Reviewed, UniProtKB/Swiss-Prot Q96G03 (PGM2_HUMAN)

Names and origin

Protein names

Recommended name:
    Phosphoglucomutase-2
      Short name=PGM 2
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase 2

Gene names

Name:	PGM2
ORF Names:	MSTP006

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	This enzyme participates in both the breakdown and synthesis of glucose By similarity.
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the phosphohexose mutase family.

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
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucomutase activity Inferred from electronic annotation. Source: EC
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.8
	Modified residue	492	1	N6-acetyllysine Ref.10
Natural variations
	Natural variant	10	1	G → D: dbSNP rs17856324. Ref.4 Ref.6		VAR_027968
	Natural variant	488	1	E → D: dbSNP rs10001580.		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)
	Q96G03-1 [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: 11230166] [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: 14702039] [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: 15489334] [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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14, ACETYLATION AT ALA-2. Tissue: Platelet.
[8]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, MASS SPECTROMETRY.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-492, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Hs.23363 Hs.607816
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q96G03.
PTM databases
PhosphoSite	Q96G03.
Proteomic databases
PeptideAtlas	Q96G03.
PRIDE	Q96G03.
Genome annotation databases
Ensembl	ENST00000381967; ENSP00000371393; ENSG00000169299; Homo sapiens. [Genome view]
GeneID	55276.
KEGG	hsa:55276.
NMPDR	fig|9606.3.peg.24022.
UCSC	uc003gta.1. human.
Organism-specific databases
CTD	55276.
GeneCards	GC04P037504.
HGNC	HGNC:8906. PGM2.
MIM	172000. gene.
Orphanet	711. Phosphoglucomutase deficiency.
PharmGKB	PA33243.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q96G03.
HOVERGEN	Q96G03.
OMA	PKIKCYY.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13390.
BRENDA	5.4.2.2. 247.
Gene expression databases
ArrayExpress	Q96G03.
Bgee	Q96G03.
CleanEx	HS_PGM2.
Genevestigator	Q96G03.
GermOnline	ENSG00000169299. Homo sapiens.
Family and domain databases
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. IPR016066. A-D-PHexomutase_CS. IPR005841. A-D-PHexomutase_N. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 2 hits.
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	November 3, 2009
This is version 74 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.