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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]. It is 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. Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.29 Ref.30 Ref.31
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
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.10

Chain

2 – 417

416

Phosphoglycerate kinase 1

PRO_0000145831

Regions

Nucleotide binding

373 – 376

4

ATP By similarity

Region

24 – 26

3

Substrate binding By similarity

Region

63 – 66

4

Substrate binding By similarity

Sites

Binding site

39

1

Substrate By similarity

Binding site

123

1

Substrate By similarity

Binding site

171

1

Substrate By similarity

Binding site

220

1

ATP By similarity

Binding site

313

1

ATP; via carbonyl oxygen By similarity

Binding site

344

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine

Modified residue

11

1

N6-acetyllysine Ref.19

Modified residue

30

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 Ref.19

Modified residue

136

1

Phosphoserine Ref.16

Modified residue

146

1

N6-acetyllysine Ref.19

Modified residue

196

1

Phosphotyrosine Ref.14

Modified residue

199

1

N6-acetyllysine Ref.19

Modified residue

203

1

Phosphoserine Ref.15 Ref.17 Ref.18

Modified residue

243

1

Phosphothreonine Ref.17

Modified residue

267

1

N6-acetyllysine Ref.19

Modified residue

291

1

N6-acetyllysine Ref.19

Modified residue

323

1

N6-acetyllysine Ref.19

Modified residue

390

1

Phosphoserine By similarity

Modified residue

406

1

N6-acetyllysine Ref.19

Natural variations

Natural variant

88

1

L → P in PGK1D; with congenital non-spherocytic anemia; variant Matsue. Ref.25

VAR_006076

Natural variant

158

1

G → V in PGK1D; with chronic hemolytic anemia; variant Shizuoka. Ref.29

VAR_006077

Natural variant

164

1

D → V in PGK1D; with chronic hemolytic anemia and mental retardation; variant Amiens. Ref.22

VAR_006078

Natural variant

191

1

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

VAR_006079

Natural variant

206

1

R → P in PGK1D; with chronic hemolytic anemia; variant Uppsala. Ref.31

VAR_006080

Natural variant

252

1

E → A in PGK1D; with chronic hemolytic anemia; variant Antwerp. Ref.23

VAR_006081

Natural variant

266

1

V → M in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo. Ref.30

VAR_006082

Natural variant

268

1

D → N in Munchen; 21% of activity. Ref.27 Ref.28

VAR_006083

Natural variant

285

1

D → V in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity. Ref.24

VAR_006084

Natural variant

315

1

D → N in PGK1D; with rhabdomyolysis; variant Creteil. Ref.22

VAR_006085

Natural variant

316

1

C → R in PGK1D; with chronic hemolytic anemia; variant Michigan. Ref.26

VAR_006086

Natural variant

352

1

T → N. Ref.28

VAR_006087

Experimental info

Sequence conflict

39

1

Missing AA sequence Ref.10

Sequence conflict

370

1

I → T in CAG32997. Ref.5

Secondary structure

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417

Helix Strand Turn

Details...

Helix

9 – 11

3

Beta strand

18 – 22

5

Beta strand

33 – 35

3

Helix

38 – 52

15

Beta strand

56 – 61

6

Turn

73 – 75

3

Helix

79 – 89

11

Beta strand

94 – 97

4

Beta strand

99 – 101

3

Helix

102 – 109

8

Beta strand

115 – 119

5

Helix

122 – 124

3

Helix

126 – 129

4

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

218 – 220

3

Helix

221 – 228

8

Beta strand

232 – 236

5

Helix

238 – 240

3

Helix

241 – 249

9

Helix

260 – 263

4

Helix

266 – 276

11

Beta strand

279 – 281

3

Beta strand

284 – 293

10

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 – 371

4

Beta strand

388 – 392

5

Helix

397 – 403

7

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: 6188151] [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: 2995995] [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]	"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].
[6]	"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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Skin and Uterus.
[8]	"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: 6099325] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[9]	"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: 2814502] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
[10]	"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: 7391027] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-417. Tissue: Erythrocyte.
[11]	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.
[12]	"Functional identity of a primer recognition protein as phosphoglycerate kinase." Jindal H.K., Vishwanatha J.K. J. Biol. Chem. 265:6540-6543(1990) [PubMed: 2324090] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Placenta.
[13]	"Hematologically important mutations: molecular abnormalities of phosphoglycerate kinase." Yoshida A. Blood Cells Mol. Dis. 22:265-267(1996) [PubMed: 9075577] [Abstract] Cited for: REVIEW ON VARIANTS.
[14]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196, MASS SPECTROMETRY.
[15]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-243, 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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY. 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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-30; LYS-48; LYS-75; LYS-86; LYS-97; LYS-131; LYS-146; LYS-199; LYS-267; LYS-291; LYS-323 AND LYS-406, MASS SPECTROMETRY.
[20]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"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: 8673469] [Abstract] Cited for: VARIANT PGK1D LYS-191 DEL.
[22]	"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: 8043870] [Abstract] Cited for: VARIANTS PGK1D VAL-164 AND ASN-315.
[23]	"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: 8615693] [Abstract] Cited for: VARIANT PGK1D ALA-252.
[24]	"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: 9744480] [Abstract] Cited for: VARIANT PGK1D VAL-285.
[25]	"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: 2001457] [Abstract] Cited for: VARIANT PGK1D PRO-88.
[26]	"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: 1586722] [Abstract] Cited for: VARIANT PGK1D ARG-316.
[27]	"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: 7391028] [Abstract] Cited for: VARIANT MUNCHEN ASN-268.
[28]	"Structure and function of normal and variant human phosphoglycerate kinase." Huang I.-Y., Fujii H., Yoshida A. Hemoglobin 4:601-609(1980) [PubMed: 7440217] [Abstract] Cited for: VARIANT MUNCHEN ASN-268, VARIANT ASN-352.
[29]	"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: 1547346] [Abstract] Cited for: VARIANT PGK1D VAL-158.
[30]	"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: 6941312] [Abstract] Cited for: VARIANT PGK1D MET-266.
[31]	"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: 6933565] [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.
CR456716 mRNA. Translation: CAG32997.1.
AL049589 Genomic DNA. Translation: CAI42951.1.
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.

SMR

P00558. Positions 5-417.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00558. 23 interactions.

MINT

MINT-1131047.

STRING

P00558.

PTM databases

PhosphoSite

P00558.

Polymorphism databases

DMDM

52788229.

2D gel databases

Aarhus/Ghent-2DPAGE

3308. NEPHGE.

DOSAC-COBS-2DPAGE

P00558.

OGP

P00558.

REPRODUCTION-2DPAGE

IPI00169383.
P00558.

UCD-2DPAGE

P00558.

Proteomic databases

PeptideAtlas

P00558.

PRIDE

P00558.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373316; ENSP00000362413; ENSG00000102144.

GeneID

5230.

KEGG

hsa:5230.

NMPDR

fig|9606.3.peg.33025.

UCSC

uc004ecz.2. human.

Organism-specific databases

CTD

5230.

GeneCards

GC0XP077246.

H-InvDB

HIX0056104.

HGNC

HGNC:8896. PGK1.

HPA

CAB010065.

MIM

300653. phenotype.
311800. gene.

neXtProt

NX_P00558.

Orphanet

713. Phosphoglycerate kinase 1 deficiency.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16829.

GeneTree

ENSGT00390000008820.

HOGENOM

HBG453500.

HOVERGEN

HBG008177.

InParanoid

P00558.

OMA

ASCCAKW.

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_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpress

P00558.

Bgee

P00558.

CleanEx

HS_PGK1.

Genevestigator

P00558.

GermOnline

ENSG00000102144. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.40.50.1270. Phosphoglycerate_kinase_C. 1 hit.
G3DSA:3.40.50.1260. Phosphoglycerate_kinase_N. 1 hit.

KO

K00927.

PANTHER

PTHR11406. PGK. 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

NextBio

20218.

SOURCE

Search...

Entry information

Entry name

PGK1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 143 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.