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Protein

Phosphoglucomutase-2

Gene

PGM2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. May also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. Has low glucose 1,6-bisphosphate synthase activity.1 Publication

Catalytic activityi

Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate.
2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-alpha-D-ribose 5-phosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Kineticsi

  1. KM=45.7 µM for alpha-D-ribose 1-phosphate1 Publication
  2. KM=4.1 µM for 2-deoxy-alpha-D-ribose 1-phosphate1 Publication
  3. KM=114 µM for alpha-D-glucose 1-phosphate1 Publication
  1. Vmax=104.3 µmol/min/mg enzyme with alpha-D-ribose 1-phosphate as substrate1 Publication
  2. Vmax=20.8 µmol/min/mg enzyme with 2-deoxy-alpha-D-ribose 1-phosphate as substrate1 Publication
  3. Vmax=22.8 µmol/min/mg enzyme with alpha-D-glucose 1-phosphate as substrate1 Publication

Pathwayi: 2-deoxy-D-ribose 1-phosphate degradation

This protein is involved in step 1 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Phosphoglucomutase-2 (PGM2)
  2. Deoxyribose-phosphate aldolase (DERA)
This subpathway is part of the pathway 2-deoxy-D-ribose 1-phosphate degradation, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate, the pathway 2-deoxy-D-ribose 1-phosphate degradation and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei59SubstrateBy similarity1
Binding sitei63SubstrateBy similarity1
Active sitei165Phosphoserine intermediateBy similarity1
Metal bindingi165Magnesium; via phosphate groupBy similarity1
Metal bindingi322MagnesiumBy similarity1
Metal bindingi324MagnesiumBy similarity1
Metal bindingi326MagnesiumBy similarity1
Binding sitei400SubstrateBy similarity1
Binding sitei438SubstrateBy similarity1

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphoglucomutase activity Source: Reactome
  • phosphopentomutase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS09924-MONOMER.
ZFISH:HS09924-MONOMER.
ReactomeiR-HSA-3322077. Glycogen synthesis.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-70221. Glycogen breakdown (glycogenolysis).
R-HSA-70370. Galactose catabolism.
R-HSA-71336. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKQ96G03.
UniPathwayiUPA00002; UER00467.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucomutase-2 (EC:5.4.2.2)
Short name:
PGM 2
Alternative name(s):
Glucose phosphomutase 2
Phosphodeoxyribomutase
Phosphopentomutase (EC:5.4.2.7)
Gene namesi
Name:PGM2
ORF Names:MSTP006
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:8906. PGM2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000169299.
PharmGKBiPA33243.

Polymorphism and mutation databases

BioMutaiPGM2.
DMDMi116242708.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001477812 – 612Phosphoglucomutase-2Add BLAST611

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei165PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ96G03.
MaxQBiQ96G03.
PaxDbiQ96G03.
PeptideAtlasiQ96G03.
PRIDEiQ96G03.

PTM databases

iPTMnetiQ96G03.
PhosphoSitePlusiQ96G03.
SwissPalmiQ96G03.

Expressioni

Gene expression databases

BgeeiENSG00000169299.
CleanExiHS_PGM2.
ExpressionAtlasiQ96G03. baseline and differential.
GenevisibleiQ96G03. HS.

Organism-specific databases

HPAiHPA040676.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPB1P047922EBI-4399372,EBI-352682
TINF2Q9BSI42EBI-4399372,EBI-717399

Protein-protein interaction databases

BioGridi120564. 14 interactors.
IntActiQ96G03. 5 interactors.
STRINGi9606.ENSP00000371393.

Structurei

3D structure databases

ProteinModelPortaliQ96G03.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni165 – 166Substrate bindingBy similarity2
Regioni326 – 327Substrate bindingBy similarity2
Regioni424 – 426Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiKOG1220. Eukaryota.
COG1109. LUCA.
GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
HOVERGENiHBG056917.
InParanoidiQ96G03.
KOiK15779.
OMAiPLLHDPY.
OrthoDBiEOG091G040C.
PhylomeDBiQ96G03.
TreeFamiTF300692.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96G03-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAPEGSGLG EDARLDQETA QWLRWDKNSL TLEAVKRLIA EGNKEELRKC
60 70 80 90 100
FGARMEFGTA GLRAAMGPGI SRMNDLTIIQ TTQGFCRYLE KQFSDLKQKG
110 120 130 140 150
IVISFDARAH PSSGGSSRRF ARLAATTFIS QGIPVYLFSD ITPTPFVPFT
160 170 180 190 200
VSHLKLCAGI MITASHNPKQ DNGYKVYWDN GAQIISPHDK GISQAIEENL
210 220 230 240 250
EPWPQAWDDS LIDSSPLLHN PSASINNDYF EDLKKYCFHR SVNRETKVKF
260 270 280 290 300
VHTSVHGVGH SFVQSAFKAF DLVPPEAVPE QKDPDPEFPT VKYPNPEEGK
310 320 330 340 350
GVLTLSFALA DKTKARIVLA NDPDADRLAV AEKQDSGEWR VFSGNELGAL
360 370 380 390 400
LGWWLFTSWK EKNQDRSALK DTYMLSSTVS SKILRAIALK EGFHFEETLT
410 420 430 440 450
GFKWMGNRAK QLIDQGKTVL FAFEEAIGYM CCPFVLDKDG VSAAVISAEL
460 470 480 490 500
ASFLATKNLS LSQQLKAIYV EYGYHITKAS YFICHDQETI KKLFENLRNY
510 520 530 540 550
DGKNNYPKAC GKFEISAIRD LTTGYDDSQP DKKAVLPTSK SSQMITFTFA
560 570 580 590 600
NGGVATMRTS GTEPKIKYYA ELCAPPGNSD PEQLKKELNE LVSAIEEHFF
610
QPQKYNLQPK AD
Length:612
Mass (Da):68,283
Last modified:January 23, 2007 - v4
Checksum:i82234DDE810D1F52
GO
Isoform 2 (identifier: Q96G03-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MAAPEGSG → MSSQLILR
     9-147: Missing.
     429-430: YM → KK
     431-612: Missing.

Note: No experimental confirmation available.
Show »
Length:291
Mass (Da):32,724
Checksum:i743821357CF0B3A4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti114G → A in BAD96957 (Ref. 5) Curated1
Sequence conflicti162I → V in BAA91938 (Ref. 2) Curated1
Sequence conflicti282K → R in CAB66640 (PubMed:11230166).Curated1
Sequence conflicti495E → G in BAD96957 (Ref. 5) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02796810G → D.2 PublicationsCorresponds to variant rs17856324dbSNPEnsembl.1
Natural variantiVAR_027969488E → D.Corresponds to variant rs10001580dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0562211 – 8MAAPEGSG → MSSQLILR in isoform 2. 1 Publication8
Alternative sequenceiVSP_0562229 – 147Missing in isoform 2. 1 PublicationAdd BLAST139
Alternative sequenceiVSP_056223429 – 430YM → KK in isoform 2. 1 Publication2
Alternative sequenceiVSP_056224431 – 612Missing in isoform 2. 1 PublicationAdd BLAST182

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136705 mRNA. Translation: CAB66640.1.
AF109360 mRNA. Translation: AAQ13508.1.
AK001845 mRNA. Translation: BAA91938.1.
AK303374 mRNA. Translation: BAG64430.1.
CR457274 mRNA. Translation: CAG33555.1.
AK223237 mRNA. Translation: BAD96957.1.
AC021106 Genomic DNA. No translation available.
AC108022 Genomic DNA. No translation available.
BC010087 mRNA. Translation: AAH10087.1.
CCDSiCCDS3443.1. [Q96G03-1]
RefSeqiNP_060760.2. NM_018290.3. [Q96G03-1]
UniGeneiHs.23363.
Hs.607816.

Genome annotation databases

EnsembliENST00000381967; ENSP00000371393; ENSG00000169299. [Q96G03-1]
GeneIDi55276.
KEGGihsa:55276.
UCSCiuc011byb.2. human. [Q96G03-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136705 mRNA. Translation: CAB66640.1.
AF109360 mRNA. Translation: AAQ13508.1.
AK001845 mRNA. Translation: BAA91938.1.
AK303374 mRNA. Translation: BAG64430.1.
CR457274 mRNA. Translation: CAG33555.1.
AK223237 mRNA. Translation: BAD96957.1.
AC021106 Genomic DNA. No translation available.
AC108022 Genomic DNA. No translation available.
BC010087 mRNA. Translation: AAH10087.1.
CCDSiCCDS3443.1. [Q96G03-1]
RefSeqiNP_060760.2. NM_018290.3. [Q96G03-1]
UniGeneiHs.23363.
Hs.607816.

3D structure databases

ProteinModelPortaliQ96G03.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120564. 14 interactors.
IntActiQ96G03. 5 interactors.
STRINGi9606.ENSP00000371393.

PTM databases

iPTMnetiQ96G03.
PhosphoSitePlusiQ96G03.
SwissPalmiQ96G03.

Polymorphism and mutation databases

BioMutaiPGM2.
DMDMi116242708.

Proteomic databases

EPDiQ96G03.
MaxQBiQ96G03.
PaxDbiQ96G03.
PeptideAtlasiQ96G03.
PRIDEiQ96G03.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381967; ENSP00000371393; ENSG00000169299. [Q96G03-1]
GeneIDi55276.
KEGGihsa:55276.
UCSCiuc011byb.2. human. [Q96G03-1]

Organism-specific databases

CTDi55276.
GeneCardsiPGM2.
HGNCiHGNC:8906. PGM2.
HPAiHPA040676.
MIMi172000. gene.
neXtProtiNX_Q96G03.
OpenTargetsiENSG00000169299.
PharmGKBiPA33243.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1220. Eukaryota.
COG1109. LUCA.
GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
HOVERGENiHBG056917.
InParanoidiQ96G03.
KOiK15779.
OMAiPLLHDPY.
OrthoDBiEOG091G040C.
PhylomeDBiQ96G03.
TreeFamiTF300692.

Enzyme and pathway databases

UniPathwayiUPA00002; UER00467.
BioCyciMetaCyc:HS09924-MONOMER.
ZFISH:HS09924-MONOMER.
ReactomeiR-HSA-3322077. Glycogen synthesis.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-70221. Glycogen breakdown (glycogenolysis).
R-HSA-70370. Galactose catabolism.
R-HSA-71336. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKQ96G03.

Miscellaneous databases

ChiTaRSiPGM2. human.
GeneWikiiPGM2.
GenomeRNAii55276.
PROiQ96G03.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000169299.
CleanExiHS_PGM2.
ExpressionAtlasiQ96G03. baseline and differential.
GenevisibleiQ96G03. HS.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGM2_HUMAN
AccessioniPrimary (citable) accession number: Q96G03
Secondary accession number(s): B4E0G8
, Q53FP5, Q5QTR0, Q9H0P9, Q9NV22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 145 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.