PGK1_HUMAN
ID PGK1_HUMAN Reviewed; 417 AA.
AC P00558; A8K4W6; B7Z7A9; Q5J7W1; Q6IBT6; Q8NI87;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 238.
DE RecName: Full=Phosphoglycerate kinase 1;
DE EC=2.7.2.3 {ECO:0000269|PubMed:30323285};
DE AltName: Full=Cell migration-inducing gene 10 protein;
DE AltName: Full=Primer recognition protein 2;
DE Short=PRP 2;
GN Name=PGK1; Synonyms=PGKA; ORFNames=MIG10, OK/SW-cl.110;
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).
RC TISSUE=Liver;
RX PubMed=6188151; DOI=10.1073/pnas.80.2.472;
RA Michelson A.M., Markham A.F., Orkin S.H.;
RT "Isolation and DNA sequence of a full-length cDNA clone for human X
RT chromosome-encoded phosphoglycerate kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:472-476(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2995995; DOI=10.1073/pnas.82.20.6965;
RA Michelson A.M., Blake C.C., Evans S.T., Orkin S.H.;
RT "Structure of the human phosphoglycerate kinase gene and the intron-
RT mediated evolution and dispersal of the nucleotide-binding domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6965-6969(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a human migration-inducing gene 10 (MIG10).";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, 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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=6099325; DOI=10.1016/0378-1119(84)90016-7;
RA Singer-Sam J., Keith D.H., Tani K., Simmer R.L., Shively L., Lindsay S.,
RA Yoshida A., Riggs A.D.;
RT "Sequence of the promoter region of the gene for human X-linked 3-
RT phosphoglycerate kinase].";
RL Gene 32:409-417(1984).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX PubMed=2814502; DOI=10.1126/science.2814502;
RA Pfeifer G.P., Steigerwald S.D., Mueller P.R., Wold B., Riggs A.D.;
RT "Genomic sequencing and methylation analysis by ligation mediated PCR.";
RL Science 246:810-813(1989).
RN [12]
RP PROTEIN SEQUENCE OF 2-417.
RC TISSUE=Erythrocyte;
RX PubMed=7391027; DOI=10.1016/s0021-9258(18)43754-4;
RA Huang I.-Y., Welch C.D., Yoshida A.;
RT "Complete amino acid sequence of human phosphoglycerate kinase. Cyanogen
RT bromide peptides and complete amino acid sequence.";
RL J. Biol. Chem. 255:6412-6420(1980).
RN [13]
RP PROTEIN SEQUENCE OF 23-30; 76-86; 107-123; 157-171; 200-216; 221-264;
RP 280-297; 333-350; 366-382 AND 389-417, AND IDENTIFICATION BY MASS
RP 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 [14]
RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=2324090; DOI=10.1016/s0021-9258(19)39179-3;
RA Jindal H.K., Vishwanatha J.K.;
RT "Functional identity of a primer recognition protein as phosphoglycerate
RT kinase.";
RL J. Biol. Chem. 265:6540-6543(1990).
RN [15]
RP REVIEW ON VARIANTS.
RX PubMed=9075577; DOI=10.1006/bcmd.1996.0108;
RA Yoshida A.;
RT "Hematologically important mutations: molecular abnormalities of
RT phosphoglycerate kinase.";
RL Blood Cells Mol. Dis. 22:265-267(1996).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [19]
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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-48; LYS-75; LYS-86;
RP LYS-97; LYS-131; LYS-146; LYS-199; LYS-267 AND LYS-291, AND IDENTIFICATION
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, 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 [22]
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 [23]
RP MALONYLATION AT LYS-131.
RX PubMed=21908771; DOI=10.1074/mcp.m111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W.,
RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, 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 [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-4 AND SER-203, 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, 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 [28]
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 [29]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26677959; DOI=10.1093/humrep/dev301;
RA Liu X.X., Zhang H., Shen X.F., Liu F.J., Liu J., Wang W.J.;
RT "Characteristics of testis-specific phosphoglycerate kinase 2 and its
RT association with human sperm quality.";
RL Hum. Reprod. 31:273-279(2016).
RN [30]
RP HYDROXYBUTYRYLATION AT LYS-220.
RX PubMed=29192674; DOI=10.1038/cr.2017.149;
RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J.,
RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.;
RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation
RT pathway.";
RL Cell Res. 28:111-125(2018).
RN [31]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND ACTIVITY REGULATION.
RX PubMed=30323285; DOI=10.1038/s41586-018-0622-0;
RA Bollong M.J., Lee G., Coukos J.S., Yun H., Zambaldo C., Chang J.W.,
RA Chin E.N., Ahmad I., Chatterjee A.K., Lairson L.L., Schultz P.G.,
RA Moellering R.E.;
RT "A metabolite-derived protein modification integrates glycolysis with
RT KEAP1-NRF2 signalling.";
RL Nature 562:600-604(2018).
RN [32]
RP HYDROXYBUTYRYLATION AT LYS-97; LYS-216 AND LYS-323.
RX PubMed=29775581; DOI=10.1016/j.molcel.2018.04.011;
RA Huang H., Tang S., Ji M., Tang Z., Shimada M., Liu X., Qi S.,
RA Locasale J.W., Roeder R.G., Zhao Y., Li X.;
RT "p300-mediated lysine 2-hydroxyisobutyrylation regulates glycolysis.";
RL Mol. Cell 70:663-678(2018).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH PHOSPHOGLYCERATE;
RP L-ADP; D-ADP; L-CDP AND D-CDP, AND SUBSTRATE-BINDING SITES.
RX PubMed=18463139; DOI=10.1093/nar/gkn212;
RA Gondeau C., Chaloin L., Lallemand P., Roy B., Perigaud C., Barman T.,
RA Varga A., Vas M., Lionne C., Arold S.T.;
RT "Molecular basis for the lack of enantioselectivity of human 3-
RT phosphoglycerate kinase.";
RL Nucleic Acids Res. 36:3620-3629(2008).
RN [34]
RP VARIANT PGK1D LYS-191 DEL.
RX PubMed=8673469; DOI=10.1006/bcmd.1995.0020;
RA Yoshida A., Twele T.W., Dave V., Beutler E.;
RT "Molecular abnormality of a phosphoglycerate kinase variant (PGK-
RT Alabama).";
RL Blood Cells Mol. Dis. 21:179-181(1995).
RN [35]
RP VARIANTS PGK1D VAL-164 AND ASN-315.
RX PubMed=8043870;
RA Cohen-Solal M., Valentin C., Plassa F., Guillemin G., Danze F., Jaisson F.,
RA Rosa R.;
RT "Identification of new mutations in two phosphoglycerate kinase (PGK)
RT variants expressing different clinical syndromes: PGK Creteil and PGK
RT Amiens.";
RL Blood 84:898-903(1994).
RN [36]
RP VARIANT PGK1D ALA-252.
RX PubMed=8615693; DOI=10.1006/abbi.1996.0089;
RA Ookawara T., Dave V., Willems P., Martin J.J., de Barsy T., Matthys E.,
RA Yoshida A.;
RT "Retarded and aberrant splicings caused by single exon mutation in a
RT phosphoglycerate kinase variant.";
RL Arch. Biochem. Biophys. 327:35-40(1996).
RN [37]
RP VARIANT PGK1D VAL-285.
RX PubMed=9744480;
RX DOI=10.1002/(sici)1098-1004(1998)12:4<280::aid-humu10>3.0.co;2-v;
RA Valentin C., Birgens H., Craescu C.T., Broedum-Nielsen K., Cohen-Solal M.;
RT "A phosphoglycerate kinase mutant (PGK Herlev; D285V) in a Danish patient
RT with isolated chronic hemolytic anemia: mechanism of mutation and
RT structure-function relationships.";
RL Hum. Mutat. 12:280-287(1998).
RN [38]
RP VARIANT PGK1D PRO-88.
RX PubMed=2001457;
RA Maeda M., Yoshida A.;
RT "Molecular defect of a phosphoglycerate kinase variant (PGK-Matsue)
RT associated with hemolytic anemia: Leu-->Pro substitution caused by
RT T/A-->C/G transition in exon 3.";
RL Blood 77:1348-1352(1991).
RN [39]
RP VARIANT PGK1D ARG-316.
RX PubMed=1586722;
RA Maeda M., Bawle E.V., Kulkarni R., Beutler E., Yoshida A.;
RT "Molecular abnormalities of a phosphoglycerate kinase variant generated by
RT spontaneous mutation.";
RL Blood 79:2759-2762(1992).
RN [40]
RP VARIANT MUNCHEN ASN-268, CATALYTIC ACTIVITY, FUNCTION, AND PATHWAY.
RX PubMed=7391028; DOI=10.1016/s0021-9258(18)43755-6;
RA Fujii H., Krietsch W.K.G., Yoshida A.;
RT "A single amino acid substitution (Asp leads to Asn) in a phosphoglycerate
RT kinase variant (PGK Munchen) associated with enzyme deficiency.";
RL J. Biol. Chem. 255:6421-6423(1980).
RN [41]
RP VARIANT MUNCHEN ASN-268, AND VARIANT ASN-352.
RX PubMed=7440217; DOI=10.3109/03630268008997730;
RA Huang I.-Y., Fujii H., Yoshida A.;
RT "Structure and function of normal and variant human phosphoglycerate
RT kinase.";
RL Hemoglobin 4:601-609(1980).
RN [42]
RP VARIANT PGK1D VAL-158.
RX PubMed=1547346;
RA Fujii H., Kanno H., Hirono A., Shiomura T., Miwa S.;
RT "A single amino acid substitution (157 Gly-->Val) in a phosphoglycerate
RT kinase variant (PGK Shizuoka) associated with chronic hemolysis and
RT myoglobinuria.";
RL Blood 79:1582-1585(1992).
RN [43]
RP VARIANT PGK1D MET-266.
RX PubMed=6941312; DOI=10.1073/pnas.78.4.2587;
RA Fujii H., Chen S.-H., Akatsuka J., Miwa S., Yoshida A.;
RT "Use of cultured lymphoblastoid cells for the study of abnormal enzymes:
RT molecular abnormality of a phosphoglycerate kinase variant associated with
RT hemolytic anemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:2587-2590(1981).
RN [44]
RP VARIANT PGK1D PRO-206.
RX PubMed=6933565; DOI=10.1073/pnas.77.9.5461;
RA Fujii H., Yoshida A.;
RT "Molecular abnormality of phosphoglycerate kinase-Uppsala associated with
RT chronic nonspherocytic hemolytic anemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:5461-5465(1980).
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 (PubMed:30323285,
CC PubMed:7391028). In addition to its role as a glycolytic enzyme, it
CC seems that PGK-1 acts as a polymerase alpha cofactor protein (primer
CC recognition protein) (PubMed:2324090). May play a role in sperm
CC motility (PubMed:26677959). {ECO:0000269|PubMed:2324090,
CC ECO:0000269|PubMed:26677959, ECO:0000269|PubMed:30323285,
CC ECO:0000269|PubMed:7391028}.
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:0000269|PubMed:30323285, ECO:0000269|PubMed:7391028};
CC -!- ACTIVITY REGULATION: Specifically inhibited by heterocyclic compound
CC CBR-470-0. {ECO:0000269|PubMed:30323285}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000269|PubMed:30323285,
CC ECO:0000269|PubMed:7391028}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18463139}.
CC -!- INTERACTION:
CC P00558; P04406: GAPDH; NbExp=2; IntAct=EBI-709599, EBI-354056;
CC P00558; O15379: HDAC3; NbExp=2; IntAct=EBI-709599, EBI-607682;
CC P00558; Q8TDX7: NEK7; NbExp=2; IntAct=EBI-709599, EBI-1055945;
CC P00558; P12004: PCNA; NbExp=2; IntAct=EBI-709599, EBI-358311;
CC P00558-1; O15379: HDAC3; NbExp=3; IntAct=EBI-16177310, EBI-607682;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P00558-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P00558-2; Sequence=VSP_056159;
CC -!- TISSUE SPECIFICITY: Mainly expressed in spermatogonia. Localized on the
CC principle piece in the sperm (at protein level). Expression
CC significantly decreased in the testis of elderly men.
CC {ECO:0000269|PubMed:26677959}.
CC -!- DISEASE: Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]: A
CC condition with a highly variable clinical phenotype that includes
CC hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement.
CC Patients can express one or more of these manifestations.
CC {ECO:0000269|PubMed:1547346, ECO:0000269|PubMed:1586722,
CC ECO:0000269|PubMed:2001457, ECO:0000269|PubMed:6933565,
CC ECO:0000269|PubMed:6941312, ECO:0000269|PubMed:8043870,
CC ECO:0000269|PubMed:8615693, ECO:0000269|PubMed:8673469,
CC ECO:0000269|PubMed:9744480}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Phosphoglycerate kinase entry;
CC URL="https://en.wikipedia.org/wiki/Phosphoglycerate_kinase";
CC ---------------------------------------------------------------------------
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DR EMBL; V00572; CAA23835.1; -; mRNA.
DR EMBL; L00160; AAA60078.1; -; mRNA.
DR EMBL; M11968; AAA60079.1; -; Genomic_DNA.
DR EMBL; M11958; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11959; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11960; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11961; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11962; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11963; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11964; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11965; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11966; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; M11967; AAA60079.1; JOINED; Genomic_DNA.
DR EMBL; AY423725; AAS00488.1; -; mRNA.
DR EMBL; AB062432; BAB93495.1; -; mRNA.
DR EMBL; AK291081; BAF83770.1; -; mRNA.
DR EMBL; AK301740; BAH13545.1; -; mRNA.
DR EMBL; AK312280; BAG35209.1; -; mRNA.
DR EMBL; CR456716; CAG32997.1; -; mRNA.
DR EMBL; AL049589; CAI42951.1; -; Genomic_DNA.
DR EMBL; CH471104; EAW98604.1; -; Genomic_DNA.
DR EMBL; BC023234; AAH23234.1; -; mRNA.
DR EMBL; BC103752; AAI03753.1; -; mRNA.
DR EMBL; BC104837; AAI04838.1; -; mRNA.
DR EMBL; BC113568; AAI13569.1; -; mRNA.
DR EMBL; M34017; AAA60103.1; -; Genomic_DNA.
DR CCDS; CCDS14438.1; -. [P00558-1]
DR PIR; I59050; KIHUG.
DR RefSeq; NP_000282.1; NM_000291.3. [P00558-1]
DR PDB; 2WZB; X-ray; 1.47 A; A=2-417.
DR PDB; 2WZC; X-ray; 1.50 A; A=2-417.
DR PDB; 2WZD; X-ray; 1.56 A; A=1-417.
DR PDB; 2X13; X-ray; 1.74 A; A=2-417.
DR PDB; 2X14; X-ray; 1.90 A; A=2-417.
DR PDB; 2X15; X-ray; 2.10 A; A=2-417.
DR PDB; 2XE6; X-ray; 1.74 A; A=1-417.
DR PDB; 2XE7; X-ray; 2.20 A; A=1-417.
DR PDB; 2XE8; X-ray; 1.79 A; A=1-417.
DR PDB; 2Y3I; X-ray; 2.90 A; A/D=1-416.
DR PDB; 2YBE; X-ray; 2.00 A; A=1-417.
DR PDB; 2ZGV; X-ray; 2.00 A; A=1-417.
DR PDB; 3C39; X-ray; 1.85 A; A/B=1-417.
DR PDB; 3C3A; X-ray; 2.30 A; A/B=1-417.
DR PDB; 3C3B; X-ray; 1.80 A; A/B=1-417.
DR PDB; 3C3C; X-ray; 2.40 A; A/B=1-417.
DR PDB; 3ZOZ; X-ray; 1.95 A; A=1-417.
DR PDB; 4AXX; X-ray; 1.74 A; A=1-417.
DR PDB; 4O33; X-ray; 2.10 A; A=1-417.
DR PDB; 5M1R; X-ray; 1.64 A; A=2-417.
DR PDB; 5M3U; X-ray; 1.81 A; A=2-417.
DR PDB; 5M6Z; X-ray; 1.67 A; A=2-417.
DR PDB; 5MXM; X-ray; 2.05 A; A=2-417.
DR PDB; 5NP8; X-ray; 1.90 A; A=1-417.
DR PDB; 5O7D; X-ray; 1.84 A; A=1-417.
DR PDBsum; 2WZB; -.
DR PDBsum; 2WZC; -.
DR PDBsum; 2WZD; -.
DR PDBsum; 2X13; -.
DR PDBsum; 2X14; -.
DR PDBsum; 2X15; -.
DR PDBsum; 2XE6; -.
DR PDBsum; 2XE7; -.
DR PDBsum; 2XE8; -.
DR PDBsum; 2Y3I; -.
DR PDBsum; 2YBE; -.
DR PDBsum; 2ZGV; -.
DR PDBsum; 3C39; -.
DR PDBsum; 3C3A; -.
DR PDBsum; 3C3B; -.
DR PDBsum; 3C3C; -.
DR PDBsum; 3ZOZ; -.
DR PDBsum; 4AXX; -.
DR PDBsum; 4O33; -.
DR PDBsum; 5M1R; -.
DR PDBsum; 5M3U; -.
DR PDBsum; 5M6Z; -.
DR PDBsum; 5MXM; -.
DR PDBsum; 5NP8; -.
DR PDBsum; 5O7D; -.
DR AlphaFoldDB; P00558; -.
DR SMR; P00558; -.
DR BioGRID; 111251; 235.
DR DIP; DIP-33679N; -.
DR IntAct; P00558; 68.
DR MINT; P00558; -.
DR STRING; 9606.ENSP00000362413; -.
DR BindingDB; P00558; -.
DR ChEMBL; CHEMBL2886; -.
DR DrugBank; DB04510; 3-phospho-D-glyceric acid.
DR DrugBank; DB00787; Acyclovir.
DR DrugBank; DB03909; Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB00709; Lamivudine.
DR MoonDB; P00558; Curated.
DR MoonProt; P00558; -.
DR GlyGen; P00558; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; P00558; -.
DR MetOSite; P00558; -.
DR PhosphoSitePlus; P00558; -.
DR SwissPalm; P00558; -.
DR BioMuta; PGK1; -.
DR DMDM; 52788229; -.
DR DOSAC-COBS-2DPAGE; P00558; -.
DR OGP; P00558; -.
DR REPRODUCTION-2DPAGE; IPI00169383; -.
DR REPRODUCTION-2DPAGE; P00558; -.
DR UCD-2DPAGE; P00558; -.
DR CPTAC; CPTAC-562; -.
DR CPTAC; CPTAC-563; -.
DR EPD; P00558; -.
DR jPOST; P00558; -.
DR MassIVE; P00558; -.
DR MaxQB; P00558; -.
DR PaxDb; P00558; -.
DR PeptideAtlas; P00558; -.
DR PRIDE; P00558; -.
DR ProteomicsDB; 51266; -. [P00558-1]
DR ProteomicsDB; 6847; -.
DR TopDownProteomics; P00558-1; -. [P00558-1]
DR Antibodypedia; 4108; 489 antibodies from 39 providers.
DR DNASU; 5230; -.
DR Ensembl; ENST00000373316.5; ENSP00000362413.4; ENSG00000102144.15. [P00558-1]
DR Ensembl; ENST00000644362.1; ENSP00000496140.1; ENSG00000102144.15. [P00558-2]
DR GeneID; 5230; -.
DR KEGG; hsa:5230; -.
DR MANE-Select; ENST00000373316.5; ENSP00000362413.4; NM_000291.4; NP_000282.1.
DR CTD; 5230; -.
DR DisGeNET; 5230; -.
DR GeneCards; PGK1; -.
DR HGNC; HGNC:8896; PGK1.
DR HPA; ENSG00000102144; Low tissue specificity.
DR MalaCards; PGK1; -.
DR MIM; 300653; phenotype.
DR MIM; 311800; gene.
DR neXtProt; NX_P00558; -.
DR OpenTargets; ENSG00000102144; -.
DR Orphanet; 713; Glycogen storage disease due to phosphoglycerate kinase 1 deficiency.
DR PharmGKB; PA33234; -.
DR VEuPathDB; HostDB:ENSG00000102144; -.
DR eggNOG; KOG1367; Eukaryota.
DR GeneTree; ENSGT00390000008820; -.
DR HOGENOM; CLU_025427_0_0_1; -.
DR InParanoid; P00558; -.
DR OMA; YVNDAYS; -.
DR PhylomeDB; P00558; -.
DR TreeFam; TF300489; -.
DR BioCyc; MetaCyc:HS02359-MON; -.
DR PathwayCommons; P00558; -.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR Reactome; R-HSA-9636667; Manipulation of host energy metabolism.
DR SABIO-RK; P00558; -.
DR SignaLink; P00558; -.
DR SIGNOR; P00558; -.
DR UniPathway; UPA00109; UER00185.
DR BioGRID-ORCS; 5230; 221 hits in 720 CRISPR screens.
DR ChiTaRS; PGK1; human.
DR EvolutionaryTrace; P00558; -.
DR GeneWiki; PGK1; -.
DR GenomeRNAi; 5230; -.
DR Pharos; P00558; Tchem.
DR PRO; PR:P00558; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P00558; protein.
DR Bgee; ENSG00000102144; Expressed in esophagus squamous epithelium and 206 other tissues.
DR ExpressionAtlas; P00558; baseline and differential.
DR Genevisible; P00558; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IMP:CAFA.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IMP:CAFA.
DR GO; GO:0061621; P:canonical glycolysis; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:CAFA.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IMP:CAFA.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:CAFA.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR GO; GO:0031639; P:plasminogen activation; IMP:CAFA.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR DisProt; DP02766; -.
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; Alternative splicing; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Disease variant; Glycolysis;
KW Hereditary hemolytic anemia; Hydroxylation; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7391027,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..417
FT /note="Phosphoglycerate kinase 1"
FT /id="PRO_0000145831"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18463139"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18463139"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18463139"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18463139"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18463139"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18463139"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18463139"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18463139"
FT BINDING 373..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18463139"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09411"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 48
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 48
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09411"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 76
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09411"
FT MOD_RES 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09411"
FT MOD_RES 97
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:29775581"
FT MOD_RES 97
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 131
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 131
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 191
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09411"
FT MOD_RES 196
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 216
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:29775581"
FT MOD_RES 220
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:29192674"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 323
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:29775581"
FT MOD_RES 361
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09411"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056159"
FT VARIANT 88
FT /note="L -> P (in PGK1D; with congenital non-spherocytic
FT anemia; variant Matsue; dbSNP:rs137852531)"
FT /evidence="ECO:0000269|PubMed:2001457"
FT /id="VAR_006076"
FT VARIANT 158
FT /note="G -> V (in PGK1D; with chronic hemolytic anemia;
FT variant Shizuoka; dbSNP:rs137852532)"
FT /evidence="ECO:0000269|PubMed:1547346"
FT /id="VAR_006077"
FT VARIANT 164
FT /note="D -> V (in PGK1D; with chronic hemolytic anemia and
FT intellectual disability; variant Amiens;
FT dbSNP:rs137852538)"
FT /evidence="ECO:0000269|PubMed:8043870"
FT /id="VAR_006078"
FT VARIANT 191
FT /note="Missing (in PGK1D; with chronic hemolytic anemia;
FT variant Alabama)"
FT /evidence="ECO:0000269|PubMed:8673469"
FT /id="VAR_006079"
FT VARIANT 206
FT /note="R -> P (in PGK1D; with chronic hemolytic anemia;
FT variant Uppsala; dbSNP:rs137852529)"
FT /evidence="ECO:0000269|PubMed:6933565"
FT /id="VAR_006080"
FT VARIANT 252
FT /note="E -> A (in PGK1D; with chronic hemolytic anemia;
FT variant Antwerp)"
FT /evidence="ECO:0000269|PubMed:8615693"
FT /id="VAR_006081"
FT VARIANT 266
FT /note="V -> M (in PGK1D; with chronic non-spherocytic
FT hemolytic anemia; variant Tokyo; dbSNP:rs431905501)"
FT /evidence="ECO:0000269|PubMed:6941312"
FT /id="VAR_006082"
FT VARIANT 268
FT /note="D -> N (in Munchen; 21% of activity;
FT dbSNP:rs137852528)"
FT /evidence="ECO:0000269|PubMed:7391028,
FT ECO:0000269|PubMed:7440217"
FT /id="VAR_006083"
FT VARIANT 285
FT /note="D -> V (in PGK1D; with chronic hemolytic anemia;
FT variant Herlev; 50% of activity; dbSNP:rs137852535)"
FT /evidence="ECO:0000269|PubMed:9744480"
FT /id="VAR_006084"
FT VARIANT 315
FT /note="D -> N (in PGK1D; with rhabdomyolysis; variant
FT Creteil)"
FT /evidence="ECO:0000269|PubMed:8043870"
FT /id="VAR_006085"
FT VARIANT 316
FT /note="C -> R (in PGK1D; with chronic hemolytic anemia;
FT variant Michigan; dbSNP:rs137852533)"
FT /evidence="ECO:0000269|PubMed:1586722"
FT /id="VAR_006086"
FT VARIANT 352
FT /note="T -> N (in dbSNP:rs137852530)"
FT /evidence="ECO:0000269|PubMed:7440217"
FT /id="VAR_006087"
FT CONFLICT 39
FT /note="Missing (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="I -> T (in Ref. 6; CAG32997)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:5M1R"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:5M6Z"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3C3B"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2WZB"
FT TURN 126..130
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2XE8"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3C3A"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:5M1R"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 188..202
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:2WZB"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:2WZB"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 350..364
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 376..382
FT /evidence="ECO:0007829|PDB:2WZB"
FT STRAND 388..394
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 397..404
FT /evidence="ECO:0007829|PDB:2WZB"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:2WZB"
SQ SEQUENCE 417 AA; 44615 MW; B5DFC7B5FA01767C CRC64;
MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL
MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV GPEVEKACAN PAAGSVILLE
NLRFHVEEEG KGKDASGNKV KAEPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM
AFTFLKVLNN MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ
ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV
KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNI
