P00558 (PGK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglycerate kinase 1
EC=2.7.2.3

Alternative name(s):
Cell migration-inducing gene 10 protein
Primer recognition protein 2
Short name=PRP 2

Gene names

Name:	PGK1
Synonyms:	PGKA
ORF Names:	MIG10, OK/SW-cl.110

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).
Catalytic activity	ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Involvement in disease	Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]: A condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34 Ref.35
Sequence similarities	Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Disease	Disease mutation Hereditary hemolytic anemia
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Traceable author statement. Source: Reactome glycolysis Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB phosphoglycerate kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.12

Chain

2 – 417

416

Phosphoglycerate kinase 1

PRO_0000145831

Regions

Nucleotide binding

373 – 376

4

ATP

Region

24 – 26

3

Substrate binding

Region

63 – 66

4

Substrate binding

Sites

Binding site

39

1

Substrate

Binding site

123

1

Substrate

Binding site

171

1

Substrate

Binding site

220

1

ATP

Binding site

313

1

ATP; via carbonyl oxygen

Binding site

344

1

ATP

Amino acid modifications

Modified residue

2

1

N-acetylserine

Modified residue

11

1

N6-acetyllysine Ref.19

Modified residue

48

1

N6-acetyllysine Ref.19

Modified residue

75

1

N6-acetyllysine Ref.19

Modified residue

76

1

Phosphotyrosine By similarity

Modified residue

86

1

N6-acetyllysine Ref.19

Modified residue

97

1

N6-acetyllysine Ref.19

Modified residue

131

1

N6-acetyllysine; alternate Ref.19

Modified residue

131

1

N6-malonyllysine; alternate Ref.22

Modified residue

146

1

N6-acetyllysine Ref.19

Modified residue

196

1

Phosphotyrosine Ref.16

Modified residue

199

1

N6-acetyllysine Ref.19

Modified residue

203

1

Phosphoserine Ref.17 Ref.20 Ref.23

Modified residue

267

1

N6-acetyllysine Ref.19

Modified residue

291

1

N6-acetyllysine Ref.19

Modified residue

390

1

Phosphoserine By similarity

Natural variations

Natural variant

88

1

L → P in PGK1D; with congenital non-spherocytic anemia; variant Matsue. Ref.29

VAR_006076

Natural variant

158

1

G → V in PGK1D; with chronic hemolytic anemia; variant Shizuoka. Ref.33

VAR_006077

Natural variant

164

1

D → V in PGK1D; with chronic hemolytic anemia and mental retardation; variant Amiens. Ref.26

VAR_006078

Natural variant

191

1

Missing in PGK1D; with chronic hemolytic anemia; variant Alabama. Ref.25

VAR_006079

Natural variant

206

1

R → P in PGK1D; with chronic hemolytic anemia; variant Uppsala. Ref.35

VAR_006080

Natural variant

252

1

E → A in PGK1D; with chronic hemolytic anemia; variant Antwerp. Ref.27

VAR_006081

Natural variant

266

1

V → M in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo. Ref.34

VAR_006082

Natural variant

268

1

D → N in Munchen; 21% of activity. Ref.31 Ref.32

VAR_006083

Natural variant

285

1

D → V in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity. Ref.28

VAR_006084

Natural variant

315

1

D → N in PGK1D; with rhabdomyolysis; variant Creteil. Ref.26

VAR_006085

Natural variant

316

1

C → R in PGK1D; with chronic hemolytic anemia; variant Michigan. Ref.30

VAR_006086

Natural variant

352

1

T → N. Ref.32

VAR_006087

Experimental info

Sequence conflict

39

1

Missing AA sequence Ref.12

Sequence conflict

370

1

I → T in CAG32997. Ref.6

Secondary structure

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417

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Helix

9 – 11

3

Beta strand

18 – 22

5

Beta strand

29 – 32

4

Beta strand

33 – 35

3

Helix

38 – 52

15

Beta strand

56 – 61

6

Helix

73 – 76

4

Helix

79 – 89

11

Beta strand

94 – 97

4

Beta strand

99 – 101

3

Helix

102 – 109

8

Beta strand

115 – 118

4

Helix

122 – 124

3

Turn

126 – 130

5

Beta strand

131 – 133

3

Beta strand

135 – 137

3

Beta strand

139 – 141

3

Helix

144 – 156

13

Beta strand

159 – 163

5

Helix

166 – 168

3

Helix

174 – 177

4

Beta strand

184 – 186

3

Helix

188 – 202

15

Beta strand

206 – 212

7

Helix

217 – 220

4

Helix

221 – 223

3

Helix

224 – 227

4

Turn

228 – 230

3

Beta strand

232 – 236

5

Helix

238 – 240

3

Helix

241 – 249

9

Helix

260 – 263

4

Helix

266 – 275

10

Beta strand

279 – 281

3

Beta strand

285 – 293

9

Beta strand

298 – 302

5

Turn

303 – 305

3

Beta strand

312 – 316

5

Helix

318 – 330

13

Beta strand

332 – 338

7

Helix

346 – 348

3

Helix

350 – 364

15

Beta strand

368 – 373

6

Helix

376 – 382

7

Beta strand

388 – 394

7

Helix

397 – 404

8

Helix

409 – 412

4

Sequences

	Sequence		Length	Mass (Da)
	P00558 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B5DFC7B5FA01767C	FASTA	417	44,615
	10 20 30 40 50 60 MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL 70 80 90 100 110 120 MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV GPEVEKACAN PAAGSVILLE 130 140 150 160 170 180 NLRFHVEEEG KGKDASGNKV KAEPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN 190 200 210 220 230 240 LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM 250 260 270 280 290 300 AFTFLKVLNN MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ 310 320 330 340 350 360 ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV 370 380 390 400 410 KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and DNA sequence of a full-length cDNA clone for human X chromosome-encoded phosphoglycerate kinase." Michelson A.M., Markham A.F., Orkin S.H. Proc. Natl. Acad. Sci. U.S.A. 80:472-476(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Structure of the human phosphoglycerate kinase gene and the intron-mediated evolution and dispersal of the nucleotide-binding domain." Michelson A.M., Blake C.C., Evans S.T., Orkin S.H. Proc. Natl. Acad. Sci. U.S.A. 82:6965-6969(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Identification of a human migration-inducing gene 10 (MIG10)." Kim J.W. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients." Shichijo S., Itoh K. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon adenocarcinoma.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Skin and Uterus.
[10]	"Sequence of the promoter region of the gene for human X-linked 3-phosphoglycerate kinase]." Singer-Sam J., Keith D.H., Tani K., Simmer R.L., Shively L., Lindsay S., Yoshida A., Riggs A.D. Gene 32:409-417(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[11]	"Genomic sequencing and methylation analysis by ligation mediated PCR." Pfeifer G.P., Steigerwald S.D., Mueller P.R., Wold B., Riggs A.D. Science 246:810-813(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
[12]	"Complete amino acid sequence of human phosphoglycerate kinase. Cyanogen bromide peptides and complete amino acid sequence." Huang I.-Y., Welch C.D., Yoshida A. J. Biol. Chem. 255:6412-6420(1980) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-417. Tissue: Erythrocyte.
[13]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 23-30; 76-86; 107-123; 157-171; 200-216; 221-264; 280-297; 333-350; 366-382 AND 389-417, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[14]	"Functional identity of a primer recognition protein as phosphoglycerate kinase." Jindal H.K., Vishwanatha J.K. J. Biol. Chem. 265:6540-6543(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Placenta.
[15]	"Hematologically important mutations: molecular abnormalities of phosphoglycerate kinase." Yoshida A. Blood Cells Mol. Dis. 22:265-267(1996) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[16]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196, MASS SPECTROMETRY.
[17]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-48; LYS-75; LYS-86; LYS-97; LYS-131; LYS-146; LYS-199; LYS-267 AND LYS-291, MASS SPECTROMETRY.
[20]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"The first identification of lysine malonylation substrates and its regulatory enzyme." Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y. Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract] Cited for: MALONYLATION AT LYS-131.
[23]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY.
[24]	"Molecular basis for the lack of enantioselectivity of human 3-phosphoglycerate kinase." Gondeau C., Chaloin L., Lallemand P., Roy B., Perigaud C., Barman T., Varga A., Vas M., Lionne C., Arold S.T. Nucleic Acids Res. 36:3620-3629(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH PHOSPHOGLYCERATE; L-ADP; D-ADP; L-CDP AND D-CDP, SUBSTRATE-BINDING SITES.
[25]	"Molecular abnormality of a phosphoglycerate kinase variant (PGK-Alabama)." Yoshida A., Twele T.W., Dave V., Beutler E. Blood Cells Mol. Dis. 21:179-181(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PGK1D LYS-191 DEL.
[26]	"Identification of new mutations in two phosphoglycerate kinase (PGK) variants expressing different clinical syndromes: PGK Creteil and PGK Amiens." Cohen-Solal M., Valentin C., Plassa F., Guillemin G., Danze F., Jaisson F., Rosa R. Blood 84:898-903(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PGK1D VAL-164 AND ASN-315.
[27]	"Retarded and aberrant splicings caused by single exon mutation in a phosphoglycerate kinase variant." Ookawara T., Dave V., Willems P., Martin J.J., de Barsy T., Matthys E., Yoshida A. Arch. Biochem. Biophys. 327:35-40(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PGK1D ALA-252.
[28]	"A phosphoglycerate kinase mutant (PGK Herlev; D285V) in a Danish patient with isolated chronic hemolytic anemia: mechanism of mutation and structure-function relationships." Valentin C., Birgens H., Craescu C.T., Broedum-Nielsen K., Cohen-Solal M. Hum. Mutat. 12:280-287(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PGK1D VAL-285.
[29]	"Molecular defect of a phosphoglycerate kinase variant (PGK-Matsue) associated with hemolytic anemia: Leu-->Pro substitution caused by T/A-->C/G transition in exon 3." Maeda M., Yoshida A. Blood 77:1348-1352(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PGK1D PRO-88.
[30]	"Molecular abnormalities of a phosphoglycerate kinase variant generated by spontaneous mutation." Maeda M., Bawle E.V., Kulkarni R., Beutler E., Yoshida A. Blood 79:2759-2762(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PGK1D ARG-316.
[31]	"A single amino acid substitution (Asp leads to Asn) in a phosphoglycerate kinase variant (PGK Munchen) associated with enzyme deficiency." Fujii H., Krietsch W.K.G., Yoshida A. J. Biol. Chem. 255:6421-6423(1980) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MUNCHEN ASN-268.
[32]	"Structure and function of normal and variant human phosphoglycerate kinase." Huang I.-Y., Fujii H., Yoshida A. Hemoglobin 4:601-609(1980) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MUNCHEN ASN-268, VARIANT ASN-352.
[33]	"A single amino acid substitution (157 Gly-->Val) in a phosphoglycerate kinase variant (PGK Shizuoka) associated with chronic hemolysis and myoglobinuria." Fujii H., Kanno H., Hirono A., Shiomura T., Miwa S. Blood 79:1582-1585(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PGK1D VAL-158.
[34]	"Use of cultured lymphoblastoid cells for the study of abnormal enzymes: molecular abnormality of a phosphoglycerate kinase variant associated with hemolytic anemia." Fujii H., Chen S.-H., Akatsuka J., Miwa S., Yoshida A. Proc. Natl. Acad. Sci. U.S.A. 78:2587-2590(1981) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PGK1D MET-266.
[35]	"Molecular abnormality of phosphoglycerate kinase-Uppsala associated with chronic nonspherocytic hemolytic anemia." Fujii H., Yoshida A. Proc. Natl. Acad. Sci. U.S.A. 77:5461-5465(1980) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PGK1D PRO-206.
+	Additional computationally mapped references.

Web resources

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Phosphoglycerate kinase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00572 mRNA. Translation: CAA23835.1.
L00160 mRNA. Translation: AAA60078.1.
M11968 , M11958, M11959, M11960, M11961, M11962, M11963, M11964, M11965, M11966, M11967 Genomic DNA. Translation: AAA60079.1.
AY423725 mRNA. Translation: AAS00488.1.
AB062432 mRNA. Translation: BAB93495.1.
AK291081 mRNA. Translation: BAF83770.1.
AK312280 mRNA. Translation: BAG35209.1.
CR456716 mRNA. Translation: CAG32997.1.
AL049589 Genomic DNA. Translation: CAI42951.1.
CH471104 Genomic DNA. Translation: EAW98604.1.
BC023234 mRNA. Translation: AAH23234.1.
BC103752 mRNA. Translation: AAI03753.1.
BC104837 mRNA. Translation: AAI04838.1.
BC113568 mRNA. Translation: AAI13569.1.
M34017 Genomic DNA. Translation: AAA60103.1.

IPI

IPI00169383.

PIR

KIHUG. I59050.

RefSeq

NP_000282.1. NM_000291.3.

UniGene

Hs.78771.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WZB	X-ray	1.47	A	2-417	[»]
2WZC	X-ray	1.50	A	2-417	[»]
2WZD	X-ray	1.56	A	1-417	[»]
2X13	X-ray	1.74	A	2-417	[»]
2X14	X-ray	1.90	A	2-417	[»]
2X15	X-ray	2.10	A	2-417	[»]
2XE6	X-ray	1.74	A	1-417	[»]
2XE7	X-ray	2.20	A	1-417	[»]
2XE8	X-ray	1.79	A	1-417	[»]
2Y3I	X-ray	2.90	A/D	1-416	[»]
2YBE	X-ray	2.00	A	1-417	[»]
2ZGV	X-ray	2.00	A	1-417	[»]
3C39	X-ray	1.85	A/B	1-417	[»]
3C3A	X-ray	2.30	A/B	1-417	[»]
3C3B	X-ray	1.80	A/B	1-417	[»]
3C3C	X-ray	2.40	A/B	1-417	[»]

ProteinModelPortal

P00558.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00558. 26 interactions.

MINT

MINT-1131047.

STRING

9606.ENSP00000362413.

PTM databases

PhosphoSite

P00558.

Polymorphism databases

DMDM

52788229.

2D gel databases

DOSAC-COBS-2DPAGE

P00558.

OGP

P00558.

REPRODUCTION-2DPAGE

IPI00169383.
P00558.

UCD-2DPAGE

P00558.

Proteomic databases

PaxDb

P00558.

PeptideAtlas

P00558.

PRIDE

P00558.

Protocols and materials databases

DNASU

5230.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373316; ENSP00000362413; ENSG00000102144.
ENST00000597340; ENSP00000472461; ENSG00000269666.

GeneID

5230.

KEGG

hsa:5230.

UCSC

uc004ecz.4. human.

Organism-specific databases

CTD

5230.

GeneCards

GC0XP077246.

HGNC

HGNC:8896. PGK1.

HPA

CAB010065.
HPA045385.

MIM

300653. phenotype.
311800. gene.

neXtProt

NX_P00558.

Orphanet

713. Phosphoglycerate kinase 1 deficiency.

PharmGKB

PA33234.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0126.

HOGENOM

HOG000227107.

HOVERGEN

HBG008177.

InParanoid

P00558.

KO

K00927.

OMA

NFANGTK.

OrthoDB

EOG44MXS6.

PhylomeDB

P00558.

Enzyme and pathway databases

BRENDA

2.7.2.3. 2681.

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P00558.

UniPathway

UPA00109; UER00185.

Gene expression databases

ArrayExpress

P00558.

Bgee

P00558.

CleanEx

HS_PGK1.

Genevestigator

P00558.

GermOnline

ENSG00000102144. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.

InterPro

IPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]

PANTHER

PTHR11406. PTHR11406. 1 hit.

Pfam

PF00162. PGK. 1 hit.
[Graphical view]

PIRSF

PIRSF000724. Pgk. 1 hit.

PRINTS

PR00477. PHGLYCKINASE.

SUPFAM

SSF53748. PGK. 1 hit.

PROSITE

PS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00558.

ChEMBL

CHEMBL2886.

ChiTaRS

PGK1. human.

EvolutionaryTrace

P00558.

GenomeRNAi

5230.

NextBio

20218.

SOURCE

Search...

Entry information

Entry name

PGK1_HUMAN

Accession

Primary (citable) accession number: P00558
Secondary accession number(s): A8K4W6 , Q5J7W1, Q6IBT6, Q8NI87

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 156 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.