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Protein

Phosphoglycerate kinase 1

Gene

Pgk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). May play a role in sperm motility.By similarity

Catalytic activityi

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

Pathwayi: glycolysis

This protein is involved in step 2 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm7293), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839)
  2. Phosphoglycerate kinase 2 (Pgk2), Phosphoglycerate kinase 1 (Pgk1)
  3. no protein annotated in this organism
  4. Gamma-enolase (Eno2), Alpha-enolase (Eno1), Beta-enolase (Eno3), Enolase 4 (Eno4)
  5. Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKM (Pkm)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei39SubstrateBy similarity1
Binding sitei123SubstrateBy similarity1
Binding sitei171SubstrateBy similarity1
Binding sitei220ATPBy similarity1
Binding sitei313ATP; via carbonyl oxygenBy similarity1
Binding sitei344ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi373 – 376ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

  • glycolytic process Source: MGI
  • phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.2.3. 3474.
ReactomeiR-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.
SABIO-RKP09411.
UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase 1 (EC:2.7.2.3)
Gene namesi
Name:Pgk1
Synonyms:Pgk-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 12, Chromosome X

Organism-specific databases

MGIiMGI:97555. Pgk1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001458352 – 417Phosphoglycerate kinase 1Add BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineBy similarity1
Modified residuei4PhosphoserineBy similarity1
Modified residuei6N6-succinyllysineCombined sources1
Modified residuei11N6-acetyllysineCombined sources1
Modified residuei48N6-acetyllysine; alternateBy similarity1
Modified residuei48N6-succinyllysine; alternateCombined sources1
Modified residuei75N6-acetyllysineBy similarity1
Modified residuei76PhosphotyrosineCombined sources1
Modified residuei86N6-acetyllysineBy similarity1
Modified residuei91N6-acetyllysineCombined sources1
Modified residuei97N6-acetyllysineBy similarity1
Modified residuei131N6-acetyllysine; alternateBy similarity1
Modified residuei131N6-malonyllysine; alternateBy similarity1
Modified residuei146N6-acetyllysineBy similarity1
Modified residuei191N6-succinyllysineCombined sources1
Modified residuei196PhosphotyrosineBy similarity1
Modified residuei199N6-acetyllysineBy similarity1
Modified residuei203PhosphoserineCombined sources1
Modified residuei267N6-acetyllysineBy similarity1
Modified residuei291N6-acetyllysineCombined sources1
Modified residuei361N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP09411.
MaxQBiP09411.
PaxDbiP09411.
PeptideAtlasiP09411.
PRIDEiP09411.

2D gel databases

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

PTM databases

iPTMnetiP09411.
PhosphoSitePlusiP09411.
SwissPalmiP09411.

Expressioni

Tissue specificityi

Testis, lung, brain, skeletal muscle, liver, intestine, and kidney (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000062070.
CleanExiMM_PGK1.
ExpressionAtlasiP09411. baseline and differential.
GenevisibleiP09411. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi202133. 5 interactors.
DIPiDIP-51710N.
IntActiP09411. 7 interactors.
MINTiMINT-1854650.
STRINGi10090.ENSMUSP00000136544.

Structurei

Secondary structure

1417
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 11Combined sources3
Beta strandi18 – 22Combined sources5
Beta strandi33 – 35Combined sources3
Helixi38 – 52Combined sources15
Beta strandi56 – 61Combined sources6
Turni73 – 75Combined sources3
Helixi79 – 89Combined sources11
Beta strandi93 – 95Combined sources3
Beta strandi99 – 101Combined sources3
Helixi102 – 109Combined sources8
Beta strandi115 – 118Combined sources4
Helixi122 – 124Combined sources3
Turni126 – 129Combined sources4
Beta strandi130 – 133Combined sources4
Beta strandi139 – 141Combined sources3
Helixi144 – 155Combined sources12
Beta strandi159 – 163Combined sources5
Helixi166 – 168Combined sources3
Helixi174 – 177Combined sources4
Beta strandi184 – 186Combined sources3
Helixi188 – 202Combined sources15
Beta strandi206 – 212Combined sources7
Helixi218 – 220Combined sources3
Helixi221 – 228Combined sources8
Beta strandi232 – 236Combined sources5
Helixi238 – 240Combined sources3
Helixi241 – 249Combined sources9
Helixi260 – 263Combined sources4
Helixi266 – 276Combined sources11
Beta strandi279 – 281Combined sources3
Beta strandi284 – 293Combined sources10
Beta strandi298 – 302Combined sources5
Turni303 – 305Combined sources3
Beta strandi312 – 316Combined sources5
Helixi318 – 330Combined sources13
Beta strandi332 – 338Combined sources7
Helixi346 – 348Combined sources3
Helixi350 – 364Combined sources15
Beta strandi368 – 376Combined sources9
Beta strandi389 – 394Combined sources6
Helixi396 – 403Combined sources8
Helixi409 – 412Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4O3FX-ray2.11A1-417[»]
ProteinModelPortaliP09411.
SMRiP09411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 26Substrate bindingBy similarity3
Regioni63 – 66Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the phosphoglycerate kinase family.Curated

Phylogenomic databases

eggNOGiKOG1367. Eukaryota.
COG0126. LUCA.
GeneTreeiENSGT00390000008820.
HOGENOMiHOG000227107.
HOVERGENiHBG008177.
InParanoidiP09411.
KOiK00927.
OMAiIKHCLDH.
OrthoDBiEOG091G08S6.
PhylomeDBiP09411.
TreeFamiTF300489.

Family and domain databases

CDDicd00318. Phosphoglycerate_kinase. 1 hit.
Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase. 1 hit.
InterProiIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC
60 70 80 90 100
LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAAELKSLLG KDVLFLKDCV
110 120 130 140 150
GPEVENACAN PAAGTVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIDAF
160 170 180 190 200
RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA
210 220 230 240 250
LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN
260 270 280 290 300
MEIGTSLYDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ
310 320 330 340 350
ATVASGIPAG WMGLDCGTES SKKYAEAVGR AKQIVWNGPV GVFEWEAFAR
360 370 380 390 400
GTKSLMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL
410
ELLEGKVLPG VDALSNV
Length:417
Mass (Da):44,550
Last modified:May 1, 2007 - v4
Checksum:i5E2EE194FF9D8CEE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56K → N in AAA70267 (PubMed:3542714).Curated1
Sequence conflicti184K → R in BAE26693 (PubMed:16141072).Curated1
Sequence conflicti265I → V in BAE37790 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30339.1.
PIRiA25567.
RefSeqiNP_032854.2. NM_008828.3.
UniGeneiMm.316355.
Mm.336204.
Mm.336205.

Genome annotation databases

EnsembliENSMUST00000081593; ENSMUSP00000080302; ENSMUSG00000062070.
ENSMUST00000085735; ENSMUSP00000136544; ENSMUSG00000066632.
GeneIDi18655.
KEGGimmu:18655.
UCSCiuc009ubo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30339.1.
PIRiA25567.
RefSeqiNP_032854.2. NM_008828.3.
UniGeneiMm.316355.
Mm.336204.
Mm.336205.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4O3FX-ray2.11A1-417[»]
ProteinModelPortaliP09411.
SMRiP09411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202133. 5 interactors.
DIPiDIP-51710N.
IntActiP09411. 7 interactors.
MINTiMINT-1854650.
STRINGi10090.ENSMUSP00000136544.

PTM databases

iPTMnetiP09411.
PhosphoSitePlusiP09411.
SwissPalmiP09411.

2D gel databases

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

Proteomic databases

EPDiP09411.
MaxQBiP09411.
PaxDbiP09411.
PeptideAtlasiP09411.
PRIDEiP09411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081593; ENSMUSP00000080302; ENSMUSG00000062070.
ENSMUST00000085735; ENSMUSP00000136544; ENSMUSG00000066632.
GeneIDi18655.
KEGGimmu:18655.
UCSCiuc009ubo.2. mouse.

Organism-specific databases

CTDi5230.
MGIiMGI:97555. Pgk1.

Phylogenomic databases

eggNOGiKOG1367. Eukaryota.
COG0126. LUCA.
GeneTreeiENSGT00390000008820.
HOGENOMiHOG000227107.
HOVERGENiHBG008177.
InParanoidiP09411.
KOiK00927.
OMAiIKHCLDH.
OrthoDBiEOG091G08S6.
PhylomeDBiP09411.
TreeFamiTF300489.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.
BRENDAi2.7.2.3. 3474.
ReactomeiR-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.
SABIO-RKP09411.

Miscellaneous databases

PROiP09411.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000062070.
CleanExiMM_PGK1.
ExpressionAtlasiP09411. baseline and differential.
GenevisibleiP09411. MM.

Family and domain databases

CDDicd00318. Phosphoglycerate_kinase. 1 hit.
Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase. 1 hit.
InterProiIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGK1_MOUSE
AccessioniPrimary (citable) accession number: P09411
Secondary accession number(s): Q3TPE6, Q3UKV8, Q5XJE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 1, 2007
Last modified: November 2, 2016
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.