expressed in superior frontal gyrus and 96 other tissues.
DR ExpressionAtlas; P18669; baseline and differential.
DR Genevisible; P18669; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IDA:UniProtKB.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IDA:UniProtKB.
DR GO; GO:0006110; P:regulation of glycolytic process; IDA:UniProtKB.
DR GO; GO:0043456; P:regulation of pentose-phosphate shunt; IDA:UniProtKB.
DR GO; GO:0045730; P:respiratory burst; IDA:UniProtKB.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Glycolysis;
KW Hydrolase; Isomerase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2846554"
FT CHAIN 2..254
FT /note="Phosphoglycerate mutase 1"
FT /id="PRO_0000179825"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000269|PubMed:23653202,
FT ECO:0000305|PubMed:15883004"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:15883004"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15883004,
FT ECO:0000269|PubMed:23653202"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15883004,
FT ECO:0000269|PubMed:23653202"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q3JWH7"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15883004"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15883004,
FT ECO:0000269|PubMed:23653202"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15883004"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q3JWH7"
FT SITE 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:23653202"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1"
FT MOD_RES 251
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22157007"
FT MOD_RES 251
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1"
FT MOD_RES 253
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22157007"
FT MOD_RES 254
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22157007"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4GPZ"
FT TURN 15..20
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 32..47
FT /evidence="ECO:0007829|PDB:4GPZ"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:4GPZ"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4GPZ"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 156..170
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:4GPZ"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:4GPZ"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5Y2I"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:4GPZ"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4GPZ"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:4GPZ"
SQ SEQUENCE 254 AA; 28804 MW; 6DC0852BEBB22409 CRC64;
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ
KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD
VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR
VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR
KAMEAVAAQG KAKK
