UniProt Accession

 PGK1_HUMAN; P00558; A8K4W6; Q5J7W1; Q6IBT6; Q8NI87 

Genbank Protein ID

 V00572; L00160; M11968; M11958; M11959; M11960; M11961; M11962; M11963; M11964; M11965; M11966; M11967; AY423725; AB062432; AK291081; AK312280; CR456716; AL049589; CH471104; BC023234; BC103752; BC104837; BC113568; M34017 

Genbank Nucleotide ID

 CAA23835.1; AAA60078.1; AAA60079.1; AAA60079.1; AAA60079.1; AAA60079.1; AAA60079.1; AAA60079.1; AAA60079.1; AAA60079.1; AAA60079.1; AAA60079.1; AAA60079.1; AAS00488.1; BAB93495.1; BAF83770.1; BAG35209.1; CAG32997.1; CAI42951.1; EAW98604.1; AAH23234.1; AAI03753.1; AAI04838.1; AAI13569.1; AAA60103.1 

Protein Name

 Phosphoglycerate kinase 1 

Protein Synonyms/Alias

 Cell migration-inducing gene 10 protein; Primer recognition protein 2; PRP 2 

Gene Name

 PGK1 

Gene Synonyms/Alias

 PGKA; MIG10; OK/SW-cl.110 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MSLSNKLTLDKLD	ubiquitination	[1]
11	SNKLTLDKLDVKGKR	acetylation	[2]
11	SNKLTLDKLDVKGKR	ubiquitination	[1, 3]
15	TLDKLDVKGKRVVMR	ubiquitination	[1]
17	DKLDVKGKRVVMRVD	ubiquitination	[1]
30	VDFNVPMKNNQITNN	acetylation	[2]
30	VDFNVPMKNNQITNN	ubiquitination	[1, 3, 4, 5, 6]
41	ITNNQRIKAAVPSIK	ubiquitination	[1]
48	KAAVPSIKFCLDNGA	acetylation	[2]
48	KAAVPSIKFCLDNGA	ubiquitination	[1, 3]
75	DGVPMPDKYSLEPVA	acetylation	[2]
75	DGVPMPDKYSLEPVA	ubiquitination	[1, 3]
86	EPVAVELKSLLGKDV	acetylation	[2]
86	EPVAVELKSLLGKDV	ubiquitination	[3, 4, 6]
91	ELKSLLGKDVLFLKD	acetylation	[2]
91	ELKSLLGKDVLFLKD	ubiquitination	[1, 3, 4, 6]
97	GKDVLFLKDCVGPEV	acetylation	[2]
97	GKDVLFLKDCVGPEV	ubiquitination	[1, 3, 5]
106	CVGPEVEKACANPAA	ubiquitination	[1]
131	FHVEEEGKGKDASGN	acetylation	[2]
131	FHVEEEGKGKDASGN	malonylation	[7]
131	FHVEEEGKGKDASGN	ubiquitination	[1]
141	DASGNKVKAEPAKIE	ubiquitination	[1, 4]
146	KVKAEPAKIEAFRAS	acetylation	[2]
146	KVKAEPAKIEAFRAS	ubiquitination	[1, 3]
156	AFRASLSKLGDVYVN	acetylation	[2]
156	AFRASLSKLGDVYVN	ubiquitination	[1, 3, 4, 5]
184	VGVNLPQKAGGFLMK	ubiquitination	[1, 3, 5]
191	KAGGFLMKKELNYFA	ubiquitination	[1]
192	AGGFLMKKELNYFAK	ubiquitination	[1, 3]
199	KELNYFAKALESPER	acetylation	[2]
199	KELNYFAKALESPER	ubiquitination	[1, 3, 4, 6]
216	LAILGGAKVADKIQL	ubiquitination	[1, 3, 4, 6]
220	GGAKVADKIQLINNM	acetylation	[8]
220	GGAKVADKIQLINNM	ubiquitination	[1, 3, 4, 6]
246	GMAFTFLKVLNNMEI	ubiquitination	[4]
264	LFDEEGAKIVKDLMS	ubiquitination	[1, 4, 6, 9]
267	EEGAKIVKDLMSKAE	acetylation	[2]
267	EEGAKIVKDLMSKAE	ubiquitination	[1, 3]
272	IVKDLMSKAEKNGVK	ubiquitination	[1]
279	KAEKNGVKITLPVDF	ubiquitination	[1]
291	VDFVTADKFDENAKT	acetylation	[2]
291	VDFVTADKFDENAKT	ubiquitination	[1, 3, 4]
322	DCGPESSKKYAEAVT	ubiquitination	[1]
323	CGPESSKKYAEAVTR	acetylation	[2]
323	CGPESSKKYAEAVTR	ubiquitination	[1]
332	AEAVTRAKQIVWNGP	ubiquitination	[4]
353	EAFARGTKALMDEVV	ubiquitination	[1, 6]
361	ALMDEVVKATSRGCI	ubiquitination	[1, 3, 4, 5]
382	DTATCCAKWNTEDKV	ubiquitination	[1]
388	AKWNTEDKVSHVSTG	ubiquitination	[1]
406	SLELLEGKVLPGVDA	acetylation	[2]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] 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 BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y.
 Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. [PMID: 21908771]
 [8] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [9] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048] 

Functional Description

 In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). 

Sequence Annotation

 NP_BIND 373 376 ATP.
 REGION 24 26 Substrate binding.
 REGION 63 66 Substrate binding.
 BINDING 39 39 Substrate.
 BINDING 123 123 Substrate.
 BINDING 171 171 Substrate.
 BINDING 220 220 ATP.
 BINDING 313 313 ATP; via carbonyl oxygen.
 BINDING 344 344 ATP.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 11 11 N6-acetyllysine.
 MOD_RES 48 48 N6-acetyllysine.
 MOD_RES 75 75 N6-acetyllysine.
 MOD_RES 76 76 Phosphotyrosine (By similarity).
 MOD_RES 86 86 N6-acetyllysine.
 MOD_RES 97 97 N6-acetyllysine.
 MOD_RES 131 131 N6-acetyllysine; alternate.
 MOD_RES 131 131 N6-malonyllysine; alternate.
 MOD_RES 146 146 N6-acetyllysine.
 MOD_RES 196 196 Phosphotyrosine.
 MOD_RES 199 199 N6-acetyllysine.
 MOD_RES 203 203 Phosphoserine.
 MOD_RES 267 267 N6-acetyllysine.
 MOD_RES 291 291 N6-acetyllysine.
 MOD_RES 390 390 Phosphoserine (By similarity).  

Keyword

 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Glycolysis; Hereditary hemolytic anemia; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 417 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; ISS:UniProtKB.
 GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
 GO:0006094; P:gluconeogenesis; TAS:Reactome.
 GO:0006096; P:glycolysis; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 

Interpro

 IPR001576; Phosphoglycerate_kinase.
 IPR015901; Phosphoglycerate_kinase_C.
 IPR015911; Phosphoglycerate_kinase_CS.
 IPR015824; Phosphoglycerate_kinase_N. 

Pfam

 PF00162; PGK 

SMART

  

PROSITE

 PS00111; PGLYCERATE_KINASE 

PRINTS

 PR00477; PHGLYCKINASE.