Reviewed, UniProtKB/Swiss-Prot P09411 (PGK1_MOUSE)

Names and origin

Protein names

Recommended name:
    Phosphoglycerate kinase 1
    EC=2.7.2.3

Gene names

Name:	Pgk1
Synonyms:	Pgk-1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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)

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 By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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 By similarity
	Chain	2 – 417	416	Phosphoglycerate kinase 1		PRO_0000145835
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	11	1	N6-acetyllysine By similarity
	Modified residue	30	1	N6-acetyllysine By similarity
	Modified residue	48	1	N6-acetyllysine By similarity
	Modified residue	75	1	N6-acetyllysine By similarity
	Modified residue	76	1	Phosphotyrosine Ref.11
	Modified residue	86	1	N6-acetyllysine By similarity
	Modified residue	97	1	N6-acetyllysine By similarity
	Modified residue	131	1	N6-acetyllysine By similarity
	Modified residue	136	1	Phosphoserine By similarity
	Modified residue	146	1	N6-acetyllysine By similarity
	Modified residue	196	1	Phosphotyrosine Ref.11
	Modified residue	199	1	N6-acetyllysine By similarity
	Modified residue	203	1	Phosphoserine Ref.12 Ref.13 Ref.14
	Modified residue	243	1	Phosphothreonine By similarity
	Modified residue	267	1	N6-acetyllysine By similarity
	Modified residue	291	1	N6-acetyllysine By similarity
	Modified residue	323	1	N6-acetyllysine By similarity
	Modified residue	390	1	Phosphoserine Ref.10
	Modified residue	406	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	56	1	K → N in AAA70267. Ref.1
	Sequence conflict	184	1	K → R in BAE26693. Ref.2
	Sequence conflict	265	1	I → V in BAE37790. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P09411-1 [UniParc]. Last modified May 1, 2007. Version 4. Checksum: 5E2EE194FF9D8CEE	FASTA	417	44,550
	10 20 30 40 50 60 MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL 70 80 90 100 110 120 MSHLGRPDGV PMPDKYSLEP VAAELKSLLG KDVLFLKDCV GPEVENACAN PAAGTVILLE 130 140 150 160 170 180 NLRFHVEEEG KGKDASGNKV KAEPAKIDAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN 190 200 210 220 230 240 LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM 250 260 270 280 290 300 AFTFLKVLNN MEIGTSLYDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ 310 320 330 340 350 360 ATVASGIPAG WMGLDCGTES SKKYAEAVGR AKQIVWNGPV GVFEWEAFAR GTKSLMDEVV 370 380 390 400 410 KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of a cDNA clone containing the entire coding region for mouse X-chromosome-linked phosphoglycerate kinase." Mori N., Singer-Sam J., Lee C.-Y., Riggs A.D. Gene 45:275-280(1986) [PubMed: 3542714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Eye and Placenta.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"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]. Strain: 129 and C57BL/6. Tissue: Brain and Mammary tumor.
[5]	"Cloning and expression of the mouse pgk-1 gene and the nucleotide sequence of its promoter." Adra C.N., Boer P.H., McBurney M.W. Gene 60:65-74(1987) [PubMed: 3440520] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[6]	"Selective activation of testis-specific genes in cultured rat spermatogenic cells." Tamaru M., Nagao Y., Taira M., Tatibana M., Masamune Y., Nakanishi Y. Biochim. Biophys. Acta 1049:331-338(1990) [PubMed: 2166582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[7]	"Polymorphisms in the coding and noncoding regions of murine Pgk-1 alleles." Boer P.H., Potten H., Adra C.N., Jardine K., Mullhofer G., McBurney M.W. Biochem. Genet. 28:299-308(1990) [PubMed: 1975492] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[8]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 23-30; 76-86; 98-123; 157-184; 193-216; 247-264; 280-297; 333-350 AND 389-417, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[9]	"Evolutionary conservation of the substrate-binding cleft of phosphoglycerate kinases." Mori N., Singer-Sam J., Riggs A.D. FEBS Lett. 204:313-317(1986) [PubMed: 3525226] [Abstract] Cited for: DISCUSSION OF SEQUENCE.
[10]	"Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed: 15648052] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, MASS SPECTROMETRY. Tissue: Brain.
[11]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76 AND TYR-196, MASS SPECTROMETRY. Tissue: Brain.
[12]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY. Tissue: Brain cortex.
[13]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY.
[14]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M15668 mRNA. Translation: AAA70267.1. AK145846 mRNA. Translation: BAE26693.1. AK167710 mRNA. Translation: BAE39754.1. AK167459 mRNA. Translation: BAE39544.1. AK167441 mRNA. Translation: BAE39527.1. AK133877 mRNA. Translation: BAE21906.1. AK164440 mRNA. Translation: BAE37790.1. BX469914 Genomic DNA. Translation: CAM17784.1. BC083355 mRNA. Translation: AAH83355.1. BC108372 mRNA. Translation: AAI08373.1. M18735 Genomic DNA. Translation: AAA39919.1. X55309 Genomic DNA. Translation: CAA39013.1. X15339 Genomic DNA. Translation: CAA33391.1.
IPI	IPI00555069.
PIR	A25567.
RefSeq	NP_032854.2.
UniGene	Mm.336204 Mm.336205
3D structure databases
SMR	P09411. Positions 2-417.
ModBase	Search...
Protein-protein interaction databases
STRING	P09411.
PTM databases
PhosphoSite	P09411.
2-D gel databases
SWISS-2DPAGE	P09411.
REPRODUCTION-2DPAGE	P09411.
Proteomic databases
PRIDE	P09411.
Genome annotation databases
Ensembl	ENSMUST00000081593; ENSMUSP00000080302; ENSMUSG00000062070; Mus musculus. [Genome view]
GeneID	18655.
KEGG	mmu:18655.
Organism-specific databases
CTD	18655.
MGI	MGI:97555. Pgk1.
Phylogenomic databases
eggNOG	roNOG09572.
HOGENOM	HBG453500.
HOVERGEN	P09411.
InParanoid	P09411.
OMA	DHGAKSV.
OrthoDB	EOG94QWMF.
PhylomeDB	P09411.
Enzyme and pathway databases
BRENDA	2.7.2.3. 244.
Gene expression databases
Bgee	P09411.
CleanEx	MM_PGK1.
Genevestigator	P09411.
GermOnline	ENSMUSG00000062070. Mus musculus. ENSMUSG00000066632. Mus musculus. ENSMUSG00000069008. Mus musculus.
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.
PANTHER	PTHR11406. PGK. 1 hit.
Pfam	PF00162. PGK. 1 hit. [Graphical view]
PRINTS	PR00477. PHGLYCKINASE.
PROSITE	PS00111. PGLYCERATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	294662.
SOURCE	Search...

Entry information

Entry name

PGK1_MOUSE

Accession

Primary (citable) accession number: P09411
Secondary accession number(s): Q3TPE6, Q3UKV8, Q5XJE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	May 1, 2007
Last modified:	January 19, 2010
This is version 96 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)