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P00558 (PGK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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). HAMAP-Rule MF_00145

Catalytic activity

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. HAMAP-Rule MF_00145

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. HAMAP-Rule MF_00145

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00145.

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.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.34 Ref.35 Ref.36

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GAPDHP044062EBI-709599,EBI-354056

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12 Ref.24
Chain2 – 417416Phosphoglycerate kinase 1 HAMAP-Rule MF_00145
PRO_0000145831

Regions

Nucleotide binding373 – 3764ATP HAMAP-Rule MF_00145
Region24 – 263Substrate binding HAMAP-Rule MF_00145
Region63 – 664Substrate binding HAMAP-Rule MF_00145

Sites

Binding site391Substrate
Binding site1231Substrate
Binding site1711Substrate
Binding site2201ATP
Binding site3131ATP; via carbonyl oxygen
Binding site3441ATP

Amino acid modifications

Modified residue21N-acetylserine Ref.24
Modified residue61N6-succinyllysine By similarity
Modified residue111N6-acetyllysine Ref.19
Modified residue481N6-acetyllysine; alternate Ref.19
Modified residue481N6-succinyllysine; alternate By similarity
Modified residue751N6-acetyllysine Ref.19
Modified residue761Phosphotyrosine By similarity
Modified residue861N6-acetyllysine Ref.19
Modified residue911N6-acetyllysine By similarity
Modified residue971N6-acetyllysine Ref.19
Modified residue1311N6-acetyllysine; alternate Ref.19
Modified residue1311N6-malonyllysine; alternate Ref.22
Modified residue1461N6-acetyllysine Ref.19
Modified residue1911N6-succinyllysine By similarity
Modified residue1961Phosphotyrosine Ref.16
Modified residue1991N6-acetyllysine Ref.19
Modified residue2031Phosphoserine Ref.17 Ref.20 Ref.23
Modified residue2671N6-acetyllysine Ref.19
Modified residue2911N6-acetyllysine Ref.19
Modified residue3611N6-acetyllysine By similarity

Natural variations

Natural variant881L → P in PGK1D; with congenital non-spherocytic anemia; variant Matsue. Ref.30
VAR_006076
Natural variant1581G → V in PGK1D; with chronic hemolytic anemia; variant Shizuoka. Ref.34
VAR_006077
Natural variant1641D → V in PGK1D; with chronic hemolytic anemia and mental retardation; variant Amiens. Ref.27
VAR_006078
Natural variant1911Missing in PGK1D; with chronic hemolytic anemia; variant Alabama. Ref.26
VAR_006079
Natural variant2061R → P in PGK1D; with chronic hemolytic anemia; variant Uppsala. Ref.36
VAR_006080
Natural variant2521E → A in PGK1D; with chronic hemolytic anemia; variant Antwerp. Ref.28
VAR_006081
Natural variant2661V → M in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo. Ref.35
VAR_006082
Natural variant2681D → N in Munchen; 21% of activity. Ref.32 Ref.33
VAR_006083
Natural variant2851D → V in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity. Ref.29
VAR_006084
Natural variant3151D → N in PGK1D; with rhabdomyolysis; variant Creteil. Ref.27
VAR_006085
Natural variant3161C → R in PGK1D; with chronic hemolytic anemia; variant Michigan. Ref.31
VAR_006086
Natural variant3521T → N. Ref.33
VAR_006087

Experimental info

Sequence conflict391Missing AA sequence Ref.12
Sequence conflict3701I → T in CAG32997. Ref.6

Secondary structure

......................................................................................... 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00558 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B5DFC7B5FA01767C

FASTA41744,615
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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 expand/collapse EMBL AC list , 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.
PIRKIHUG. I59050.
RefSeqNP_000282.1. NM_000291.3.
UniGeneHs.78771.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WZBX-ray1.47A2-417[»]
2WZCX-ray1.50A2-417[»]
2WZDX-ray1.56A1-417[»]
2X13X-ray1.74A2-417[»]
2X14X-ray1.90A2-417[»]
2X15X-ray2.10A2-417[»]
2XE6X-ray1.74A1-417[»]
2XE7X-ray2.20A1-417[»]
2XE8X-ray1.79A1-417[»]
2Y3IX-ray2.90A/D1-416[»]
2YBEX-ray2.00A1-417[»]
2ZGVX-ray2.00A1-417[»]
3C39X-ray1.85A/B1-417[»]
3C3AX-ray2.30A/B1-417[»]
3C3BX-ray1.80A/B1-417[»]
3C3CX-ray2.40A/B1-417[»]
4AXXX-ray1.74A1-417[»]
ProteinModelPortalP00558.
SMRP00558. Positions 5-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111251. 49 interactions.
IntActP00558. 29 interactions.
MINTMINT-1131047.
STRING9606.ENSP00000362413.

Chemistry

BindingDBP00558.
ChEMBLCHEMBL2096677.

PTM databases

PhosphoSiteP00558.

Polymorphism databases

DMDM52788229.

2D gel databases

DOSAC-COBS-2DPAGEP00558.
OGPP00558.
REPRODUCTION-2DPAGEIPI00169383.
P00558.
UCD-2DPAGEP00558.

Proteomic databases

PaxDbP00558.
PeptideAtlasP00558.
PRIDEP00558.

Protocols and materials databases

DNASU5230.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373316; ENSP00000362413; ENSG00000102144.
ENST00000597340; ENSP00000472461; ENSG00000269666.
GeneID5230.
KEGGhsa:5230.
UCSCuc004ecz.4. human.

Organism-specific databases

CTD5230.
GeneCardsGC0XP077246.
HGNCHGNC:8896. PGK1.
HPACAB010065.
HPA045385.
MIM300653. phenotype.
311800. gene.
neXtProtNX_P00558.
Orphanet713. Glycogen storage disease due to phosphoglycerate kinase 1 deficiency.
PharmGKBPA33234.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
HOVERGENHBG008177.
InParanoidP00558.
KOK00927.
OMANFANGTK.
PhylomeDBP00558.
TreeFamTF300489.

Enzyme and pathway databases

BioCycMetaCyc:HS02359-MONOMER.
BRENDA2.7.2.3. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP00558.
UniPathwayUPA00109; UER00185.

Gene expression databases

ArrayExpressP00558.
BgeeP00558.
CleanExHS_PGK1.
GenevestigatorP00558.

Family and domain databases

Gene3D3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPMF_00145. Phosphoglyc_kinase.
InterProIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERPTHR11406. PTHR11406. 1 hit.
PfamPF00162. PGK. 1 hit.
[Graphical view]
PIRSFPIRSF000724. Pgk. 1 hit.
PRINTSPR00477. PHGLYCKINASE.
SUPFAMSSF53748. SSF53748. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPGK1. human.
EvolutionaryTraceP00558.
GeneWikiPGK1.
GenomeRNAi5230.
NextBio20218.
PROP00558.
SOURCESearch...

Entry information

Entry namePGK1_HUMAN
AccessionPrimary (citable) accession number: P00558
Secondary accession number(s): A8K4W6 expand/collapse secondary AC list , Q5J7W1, Q6IBT6, Q8NI87
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM