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Phosphoglucomutase-2 (PGM 2) (EC 5.4.2.2) (Glucose phosphomutase 2) (Phosphodeoxyribomutase) (Phosphoglucomutase-1) (Phosphopentomutase) (EC 5.4.2.7)

 PGM2_MOUSE              Reviewed;         620 AA.
Q7TSV4; Q8K0P7; Q9CRS8;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
23-MAY-2018, entry version 125.
RecName: Full=Phosphoglucomutase-2;
Short=PGM 2;
EC=5.4.2.2;
AltName: Full=Glucose phosphomutase 2;
AltName: Full=Phosphodeoxyribomutase;
AltName: Full=Phosphoglucomutase-1;
AltName: Full=Phosphopentomutase;
EC=5.4.2.7;
Name=Pgm2; Synonyms=Pgm1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon, and Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-620.
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
TISSUE SPECIFICITY.
PubMed=17804405; DOI=10.1074/jbc.M706818200;
Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M.,
Van Schaftingen E.;
"Molecular identification of mammalian phosphopentomutase and glucose-
1,6-bisphosphate synthase, two members of the alpha-D-
phosphohexomutase family.";
J. Biol. Chem. 282:31844-31851(2007).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Alpha-D-glucose 1-phosphate = alpha-D-glucose
6-phosphate.
-!- CATALYTIC ACTIVITY: Alpha-D-ribose 1-phosphate = D-ribose 5-
phosphate.
-!- CATALYTIC ACTIVITY: 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-
alpha-D-ribose 5-phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
-!- 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 {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in lung, spleen and thymus.
Expressed at lower levels in liver, brain, kidney, skeletal
muscle, testis and heart. {ECO:0000269|PubMed:17804405}.
-!- SIMILARITY: Belongs to the phosphohexose mutase family.
{ECO:0000305}.
-!- CAUTION: There is a known reversal of the Pgm1 and Pgm2
nomenclature applied to mouse versus other vertebrates. The
official name of this gene in mouse is Pgm1 but it is the ortholog
of other vertebrate PGM2 genes. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC030869; AAH30869.1; -; mRNA.
EMBL; BC052762; AAH52762.1; -; mRNA.
EMBL; AK014332; BAB29278.1; -; mRNA.
CCDS; CCDS19300.1; -.
RefSeq; NP_079976.1; NM_025700.2.
UniGene; Mm.2325; -.
ProteinModelPortal; Q7TSV4; -.
IntAct; Q7TSV4; 1.
MINT; Q7TSV4; -.
STRING; 10090.ENSMUSP00000084582; -.
iPTMnet; Q7TSV4; -.
PhosphoSitePlus; Q7TSV4; -.
SwissPalm; Q7TSV4; -.
EPD; Q7TSV4; -.
MaxQB; Q7TSV4; -.
PaxDb; Q7TSV4; -.
PeptideAtlas; Q7TSV4; -.
PRIDE; Q7TSV4; -.
Ensembl; ENSMUST00000087324; ENSMUSP00000084582; ENSMUSG00000029171.
GeneID; 66681; -.
KEGG; mmu:66681; -.
UCSC; uc008xmi.1; mouse.
CTD; 5236; -.
MGI; MGI:97564; Pgm1.
eggNOG; KOG1220; Eukaryota.
eggNOG; COG1109; LUCA.
GeneTree; ENSGT00390000017247; -.
HOGENOM; HOG000268676; -.
HOVERGEN; HBG056917; -.
InParanoid; Q7TSV4; -.
KO; K15779; -.
OMA; AIGYMCC; -.
OrthoDB; EOG091G040C; -.
PhylomeDB; Q7TSV4; -.
TreeFam; TF300692; -.
Reactome; R-MMU-3322077; Glycogen synthesis.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
Reactome; R-MMU-70370; Galactose catabolism.
Reactome; R-MMU-71336; Pentose phosphate pathway (hexose monophosphate shunt).
UniPathway; UPA00002; UER00467.
ChiTaRS; Pgm2; mouse.
PRO; PR:Q7TSV4; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029171; -.
ExpressionAtlas; Q7TSV4; baseline and differential.
Genevisible; Q7TSV4; MM.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004614; F:phosphoglucomutase activity; IDA:MGI.
GO; GO:0008973; F:phosphopentomutase activity; ISO:MGI.
GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0006006; P:glucose metabolic process; IDA:MGI.
InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
InterPro; IPR005843; A-D-PHexomutase_C.
InterPro; IPR036900; A-D-PHexomutase_C_sf.
InterPro; IPR016066; A-D-PHexomutase_CS.
Pfam; PF02878; PGM_PMM_I; 1.
Pfam; PF02879; PGM_PMM_II; 1.
Pfam; PF02880; PGM_PMM_III; 1.
Pfam; PF00408; PGM_PMM_IV; 1.
SUPFAM; SSF53738; SSF53738; 3.
SUPFAM; SSF55957; SSF55957; 1.
PROSITE; PS00710; PGM_PMM; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Complete proteome; Cytoplasm;
Glucose metabolism; Isomerase; Magnesium; Metal-binding;
Phosphoprotein; Reference proteome.
CHAIN 1 620 Phosphoglucomutase-2.
/FTId=PRO_0000147782.
REGION 173 174 Substrate binding.
{ECO:0000250|UniProtKB:P00949}.
REGION 334 335 Substrate binding.
{ECO:0000250|UniProtKB:P00949}.
REGION 432 434 Substrate binding.
{ECO:0000250|UniProtKB:P00949}.
ACT_SITE 173 173 Phosphoserine intermediate.
{ECO:0000250|UniProtKB:P00949}.
METAL 173 173 Magnesium; via phosphate group.
{ECO:0000250|UniProtKB:P00949}.
METAL 330 330 Magnesium.
{ECO:0000250|UniProtKB:P00949}.
METAL 332 332 Magnesium.
{ECO:0000250|UniProtKB:P00949}.
METAL 334 334 Magnesium.
{ECO:0000250|UniProtKB:P00949}.
BINDING 67 67 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 71 71 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 408 408 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 446 446 Substrate.
{ECO:0000250|UniProtKB:P00949}.
MOD_RES 173 173 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
SEQUENCE 620 AA; 68748 MW; F2535A3F700EFD50 CRC64;
MAAATPTETP APEGSGLGMD ARLDQETAQW LRWDQNPLTS ESVKQLIAGG NKEELRKCFG
ARMEFGTAGL RAPMGAGISR MNDLTIIQTT QGFCRYLEKQ FSDLKQRGVV ISFDARAHPA
SGGSSRRFAR LAATAFITQG VPVYLFSDIT PTPFVPYTVS HLKLCAGIMI TASHNPKQDN
GYKVYWDNGA QIISPHDRGI SQAIEENLEP WPQAWEESLV DSSPLLHNPS ASIGNDYFED
LKKYCFHRTV NKESKVKFVH TSVHGVGHEF VQLAFKAFDL APPEAVPQQK DPDPEFPTVK
YPNPEEGKGV LTLSFALADK IKAKIVLAND PDADRLAVAE KQDSGEWRVF SGNELGALLG
WWLFTSWKEK NQDQSNLKDT YMLSSTVSSK ILRAIALKEG FHFEETLTGF KWMGNRAQQL
GDQGKTVLFA FEEAIGYMCC PFVLDKDGVS AAVICAELAS FLATKNLSLS QQLNAIYVEY
GYHITTASYF ICHDQGTIQN LFGNLRNYDG KNNYPKMCGK FEISAIRDLT TGYDDSQPDK
KAVLPTSKSS QMITFTFANG GVATMRTSGT EPKIKYYAEL CAPPGNSDPE HLKKELDELV
GAIEEHFFQP QKYNLQPKAE


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