SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q96G03

- PGM2_HUMAN

UniProt

Q96G03 - PGM2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Phosphoglucomutase-2
Gene
PGM2, MSTP006
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 magnesium 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-phosphate
  3. 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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei165 – 1651Phosphoserine intermediate By similarity
Metal bindingi165 – 1651Magnesium; via phosphate group By similarity
Metal bindingi322 – 3221Magnesium By similarity
Metal bindingi324 – 3241Magnesium By similarity
Metal bindingi326 – 3261Magnesium By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. phosphoglucomutase activity Source: RefGenome
  3. phosphopentomutase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. deoxyribose phosphate catabolic process Source: UniProtKB-UniPathway
  3. galactose catabolic process Source: RefGenome
  4. glucose metabolic process Source: RefGenome
  5. glycogen biosynthetic process Source: RefGenome
  6. glycogen catabolic process Source: Reactome
  7. small molecule metabolic process Source: Reactome
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.
ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
REACT_169208. Glycogen synthesis.
REACT_532. Galactose catabolism.
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
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:8906. PGM2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33243.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 612611Phosphoglucomutase-2
PRO_0000147781Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei165 – 1651Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96G03.
PaxDbiQ96G03.
PeptideAtlasiQ96G03.
PRIDEiQ96G03.

PTM databases

PhosphoSiteiQ96G03.

Expressioni

Gene expression databases

ArrayExpressiQ96G03.
BgeeiQ96G03.
CleanExiHS_PGM2.
GenevestigatoriQ96G03.

Organism-specific databases

HPAiHPA040676.

Interactioni

Protein-protein interaction databases

BioGridi120564. 7 interactions.
STRINGi9606.ENSP00000371393.

Structurei

3D structure databases

ProteinModelPortaliQ96G03.
SMRiQ96G03. Positions 57-205.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1109.
HOGENOMiHOG000268676.
HOVERGENiHBG056917.
InParanoidiQ96G03.
KOiK15779.
OMAiRWDKNPL.
OrthoDBiEOG715Q3R.
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]

Sequencei

Sequence statusi: Complete.

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

Q96G03-1 [UniParc]FASTAAdd to Basket

« Hide

MAAPEGSGLG EDARLDQETA QWLRWDKNSL TLEAVKRLIA EGNKEELRKC    50
FGARMEFGTA GLRAAMGPGI SRMNDLTIIQ TTQGFCRYLE KQFSDLKQKG 100
IVISFDARAH PSSGGSSRRF ARLAATTFIS QGIPVYLFSD ITPTPFVPFT 150
VSHLKLCAGI MITASHNPKQ DNGYKVYWDN GAQIISPHDK GISQAIEENL 200
EPWPQAWDDS LIDSSPLLHN PSASINNDYF EDLKKYCFHR SVNRETKVKF 250
VHTSVHGVGH SFVQSAFKAF DLVPPEAVPE QKDPDPEFPT VKYPNPEEGK 300
GVLTLSFALA DKTKARIVLA NDPDADRLAV AEKQDSGEWR VFSGNELGAL 350
LGWWLFTSWK EKNQDRSALK DTYMLSSTVS SKILRAIALK EGFHFEETLT 400
GFKWMGNRAK QLIDQGKTVL FAFEEAIGYM CCPFVLDKDG VSAAVISAEL 450
ASFLATKNLS LSQQLKAIYV EYGYHITKAS YFICHDQETI KKLFENLRNY 500
DGKNNYPKAC GKFEISAIRD LTTGYDDSQP DKKAVLPTSK SSQMITFTFA 550
NGGVATMRTS GTEPKIKYYA ELCAPPGNSD PEQLKKELNE LVSAIEEHFF 600
QPQKYNLQPK AD 612
Length:612
Mass (Da):68,283
Last modified:January 23, 2007 - v4
Checksum:i82234DDE810D1F52
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101G → D.2 Publications
Corresponds to variant rs17856324 [ dbSNP | Ensembl ].
VAR_027968
Natural varianti488 – 4881E → D.
Corresponds to variant rs10001580 [ dbSNP | Ensembl ].
VAR_027969

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141G → A in BAD96957. 1 Publication
Sequence conflicti162 – 1621I → V in BAA91938. 1 Publication
Sequence conflicti282 – 2821K → R in CAB66640. 1 Publication
Sequence conflicti495 – 4951E → G in BAD96957. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3443.1.
RefSeqiNP_060760.2. NM_018290.3.
UniGeneiHs.23363.
Hs.607816.

Genome annotation databases

EnsembliENST00000381967; ENSP00000371393; ENSG00000169299.
GeneIDi55276.
KEGGihsa:55276.
UCSCiuc011byb.1. human.

Polymorphism databases

DMDMi116242708.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3443.1.
RefSeqi NP_060760.2. NM_018290.3.
UniGenei Hs.23363.
Hs.607816.

3D structure databases

ProteinModelPortali Q96G03.
SMRi Q96G03. Positions 57-205.
ModBasei Search...

Protein-protein interaction databases

BioGridi 120564. 7 interactions.
STRINGi 9606.ENSP00000371393.

PTM databases

PhosphoSitei Q96G03.

Polymorphism databases

DMDMi 116242708.

Proteomic databases

MaxQBi Q96G03.
PaxDbi Q96G03.
PeptideAtlasi Q96G03.
PRIDEi Q96G03.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381967 ; ENSP00000371393 ; ENSG00000169299 .
GeneIDi 55276.
KEGGi hsa:55276.
UCSCi uc011byb.1. human.

Organism-specific databases

CTDi 55276.
GeneCardsi GC04P037828.
HGNCi HGNC:8906. PGM2.
HPAi HPA040676.
MIMi 172000. gene.
neXtProti NX_Q96G03.
PharmGKBi PA33243.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1109.
HOGENOMi HOG000268676.
HOVERGENi HBG056917.
InParanoidi Q96G03.
KOi K15779.
OMAi RWDKNPL.
OrthoDBi EOG715Q3R.
PhylomeDBi Q96G03.
TreeFami TF300692.

Enzyme and pathway databases

UniPathwayi UPA00002 ; UER00467 .
BioCyci MetaCyc:HS09924-MONOMER.
Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).
REACT_169208. Glycogen synthesis.
REACT_532. Galactose catabolism.
SABIO-RK Q96G03.

Miscellaneous databases

GeneWikii PGM2.
GenomeRNAii 55276.
NextBioi 59409.
PROi Q96G03.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96G03.
Bgeei Q96G03.
CleanExi HS_PGM2.
Genevestigatori Q96G03.

Family and domain databases

Gene3Di 3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProi IPR005844. 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 ]
Pfami PF02878. 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 ]
PRINTSi PR00509. PGMPMM.
SUPFAMi SSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEi PS00710. PGM_PMM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPGM2_HUMAN
AccessioniPrimary (citable) accession number: Q96G03
Secondary accession number(s): Q53FP5
, Q5QTR0, Q9H0P9, Q9NV22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 121 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

External Data

Dasty 3

Similar proteinsi