Q7TSV4 (PGM2_MOUSE) 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	620 AA.
Sequence status	Complete.
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 By similarity.
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.
Tissue specificity	Highly expressed in lung, spleen and thymus. Expressed at lower levels in liver, brain, kidney, skeletal muscle, testis and heart. Ref.3
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glucose 1-phosphate metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome
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 direct assay. Source: MGI phosphopentomutase 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
	Chain	1 – 620	620	Phosphoglucomutase-2		PRO_0000147782
Sites
	Active site	173	1	Phosphoserine intermediate By similarity
	Metal binding	173	1	Magnesium; via phosphate group By similarity
	Metal binding	330	1	Magnesium By similarity
	Metal binding	332	1	Magnesium By similarity
	Metal binding	334	1	Magnesium By similarity
Amino acid modifications
	Modified residue	173	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q7TSV4 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: F2535A3F700EFD50	FASTA	620	68,748
	10 20 30 40 50 60 MAAATPTETP APEGSGLGMD ARLDQETAQW LRWDQNPLTS ESVKQLIAGG NKEELRKCFG 70 80 90 100 110 120 ARMEFGTAGL RAPMGAGISR MNDLTIIQTT QGFCRYLEKQ FSDLKQRGVV ISFDARAHPA 130 140 150 160 170 180 SGGSSRRFAR LAATAFITQG VPVYLFSDIT PTPFVPYTVS HLKLCAGIMI TASHNPKQDN 190 200 210 220 230 240 GYKVYWDNGA QIISPHDRGI SQAIEENLEP WPQAWEESLV DSSPLLHNPS ASIGNDYFED 250 260 270 280 290 300 LKKYCFHRTV NKESKVKFVH TSVHGVGHEF VQLAFKAFDL APPEAVPQQK DPDPEFPTVK 310 320 330 340 350 360 YPNPEEGKGV LTLSFALADK IKAKIVLAND PDADRLAVAE KQDSGEWRVF SGNELGALLG 370 380 390 400 410 420 WWLFTSWKEK NQDQSNLKDT YMLSSTVSSK ILRAIALKEG FHFEETLTGF KWMGNRAQQL 430 440 450 460 470 480 GDQGKTVLFA FEEAIGYMCC PFVLDKDGVS AAVICAELAS FLATKNLSLS QQLNAIYVEY 490 500 510 520 530 540 GYHITTASYF ICHDQGTIQN LFGNLRNYDG KNNYPKMCGK FEISAIRDLT TGYDDSQPDK 550 560 570 580 590 600 KAVLPTSKSS QMITFTFANG GVATMRTSGT EPKIKYYAEL CAPPGNSDPE HLKKELDELV 610 620 GAIEEHFFQP QKYNLQPKAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Strain: FVB/N. Tissue: Colon and Limb.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-620. Strain: C57BL/6J. Tissue: Head.
[3]	"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: 17804405] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC030869 mRNA. Translation: AAH30869.1. BC052762 mRNA. Translation: AAH52762.1. AK014332 mRNA. Translation: BAB29278.1.
IPI	IPI00338302.
RefSeq	NP_079976.1. NM_025700.2.
UniGene	Mm.2325.
3D structure databases
ProteinModelPortal	Q7TSV4.
SMR	Q7TSV4. Positions 557-607.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7TSV4.
PTM databases
PhosphoSite	Q7TSV4.
Proteomic databases
PRIDE	Q7TSV4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000087324; ENSMUSP00000084582; ENSMUSG00000029171.
GeneID	66681.
KEGG	mmu:66681.
UCSC	uc008xmi.1. mouse.
Organism-specific databases
CTD	5236.
MGI	MGI:97565. Pgm2.
Phylogenomic databases
eggNOG	roNOG07123.
GeneTree	ENSGT00390000017247.
HOGENOM	HBG571743.
HOVERGEN	HBG056917.
InParanoid	Q7TSV4.
OMA	NQFLFAY.
OrthoDB	EOG4VDPZ1.
PhylomeDB	Q7TSV4.
Gene expression databases
ArrayExpress	Q7TSV4.
Bgee	Q7TSV4.
Genevestigator	Q7TSV4.
GermOnline	ENSMUSG00000029171. Mus musculus.
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. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KO	K01835.
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]
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	322361.
SOURCE	Search...

Entry information

Entry name

PGM2_MOUSE

Accession

Primary (citable) accession number: Q7TSV4
Secondary accession number(s): Q8K0P7, Q9CRS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	October 1, 2003
Last modified:	November 16, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program