ID   PGK1_MOUSE              Reviewed;         417 AA.
AC   P09411; Q3TPE6; Q3UKV8; Q5XJE7;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 4.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Phosphoglycerate kinase 1;
DE            EC=2.7.2.3;
GN   Name=Pgk1; Synonyms=Pgk-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3542714; DOI=10.1016/0378-1119(86)90025-9;
RA   Mori N., Singer-Sam J., Lee C.-Y., Riggs A.D.;
RT   "The nucleotide sequence of a cDNA clone containing the entire coding
RT   region for mouse X-chromosome-linked phosphoglycerate kinase.";
RL   Gene 45:275-280(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129, and C57BL/6J; TISSUE=Brain, and Mammary tumor;
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX   PubMed=3440520; DOI=10.1016/0378-1119(87)90214-9;
RA   Adra C.N., Boer P.H., McBurney M.W.;
RT   "Cloning and expression of the mouse pgk-1 gene and the nucleotide sequence
RT   of its promoter.";
RL   Gene 60:65-74(1987).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX   PubMed=2166582; DOI=10.1016/0167-4781(90)90106-c;
RA   Tamaru M., Nagao Y., Taira M., Tatibana M., Masamune Y., Nakanishi Y.;
RT   "Selective activation of testis-specific genes in cultured rat
RT   spermatogenic cells.";
RL   Biochim. Biophys. Acta 1049:331-338(1990).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX   PubMed=1975492; DOI=10.1007/bf02401419;
RA   Boer P.H., Potten H., Adra C.N., Jardine K., Mullhofer G., McBurney M.W.;
RT   "Polymorphisms in the coding and noncoding regions of murine Pgk-1
RT   alleles.";
RL   Biochem. Genet. 28:299-308(1990).
RN   [8]
RP   PROTEIN SEQUENCE OF 23-30; 76-86; 98-123; 157-184; 193-216; 247-264;
RP   280-297; 333-350 AND 389-417, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [9]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=3525226; DOI=10.1016/0014-5793(86)80835-3;
RA   Mori N., Singer-Sam J., Riggs A.D.;
RT   "Evolutionary conservation of the substrate-binding cleft of
RT   phosphoglycerate kinases.";
RL   FEBS Lett. 204:313-317(1986).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [13]
RP   TISSUE SPECIFICITY.
RX   PubMed=19759366; DOI=10.1095/biolreprod.109.079699;
RA   Danshina P.V., Geyer C.B., Dai Q., Goulding E.H., Willis W.D., Kitto G.B.,
RA   McCarrey J.R., Eddy E.M., O'Brien D.A.;
RT   "Phosphoglycerate kinase 2 (PGK2) is essential for sperm function and male
RT   fertility in mice.";
RL   Biol. Reprod. 82:136-145(2010).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-11; LYS-91; LYS-291 AND
RP   LYS-361, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-48 AND LYS-191,
RP   CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast, and Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Catalyzes one of the two ATP producing reactions in the
CC       glycolytic pathway via the reversible conversion of 1,3-
CC       diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a
CC       glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha
CC       cofactor protein (primer recognition protein). May play a role in sperm
CC       motility. {ECO:0000250|UniProtKB:P00558}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC         Evidence={ECO:0000250|UniProtKB:P00558};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000250|UniProtKB:P00558}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00558}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Testis, lung, brain, skeletal muscle, liver,
CC       intestine, and kidney (at protein level).
CC       {ECO:0000269|PubMed:19759366}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; M15668; AAA70267.1; -; mRNA.
DR   EMBL; AK145846; BAE26693.1; -; mRNA.
DR   EMBL; AK167710; BAE39754.1; -; mRNA.
DR   EMBL; AK167459; BAE39544.1; -; mRNA.
DR   EMBL; AK167441; BAE39527.1; -; mRNA.
DR   EMBL; AK133877; BAE21906.1; -; mRNA.
DR   EMBL; AK164440; BAE37790.1; -; mRNA.
DR   EMBL; BX469914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC083355; AAH83355.1; -; mRNA.
DR   EMBL; BC108372; AAI08373.1; -; mRNA.
DR   EMBL; M18735; AAA39919.1; -; Genomic_DNA.
DR   EMBL; X55309; CAA39013.1; -; Genomic_DNA.
DR   EMBL; X15339; CAA33391.1; -; Genomic_DNA.
DR   CCDS; CCDS30339.1; -.
DR   PIR; A25567; A25567.
DR   RefSeq; NP_032854.2; NM_008828.3.
DR   PDB; 4O3F; X-ray; 2.11 A; A=1-417.
DR   PDBsum; 4O3F; -.
DR   AlphaFoldDB; P09411; -.
DR   SMR; P09411; -.
DR   BioGRID; 202133; 45.
DR   DIP; DIP-51710N; -.
DR   IntAct; P09411; 7.
DR   MINT; P09411; -.
DR   STRING; 10090.ENSMUSP00000080302; -.
DR   GlyGen; P09411; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P09411; -.
DR   MetOSite; P09411; -.
DR   PhosphoSitePlus; P09411; -.
DR   SwissPalm; P09411; -.
DR   REPRODUCTION-2DPAGE; IPI00555069; -.
DR   REPRODUCTION-2DPAGE; P09411; -.
DR   EPD; P09411; -.
DR   jPOST; P09411; -.
DR   MaxQB; P09411; -.
DR   PaxDb; 10090-ENSMUSP00000080302; -.
DR   PeptideAtlas; P09411; -.
DR   ProteomicsDB; 301806; -.
DR   Pumba; P09411; -.
DR   Antibodypedia; 4108; 562 antibodies from 39 providers.
DR   DNASU; 18655; -.
DR   Ensembl; ENSMUST00000081593.13; ENSMUSP00000080302.7; ENSMUSG00000062070.13.
DR   GeneID; 18655; -.
DR   KEGG; mmu:18655; -.
DR   UCSC; uc009ubo.2; mouse.
DR   AGR; MGI:97555; -.
DR   CTD; 5230; -.
DR   MGI; MGI:97555; Pgk1.
DR   VEuPathDB; HostDB:ENSMUSG00000062070; -.
DR   eggNOG; KOG1367; Eukaryota.
DR   GeneTree; ENSGT00390000008820; -.
DR   HOGENOM; CLU_025427_0_0_1; -.
DR   InParanoid; P09411; -.
DR   OMA; YVNDAYS; -.
DR   OrthoDB; 5477183at2759; -.
DR   PhylomeDB; P09411; -.
DR   TreeFam; TF300489; -.
DR   BRENDA; 2.7.2.3; 3474.
DR   Reactome; R-MMU-70171; Glycolysis.
DR   Reactome; R-MMU-70263; Gluconeogenesis.
DR   SABIO-RK; P09411; -.
DR   UniPathway; UPA00109; UER00185.
DR   BioGRID-ORCS; 18655; 30 hits in 76 CRISPR screens.
DR   ChiTaRS; Pgk1; mouse.
DR   PRO; PR:P09411; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; P09411; Protein.
DR   Bgee; ENSMUSG00000062070; Expressed in quadriceps femoris and 136 other cell types or tissues.
DR   ExpressionAtlas; P09411; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0045121; C:membrane raft; ISO:MGI.
DR   GO; GO:0043531; F:ADP binding; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IDA:MGI.
DR   GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; ISO:MGI.
DR   GO; GO:0061621; P:canonical glycolysis; IGI:MGI.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0006094; P:gluconeogenesis; IGI:MGI.
DR   GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; ISO:MGI.
DR   GO; GO:0006096; P:glycolytic process; IDA:MGI.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR   GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR   GO; GO:0031639; P:plasminogen activation; ISO:MGI.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 3.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF14; PHOSPHOGLYCERATE KINASE 1; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
DR   COMPLUYEAST-2DPAGE; P09411; -.
DR   SWISS-2DPAGE; P09411; -.
DR   Genevisible; P09411; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Glycolysis; Hydroxylation; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CHAIN           2..417
FT                   /note="Phosphoglycerate kinase 1"
FT                   /id="PRO_0000145835"
FT   BINDING         24..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         63..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         373..376
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         6
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         48
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         48
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         75
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         76
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   MOD_RES         86
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         91
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         97
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         97
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         131
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         131
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         146
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         191
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         196
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         199
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         216
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         220
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         267
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         291
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         323
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         361
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CONFLICT        56
FT                   /note="K -> N (in Ref. 1; AAA70267)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="K -> R (in Ref. 2; BAE26693)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265
FT                   /note="I -> V (in Ref. 2; BAE37790)"
FT                   /evidence="ECO:0000305"
FT   HELIX           9..11
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           38..52
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          56..61
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           79..89
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           102..109
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   TURN            126..129
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          130..133
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           144..155
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          159..163
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           166..168
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           174..177
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           188..202
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          206..212
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           218..220
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           221..228
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          232..236
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           238..240
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           241..249
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           260..263
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           266..276
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          279..281
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          284..293
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          298..302
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   TURN            303..305
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          312..316
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           318..330
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          332..338
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           346..348
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           350..364
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          368..376
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   STRAND          389..394
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           396..403
FT                   /evidence="ECO:0007829|PDB:4O3F"
FT   HELIX           409..412
FT                   /evidence="ECO:0007829|PDB:4O3F"
SQ   SEQUENCE   417 AA;  44550 MW;  5E2EE194FF9D8CEE CRC64;
     MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL
     MSHLGRPDGV PMPDKYSLEP VAAELKSLLG KDVLFLKDCV GPEVENACAN PAAGTVILLE
     NLRFHVEEEG KGKDASGNKV KAEPAKIDAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
     LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM
     AFTFLKVLNN MEIGTSLYDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ
     ATVASGIPAG WMGLDCGTES SKKYAEAVGR AKQIVWNGPV GVFEWEAFAR GTKSLMDEVV
     KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNV
//