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Protein

Phosphoglycerate mutase 1

Gene

Pgam1

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

Functioni

Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.
2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Tele-phosphohistidine intermediateBy similarity
Binding sitei62 – 621SubstrateBy similarity
Active sitei89 – 891Proton donor/acceptorBy similarity
Binding sitei100 – 1001SubstrateBy similarity
Sitei186 – 1861Transition state stabilizerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BRENDAi5.4.2.11. 3474.
ReactomeiR-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.
SABIO-RKQ9DBJ1.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate mutase 1 (EC:3.1.3.13, EC:5.4.2.11, EC:5.4.2.4)
Alternative name(s):
BPG-dependent PGAM 1
Phosphoglycerate mutase isozyme B
Short name:
PGAM-B
Gene namesi
Name:Pgam1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:97552. Pgam1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • myelin sheath Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 254253Phosphoglycerate mutase 1PRO_0000179826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei26 – 261PhosphotyrosineCombined sources
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei106 – 1061N6-acetyllysineCombined sources
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei251 – 2511N6-acetyllysine; alternateBy similarity
Modified residuei251 – 2511N6-succinyllysine; alternateCombined sources
Modified residuei253 – 2531N6-acetyllysineBy similarity
Modified residuei254 – 2541N6-acetyllysineBy similarity

Post-translational modificationi

Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition. Acetylation increases catalytic activity. Under glucose restriction SIRT1 levels dramatically increase and it deacetylates the enzyme (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9DBJ1.
MaxQBiQ9DBJ1.
PaxDbiQ9DBJ1.
PRIDEiQ9DBJ1.

2D gel databases

COMPLUYEAST-2DPAGEQ9DBJ1.
REPRODUCTION-2DPAGEIPI00457898.
Q9DBJ1.

PTM databases

iPTMnetiQ9DBJ1.
PhosphoSiteiQ9DBJ1.
SwissPalmiQ9DBJ1.

Expressioni

Gene expression databases

BgeeiQ9DBJ1.
CleanExiMM_PGAM1.
ExpressionAtlasiQ9DBJ1. baseline and differential.
GenevisibleiQ9DBJ1. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202130. 2 interactions.
IntActiQ9DBJ1. 7 interactions.
MINTiMINT-1854824.
STRINGi10090.ENSMUSP00000011896.

Structurei

3D structure databases

ProteinModelPortaliQ9DBJ1.
SMRiQ9DBJ1. Positions 2-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 178Substrate bindingBy similarity
Regioni23 – 242Substrate bindingBy similarity
Regioni89 – 924Substrate bindingBy similarity
Regioni116 – 1172Substrate bindingBy similarity
Regioni187 – 1882Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 13110Pro-rich

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0235. Eukaryota.
COG0588. LUCA.
GeneTreeiENSGT00390000016700.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiQ9DBJ1.
KOiK01834.
OMAiVPACECL.
OrthoDBiEOG7XM2ZV.
PhylomeDBiQ9DBJ1.
TreeFamiTF300007.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 2 hits.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9DBJ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY
60 70 80 90 100
EFDICFTSVQ KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK
110 120 130 140 150
AETAAKHGEA QVKIWRRSYD VPPPPMEPDH PFYSNISKDR RYADLTEDQL
160 170 180 190 200
PSCESLKDTI ARALPFWNEE IVPQIKEGKR VLIAAHGNSL RGIVKHLEGL
210 220 230 240 250
SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR KAMEAVAAQG

KVKK
Length:254
Mass (Da):28,832
Last modified:January 23, 2007 - v3
Checksum:i6DC09A3BEBB22409
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421G → R in AAG13955 (Ref. 1) Curated
Sequence conflicti65 – 651R → Q in AAG13955 (Ref. 1) Curated
Sequence conflicti85 – 851W → G in BAB26576 (PubMed:16141072).Curated
Sequence conflicti152 – 1521S → F in AAG13955 (Ref. 1) Curated
Sequence conflicti176 – 1761K → I in AAG13955 (Ref. 1) Curated
Sequence conflicti195 – 1973KHL → MHV in AAG13955 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF283667 mRNA. Translation: AAG13955.1.
AK004921 mRNA. Translation: BAB23672.1.
AK009905 mRNA. Translation: BAB26576.1.
BC002241 mRNA. Translation: AAH02241.1.
BC005661 mRNA. Translation: AAH05661.1.
BC066844 mRNA. Translation: AAH66844.1.
BC083090 mRNA. Translation: AAH83090.1.
CCDSiCCDS29815.1.
RefSeqiNP_075907.2. NM_023418.2.
UniGeneiMm.16783.
Mm.391589.

Genome annotation databases

EnsembliENSMUST00000011896; ENSMUSP00000011896; ENSMUSG00000011752.
GeneIDi18648.
KEGGimmu:18648.
UCSCiuc008hml.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF283667 mRNA. Translation: AAG13955.1.
AK004921 mRNA. Translation: BAB23672.1.
AK009905 mRNA. Translation: BAB26576.1.
BC002241 mRNA. Translation: AAH02241.1.
BC005661 mRNA. Translation: AAH05661.1.
BC066844 mRNA. Translation: AAH66844.1.
BC083090 mRNA. Translation: AAH83090.1.
CCDSiCCDS29815.1.
RefSeqiNP_075907.2. NM_023418.2.
UniGeneiMm.16783.
Mm.391589.

3D structure databases

ProteinModelPortaliQ9DBJ1.
SMRiQ9DBJ1. Positions 2-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202130. 2 interactions.
IntActiQ9DBJ1. 7 interactions.
MINTiMINT-1854824.
STRINGi10090.ENSMUSP00000011896.

PTM databases

iPTMnetiQ9DBJ1.
PhosphoSiteiQ9DBJ1.
SwissPalmiQ9DBJ1.

2D gel databases

COMPLUYEAST-2DPAGEQ9DBJ1.
REPRODUCTION-2DPAGEIPI00457898.
Q9DBJ1.

Proteomic databases

EPDiQ9DBJ1.
MaxQBiQ9DBJ1.
PaxDbiQ9DBJ1.
PRIDEiQ9DBJ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000011896; ENSMUSP00000011896; ENSMUSG00000011752.
GeneIDi18648.
KEGGimmu:18648.
UCSCiuc008hml.1. mouse.

Organism-specific databases

CTDi5223.
MGIiMGI:97552. Pgam1.

Phylogenomic databases

eggNOGiKOG0235. Eukaryota.
COG0588. LUCA.
GeneTreeiENSGT00390000016700.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiQ9DBJ1.
KOiK01834.
OMAiVPACECL.
OrthoDBiEOG7XM2ZV.
PhylomeDBiQ9DBJ1.
TreeFamiTF300007.

Enzyme and pathway databases

BRENDAi5.4.2.11. 3474.
ReactomeiR-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.
SABIO-RKQ9DBJ1.

Miscellaneous databases

PROiQ9DBJ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBJ1.
CleanExiMM_PGAM1.
ExpressionAtlasiQ9DBJ1. baseline and differential.
GenevisibleiQ9DBJ1. MM.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 2 hits.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Yu L.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver and Tongue.
  3. "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: C57BL/6J.
    Tissue: Embryo and Kidney.
  4. Lubec G., Klug S., Kang S.U., Yang J.W., Zigmond M.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 11-39; 47-61; 91-100; 118-138; 163-176; 181-191; 223-240 AND 242-251, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  5. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "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-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "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 LYS-106, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.

Entry informationi

Entry nameiPGAM1_MOUSE
AccessioniPrimary (citable) accession number: Q9DBJ1
Secondary accession number(s): Q9D6W0, Q9ERT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.