Q96G03 (PGM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	612 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	deoxyribose phosphate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glucose metabolic process Traceable author statement. Source: Reactome glycogen biosynthetic process Traceable author statement. Source: Reactome glycogen catabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoglucomutase activity Inferred from Biological aspect of Ancestor. Source: RefGenome phosphopentomutase activity Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 612	611	Phosphoglucomutase-2		PRO_0000147781
Sites
	Active site	165	1	Phosphoserine intermediate By similarity
	Metal binding	165	1	Magnesium; via phosphate group By similarity
	Metal binding	322	1	Magnesium By similarity
	Metal binding	324	1	Magnesium By similarity
	Metal binding	326	1	Magnesium By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7
	Modified residue	165	1	Phosphoserine Ref.9
Natural variations
	Natural variant	10	1	G → D. Ref.4 Ref.6 Corresponds to variant rs17856324 [ dbSNP | Ensembl ].		VAR_027968
	Natural variant	488	1	E → D. Corresponds to variant rs10001580 [ dbSNP | Ensembl ].		VAR_027969
Experimental info
	Sequence conflict	114	1	G → A in BAD96957. Ref.5
	Sequence conflict	162	1	I → V in BAA91938. Ref.2
	Sequence conflict	282	1	K → R in CAB66640. Ref.1
	Sequence conflict	495	1	E → G in BAD96957. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q96G03 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 82234DDE810D1F52	FASTA	612	68,283
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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.
[11]	"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].

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.
IPI	IPI00550364.
RefSeq	NP_060760.2. NM_018290.3.
UniGene	Hs.23363. Hs.607816.
3D structure databases
ProteinModelPortal	Q96G03.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000371393.
PTM databases
PhosphoSite	Q96G03.
Polymorphism databases
DMDM	116242708.
Proteomic databases
PaxDb	Q96G03.
PeptideAtlas	Q96G03.
PRIDE	Q96G03.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000381967; ENSP00000371393; ENSG00000169299.
GeneID	55276.
KEGG	hsa:55276.
UCSC	uc011byb.1. human.
Organism-specific databases
CTD	55276.
GeneCards	GC04P037828.
HGNC	HGNC:8906. PGM2.
MIM	172000. gene.
neXtProt	NX_Q96G03.
PharmGKB	PA33243.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HOG000268676.
HOVERGEN	HBG056917.
InParanoid	Q96G03.
KO	K15779.
OMA	YDGRHDS.
OrthoDB	EOG4VDPZ1.
PhylomeDB	Q96G03.
Enzyme and pathway databases
BioCyc	MetaCyc:HS09924-MONOMER.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00002; UER00467.
Gene expression databases
ArrayExpress	Q96G03.
Bgee	Q96G03.
CleanEx	HS_PGM2.
Genevestigator	Q96G03.
GermOnline	ENSG00000169299. Homo sapiens.
Family and domain databases
Gene3D	3.40.120.10. 3 hits.
InterPro	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]
Pfam	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]
PRINTS	PR00509. PGMPMM.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	55276.
NextBio	59409.
SOURCE	Search...

Entry information

Entry name

PGM2_HUMAN

Accession

Primary (citable) accession number: Q96G03
Secondary accession number(s): Q53FP5 , Q5QTR0, Q9H0P9, Q9NV22

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 109 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.