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P09411 (PGK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate kinase 1

EC=2.7.2.3
Gene names
Name:Pgk1
Synonyms:Pgk-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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)

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 By similarity. HAMAP-Rule MF_00145

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00145.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 417416Phosphoglycerate kinase 1 HAMAP-Rule MF_00145
PRO_0000145835

Regions

Nucleotide binding373 – 3764ATP By similarity
Region24 – 263Substrate binding By similarity
Region63 – 664Substrate binding By similarity

Sites

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

Amino acid modifications

Modified residue21N-acetylserine Ref.13
Modified residue61N6-succinyllysine Ref.13
Modified residue111N6-acetyllysine Ref.13
Modified residue481N6-acetyllysine; alternate By similarity
Modified residue481N6-succinyllysine; alternate Ref.13
Modified residue751N6-acetyllysine By similarity
Modified residue761Phosphotyrosine Ref.11
Modified residue861N6-acetyllysine By similarity
Modified residue911N6-acetyllysine Ref.13
Modified residue971N6-acetyllysine By similarity
Modified residue1311N6-acetyllysine; alternate By similarity
Modified residue1311N6-malonyllysine; alternate By similarity
Modified residue1461N6-acetyllysine By similarity
Modified residue1911N6-succinyllysine Ref.13
Modified residue1961Phosphotyrosine By similarity
Modified residue1991N6-acetyllysine By similarity
Modified residue2031Phosphoserine Ref.10 Ref.12
Modified residue2671N6-acetyllysine By similarity
Modified residue2911N6-acetyllysine Ref.13
Modified residue3611N6-acetyllysine Ref.13

Experimental info

Sequence conflict561K → N in AAA70267. Ref.1
Sequence conflict1841K → R in BAE26693. Ref.2
Sequence conflict2651I → V in BAE37790. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P09411 [UniParc].

Last modified May 1, 2007. Version 4.
Checksum: 5E2EE194FF9D8CEE

FASTA41744,550
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
Cited for: DISCUSSION OF SEQUENCE.
[10]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[13]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-11; LYS-91; LYS-291 AND LYS-361, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-48 AND LYS-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
+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.
PIRA25567.
RefSeqNP_032854.2. NM_008828.3.
UniGeneMm.336204.
Mm.336205.

3D structure databases

ProteinModelPortalP09411.
SMRP09411. Positions 5-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202133. 2 interactions.
IntActP09411. 7 interactions.
MINTMINT-1854650.

PTM databases

PhosphoSiteP09411.

2D gel databases

COMPLUYEAST-2DPAGEP09411.
REPRODUCTION-2DPAGEIPI00555069.
P09411.
SWISS-2DPAGEP09411.

Proteomic databases

PaxDbP09411.
PRIDEP09411.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081593; ENSMUSP00000080302; ENSMUSG00000062070.
ENSMUST00000085735; ENSMUSP00000136544; ENSMUSG00000066632.
GeneID18655.
KEGGmmu:18655.
UCSCuc009ubo.1. mouse.

Organism-specific databases

CTD5230.
MGIMGI:97555. Pgk1.

Phylogenomic databases

eggNOGCOG0126.
GeneTreeENSGT00390000008820.
HOGENOMHOG000227107.
HOVERGENHBG008177.
InParanoidP09411.
KOK00927.
OMANFANGTK.
OrthoDBEOG74R1QN.
PhylomeDBP09411.
TreeFamTF300489.

Enzyme and pathway databases

SABIO-RKP09411.
UniPathwayUPA00109; UER00185.

Gene expression databases

BgeeP09411.
CleanExMM_PGK1.
GenevestigatorP09411.

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. mouse.
NextBio294662.
PROP09411.
SOURCESearch...

Entry information

Entry namePGK1_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot