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Q96G03 (PGM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Phosphoglucomutase-2

Short name=PGM 2
EC=5.4.2.2
Alternative name(s):
Glucose phosphomutase 2
Phosphodeoxyribomutase
Phosphopentomutase
EC=5.4.2.7
Gene names
Name:PGM2
ORF Names:MSTP006
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length612 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Catalytic activity

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.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 1/2.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the phosphohexose mutase family.

Biophysicochemical properties

Kinetic parameters:

KM=45.7 µM for alpha-D-ribose 1-phosphate Ref.8

KM=4.1 µM for 2-deoxy-alpha-D-ribose 1-phosphate

KM=114 µM for alpha-D-glucose 1-phosphate

Vmax=104.3 µmol/min/mg enzyme with alpha-D-ribose 1-phosphate as substrate

Vmax=20.8 µmol/min/mg enzyme with 2-deoxy-alpha-D-ribose 1-phosphate as substrate

Vmax=22.8 µmol/min/mg enzyme with alpha-D-glucose 1-phosphate as substrate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 612611Phosphoglucomutase-2
PRO_0000147781

Sites

Active site1651Phosphoserine intermediate By similarity
Metal binding1651Magnesium; via phosphate group By similarity
Metal binding3221Magnesium By similarity
Metal binding3241Magnesium By similarity
Metal binding3261Magnesium By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.10 Ref.13 Ref.14
Modified residue1651Phosphoserine Ref.9

Natural variations

Natural variant101G → D. Ref.4 Ref.6
Corresponds to variant rs17856324 [ dbSNP | Ensembl ].
VAR_027968
Natural variant4881E → D.
Corresponds to variant rs10001580 [ dbSNP | Ensembl ].
VAR_027969

Experimental info

Sequence conflict1141G → A in BAD96957. Ref.5
Sequence conflict1621I → V in BAA91938. Ref.2
Sequence conflict2821K → R in CAB66640. Ref.1
Sequence conflict4951E → G in BAD96957. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q96G03 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 82234DDE810D1F52

FASTA61268,283
        10         20         30         40         50         60 
MAAPEGSGLG EDARLDQETA QWLRWDKNSL TLEAVKRLIA EGNKEELRKC FGARMEFGTA 

        70         80         90        100        110        120 
GLRAAMGPGI SRMNDLTIIQ TTQGFCRYLE KQFSDLKQKG IVISFDARAH PSSGGSSRRF 

       130        140        150        160        170        180 
ARLAATTFIS QGIPVYLFSD ITPTPFVPFT VSHLKLCAGI MITASHNPKQ DNGYKVYWDN 

       190        200        210        220        230        240 
GAQIISPHDK GISQAIEENL EPWPQAWDDS LIDSSPLLHN PSASINNDYF EDLKKYCFHR 

       250        260        270        280        290        300 
SVNRETKVKF VHTSVHGVGH SFVQSAFKAF DLVPPEAVPE QKDPDPEFPT VKYPNPEEGK 

       310        320        330        340        350        360 
GVLTLSFALA DKTKARIVLA NDPDADRLAV AEKQDSGEWR VFSGNELGAL LGWWLFTSWK 

       370        380        390        400        410        420 
EKNQDRSALK DTYMLSSTVS SKILRAIALK EGFHFEETLT GFKWMGNRAK QLIDQGKTVL 

       430        440        450        460        470        480 
FAFEEAIGYM CCPFVLDKDG VSAAVISAEL ASFLATKNLS LSQQLKAIYV EYGYHITKAS 

       490        500        510        520        530        540 
YFICHDQETI KKLFENLRNY DGKNNYPKAC GKFEISAIRD LTTGYDDSQP DKKAVLPTSK 

       550        560        570        580        590        600 
SSQMITFTFA NGGVATMRTS GTEPKIKYYA ELCAPPGNSD PEQLKKELNE LVSAIEEHFF 

       610 
QPQKYNLQPK AD 

« Hide

References

« Hide 'large scale' references
[1]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y., Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J., Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L. expand/collapse author list , Jiang Y.X., Zhao X.W., Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Aorta.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-10.
[5]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Gastric mucosa.
[6]"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], VARIANT ASP-10.
Tissue: Muscle.
[7]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14, ACETYLATION AT ALA-2.
Tissue: Platelet.
[8]"Molecular identification of mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase family."
Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M., Van Schaftingen E.
J. Biol. Chem. 282:31844-31851(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL136705 mRNA. Translation: CAB66640.1.
AK001845 mRNA. Translation: BAA91938.1.
AF109360 mRNA. Translation: AAQ13508.1.
CR457274 mRNA. Translation: CAG33555.1.
AK223237 mRNA. Translation: BAD96957.1.
BC010087 mRNA. Translation: AAH10087.1.
CCDSCCDS3443.1.
RefSeqNP_060760.2. NM_018290.3.
UniGeneHs.23363.
Hs.607816.

3D structure databases

ProteinModelPortalQ96G03.
SMRQ96G03. Positions 57-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120564. 7 interactions.
STRING9606.ENSP00000371393.

PTM databases

PhosphoSiteQ96G03.

Polymorphism databases

DMDM116242708.

Proteomic databases

MaxQBQ96G03.
PaxDbQ96G03.
PeptideAtlasQ96G03.
PRIDEQ96G03.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381967; ENSP00000371393; ENSG00000169299.
GeneID55276.
KEGGhsa:55276.
UCSCuc011byb.1. human.

Organism-specific databases

CTD55276.
GeneCardsGC04P037828.
HGNCHGNC:8906. PGM2.
HPAHPA040676.
MIM172000. gene.
neXtProtNX_Q96G03.
PharmGKBPA33243.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268676.
HOVERGENHBG056917.
InParanoidQ96G03.
KOK15779.
OMARWDKNPL.
OrthoDBEOG715Q3R.
PhylomeDBQ96G03.
TreeFamTF300692.

Enzyme and pathway databases

BioCycMetaCyc:HS09924-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ96G03.
UniPathwayUPA00002; UER00467.

Gene expression databases

ArrayExpressQ96G03.
BgeeQ96G03.
CleanExHS_PGM2.
GenevestigatorQ96G03.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProIPR005844. 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]
PfamPF02878. 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]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPGM2.
GenomeRNAi55276.
NextBio59409.
PROQ96G03.
SOURCESearch...

Entry information

Entry namePGM2_HUMAN
AccessionPrimary (citable) accession number: Q96G03
Secondary accession number(s): Q53FP5 expand/collapse secondary AC list , Q5QTR0, Q9H0P9, Q9NV22
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 120 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM