Full text data of PGK1
PGK1
(PGKA)
[Confidence: high (present in two of the MS resources)]
Phosphoglycerate kinase 1; 2.7.2.3 (Cell migration-inducing gene 10 protein; Primer recognition protein 2; PRP 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosphoglycerate kinase 1; 2.7.2.3 (Cell migration-inducing gene 10 protein; Primer recognition protein 2; PRP 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00169383
IPI00169383 Phosphoglycerete kinase 1 Phosphoglycerete kinase 1 membrane n/a n/a n/a n/a n/a n/a n/a n/a 3 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a glycolysis, cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00169383 Phosphoglycerete kinase 1 Phosphoglycerete kinase 1 membrane n/a n/a n/a n/a n/a n/a n/a n/a 3 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a glycolysis, cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P00558
ID PGK1_HUMAN Reviewed; 417 AA.
AC P00558; A8K4W6; Q5J7W1; Q6IBT6; Q8NI87;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 163.
DE RecName: Full=Phosphoglycerate kinase 1;
DE EC=2.7.2.3;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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].
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].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive 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].
RC TISSUE=Cerebellum;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: 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.,
RA Lindsay S., 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
RT PCR.";
RL Science 246:810-813(1989).
RN [12]
RP PROTEIN SEQUENCE OF 2-417.
RC TISSUE=Erythrocyte;
RX PubMed=7391027;
RA Huang I.-Y., Welch C.D., Yoshida A.;
RT "Complete amino acid sequence of human phosphoglycerate kinase.
RT Cyanogen 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 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 [14]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Placenta;
RX PubMed=2324090;
RA Jindal H.K., Vishwanatha J.K.;
RT "Functional identity of a primer recognition protein as
RT phosphoglycerate 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [18]
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 [19]
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 MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
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.,
RA Buerckstuemmer T., 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 [22]
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.,
RA He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
RA Dai J., 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH
RP PHOSPHOGLYCERATE; L-ADP; D-ADP; L-CDP AND D-CDP, AND SUBSTRATE-BINDING
RP 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 [26]
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 [27]
RP VARIANTS PGK1D VAL-164 AND ASN-315.
RX PubMed=8043870;
RA Cohen-Solal M., Valentin C., Plassa F., Guillemin G., Danze F.,
RA Jaisson F., 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 [28]
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.,
RA Matthys E., 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 [29]
RP VARIANT PGK1D VAL-285.
RX PubMed=9744480;
RX DOI=10.1002/(SICI)1098-1004(1998)12:4<280::AID-HUMU10>3.3.CO;2-Z;
RA Valentin C., Birgens H., Craescu C.T., Broedum-Nielsen K.,
RA Cohen-Solal M.;
RT "A phosphoglycerate kinase mutant (PGK Herlev; D285V) in a Danish
RT patient with isolated chronic hemolytic anemia: mechanism of mutation
RT and structure-function relationships.";
RL Hum. Mutat. 12:280-287(1998).
RN [30]
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 [31]
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
RT generated by spontaneous mutation.";
RL Blood 79:2759-2762(1992).
RN [32]
RP VARIANT MUNCHEN ASN-268.
RX PubMed=7391028;
RA Fujii H., Krietsch W.K.G., Yoshida A.;
RT "A single amino acid substitution (Asp leads to Asn) in a
RT phosphoglycerate kinase variant (PGK Munchen) associated with enzyme
RT deficiency.";
RL J. Biol. Chem. 255:6421-6423(1980).
RN [33]
RP VARIANT MUNCHEN ASN-268, AND VARIANT ASN-352.
RX PubMed=7440217;
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 [34]
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
RT phosphoglycerate kinase variant (PGK Shizuoka) associated with chronic
RT hemolysis and myoglobinuria.";
RL Blood 79:1582-1585(1992).
RN [35]
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
RT enzymes: molecular abnormality of a phosphoglycerate kinase variant
RT associated with hemolytic anemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:2587-2590(1981).
RN [36]
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
RT with chronic nonspherocytic hemolytic anemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:5461-5465(1980).
CC -!- FUNCTION: In addition to its role as a glycolytic enzyme, it seems
CC that PGK-1 acts as a polymerase alpha cofactor protein (primer
CC recognition protein).
CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
CC D-glyceroyl phosphate.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P04406:GAPDH; NbExp=2; IntAct=EBI-709599, EBI-354056;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISEASE: Phosphoglycerate kinase 1 deficiency (PGK1D)
CC [MIM:300653]: A condition with a highly variable clinical
CC phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy
CC and neurologic involvement. Patients can express one or more of
CC these manifestations. Note=The disease is caused by mutations
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PGK1";
CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC polymorphism database;
CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename;=PGK1";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Phosphoglycerate kinase entry;
CC URL="http://en.wikipedia.org/wiki/Phosphoglycerate_kinase";
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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; 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 PIR; I59050; KIHUG.
DR RefSeq; NP_000282.1; NM_000291.3.
DR UniGene; Hs.78771; -.
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; 4AXX; X-ray; 1.74 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; 4AXX; -.
DR ProteinModelPortal; P00558; -.
DR SMR; P00558; 5-417.
DR IntAct; P00558; 29.
DR MINT; MINT-1131047; -.
DR STRING; 9606.ENSP00000362413; -.
DR BindingDB; P00558; -.
DR ChEMBL; CHEMBL2096677; -.
DR PhosphoSite; P00558; -.
DR DMDM; 52788229; -.
DR DOSAC-COBS-2DPAGE; P00558; -.
DR OGP; P00558; -.
DR REPRODUCTION-2DPAGE; IPI00169383; -.
DR REPRODUCTION-2DPAGE; P00558; -.
DR UCD-2DPAGE; P00558; -.
DR PaxDb; P00558; -.
DR PeptideAtlas; P00558; -.
DR PRIDE; P00558; -.
DR DNASU; 5230; -.
DR Ensembl; ENST00000373316; ENSP00000362413; ENSG00000102144.
DR Ensembl; ENST00000597340; ENSP00000472461; ENSG00000269666.
DR GeneID; 5230; -.
DR KEGG; hsa:5230; -.
DR UCSC; uc004ecz.4; human.
DR CTD; 5230; -.
DR GeneCards; GC0XP077246; -.
DR HGNC; HGNC:8896; PGK1.
DR HPA; CAB010065; -.
DR HPA; HPA045385; -.
DR MIM; 300653; phenotype.
DR MIM; 311800; gene.
DR neXtProt; NX_P00558; -.
DR Orphanet; 713; Glycogen storage disease due to phosphoglycerate kinase 1 deficiency.
DR PharmGKB; PA33234; -.
DR eggNOG; COG0126; -.
DR HOGENOM; HOG000227107; -.
DR HOVERGEN; HBG008177; -.
DR InParanoid; P00558; -.
DR KO; K00927; -.
DR OMA; NFANGTK; -.
DR PhylomeDB; P00558; -.
DR BioCyc; MetaCyc:HS02359-MONOMER; -.
DR BRENDA; 2.7.2.3; 2681.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P00558; -.
DR UniPathway; UPA00109; UER00185.
DR ChiTaRS; PGK1; human.
DR EvolutionaryTrace; P00558; -.
DR GeneWiki; PGK1; -.
DR GenomeRNAi; 5230; -.
DR NextBio; 20218; -.
DR PRO; PR:P00558; -.
DR ArrayExpress; P00558; -.
DR Bgee; P00558; -.
DR CleanEx; HS_PGK1; -.
DR Genevestigator; P00558; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0006096; P:glycolysis; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.1260; -; 1.
DR Gene3D; 3.40.50.1270; -; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015901; Phosphoglycerate_kinase_C.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disease mutation; Glycolysis;
KW Hereditary hemolytic anemia; Kinase; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Reference proteome; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 417 Phosphoglycerate kinase 1.
FT /FTId=PRO_0000145831.
FT NP_BIND 373 376 ATP.
FT REGION 24 26 Substrate binding.
FT REGION 63 66 Substrate binding.
FT BINDING 39 39 Substrate.
FT BINDING 123 123 Substrate.
FT BINDING 171 171 Substrate.
FT BINDING 220 220 ATP.
FT BINDING 313 313 ATP; via carbonyl oxygen.
FT BINDING 344 344 ATP.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 11 11 N6-acetyllysine.
FT MOD_RES 48 48 N6-acetyllysine.
FT MOD_RES 75 75 N6-acetyllysine.
FT MOD_RES 76 76 Phosphotyrosine (By similarity).
FT MOD_RES 86 86 N6-acetyllysine.
FT MOD_RES 97 97 N6-acetyllysine.
FT MOD_RES 131 131 N6-acetyllysine; alternate.
FT MOD_RES 131 131 N6-malonyllysine; alternate.
FT MOD_RES 146 146 N6-acetyllysine.
FT MOD_RES 196 196 Phosphotyrosine.
FT MOD_RES 199 199 N6-acetyllysine.
FT MOD_RES 203 203 Phosphoserine.
FT MOD_RES 267 267 N6-acetyllysine.
FT MOD_RES 291 291 N6-acetyllysine.
FT VARIANT 88 88 L -> P (in PGK1D; with congenital non-
FT spherocytic anemia; variant Matsue).
FT /FTId=VAR_006076.
FT VARIANT 158 158 G -> V (in PGK1D; with chronic hemolytic
FT anemia; variant Shizuoka).
FT /FTId=VAR_006077.
FT VARIANT 164 164 D -> V (in PGK1D; with chronic hemolytic
FT anemia and mental retardation; variant
FT Amiens).
FT /FTId=VAR_006078.
FT VARIANT 191 191 Missing (in PGK1D; with chronic hemolytic
FT anemia; variant Alabama).
FT /FTId=VAR_006079.
FT VARIANT 206 206 R -> P (in PGK1D; with chronic hemolytic
FT anemia; variant Uppsala).
FT /FTId=VAR_006080.
FT VARIANT 252 252 E -> A (in PGK1D; with chronic hemolytic
FT anemia; variant Antwerp).
FT /FTId=VAR_006081.
FT VARIANT 266 266 V -> M (in PGK1D; with chronic non-
FT spherocytic hemolytic anemia; variant
FT Tokyo).
FT /FTId=VAR_006082.
FT VARIANT 268 268 D -> N (in Munchen; 21% of activity).
FT /FTId=VAR_006083.
FT VARIANT 285 285 D -> V (in PGK1D; with chronic hemolytic
FT anemia; variant Herlev; 50% of activity).
FT /FTId=VAR_006084.
FT VARIANT 315 315 D -> N (in PGK1D; with rhabdomyolysis;
FT variant Creteil).
FT /FTId=VAR_006085.
FT VARIANT 316 316 C -> R (in PGK1D; with chronic hemolytic
FT anemia; variant Michigan).
FT /FTId=VAR_006086.
FT VARIANT 352 352 T -> N.
FT /FTId=VAR_006087.
FT CONFLICT 39 39 Missing (in Ref. 12; AA sequence).
FT CONFLICT 370 370 I -> T (in Ref. 6; CAG32997).
FT STRAND 4 6
FT HELIX 9 11
FT STRAND 18 22
FT STRAND 29 32
FT STRAND 33 35
FT HELIX 38 52
FT STRAND 56 61
FT HELIX 73 76
FT HELIX 79 89
FT STRAND 94 97
FT STRAND 99 101
FT HELIX 102 109
FT STRAND 115 118
FT HELIX 122 124
FT TURN 126 130
FT STRAND 131 133
FT STRAND 135 137
FT STRAND 139 141
FT HELIX 144 156
FT STRAND 159 163
FT HELIX 166 168
FT HELIX 174 177
FT STRAND 184 186
FT HELIX 188 202
FT STRAND 206 212
FT HELIX 217 220
FT HELIX 221 223
FT HELIX 224 227
FT TURN 228 230
FT STRAND 232 236
FT HELIX 238 240
FT HELIX 241 249
FT HELIX 260 263
FT HELIX 266 275
FT STRAND 279 281
FT STRAND 285 293
FT STRAND 298 302
FT TURN 303 305
FT STRAND 312 316
FT HELIX 318 330
FT STRAND 332 338
FT HELIX 346 348
FT HELIX 350 364
FT STRAND 368 373
FT HELIX 376 382
FT STRAND 388 394
FT HELIX 397 404
FT HELIX 409 412
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
//
ID PGK1_HUMAN Reviewed; 417 AA.
AC P00558; A8K4W6; Q5J7W1; Q6IBT6; Q8NI87;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 163.
DE RecName: Full=Phosphoglycerate kinase 1;
DE EC=2.7.2.3;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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].
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].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive 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].
RC TISSUE=Cerebellum;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: 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.,
RA Lindsay S., 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
RT PCR.";
RL Science 246:810-813(1989).
RN [12]
RP PROTEIN SEQUENCE OF 2-417.
RC TISSUE=Erythrocyte;
RX PubMed=7391027;
RA Huang I.-Y., Welch C.D., Yoshida A.;
RT "Complete amino acid sequence of human phosphoglycerate kinase.
RT Cyanogen 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 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 [14]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Placenta;
RX PubMed=2324090;
RA Jindal H.K., Vishwanatha J.K.;
RT "Functional identity of a primer recognition protein as
RT phosphoglycerate 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [18]
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 [19]
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 MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
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.,
RA Buerckstuemmer T., 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 [22]
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.,
RA He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
RA Dai J., 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH
RP PHOSPHOGLYCERATE; L-ADP; D-ADP; L-CDP AND D-CDP, AND SUBSTRATE-BINDING
RP 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 [26]
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 [27]
RP VARIANTS PGK1D VAL-164 AND ASN-315.
RX PubMed=8043870;
RA Cohen-Solal M., Valentin C., Plassa F., Guillemin G., Danze F.,
RA Jaisson F., 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 [28]
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.,
RA Matthys E., 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 [29]
RP VARIANT PGK1D VAL-285.
RX PubMed=9744480;
RX DOI=10.1002/(SICI)1098-1004(1998)12:4<280::AID-HUMU10>3.3.CO;2-Z;
RA Valentin C., Birgens H., Craescu C.T., Broedum-Nielsen K.,
RA Cohen-Solal M.;
RT "A phosphoglycerate kinase mutant (PGK Herlev; D285V) in a Danish
RT patient with isolated chronic hemolytic anemia: mechanism of mutation
RT and structure-function relationships.";
RL Hum. Mutat. 12:280-287(1998).
RN [30]
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 [31]
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
RT generated by spontaneous mutation.";
RL Blood 79:2759-2762(1992).
RN [32]
RP VARIANT MUNCHEN ASN-268.
RX PubMed=7391028;
RA Fujii H., Krietsch W.K.G., Yoshida A.;
RT "A single amino acid substitution (Asp leads to Asn) in a
RT phosphoglycerate kinase variant (PGK Munchen) associated with enzyme
RT deficiency.";
RL J. Biol. Chem. 255:6421-6423(1980).
RN [33]
RP VARIANT MUNCHEN ASN-268, AND VARIANT ASN-352.
RX PubMed=7440217;
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 [34]
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
RT phosphoglycerate kinase variant (PGK Shizuoka) associated with chronic
RT hemolysis and myoglobinuria.";
RL Blood 79:1582-1585(1992).
RN [35]
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
RT enzymes: molecular abnormality of a phosphoglycerate kinase variant
RT associated with hemolytic anemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:2587-2590(1981).
RN [36]
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
RT with chronic nonspherocytic hemolytic anemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:5461-5465(1980).
CC -!- FUNCTION: In addition to its role as a glycolytic enzyme, it seems
CC that PGK-1 acts as a polymerase alpha cofactor protein (primer
CC recognition protein).
CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
CC D-glyceroyl phosphate.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P04406:GAPDH; NbExp=2; IntAct=EBI-709599, EBI-354056;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISEASE: Phosphoglycerate kinase 1 deficiency (PGK1D)
CC [MIM:300653]: A condition with a highly variable clinical
CC phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy
CC and neurologic involvement. Patients can express one or more of
CC these manifestations. Note=The disease is caused by mutations
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PGK1";
CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC polymorphism database;
CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename;=PGK1";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Phosphoglycerate kinase entry;
CC URL="http://en.wikipedia.org/wiki/Phosphoglycerate_kinase";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; 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 PIR; I59050; KIHUG.
DR RefSeq; NP_000282.1; NM_000291.3.
DR UniGene; Hs.78771; -.
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; 4AXX; X-ray; 1.74 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; 4AXX; -.
DR ProteinModelPortal; P00558; -.
DR SMR; P00558; 5-417.
DR IntAct; P00558; 29.
DR MINT; MINT-1131047; -.
DR STRING; 9606.ENSP00000362413; -.
DR BindingDB; P00558; -.
DR ChEMBL; CHEMBL2096677; -.
DR PhosphoSite; P00558; -.
DR DMDM; 52788229; -.
DR DOSAC-COBS-2DPAGE; P00558; -.
DR OGP; P00558; -.
DR REPRODUCTION-2DPAGE; IPI00169383; -.
DR REPRODUCTION-2DPAGE; P00558; -.
DR UCD-2DPAGE; P00558; -.
DR PaxDb; P00558; -.
DR PeptideAtlas; P00558; -.
DR PRIDE; P00558; -.
DR DNASU; 5230; -.
DR Ensembl; ENST00000373316; ENSP00000362413; ENSG00000102144.
DR Ensembl; ENST00000597340; ENSP00000472461; ENSG00000269666.
DR GeneID; 5230; -.
DR KEGG; hsa:5230; -.
DR UCSC; uc004ecz.4; human.
DR CTD; 5230; -.
DR GeneCards; GC0XP077246; -.
DR HGNC; HGNC:8896; PGK1.
DR HPA; CAB010065; -.
DR HPA; HPA045385; -.
DR MIM; 300653; phenotype.
DR MIM; 311800; gene.
DR neXtProt; NX_P00558; -.
DR Orphanet; 713; Glycogen storage disease due to phosphoglycerate kinase 1 deficiency.
DR PharmGKB; PA33234; -.
DR eggNOG; COG0126; -.
DR HOGENOM; HOG000227107; -.
DR HOVERGEN; HBG008177; -.
DR InParanoid; P00558; -.
DR KO; K00927; -.
DR OMA; NFANGTK; -.
DR PhylomeDB; P00558; -.
DR BioCyc; MetaCyc:HS02359-MONOMER; -.
DR BRENDA; 2.7.2.3; 2681.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P00558; -.
DR UniPathway; UPA00109; UER00185.
DR ChiTaRS; PGK1; human.
DR EvolutionaryTrace; P00558; -.
DR GeneWiki; PGK1; -.
DR GenomeRNAi; 5230; -.
DR NextBio; 20218; -.
DR PRO; PR:P00558; -.
DR ArrayExpress; P00558; -.
DR Bgee; P00558; -.
DR CleanEx; HS_PGK1; -.
DR Genevestigator; P00558; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0006096; P:glycolysis; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.1260; -; 1.
DR Gene3D; 3.40.50.1270; -; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015901; Phosphoglycerate_kinase_C.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disease mutation; Glycolysis;
KW Hereditary hemolytic anemia; Kinase; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Reference proteome; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 417 Phosphoglycerate kinase 1.
FT /FTId=PRO_0000145831.
FT NP_BIND 373 376 ATP.
FT REGION 24 26 Substrate binding.
FT REGION 63 66 Substrate binding.
FT BINDING 39 39 Substrate.
FT BINDING 123 123 Substrate.
FT BINDING 171 171 Substrate.
FT BINDING 220 220 ATP.
FT BINDING 313 313 ATP; via carbonyl oxygen.
FT BINDING 344 344 ATP.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 11 11 N6-acetyllysine.
FT MOD_RES 48 48 N6-acetyllysine.
FT MOD_RES 75 75 N6-acetyllysine.
FT MOD_RES 76 76 Phosphotyrosine (By similarity).
FT MOD_RES 86 86 N6-acetyllysine.
FT MOD_RES 97 97 N6-acetyllysine.
FT MOD_RES 131 131 N6-acetyllysine; alternate.
FT MOD_RES 131 131 N6-malonyllysine; alternate.
FT MOD_RES 146 146 N6-acetyllysine.
FT MOD_RES 196 196 Phosphotyrosine.
FT MOD_RES 199 199 N6-acetyllysine.
FT MOD_RES 203 203 Phosphoserine.
FT MOD_RES 267 267 N6-acetyllysine.
FT MOD_RES 291 291 N6-acetyllysine.
FT VARIANT 88 88 L -> P (in PGK1D; with congenital non-
FT spherocytic anemia; variant Matsue).
FT /FTId=VAR_006076.
FT VARIANT 158 158 G -> V (in PGK1D; with chronic hemolytic
FT anemia; variant Shizuoka).
FT /FTId=VAR_006077.
FT VARIANT 164 164 D -> V (in PGK1D; with chronic hemolytic
FT anemia and mental retardation; variant
FT Amiens).
FT /FTId=VAR_006078.
FT VARIANT 191 191 Missing (in PGK1D; with chronic hemolytic
FT anemia; variant Alabama).
FT /FTId=VAR_006079.
FT VARIANT 206 206 R -> P (in PGK1D; with chronic hemolytic
FT anemia; variant Uppsala).
FT /FTId=VAR_006080.
FT VARIANT 252 252 E -> A (in PGK1D; with chronic hemolytic
FT anemia; variant Antwerp).
FT /FTId=VAR_006081.
FT VARIANT 266 266 V -> M (in PGK1D; with chronic non-
FT spherocytic hemolytic anemia; variant
FT Tokyo).
FT /FTId=VAR_006082.
FT VARIANT 268 268 D -> N (in Munchen; 21% of activity).
FT /FTId=VAR_006083.
FT VARIANT 285 285 D -> V (in PGK1D; with chronic hemolytic
FT anemia; variant Herlev; 50% of activity).
FT /FTId=VAR_006084.
FT VARIANT 315 315 D -> N (in PGK1D; with rhabdomyolysis;
FT variant Creteil).
FT /FTId=VAR_006085.
FT VARIANT 316 316 C -> R (in PGK1D; with chronic hemolytic
FT anemia; variant Michigan).
FT /FTId=VAR_006086.
FT VARIANT 352 352 T -> N.
FT /FTId=VAR_006087.
FT CONFLICT 39 39 Missing (in Ref. 12; AA sequence).
FT CONFLICT 370 370 I -> T (in Ref. 6; CAG32997).
FT STRAND 4 6
FT HELIX 9 11
FT STRAND 18 22
FT STRAND 29 32
FT STRAND 33 35
FT HELIX 38 52
FT STRAND 56 61
FT HELIX 73 76
FT HELIX 79 89
FT STRAND 94 97
FT STRAND 99 101
FT HELIX 102 109
FT STRAND 115 118
FT HELIX 122 124
FT TURN 126 130
FT STRAND 131 133
FT STRAND 135 137
FT STRAND 139 141
FT HELIX 144 156
FT STRAND 159 163
FT HELIX 166 168
FT HELIX 174 177
FT STRAND 184 186
FT HELIX 188 202
FT STRAND 206 212
FT HELIX 217 220
FT HELIX 221 223
FT HELIX 224 227
FT TURN 228 230
FT STRAND 232 236
FT HELIX 238 240
FT HELIX 241 249
FT HELIX 260 263
FT HELIX 266 275
FT STRAND 279 281
FT STRAND 285 293
FT STRAND 298 302
FT TURN 303 305
FT STRAND 312 316
FT HELIX 318 330
FT STRAND 332 338
FT HELIX 346 348
FT HELIX 350 364
FT STRAND 368 373
FT HELIX 376 382
FT STRAND 388 394
FT HELIX 397 404
FT HELIX 409 412
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
//
MIM
300653
*RECORD*
*FIELD* NO
300653
*FIELD* TI
#300653 PHOSPHOGLYCERATE KINASE 1 DEFICIENCY
;;PGK1 DEFICIENCY
*FIELD* TX
A number sign (#) is used with this entry because phosphoglycerate
read morekinase-1 deficiency is caused by mutation in the PGK1 gene (311800).
DESCRIPTION
Phosphoglycerate kinase-1 deficiency is an X-linked recessive condition
with a highly variable clinical phenotype that includes hemolytic
anemia, myopathy, and neurologic involvement. Patients can express 1, 2,
or all 3 of these manifestations (Shirakawa et al., 2006).
CLINICAL FEATURES
Kraus et al. (1968) attributed lifelong anemia in a 63-year-old
Caucasian woman to deficiency of red cell phosphoglycerate kinase.
Although no relatives were available for study, the proband's mother and
2 of her sibs had a history of anemia. Valentine et al. (1969) found
hemolytic anemia with deficient red and white cell phosphoglycerate
kinase in a large Chinese kindred. Mild hemolysis was present in
presumed heterozygotes.
Guis et al. (1987) reported a boy with hemolytic anemia but no
neuromuscular manifestations who was found to have a PGK variant termed
'San Francisco.' The anemia was severe and partially transfusion
dependent. Guis et al. (1987) suggested that unusual stability of the
mutant enzyme and a continuing ability to synthesize at least limited
amounts of enzyme had protected nonerythroid tissues. In contrast,
mature red cells, lacking the ability to synthesize new proteins, had a
severely compromised life span.
Rosa et al. (1982) reported a man with episodes of rhabdomyolysis and
acute renal failure who did not have hemolysis. He had a severe
deficiency of PGK in muscle, white blood cells, red blood cells, and
platelets. His mother and 2 daughters had a partial enzyme defect in red
blood cells, suggesting X-linked recessive transmission. DiMauro et al.
(1983) reported a 14-year-old boy with recurrent myoglobinuria and renal
failure after intense exercise. Muscle PGK activity was 5% of normal
values in the patient and was decreased in his mother but normal in his
father.
Tonin et al. (1993) reported a 37-year-old man with exercise
intolerance, myalgia, recurrent myoglobinuria, and retinitis pigmentosa
who had decreased PGK activity.
Sugie et al. (1994) demonstrated PGK deficiency in 3 unrelated men who
presented with myoglobinuria. All 3 were mentally retarded, and 2 had
epilepsy. The patient who did not have epilepsy was the only one of the
3 who showed any hemolytic anemia. Sugie et al. (1994) noted that
organ-specific isozymes or posttranslational modification are not the
explanation for the variable involvement of hematopoietic, muscle and
nervous tissue since enzymes derived from different tissues in the same
individual do not differ in physical and biochemical characteristics.
The variable clinical features of the disease were thought to be the
consequence of the unique biochemical properties of the individual PGK
mutants.
Noel et al. (2005) reported 2 unrelated boys of Spanish origin with PGK1
deficiency. At the age of 2 years, the first child was hospitalized for
a febrile episode associated with severe anemia and jaundice, for which
exchange transfusion was given. Subsequently, several similar hemolytic
crises occurred, mainly due to viral infections, and exchange
transfusion was required on 2 occasions. Due to the persistence of the
microcytosis, a molecular study for thalassemia was performed, leading
to the secondary diagnosis of heterozygosity for the alpha(-3.7)
mutation. At 7 years of age the hemolytic crises were associated with a
progressive neurologic impairment leading to mental deterioration. No
muscular dystrophy could be demonstrated. The second child, who was from
Murcia, had required blood transfusions from birth every 3 to 4 weeks
for hemolytic anemia. The diagnosis of PGK deficiency was made when he
was 6 years old. An older sister and younger brother were healthy and
the mother had a history of 2 previous abortions. Accordingly, the
patient's mother had been strictly monitored during the antenatal period
because of the risk of abortion at the tenth week of gestation, and the
patient was delivered by cesarean section. There was severe neonatal
anemia, hyperbilirubinemia, hepatosplenomegaly, and purpura requiring
intensive care. At 2 years of age, the patient was hospitalized due to a
hemolytic crisis in association with severe encephalopathy without
environmental cause, spastic tetraparesis, and psychomotor delay. The
anemia was associated with severe and progressive encephalopathy with
cortical and subcortical atrophy verified by cranial CT, and epileptic
crises. He died of severe encephalopathy at 7 years of age.
Flanagan et al. (2006) reported 2 boys of a white American family with
PGK1 deficiency who presented with hemolytic anemia, seizures, and
developmental delay. One of the boys also had hemiplegic migraines,
retinal dystrophy, and muscle fatigue after exertion. Erythrocyte PGK
enzyme activity was less than 5% of normal. Genetic analysis identified
a mutation in the PGK1 gene (311800.0013).
Shirakawa et al. (2006) reported a 33-year-old Japanese man with PGK1
deficiency manifesting as mental retardation and exertional myopathy,
but without hemolytic anemia. He also had short stature, high-arched
palate, and brachydactyly. Laboratory studies showed no evidence of
hemolytic anemia, but serum creatine kinase and myoglobin were
increased. PGK1 activity was 9.0% and 13.6% of control values in muscle
and red blood cells, respectively. PGK1 activity in red blood cells of
his mother was 60.7%.
Spiegel et al. (2009) reported an 18-year-old man of Arab Bedouin
descent with PGK1 deficiency confirmed by genetic analysis (T378P;
311800.0015). He had a purely myopathic phenotype, with onset of muscle
cramps and exercise-induced pigmenturia at age 7 years. He had no
evidence of hemolytic anemia or neurologic involvement; serum creatine
kinase was increased. Biochemical studies showed decreased PGK1 activity
in muscle (0.9% of control values) and erythrocytes (1.6%). The
patient's unaffected mother and 2 sisters were heterozygous for the
mutation.
MOLECULAR GENETICS
In a patient with chronic hemolytic anemia associated with deficiency of
PGK activity, Fujii and Yoshida (1980) used peptide mapping analysis to
identify an R206P substitution (311800.0002) in the PGK1 protein.
In a 27-year-old Japanese male with PGK1 deficiency, Fujii et al. (1992)
identified a mutation in the PGK1 gene (311800.0006). The patient had
chronic hemolytic anemia and myoglobinuria, manifested by nausea,
anorexia, and muscle weakness after exercise, beginning at the age of
10. There was no family history of anemia or neuromuscular disease.
In affected members of the Chinese family reported by Valentine et al.
(1969), Turner et al. (1995) identified a mutation in the PGK1 gene
(311800.0013).
In a patient with PGK1 deficiency manifest as myopathy (Sugie et al.,
1989), Sugie et al. (1998) identified a mutation in the PGK1 gene
(311800.0009).
In 2 unrelated patients of Spanish origin with PGK1 deficiency manifest
as severe lifelong chronic hemolytic anemia and progressive neurologic
impairment, Noel et al. (2005) identified 2 different mutations in the
PGK1 gene (311800.0011 and 311800.00012, respectively).
In a Japanese man with PGK1 deficiency, Shirakawa et al. (2006)
identified a mutation in the PGK1 gene (311800.0014). He had mental
retardation and recurrent myoglobinuria, but no hemolytic anemia.
*FIELD* RF
1. DiMauro, S.; Dalakas, M.; Miranda, A. S.: Phosphoglycerate kinase
deficiency: another cause of recurrent myoglobinuria. Ann. Neurol. 13:
11-19, 1983.
2. Flanagan, J. M.; Rhodes, M.; Wilson, M.; Beutler, E.: The identification
of a recurrent phosphoglycerate kinase mutation associated with chronic
haemolytic anaemia and neurological dysfunction in a family from USA. Brit.
J. Haemat. 134: 233-237, 2006.
3. Fujii, H.; Kanno, H.; Hirono, A.; Shiomura, T.; Miwa, S.: A single
amino acid substitution (157gly-to-val) in a phosphoglycerate kinase
variant (PGK Shizuoka) associated with chronic hemolysis and myoglobinuria. Blood 79:
1582-1585, 1992.
4. Fujii, H.; Yoshida, A.: Molecular abnormality of phosphoglycerate
kinase-Uppsala associated with chronic nonspherocytic hemolytic anemia. Proc.
Nat. Acad. Sci. 77: 5461-5465, 1980.
5. Guis, M. S.; Karadsheh, N.; Mentzer, W. C.: Phosphoglycerate kinase
San Francisco: a new variant associated with hemolytic anemia but
not with neuromuscular manifestations. Am. J. Hemat. 25: 175-182,
1987.
6. Kraus, A. P.; Langston, M. F., Jr.; Lynch, B. L.: Red cell phosphoglycerate
kinase deficiency: a new cause of non-spherocytic hemolytic anemia. Biochem.
Biophys. Res. Commun. 30: 173-177, 1968.
7. Noel, N.; Flanagan, J.; Kalko, S. G.; Bajo, M. J. R.; Manu, M.
M.; Fuster, J. L. G.; Beutler, E.; Corrons, J.-L. V.: Two new phosphoglycerate
kinase mutations associated with chronic haemolytic anaemia and neurological
dysfunction in two patients from Spain. Brit. J. Haemat. 132: 523-529,
2005.
8. Rosa, R.; George, C.; Fardeau, M.; Calvin, M. C.; Rapin, M.; Rosa,
J.: A new case of phosphoglycerate kinase deficiency: PGK Creteil
associated with rhabdomyolysis and lacking hemolytic anemia. Blood 60:
84-91, 1982.
9. Shirakawa, K.; Takahashi, Y.; Miyajima, H.: Intronic mutation
in the PGK1 gene may cause recurrent myoglobinuria by aberrant splicing. Neurology 66:
925-927, 2006.
10. Spiegel, R.; Gomez, E. A.; Akman, H. O.; Krishna, S.; Horovitz,
Y.; DiMauro, S.: Myopathic form of phosphoglycerate kinase (PGK)
deficiency: a new case and pathogenic considerations. Neuromusc.
Disord. 19: 207-211, 2009.
11. Sugie, H.; Sugie, Y.; Ito, M.; Fukuda, T.: A novel missense mutation
(837T-C) in the phosphoglycerate kinase gene of a patient with a myopathic
form of phosphoglycerate kinase deficiency. J. Child Neurol. 13:
95-97, 1998.
12. Sugie, H.; Sugie, Y.; Nishida, M.; Ito, M.; Tsurui, S.; Suzuki,
M.; Miyamoto, R.; Igarashi, Y.: Recurrent myoglobinuria in a child
with mental retardation: phosphoglycerate kinase deficiency. J.
Child Neurol. 4: 95-99, 1989.
13. Sugie, H.; Sugie, Y.; Tsurui, S.; Ito, M.: Phosphoglycerate kinase
deficiency. (Letter) Neurology 44: 1364-1365, 1994.
14. Tonin, P.; Shanske, S.; Miranda, A. F.; Brownell, A. K.; Wyse,
J. P.; Tsujino, S.; Di Mauro, S.: Phosphoglycerate kinase deficiency:
biochemical and molecular genetic studies in a new myopathic variant. Neurology 43:
387-391, 1993.
15. Turner, G.; Fletcher, J.; Elber, J.; Yanagawa, Y.; Dave, V.; Yoshida,
A.: Molecular defect of a phosphoglycerate kinase variant associated
with haemolytic anaemia and neurological disorders in a large kindred. Brit.
J. Haemat. 91: 60-65, 1995.
16. Valentine, W. N.; Hsieh, H.-S.; Paglia, D. E.; Anderson, H. M.;
Baughan, M. A.; Jaffe, E. R.; Garson, O. M.: Hereditary hemolytic
anemia associated with phosphoglycerate kinase deficiency in erythrocytes
and leukocytes: a probable X-chromosome-linked syndrome. New Eng.
J. Med. 280: 528-534, 1969.
*FIELD* CS
INHERITANCE:
X-linked recessive
HEAD AND NECK:
[Eyes];
Retinal dystrophy (rare);
Loss of vision (rare)
GENITOURINARY:
[Kidneys];
Renal failure may occur with myoglobinuria
MUSCLE, SOFT TISSUE:
Myopathy in approximately 45% of patients;
Muscle cramps with exercise;
Rhabdomyolysis;
Exercise intolerance
NEUROLOGIC:
[Central nervous system];
Central nervous system involvement in approximately 50% of patients;
Developmental delay;
Mental retardation;
Speech delay;
Seizures;
Hemiplegic migraines;
Ataxia;
[Behavioral/psychiatric manifestations];
Emotional instability
HEMATOLOGY:
Hemolytic anemia in approximately 60% of patients
LABORATORY ABNORMALITIES:
Myoglobinuria after exertion;
Decreased hemoglobin;
Increased serum bilirubin;
Increased reticulocyte count;
Decreased activity of phosphoglycerate kinase 1
MISCELLANEOUS:
Highly variable phenotype;
Variable age at onset (range infancy to adult);
Heterozygous females may exhibit variable degrees of enzyme deficiency
MOLECULAR BASIS:
Caused by mutation in the phosphoglycerate kinase 1 gene (PGK1, 311800.0002).
*FIELD* CD
Cassandra L. Kniffin: 6/26/2007
*FIELD* ED
joanna: 03/19/2008
ckniffin: 6/27/2007
*FIELD* CN
Cassandra L. Kniffin - updated: 11/4/2009
*FIELD* CD
Cassandra L. Kniffin: 6/26/2007
*FIELD* ED
wwang: 11/18/2009
ckniffin: 11/4/2009
carol: 7/2/2007
ckniffin: 6/27/2007
*RECORD*
*FIELD* NO
300653
*FIELD* TI
#300653 PHOSPHOGLYCERATE KINASE 1 DEFICIENCY
;;PGK1 DEFICIENCY
*FIELD* TX
A number sign (#) is used with this entry because phosphoglycerate
read morekinase-1 deficiency is caused by mutation in the PGK1 gene (311800).
DESCRIPTION
Phosphoglycerate kinase-1 deficiency is an X-linked recessive condition
with a highly variable clinical phenotype that includes hemolytic
anemia, myopathy, and neurologic involvement. Patients can express 1, 2,
or all 3 of these manifestations (Shirakawa et al., 2006).
CLINICAL FEATURES
Kraus et al. (1968) attributed lifelong anemia in a 63-year-old
Caucasian woman to deficiency of red cell phosphoglycerate kinase.
Although no relatives were available for study, the proband's mother and
2 of her sibs had a history of anemia. Valentine et al. (1969) found
hemolytic anemia with deficient red and white cell phosphoglycerate
kinase in a large Chinese kindred. Mild hemolysis was present in
presumed heterozygotes.
Guis et al. (1987) reported a boy with hemolytic anemia but no
neuromuscular manifestations who was found to have a PGK variant termed
'San Francisco.' The anemia was severe and partially transfusion
dependent. Guis et al. (1987) suggested that unusual stability of the
mutant enzyme and a continuing ability to synthesize at least limited
amounts of enzyme had protected nonerythroid tissues. In contrast,
mature red cells, lacking the ability to synthesize new proteins, had a
severely compromised life span.
Rosa et al. (1982) reported a man with episodes of rhabdomyolysis and
acute renal failure who did not have hemolysis. He had a severe
deficiency of PGK in muscle, white blood cells, red blood cells, and
platelets. His mother and 2 daughters had a partial enzyme defect in red
blood cells, suggesting X-linked recessive transmission. DiMauro et al.
(1983) reported a 14-year-old boy with recurrent myoglobinuria and renal
failure after intense exercise. Muscle PGK activity was 5% of normal
values in the patient and was decreased in his mother but normal in his
father.
Tonin et al. (1993) reported a 37-year-old man with exercise
intolerance, myalgia, recurrent myoglobinuria, and retinitis pigmentosa
who had decreased PGK activity.
Sugie et al. (1994) demonstrated PGK deficiency in 3 unrelated men who
presented with myoglobinuria. All 3 were mentally retarded, and 2 had
epilepsy. The patient who did not have epilepsy was the only one of the
3 who showed any hemolytic anemia. Sugie et al. (1994) noted that
organ-specific isozymes or posttranslational modification are not the
explanation for the variable involvement of hematopoietic, muscle and
nervous tissue since enzymes derived from different tissues in the same
individual do not differ in physical and biochemical characteristics.
The variable clinical features of the disease were thought to be the
consequence of the unique biochemical properties of the individual PGK
mutants.
Noel et al. (2005) reported 2 unrelated boys of Spanish origin with PGK1
deficiency. At the age of 2 years, the first child was hospitalized for
a febrile episode associated with severe anemia and jaundice, for which
exchange transfusion was given. Subsequently, several similar hemolytic
crises occurred, mainly due to viral infections, and exchange
transfusion was required on 2 occasions. Due to the persistence of the
microcytosis, a molecular study for thalassemia was performed, leading
to the secondary diagnosis of heterozygosity for the alpha(-3.7)
mutation. At 7 years of age the hemolytic crises were associated with a
progressive neurologic impairment leading to mental deterioration. No
muscular dystrophy could be demonstrated. The second child, who was from
Murcia, had required blood transfusions from birth every 3 to 4 weeks
for hemolytic anemia. The diagnosis of PGK deficiency was made when he
was 6 years old. An older sister and younger brother were healthy and
the mother had a history of 2 previous abortions. Accordingly, the
patient's mother had been strictly monitored during the antenatal period
because of the risk of abortion at the tenth week of gestation, and the
patient was delivered by cesarean section. There was severe neonatal
anemia, hyperbilirubinemia, hepatosplenomegaly, and purpura requiring
intensive care. At 2 years of age, the patient was hospitalized due to a
hemolytic crisis in association with severe encephalopathy without
environmental cause, spastic tetraparesis, and psychomotor delay. The
anemia was associated with severe and progressive encephalopathy with
cortical and subcortical atrophy verified by cranial CT, and epileptic
crises. He died of severe encephalopathy at 7 years of age.
Flanagan et al. (2006) reported 2 boys of a white American family with
PGK1 deficiency who presented with hemolytic anemia, seizures, and
developmental delay. One of the boys also had hemiplegic migraines,
retinal dystrophy, and muscle fatigue after exertion. Erythrocyte PGK
enzyme activity was less than 5% of normal. Genetic analysis identified
a mutation in the PGK1 gene (311800.0013).
Shirakawa et al. (2006) reported a 33-year-old Japanese man with PGK1
deficiency manifesting as mental retardation and exertional myopathy,
but without hemolytic anemia. He also had short stature, high-arched
palate, and brachydactyly. Laboratory studies showed no evidence of
hemolytic anemia, but serum creatine kinase and myoglobin were
increased. PGK1 activity was 9.0% and 13.6% of control values in muscle
and red blood cells, respectively. PGK1 activity in red blood cells of
his mother was 60.7%.
Spiegel et al. (2009) reported an 18-year-old man of Arab Bedouin
descent with PGK1 deficiency confirmed by genetic analysis (T378P;
311800.0015). He had a purely myopathic phenotype, with onset of muscle
cramps and exercise-induced pigmenturia at age 7 years. He had no
evidence of hemolytic anemia or neurologic involvement; serum creatine
kinase was increased. Biochemical studies showed decreased PGK1 activity
in muscle (0.9% of control values) and erythrocytes (1.6%). The
patient's unaffected mother and 2 sisters were heterozygous for the
mutation.
MOLECULAR GENETICS
In a patient with chronic hemolytic anemia associated with deficiency of
PGK activity, Fujii and Yoshida (1980) used peptide mapping analysis to
identify an R206P substitution (311800.0002) in the PGK1 protein.
In a 27-year-old Japanese male with PGK1 deficiency, Fujii et al. (1992)
identified a mutation in the PGK1 gene (311800.0006). The patient had
chronic hemolytic anemia and myoglobinuria, manifested by nausea,
anorexia, and muscle weakness after exercise, beginning at the age of
10. There was no family history of anemia or neuromuscular disease.
In affected members of the Chinese family reported by Valentine et al.
(1969), Turner et al. (1995) identified a mutation in the PGK1 gene
(311800.0013).
In a patient with PGK1 deficiency manifest as myopathy (Sugie et al.,
1989), Sugie et al. (1998) identified a mutation in the PGK1 gene
(311800.0009).
In 2 unrelated patients of Spanish origin with PGK1 deficiency manifest
as severe lifelong chronic hemolytic anemia and progressive neurologic
impairment, Noel et al. (2005) identified 2 different mutations in the
PGK1 gene (311800.0011 and 311800.00012, respectively).
In a Japanese man with PGK1 deficiency, Shirakawa et al. (2006)
identified a mutation in the PGK1 gene (311800.0014). He had mental
retardation and recurrent myoglobinuria, but no hemolytic anemia.
*FIELD* RF
1. DiMauro, S.; Dalakas, M.; Miranda, A. S.: Phosphoglycerate kinase
deficiency: another cause of recurrent myoglobinuria. Ann. Neurol. 13:
11-19, 1983.
2. Flanagan, J. M.; Rhodes, M.; Wilson, M.; Beutler, E.: The identification
of a recurrent phosphoglycerate kinase mutation associated with chronic
haemolytic anaemia and neurological dysfunction in a family from USA. Brit.
J. Haemat. 134: 233-237, 2006.
3. Fujii, H.; Kanno, H.; Hirono, A.; Shiomura, T.; Miwa, S.: A single
amino acid substitution (157gly-to-val) in a phosphoglycerate kinase
variant (PGK Shizuoka) associated with chronic hemolysis and myoglobinuria. Blood 79:
1582-1585, 1992.
4. Fujii, H.; Yoshida, A.: Molecular abnormality of phosphoglycerate
kinase-Uppsala associated with chronic nonspherocytic hemolytic anemia. Proc.
Nat. Acad. Sci. 77: 5461-5465, 1980.
5. Guis, M. S.; Karadsheh, N.; Mentzer, W. C.: Phosphoglycerate kinase
San Francisco: a new variant associated with hemolytic anemia but
not with neuromuscular manifestations. Am. J. Hemat. 25: 175-182,
1987.
6. Kraus, A. P.; Langston, M. F., Jr.; Lynch, B. L.: Red cell phosphoglycerate
kinase deficiency: a new cause of non-spherocytic hemolytic anemia. Biochem.
Biophys. Res. Commun. 30: 173-177, 1968.
7. Noel, N.; Flanagan, J.; Kalko, S. G.; Bajo, M. J. R.; Manu, M.
M.; Fuster, J. L. G.; Beutler, E.; Corrons, J.-L. V.: Two new phosphoglycerate
kinase mutations associated with chronic haemolytic anaemia and neurological
dysfunction in two patients from Spain. Brit. J. Haemat. 132: 523-529,
2005.
8. Rosa, R.; George, C.; Fardeau, M.; Calvin, M. C.; Rapin, M.; Rosa,
J.: A new case of phosphoglycerate kinase deficiency: PGK Creteil
associated with rhabdomyolysis and lacking hemolytic anemia. Blood 60:
84-91, 1982.
9. Shirakawa, K.; Takahashi, Y.; Miyajima, H.: Intronic mutation
in the PGK1 gene may cause recurrent myoglobinuria by aberrant splicing. Neurology 66:
925-927, 2006.
10. Spiegel, R.; Gomez, E. A.; Akman, H. O.; Krishna, S.; Horovitz,
Y.; DiMauro, S.: Myopathic form of phosphoglycerate kinase (PGK)
deficiency: a new case and pathogenic considerations. Neuromusc.
Disord. 19: 207-211, 2009.
11. Sugie, H.; Sugie, Y.; Ito, M.; Fukuda, T.: A novel missense mutation
(837T-C) in the phosphoglycerate kinase gene of a patient with a myopathic
form of phosphoglycerate kinase deficiency. J. Child Neurol. 13:
95-97, 1998.
12. Sugie, H.; Sugie, Y.; Nishida, M.; Ito, M.; Tsurui, S.; Suzuki,
M.; Miyamoto, R.; Igarashi, Y.: Recurrent myoglobinuria in a child
with mental retardation: phosphoglycerate kinase deficiency. J.
Child Neurol. 4: 95-99, 1989.
13. Sugie, H.; Sugie, Y.; Tsurui, S.; Ito, M.: Phosphoglycerate kinase
deficiency. (Letter) Neurology 44: 1364-1365, 1994.
14. Tonin, P.; Shanske, S.; Miranda, A. F.; Brownell, A. K.; Wyse,
J. P.; Tsujino, S.; Di Mauro, S.: Phosphoglycerate kinase deficiency:
biochemical and molecular genetic studies in a new myopathic variant. Neurology 43:
387-391, 1993.
15. Turner, G.; Fletcher, J.; Elber, J.; Yanagawa, Y.; Dave, V.; Yoshida,
A.: Molecular defect of a phosphoglycerate kinase variant associated
with haemolytic anaemia and neurological disorders in a large kindred. Brit.
J. Haemat. 91: 60-65, 1995.
16. Valentine, W. N.; Hsieh, H.-S.; Paglia, D. E.; Anderson, H. M.;
Baughan, M. A.; Jaffe, E. R.; Garson, O. M.: Hereditary hemolytic
anemia associated with phosphoglycerate kinase deficiency in erythrocytes
and leukocytes: a probable X-chromosome-linked syndrome. New Eng.
J. Med. 280: 528-534, 1969.
*FIELD* CS
INHERITANCE:
X-linked recessive
HEAD AND NECK:
[Eyes];
Retinal dystrophy (rare);
Loss of vision (rare)
GENITOURINARY:
[Kidneys];
Renal failure may occur with myoglobinuria
MUSCLE, SOFT TISSUE:
Myopathy in approximately 45% of patients;
Muscle cramps with exercise;
Rhabdomyolysis;
Exercise intolerance
NEUROLOGIC:
[Central nervous system];
Central nervous system involvement in approximately 50% of patients;
Developmental delay;
Mental retardation;
Speech delay;
Seizures;
Hemiplegic migraines;
Ataxia;
[Behavioral/psychiatric manifestations];
Emotional instability
HEMATOLOGY:
Hemolytic anemia in approximately 60% of patients
LABORATORY ABNORMALITIES:
Myoglobinuria after exertion;
Decreased hemoglobin;
Increased serum bilirubin;
Increased reticulocyte count;
Decreased activity of phosphoglycerate kinase 1
MISCELLANEOUS:
Highly variable phenotype;
Variable age at onset (range infancy to adult);
Heterozygous females may exhibit variable degrees of enzyme deficiency
MOLECULAR BASIS:
Caused by mutation in the phosphoglycerate kinase 1 gene (PGK1, 311800.0002).
*FIELD* CD
Cassandra L. Kniffin: 6/26/2007
*FIELD* ED
joanna: 03/19/2008
ckniffin: 6/27/2007
*FIELD* CN
Cassandra L. Kniffin - updated: 11/4/2009
*FIELD* CD
Cassandra L. Kniffin: 6/26/2007
*FIELD* ED
wwang: 11/18/2009
ckniffin: 11/4/2009
carol: 7/2/2007
ckniffin: 6/27/2007
MIM
311800
*RECORD*
*FIELD* NO
311800
*FIELD* TI
*311800 PHOSPHOGLYCERATE KINASE 1; PGK1
;;3-@PHOSPHOGLYCEROKINASE;;
PGKA
PHOSPHOGLYCERATE KINASE 1 PSEUDOGENE 1, INCLUDED; PGK1P1, INCLUDED;;
read morePHOSPHOGLYCERATE KINASE 1 PSEUDOGENE 2, INCLUDED; PGK1P2, INCLUDED
*FIELD* TX
DESCRIPTION
The PGK1 gene encodes phosphoglycerate kinase-1, also known as
ATP:3-phosphoglycerate 1-phosphotransferase (EC 2.7.2.3), which
catalyzes the reversible conversion of 1,3-diphosphoglycerate to
3-phosphoglycerate during glycolysis, generating one molecule of ATP.
PGK1 is distinguished from testicular PGK2 (172270), which maps to
chromosome 6p21.
CLONING
Michelson et al. (1983) isolated a full-length cDNA clone of PGK from a
human fetal liver cDNA library using synthetic oligonucleotide mixtures
as hybridization probes. The deduced protein contains 417 amino acid
residues. Southern blot analysis of human genomic DNAs showed a complex
pattern of hybridizing fragments, 2 of which were non-X in origin. The
results were interpreted as reflecting the existence of a small family
of dispersed PGK or PGK-like genes.
Using a mixture of synthetic oligodeoxyribonucleotides, Singer-Sam et
al. (1983) isolated a cDNA encoding amino acids 291-296 of PGK.
GENE STRUCTURE
The human PGK1 gene contains 11 exons and spans approximately 23
kilobases (Michelson et al., 1985).
GENE FUNCTION
Disulfide bonds in secreted proteins are considered to be inert because
of the oxidizing nature of the extracellular milieu. An exception to
this rule is a reductase secreted by tumor cells that reduces disulfide
bonds in the serine proteinase plasmin. Reduction of plasmin initiates
proteolytic cleavage in the kringle 5 domain and release of the tumor
blood vessel inhibitor angiostatin. New blood vessel formation or
angiogenesis is critical for tumor expansion and metastasis. Lay et al.
(2000) showed that the plasmin reductase isolated from conditioned
medium of fibrosarcoma cells is the glycolytic enzyme phosphoglycerate
kinase. Recombinant phosphoglycerate kinase had the same specific
activity as the fibrosarcoma-derived protein. Plasma of mice bearing
fibrosarcoma tumors contained several-fold more phosphoglycerate kinase,
as compared with mice without tumors. Administration of phosphoglycerate
kinase to tumor-bearing mice caused an increase in plasma levels of
angiostatin, and a decrease in tumor vascularity and rate of tumor
growth. Lay et al. (2000) concluded that phosphoglycerate kinase not
only functions in glycolysis but is secreted by tumor cells and
participates in the angiogenic process as a disulfide reductase.
MAPPING
By somatic cell hybridization, Grzeschik et al. (1972) concluded that
the PGK locus was on the long arm of the X chromosome. From the study of
chromosomal aberrations in cell hybridization systems, Ricciuti and
Ruddle (1973) concluded that the order on the X chromosome was
centromere--PGK--HPRT (308000)--G6PD (305900). The conclusion was based
on their own work with the KOP 14-X translocation, and on Park Gerald's
with a 19-X translocation and Bootsma's with a 3-X translocation. All 3
had breaks involving the long arm of the X chromosome, each at a
different site. From study of radiation-induced segregants in which
irradiated human cells are rescued by fusion with hamster cells, Goss
and Harris (1977) showed that the order of the 4 loci is PGK: alpha-GAL
(300644): HPRT: G6PD and that the 3 intervals between these 4 loci are,
in relative terms, 0.33, 0.30, and 0.23.
Willard et al. (1985) used a cDNA for human PGK to map the functional
PGK1 gene to Xq13. Evidence reported by Verga et al. (1991) suggested
that PGK1, which is distal to the Menkes disease gene (309400), may be
located in Xq13.3.
PGK is X-linked in the kangaroo (Cooper et al., 1971). Alpha-GALA, HPRT,
PGK and G6PD are X-linked in the rabbit, according to mouse-rabbit
hybrid cell studies (Cianfriglia et al., 1979; Echard and Gillois,
1979). By comparable methods, Hors-Cayla et al. (1979) found them to be
X-linked also in cattle. According to cell hybridization studies, HPRT,
G6PD and PGK are X-linked in the pig (Gellin et al., 1979) and in sheep
(Saidi et al., 1979).
- Pseudogenes
One pseudogene of PGK1 (PGK1P1) is on Xq at Xq11-Xq13, proximal to the
expressed PGK1 gene at Xq13 (Michelson et al., 1985; Willard et al.,
1985). The pseudogene was mapped by somatic hybrid cell and in situ
hybridization methods using a cloned DNA probe in each case.
Willard et al. (1985) identified a 10-kb PGK-related DNA sequence on
human chromosome 19, which the authors suggested could represent a
pseudogene, the putative testes-specific PGK gene, or some other related
gene. Gartler et al. (1986) mapped a 1-kb PGK sequence to chromosome 19,
which represents the second pseudogene PGK1P2.
MOLECULAR GENETICS
Chen et al. (1971) described an electrophoretic variant of PGK with
enzyme activity in the normal range. Using a PGK cDNA probe, Hutz et al.
(1984) identified a common DNA polymorphism with the restriction enzyme
PstI. About 48% of females in all ethnic groups were found to be
heterozygous. Data on gene frequencies of allelic variants were
tabulated by Roychoudhury and Nei (1988).
- Phosphoglycerate Kinase-1 Deficiency
In a patient with chronic hemolytic anemia associated with deficiency of
PGK1 activity (300653), Fujii and Yoshida (1980) used peptide mapping
analysis to identify an arg206-to-pro (R206P; 311800.0002) substitution
in the PGK1 protein. The PGK1 variant was referred to as 'Uppsala.'
Sugie et al. (1998) described an 837T-C mutation (311800.0009) in the
PGK gene of a patient with PGK Hamamatsu and the myopathic form of PGK1
deficiency.
In 2 unrelated boys of Spanish origin with severe lifelong chronic
hemolytic anemia and progressive neurologic impairment, Noel et al.
(2005) identified 2 different mutations in the PGK1 gene (311800.0011
and 311800.0012, respectively).
Spiegel et al. (2009) reported an 18-year-old man of Arab Bedouin
descent with PGK1 deficiency confirmed by genetic analysis (T378P;
311800.0015). He had a purely myopathic phenotype, with onset of muscle
cramps and exercise-induced pigmenturia at age 7 years. He had no
evidence of hemolytic anemia or neurologic involvement; serum creatine
kinase was increased. Biochemical studies showed decreased PGK1 activity
in muscle (0.9% of control values) and erythrocytes (1.6%). The
patient's unaffected mother and 2 sisters were heterozygous for the
mutation.
*FIELD* AV
.0001
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MUNCHEN
PGK1, ASP268ASN
By peptide mapping analysis, Fujii et al. (1980) found an asp268-to-asn
(D268N) substitution in the PGK1 enzyme that was associated with mild
enzymatic deficiency (21% of normal activity) and was heat-unstable.
There was no hemolytic anemia or accumulation of intermediate
metabolites. Krietsch et al. (1977, 1980) described a large German
kindred with PGK Munchen. Although the variant showed decreased
activity, none of the carriers had overt clinical symptoms.
.0002
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, UPPSALA
PGK1, ARG206PRO
In a patient with chronic hemolytic anemia associated with deficiency of
PGK activity (300653), Fujii and Yoshida (1980) used peptide mapping
analysis to identify an arg206-to-pro (R206P) substitution in the PGK1
protein.
.0003
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, TOKYO
PGK1, VAL266MET
In a patient with chronic nonspherocytic hemolytic anemia and neurologic
disturbances due to PGK1 deficiency (300653), Fujii et al. (1981) used
peptide mapping analysis to identify a val266-to-met (V266M)
substitution in the PGK1 enzyme. The variant enzyme had 16% activity
compared to controls.
.0004
PHOSPHOGLYCERATE KINASE 1, PGK II
PGK1, THR352ASN
Chen et al. (1971) found an electrophoretic polymorphism of PGK in a New
Guinea population, where the frequency of a variant enzyme, termed 'PGK
II,' showed a gene frequency of about 0.014. In starch gel
electrophoresis, the variant enzyme moved toward the anode faster than
the normal enzyme. Yoshida et al. (1972) found that the PGK II variant
had a substitution of threonine to asparagine. The same substitution was
found in a Samoan male. Fujii et al. (1981) stated that the thr-to-asn
change was at position 352. The variant was not associated with enzyme
deficiency.
.0005
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MATSUE
PGK1, LEU88PRO
PGK Matsue is an electrophoretic variant associated with severe enzyme
deficiency, congenital nonspherocytic anemia, and mental disorders
(300653) (Miwa et al., 1972). In a cell line from a patient who died at
age 9 from complications of pneumonia, Maeda and Yoshida (1991), who
found a T/A-to-C/G transition in exon 3 of the PGK gene, resulting in a
leu88-to-pro (L88P) substitution. The nucleotide change created an
additional NciI cleavage site. Because the substitution was expected to
induce serious perturbation and instability in the protein structure,
Maeda and Yoshida (1991) suspected that the severe enzyme deficiency was
caused mainly by more rapid in vivo denaturation and degradation of the
variant enzyme.
Tani et al. (1985) found that PGK Matsue enzyme activity was about 5% of
control values. PGK Matsue mRNA was present in normal amounts in
fibroblasts, suggesting the enzyme deficiency was due to a 7- to 10-fold
increase in degradation of the mutant enzyme.
.0006
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, SHIZUOKA
PGK1, GLY157VAL
In a 27-year-old Japanese male with PGK1 deficiency (300653), Fujii et
al. (1992) identified a 473G-T transversion in the PGK1 gene, resulting
in a gly157-to-val (G157V) substitution The mutation created a new BstXI
cleavage site in exon 5. The patient had chronic hemolytic anemia and
myoglobinuria, manifested by nausea, anorexia, and muscle weakness after
exercise, beginning at the age of 10. There was no family history of
anemia or neuromuscular disease.
.0007
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MICHIGAN
PGK1, CYS315ARG
In a 14-year-old boy with mental retardation, a behavior disorder, and
episodic hemolytic anemia due to PGK1 deficiency (300653), Maeda et al.
(1992) identified a T-to-C transition in exon 9 of the PGK1 gene,
resulting in a cys315-to-arg (C315R) substitution. The nucleotide
substitution created an additional AvaII cleavage site in the variant
gene. Since the variant gene was not detected in the proband's mother
and sibs, it must have originated by de novo mutation during oogenesis.
Because the variant was found in Michigan, it was designated 'PGK
Michigan.'
.0008
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, ALABAMA
PGK1, 3-BP DEL, LYS191DEL
In a 37-year-old white male school teacher with PGK1 deficiency
(300653), Yoshida et al. (1995) identified a 3-bp deletion in exon 7 of
the PGK gene, resulting in a deletion of lys191 in a highly conserved
region within alpha-helix 7 of the protein. The patient had had
infrequent episodes of jaundice prompting a diagnosis of hepatitis. The
authors noted that deletion of lysine could cause molecular instability,
as suggested by the rapid in vitro inactivation of the variant PGK in
this patient.
.0009
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, HAMAMATSU
PGK1, ILE252THR
In an 11-year-old boy with PGK1 deficiency (300653), Sugie et al. (1998)
identified an 837T-C transition in the PGK1 gene, resulting in an
ile252-to-thr (I252T) substitution. The boy was mentally retarded and
had had recurrent episodes of convulsions followed by generalized
myalgia, muscle weakness, and pigmenturia.
Bischof et al. (2006) demonstrated that the I252T mutation originates by
gene conversion from a processed pseudogene. A PGK1 pseudogene (PGK1P1)
carries the 837T-C transition that produces the I252T substitution
associated with phosphoglycerate kinase deficiency.
.0010
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, HERLEV
PGK1, ASP285VAL
In a Danish patient with PGK1 deficiency (300653), Valentin et al.
(1998) identified an asp285-to-val (D285V) substitution in the PGK1
gene. The patient had isolated hemolytic anemia without neurologic or
muscular disorders. The mutated gene was expressed only partially; both
normal and substituted nucleotides were found at the same position in a
ratio of approximately 1:9. Valentin et al. (1998) presumed that somatic
mutation with mosaicism was the likely explanation for the relatively
mild phenotype.
.0011
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, BARCELONA
PGK1, ILE46ASN
In a Spanish boy with PGK1 deficiency (300653), Noel et al. (2005)
identified a 140T-A transversion in the PGK1 gene, resulting in an
ile46-to-asn (I46N) substitution. He had a long history of chronic
hemolytic anemia and progressive neurologic impairment leading to mental
deterioration. No muscular dystrophy could be demonstrated. The mutation
was present in heterozygous state in the patient's mother. Based on the
crystal structure of porcine PGK, the I46N mutation did not modify any
of the PGK binding sites for ATP or 3PG, so the consequences must be
related to a loss of the enzyme stability rather than a decrease of
enzyme catalytic function.
.0012
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MURCIA
PGK1, SER319ASN
In a boy from Murcia with PGK1 deficiency (300653), Noel et al. (2005)
identified a 958G-A transition in the PGK1 gene, resulting in a
ser319-to-asn (S319N) substitution. He had severe hemolytic anemia,
encephalopathy, and seizures, and died at age 7 years. His mother and
sister were heterozygous for the mutation. Based on the crystal
structure of porcine PGK, the S319N mutation did not modify any of the
PGK binding sites for ATP or 3PG, so the consequences must be related to
a loss of the enzyme stability rather than a decrease of enzyme
catalytic function.
.0013
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, AMIENS
PGK1, ASP164VAL
In 2 affected boys of a white American family with PGK1 deficiency
(300653), Flanagan et al. (2006) identified a 491A-T transversion in
exon 5 of the PGK1 gene, resulting in an asp164-to-val (D164V)
substitution. The 2 boys presented with hemolytic anemia, seizures, and
developmental delay. The diagnosis of PGK deficiency was based on an
erythrocyte PGK enzyme activity level of less than 5% of normal and
identification of the D164V mutation. This mutation had previously been
designated PGK-Amiens and described in a French PGK patient (Cohen-Solal
et al., 1994) and in a large family of Chinese extraction living in New
York (Valentine et al., 1969; Turner et al., 1995). The proband in the
family reported by Flanagan et al. (2006) also had hemiplegic migraines,
retinal dystrophy, and muscle fatigue. The 3 families in which this
mutation had been described appeared to represent recurrent mutations.
This variant has also been referred to as PGK NEW YORK.
.0014
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, FUKUROI
PGK1, IVS7DS, G-A, +5
In a 33-year-old Japanese man with PGK1 deficiency (300653), Shirakawa
et al. (2006) identified a G-to-A transition in intron 7 of the PGK1
gene, resulting in aberrant splicing and a catalytically inactive
protein. The patient had mental retardation and exertional
myoglobinuria, but no evidence of hemolytic anemia. PGK1 enzyme activity
was 8.9% and 13.6% of control values in muscle and red blood cells,
respectively.
.0015
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, AFULA
PGK1, THR378PRO
In an 18-year-old man of Arab Bedouin descent with PGK1 deficiency
(300653), Spiegel et al. (2009) identified a 1132A-C transversion in
exon 10 of the PGK1 gene, resulting in a thr378-to-pro (T378P)
substitution in a highly conserved residue. The patient had a myopathic
phenotype, with onset of muscle cramps and exercise-induced pigmenturia
at age 7 years. He had no evidence of hemolytic anemia or neurologic
involvement; serum creatine kinase was increased. Protein structural
analysis predicted that the mutation would destabilize an alpha-helix
and interfere with the contact of domains responsible for proper
catalytic interactions with nucleotide phosphates. Biochemical studies
showed decreased PGK1 activity in muscle (0.9% of control values) and
erythrocytes (1.6%). The patient's unaffected mother and 2 sisters were
heterozygous for the mutation.
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and Krietsch (1977); Shows and Brown (1975); Sugie et al. (1989);
Sugie et al. (1994); Yoshida and Miwa (1974)
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52. Yoshida, A.; Twele, T. W.; Dave, V.; Beutler, E.: Molecular abnormality
of a phosphoglycerate kinase variant (PGK-Alabama). Blood Cells Mol.
Dis. 21: 179-181, 1995.
53. Yoshida, A.; Watanabe, S.; Chen, S.-H.; Giblett, E. R.; Malcolm,
L. A.: Human phosphoglycerate kinase II: structure of a variant enzyme. J.
Biol. Chem. 247: 446-449, 1972.
*FIELD* CN
Cassandra L. Kniffin - updated: 11/4/2009
Cassandra L. Kniffin - reorganized: 7/2/2007
Victor A. McKusick - updated: 9/19/2006
Victor A. McKusick - updated: 7/12/2006
Victor A. McKusick - updated: 3/28/2006
Ada Hamosh - updated: 12/21/2000
Victor A. McKusick - updated: 9/18/1998
Victor A. McKusick - updated: 5/19/1998
*FIELD* CD
Victor A. McKusick: 6/24/1986
*FIELD* ED
terry: 04/12/2012
wwang: 11/18/2009
ckniffin: 11/4/2009
carol: 7/2/2007
ckniffin: 7/2/2007
ckniffin: 6/27/2007
carol: 3/28/2007
wwang: 10/3/2006
terry: 9/19/2006
alopez: 7/19/2006
terry: 7/12/2006
alopez: 3/29/2006
terry: 3/28/2006
carol: 11/18/2005
carol: 12/23/2000
terry: 12/21/2000
dkim: 9/23/1998
terry: 9/18/1998
dholmes: 7/2/1998
terry: 6/3/1998
carol: 5/30/1998
terry: 5/28/1998
terry: 5/19/1998
mark: 1/18/1997
terry: 4/15/1996
terry: 4/8/1996
carol: 11/21/1994
warfield: 3/14/1994
mimadm: 2/28/1994
carol: 12/17/1993
carol: 12/6/1993
carol: 11/22/1993
*RECORD*
*FIELD* NO
311800
*FIELD* TI
*311800 PHOSPHOGLYCERATE KINASE 1; PGK1
;;3-@PHOSPHOGLYCEROKINASE;;
PGKA
PHOSPHOGLYCERATE KINASE 1 PSEUDOGENE 1, INCLUDED; PGK1P1, INCLUDED;;
read morePHOSPHOGLYCERATE KINASE 1 PSEUDOGENE 2, INCLUDED; PGK1P2, INCLUDED
*FIELD* TX
DESCRIPTION
The PGK1 gene encodes phosphoglycerate kinase-1, also known as
ATP:3-phosphoglycerate 1-phosphotransferase (EC 2.7.2.3), which
catalyzes the reversible conversion of 1,3-diphosphoglycerate to
3-phosphoglycerate during glycolysis, generating one molecule of ATP.
PGK1 is distinguished from testicular PGK2 (172270), which maps to
chromosome 6p21.
CLONING
Michelson et al. (1983) isolated a full-length cDNA clone of PGK from a
human fetal liver cDNA library using synthetic oligonucleotide mixtures
as hybridization probes. The deduced protein contains 417 amino acid
residues. Southern blot analysis of human genomic DNAs showed a complex
pattern of hybridizing fragments, 2 of which were non-X in origin. The
results were interpreted as reflecting the existence of a small family
of dispersed PGK or PGK-like genes.
Using a mixture of synthetic oligodeoxyribonucleotides, Singer-Sam et
al. (1983) isolated a cDNA encoding amino acids 291-296 of PGK.
GENE STRUCTURE
The human PGK1 gene contains 11 exons and spans approximately 23
kilobases (Michelson et al., 1985).
GENE FUNCTION
Disulfide bonds in secreted proteins are considered to be inert because
of the oxidizing nature of the extracellular milieu. An exception to
this rule is a reductase secreted by tumor cells that reduces disulfide
bonds in the serine proteinase plasmin. Reduction of plasmin initiates
proteolytic cleavage in the kringle 5 domain and release of the tumor
blood vessel inhibitor angiostatin. New blood vessel formation or
angiogenesis is critical for tumor expansion and metastasis. Lay et al.
(2000) showed that the plasmin reductase isolated from conditioned
medium of fibrosarcoma cells is the glycolytic enzyme phosphoglycerate
kinase. Recombinant phosphoglycerate kinase had the same specific
activity as the fibrosarcoma-derived protein. Plasma of mice bearing
fibrosarcoma tumors contained several-fold more phosphoglycerate kinase,
as compared with mice without tumors. Administration of phosphoglycerate
kinase to tumor-bearing mice caused an increase in plasma levels of
angiostatin, and a decrease in tumor vascularity and rate of tumor
growth. Lay et al. (2000) concluded that phosphoglycerate kinase not
only functions in glycolysis but is secreted by tumor cells and
participates in the angiogenic process as a disulfide reductase.
MAPPING
By somatic cell hybridization, Grzeschik et al. (1972) concluded that
the PGK locus was on the long arm of the X chromosome. From the study of
chromosomal aberrations in cell hybridization systems, Ricciuti and
Ruddle (1973) concluded that the order on the X chromosome was
centromere--PGK--HPRT (308000)--G6PD (305900). The conclusion was based
on their own work with the KOP 14-X translocation, and on Park Gerald's
with a 19-X translocation and Bootsma's with a 3-X translocation. All 3
had breaks involving the long arm of the X chromosome, each at a
different site. From study of radiation-induced segregants in which
irradiated human cells are rescued by fusion with hamster cells, Goss
and Harris (1977) showed that the order of the 4 loci is PGK: alpha-GAL
(300644): HPRT: G6PD and that the 3 intervals between these 4 loci are,
in relative terms, 0.33, 0.30, and 0.23.
Willard et al. (1985) used a cDNA for human PGK to map the functional
PGK1 gene to Xq13. Evidence reported by Verga et al. (1991) suggested
that PGK1, which is distal to the Menkes disease gene (309400), may be
located in Xq13.3.
PGK is X-linked in the kangaroo (Cooper et al., 1971). Alpha-GALA, HPRT,
PGK and G6PD are X-linked in the rabbit, according to mouse-rabbit
hybrid cell studies (Cianfriglia et al., 1979; Echard and Gillois,
1979). By comparable methods, Hors-Cayla et al. (1979) found them to be
X-linked also in cattle. According to cell hybridization studies, HPRT,
G6PD and PGK are X-linked in the pig (Gellin et al., 1979) and in sheep
(Saidi et al., 1979).
- Pseudogenes
One pseudogene of PGK1 (PGK1P1) is on Xq at Xq11-Xq13, proximal to the
expressed PGK1 gene at Xq13 (Michelson et al., 1985; Willard et al.,
1985). The pseudogene was mapped by somatic hybrid cell and in situ
hybridization methods using a cloned DNA probe in each case.
Willard et al. (1985) identified a 10-kb PGK-related DNA sequence on
human chromosome 19, which the authors suggested could represent a
pseudogene, the putative testes-specific PGK gene, or some other related
gene. Gartler et al. (1986) mapped a 1-kb PGK sequence to chromosome 19,
which represents the second pseudogene PGK1P2.
MOLECULAR GENETICS
Chen et al. (1971) described an electrophoretic variant of PGK with
enzyme activity in the normal range. Using a PGK cDNA probe, Hutz et al.
(1984) identified a common DNA polymorphism with the restriction enzyme
PstI. About 48% of females in all ethnic groups were found to be
heterozygous. Data on gene frequencies of allelic variants were
tabulated by Roychoudhury and Nei (1988).
- Phosphoglycerate Kinase-1 Deficiency
In a patient with chronic hemolytic anemia associated with deficiency of
PGK1 activity (300653), Fujii and Yoshida (1980) used peptide mapping
analysis to identify an arg206-to-pro (R206P; 311800.0002) substitution
in the PGK1 protein. The PGK1 variant was referred to as 'Uppsala.'
Sugie et al. (1998) described an 837T-C mutation (311800.0009) in the
PGK gene of a patient with PGK Hamamatsu and the myopathic form of PGK1
deficiency.
In 2 unrelated boys of Spanish origin with severe lifelong chronic
hemolytic anemia and progressive neurologic impairment, Noel et al.
(2005) identified 2 different mutations in the PGK1 gene (311800.0011
and 311800.0012, respectively).
Spiegel et al. (2009) reported an 18-year-old man of Arab Bedouin
descent with PGK1 deficiency confirmed by genetic analysis (T378P;
311800.0015). He had a purely myopathic phenotype, with onset of muscle
cramps and exercise-induced pigmenturia at age 7 years. He had no
evidence of hemolytic anemia or neurologic involvement; serum creatine
kinase was increased. Biochemical studies showed decreased PGK1 activity
in muscle (0.9% of control values) and erythrocytes (1.6%). The
patient's unaffected mother and 2 sisters were heterozygous for the
mutation.
*FIELD* AV
.0001
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MUNCHEN
PGK1, ASP268ASN
By peptide mapping analysis, Fujii et al. (1980) found an asp268-to-asn
(D268N) substitution in the PGK1 enzyme that was associated with mild
enzymatic deficiency (21% of normal activity) and was heat-unstable.
There was no hemolytic anemia or accumulation of intermediate
metabolites. Krietsch et al. (1977, 1980) described a large German
kindred with PGK Munchen. Although the variant showed decreased
activity, none of the carriers had overt clinical symptoms.
.0002
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, UPPSALA
PGK1, ARG206PRO
In a patient with chronic hemolytic anemia associated with deficiency of
PGK activity (300653), Fujii and Yoshida (1980) used peptide mapping
analysis to identify an arg206-to-pro (R206P) substitution in the PGK1
protein.
.0003
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, TOKYO
PGK1, VAL266MET
In a patient with chronic nonspherocytic hemolytic anemia and neurologic
disturbances due to PGK1 deficiency (300653), Fujii et al. (1981) used
peptide mapping analysis to identify a val266-to-met (V266M)
substitution in the PGK1 enzyme. The variant enzyme had 16% activity
compared to controls.
.0004
PHOSPHOGLYCERATE KINASE 1, PGK II
PGK1, THR352ASN
Chen et al. (1971) found an electrophoretic polymorphism of PGK in a New
Guinea population, where the frequency of a variant enzyme, termed 'PGK
II,' showed a gene frequency of about 0.014. In starch gel
electrophoresis, the variant enzyme moved toward the anode faster than
the normal enzyme. Yoshida et al. (1972) found that the PGK II variant
had a substitution of threonine to asparagine. The same substitution was
found in a Samoan male. Fujii et al. (1981) stated that the thr-to-asn
change was at position 352. The variant was not associated with enzyme
deficiency.
.0005
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MATSUE
PGK1, LEU88PRO
PGK Matsue is an electrophoretic variant associated with severe enzyme
deficiency, congenital nonspherocytic anemia, and mental disorders
(300653) (Miwa et al., 1972). In a cell line from a patient who died at
age 9 from complications of pneumonia, Maeda and Yoshida (1991), who
found a T/A-to-C/G transition in exon 3 of the PGK gene, resulting in a
leu88-to-pro (L88P) substitution. The nucleotide change created an
additional NciI cleavage site. Because the substitution was expected to
induce serious perturbation and instability in the protein structure,
Maeda and Yoshida (1991) suspected that the severe enzyme deficiency was
caused mainly by more rapid in vivo denaturation and degradation of the
variant enzyme.
Tani et al. (1985) found that PGK Matsue enzyme activity was about 5% of
control values. PGK Matsue mRNA was present in normal amounts in
fibroblasts, suggesting the enzyme deficiency was due to a 7- to 10-fold
increase in degradation of the mutant enzyme.
.0006
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, SHIZUOKA
PGK1, GLY157VAL
In a 27-year-old Japanese male with PGK1 deficiency (300653), Fujii et
al. (1992) identified a 473G-T transversion in the PGK1 gene, resulting
in a gly157-to-val (G157V) substitution The mutation created a new BstXI
cleavage site in exon 5. The patient had chronic hemolytic anemia and
myoglobinuria, manifested by nausea, anorexia, and muscle weakness after
exercise, beginning at the age of 10. There was no family history of
anemia or neuromuscular disease.
.0007
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MICHIGAN
PGK1, CYS315ARG
In a 14-year-old boy with mental retardation, a behavior disorder, and
episodic hemolytic anemia due to PGK1 deficiency (300653), Maeda et al.
(1992) identified a T-to-C transition in exon 9 of the PGK1 gene,
resulting in a cys315-to-arg (C315R) substitution. The nucleotide
substitution created an additional AvaII cleavage site in the variant
gene. Since the variant gene was not detected in the proband's mother
and sibs, it must have originated by de novo mutation during oogenesis.
Because the variant was found in Michigan, it was designated 'PGK
Michigan.'
.0008
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, ALABAMA
PGK1, 3-BP DEL, LYS191DEL
In a 37-year-old white male school teacher with PGK1 deficiency
(300653), Yoshida et al. (1995) identified a 3-bp deletion in exon 7 of
the PGK gene, resulting in a deletion of lys191 in a highly conserved
region within alpha-helix 7 of the protein. The patient had had
infrequent episodes of jaundice prompting a diagnosis of hepatitis. The
authors noted that deletion of lysine could cause molecular instability,
as suggested by the rapid in vitro inactivation of the variant PGK in
this patient.
.0009
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, HAMAMATSU
PGK1, ILE252THR
In an 11-year-old boy with PGK1 deficiency (300653), Sugie et al. (1998)
identified an 837T-C transition in the PGK1 gene, resulting in an
ile252-to-thr (I252T) substitution. The boy was mentally retarded and
had had recurrent episodes of convulsions followed by generalized
myalgia, muscle weakness, and pigmenturia.
Bischof et al. (2006) demonstrated that the I252T mutation originates by
gene conversion from a processed pseudogene. A PGK1 pseudogene (PGK1P1)
carries the 837T-C transition that produces the I252T substitution
associated with phosphoglycerate kinase deficiency.
.0010
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, HERLEV
PGK1, ASP285VAL
In a Danish patient with PGK1 deficiency (300653), Valentin et al.
(1998) identified an asp285-to-val (D285V) substitution in the PGK1
gene. The patient had isolated hemolytic anemia without neurologic or
muscular disorders. The mutated gene was expressed only partially; both
normal and substituted nucleotides were found at the same position in a
ratio of approximately 1:9. Valentin et al. (1998) presumed that somatic
mutation with mosaicism was the likely explanation for the relatively
mild phenotype.
.0011
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, BARCELONA
PGK1, ILE46ASN
In a Spanish boy with PGK1 deficiency (300653), Noel et al. (2005)
identified a 140T-A transversion in the PGK1 gene, resulting in an
ile46-to-asn (I46N) substitution. He had a long history of chronic
hemolytic anemia and progressive neurologic impairment leading to mental
deterioration. No muscular dystrophy could be demonstrated. The mutation
was present in heterozygous state in the patient's mother. Based on the
crystal structure of porcine PGK, the I46N mutation did not modify any
of the PGK binding sites for ATP or 3PG, so the consequences must be
related to a loss of the enzyme stability rather than a decrease of
enzyme catalytic function.
.0012
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MURCIA
PGK1, SER319ASN
In a boy from Murcia with PGK1 deficiency (300653), Noel et al. (2005)
identified a 958G-A transition in the PGK1 gene, resulting in a
ser319-to-asn (S319N) substitution. He had severe hemolytic anemia,
encephalopathy, and seizures, and died at age 7 years. His mother and
sister were heterozygous for the mutation. Based on the crystal
structure of porcine PGK, the S319N mutation did not modify any of the
PGK binding sites for ATP or 3PG, so the consequences must be related to
a loss of the enzyme stability rather than a decrease of enzyme
catalytic function.
.0013
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, AMIENS
PGK1, ASP164VAL
In 2 affected boys of a white American family with PGK1 deficiency
(300653), Flanagan et al. (2006) identified a 491A-T transversion in
exon 5 of the PGK1 gene, resulting in an asp164-to-val (D164V)
substitution. The 2 boys presented with hemolytic anemia, seizures, and
developmental delay. The diagnosis of PGK deficiency was based on an
erythrocyte PGK enzyme activity level of less than 5% of normal and
identification of the D164V mutation. This mutation had previously been
designated PGK-Amiens and described in a French PGK patient (Cohen-Solal
et al., 1994) and in a large family of Chinese extraction living in New
York (Valentine et al., 1969; Turner et al., 1995). The proband in the
family reported by Flanagan et al. (2006) also had hemiplegic migraines,
retinal dystrophy, and muscle fatigue. The 3 families in which this
mutation had been described appeared to represent recurrent mutations.
This variant has also been referred to as PGK NEW YORK.
.0014
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, FUKUROI
PGK1, IVS7DS, G-A, +5
In a 33-year-old Japanese man with PGK1 deficiency (300653), Shirakawa
et al. (2006) identified a G-to-A transition in intron 7 of the PGK1
gene, resulting in aberrant splicing and a catalytically inactive
protein. The patient had mental retardation and exertional
myoglobinuria, but no evidence of hemolytic anemia. PGK1 enzyme activity
was 8.9% and 13.6% of control values in muscle and red blood cells,
respectively.
.0015
PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, AFULA
PGK1, THR378PRO
In an 18-year-old man of Arab Bedouin descent with PGK1 deficiency
(300653), Spiegel et al. (2009) identified a 1132A-C transversion in
exon 10 of the PGK1 gene, resulting in a thr378-to-pro (T378P)
substitution in a highly conserved residue. The patient had a myopathic
phenotype, with onset of muscle cramps and exercise-induced pigmenturia
at age 7 years. He had no evidence of hemolytic anemia or neurologic
involvement; serum creatine kinase was increased. Protein structural
analysis predicted that the mutation would destabilize an alpha-helix
and interfere with the contact of domains responsible for proper
catalytic interactions with nucleotide phosphates. Biochemical studies
showed decreased PGK1 activity in muscle (0.9% of control values) and
erythrocytes (1.6%). The patient's unaffected mother and 2 sisters were
heterozygous for the mutation.
*FIELD* SA
Cooper et al. (1975); Deys et al. (1972); Huijing et al. (1973); Konrad
et al. (1973); Kozak et al. (1974); Meera Khan et al. (1971); Schwab
and Krietsch (1977); Shows and Brown (1975); Sugie et al. (1989);
Sugie et al. (1994); Yoshida and Miwa (1974)
*FIELD* RF
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33. Noel, N.; Flanagan, J.; Kalko, S. G.; Bajo, M. J. R.; Manu, M.
M.; Fuster, J. L. G.; Beutler, E.; Corrons, J.-L. V.: Two new phosphoglycerate
kinase mutations associated with chronic haemolytic anaemia and neurological
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*FIELD* CN
Cassandra L. Kniffin - updated: 11/4/2009
Cassandra L. Kniffin - reorganized: 7/2/2007
Victor A. McKusick - updated: 9/19/2006
Victor A. McKusick - updated: 7/12/2006
Victor A. McKusick - updated: 3/28/2006
Ada Hamosh - updated: 12/21/2000
Victor A. McKusick - updated: 9/18/1998
Victor A. McKusick - updated: 5/19/1998
*FIELD* CD
Victor A. McKusick: 6/24/1986
*FIELD* ED
terry: 04/12/2012
wwang: 11/18/2009
ckniffin: 11/4/2009
carol: 7/2/2007
ckniffin: 7/2/2007
ckniffin: 6/27/2007
carol: 3/28/2007
wwang: 10/3/2006
terry: 9/19/2006
alopez: 7/19/2006
terry: 7/12/2006
alopez: 3/29/2006
terry: 3/28/2006
carol: 11/18/2005
carol: 12/23/2000
terry: 12/21/2000
dkim: 9/23/1998
terry: 9/18/1998
dholmes: 7/2/1998
terry: 6/3/1998
carol: 5/30/1998
terry: 5/28/1998
terry: 5/19/1998
mark: 1/18/1997
terry: 4/15/1996
terry: 4/8/1996
carol: 11/21/1994
warfield: 3/14/1994
mimadm: 2/28/1994
carol: 12/17/1993
carol: 12/6/1993
carol: 11/22/1993