PGK1_MOUSE
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 03-AUG-2022, entry version 188.
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, Pancreas,
RC 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; 40.
DR DIP; DIP-51710N; -.
DR IntAct; P09411; 7.
DR MINT; P09411; -.
DR STRING; 10090.ENSMUSP00000080302; -.
DR iPTMnet; P09411; -.
DR PhosphoSitePlus; P09411; -.
DR SwissPalm; P09411; -.
DR COMPLUYEAST-2DPAGE; P09411; -.
DR REPRODUCTION-2DPAGE; IPI00555069; -.
DR REPRODUCTION-2DPAGE; P09411; -.
DR SWISS-2DPAGE; P09411; -.
DR EPD; P09411; -.
DR jPOST; P09411; -.
DR MaxQB; P09411; -.
DR PaxDb; P09411; -.
DR PeptideAtlas; P09411; -.
DR PRIDE; P09411; -.
DR ProteomicsDB; 301806; -.
DR Antibodypedia; 4108; 489 antibodies from 39 providers.
DR DNASU; 18655; -.
DR Ensembl; ENSMUST00000081593; ENSMUSP00000080302; ENSMUSG00000062070.
DR GeneID; 18655; -.
DR KEGG; mmu:18655; -.
DR UCSC; uc009ubo.2; mouse.
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; 838642at2759; -.
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 72 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 133 other tissues.
DR ExpressionAtlas; P09411; baseline and differential.
DR Genevisible; P09411; MM.
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:0005975; P:carbohydrate metabolic process; ISO: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: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; -; 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; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
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
