Hmdb loader
Identification
HMDB Protein ID HMDBP03741
Secondary Accession Numbers
  • 9329
Name Phosphoglucomutase-2
Synonyms
  1. Glucose phosphomutase 2
  2. PGM 2
  3. Phosphodeoxyribomutase
  4. Phosphopentomutase
Gene Name PGM2
Protein Type Unknown
Biological Properties
General Function Involved in intramolecular transferase activity, phosphotransferases
Specific 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.
Pathways
  • 2-deoxy-D-ribose 1-phosphate degradation
  • Amino sugar and nucleotide sugar metabolism
  • Galactose metabolism
  • Glycolysis / Gluconeogenesis
  • Pentose phosphate pathway
  • Purine metabolism
  • Starch and sucrose metabolism
Reactions
Glucose 1-phosphate → Glucose 6-phosphate details
Ribose 1-phosphate → D-Ribose 5-phosphate details
Deoxyribose 1-phosphate → Deoxyribose 5-phosphate details
Deoxyribose 1-phosphate → Deoxyribose 5-monophosphate details
GO Classification
Biological Process
small molecule metabolic process
glucose metabolic process
deoxyribose phosphate catabolic process
glycogen catabolic process
glycogen biosynthetic process
Cellular Component
cytosol
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
magnesium ion binding
isomerase activity
intramolecular transferase activity
intramolecular transferase activity, phosphotransferases
Molecular Function
phosphoglucomutase activity
phosphopentomutase activity
magnesium ion binding
Process
metabolic process
primary metabolic process
carbohydrate metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 4
Locus 4p14
SNPs PGM2
Gene Sequence
>1839 bp
ATGGCGGCTCCAGAAGGCAGCGGTCTAGGCGAGGACGCCCGGCTGGACCAGGAGACCGCC
CAGTGGCTGCGCTGGGACAAGAATTCCTTAACTTTGGAGGCAGTGAAACGACTAATAGCA
GAAGGTAATAAAGAAGAACTACGAAAATGTTTTGGGGCCCGAATGGAGTTTGGGACAGCT
GGCCTCCGAGCTGCTATGGGACCTGGAATTTCTCGTATGAATGACTTGACCATCATCCAG
ACTACACAGGGATTTTGCAGATACCTGGAAAAACAATTCAGTGACTTAAAGCAGAAAGGC
ATCGTGATCAGTTTTGACGCCCGAGCTCATCCATCCAGTGGGGGTAGCAGCAGAAGGTTT
GCCCGACTTGCTGCAACCACATTTATCAGTCAGGGGATTCCTGTGTACCTCTTTTCTGAT
ATAACGCCAACCCCCTTTGTGCCCTTCACAGTATCACATTTGAAACTTTGTGCTGGAATC
ATGATAACTGCATCTCACAATCCAAAGCAGGATAATGGTTATAAGGTCTATTGGGATAAT
GGAGCTCAGATCATTTCTCCTCACGATAAAGGGATTTCTCAAGCTATTGAAGAAAATCTA
GAACCGTGGCCTCAAGCTTGGGACGATTCTTTAATTGATAGCAGTCCACTTCTCCACAAT
CCGAGTGCTTCCATCAATAATGACTACTTTGAAGACCTTAAAAAGTACTGTTTCCACAGG
AGCGTGAACAGGGAGACAAAGGTGAAGTTTGTGCACACCTCTGTCCATGGGGTGGGTCAT
AGCTTTGTGCAGTCAGCTTTCAAGGCTTTTGACCTTGTTCCTCCTGAGGCTGTTCCTGAA
CAGAAAGATCCGGATCCTGAGTTTCCAACAGTGAAATACCCGAATCCCGAAGAGGGGAAA
GGTGTCTTGACTTTGTCTTTTGCTTTGGCTGACAAAACCAAGGCCAGAATTGTTTTAGCT
AACGACCCGGATGCTGATAGACTTGCTGTGGCAGAAAAGCAAGACAGTGGTGAATGGAGG
GTGTTTTCAGGCAATGAGTTGGGGGCCCTCCTGGGCTGGTGGCTTTTTACATCTTGGAAA
GAGAAGAACCAGGATCGCAGTGCTCTCAAAGACACGTACATGTTGTCCAGCACCGTCTCC
TCCAAAATCTTGCGGGCCATTGCCTTAAAGGAAGGTTTTCATTTTGAGGAAACATTAACT
GGCTTTAAGTGGATGGGAAACAGAGCCAAACAGCTAATAGACCAGGGGAAAACTGTTTTA
TTTGCATTTGAAGAAGCTATTGGATACATGTGCTGCCCTTTTGTTCTGGACAAAGATGGA
GTCAGTGCCGCTGTCATAAGTGCAGAGTTGGCTAGCTTCCTAGCAACCAAGAATTTGTCT
TTGTCTCAGCAACTAAAGGCCATTTATGTGGAGTATGGCTACCATATTACTAAAGCTTCC
TATTTTATCTGCCATGATCAAGAAACCATTAAGAAATTATTTGAAAACCTCAGAAACTAC
GATGGAAAAAATAATTATCCAAAAGCTTGTGGCAAATTTGAAATTTCTGCCATTAGGGAC
CTTACAACTGGCTATGATGATAGCCAACCTGATAAAAAAGCTGTTCTTCCCACTAGTAAA
AGCAGCCAAATGATCACCTTCACCTTTGCTAATGGAGGCGTGGCCACCATGCGCACCAGT
GGGACAGAGCCCAAAATCAAGTACTATGCAGAGCTGTGTGCCCCACCTGGGAACAGTGAT
CCTGAGCAGCTGAAGAAGGAACTGAATGAACTGGTCAGTGCTATTGAAGAACATTTTTTC
CAGCCACAGAAGTACAATCTGCAGCCAAAAGCAGACTAA
Protein Properties
Number of Residues 612
Molecular Weight 68282.765
Theoretical pI 6.722
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Phosphoglucomutase-2
MAAPEGSGLGEDARLDQETAQWLRWDKNSLTLEAVKRLIAEGNKEELRKCFGARMEFGTA
GLRAAMGPGISRMNDLTIIQTTQGFCRYLEKQFSDLKQKGIVISFDARAHPSSGGSSRRF
ARLAATTFISQGIPVYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDN
GAQIISPHDKGISQAIEENLEPWPQAWDDSLIDSSPLLHNPSASINNDYFEDLKKYCFHR
SVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLVPPEAVPEQKDPDPEFPTVKYPNPEEGK
GVLTLSFALADKTKARIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWK
EKNQDRSALKDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLIDQGKTVL
FAFEEAIGYMCCPFVLDKDGVSAAVISAELASFLATKNLSLSQQLKAIYVEYGYHITKAS
YFICHDQETIKKLFENLRNYDGKNNYPKACGKFEISAIRDLTTGYDDSQPDKKAVLPTSK
SSQMITFTFANGGVATMRTSGTEPKIKYYAELCAPPGNSDPEQLKKELNELVSAIEEHFF
QPQKYNLQPKAD
GenBank ID Protein 33337743
UniProtKB/Swiss-Prot ID Q96G03
UniProtKB/Swiss-Prot Entry Name PGM2_HUMAN
PDB IDs Not Available
GenBank Gene ID AF109360
GeneCard ID PGM2
GenAtlas ID PGM2
HGNC ID HGNC:8906
References
General References
  1. 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  6. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed:11230166 ]
  7. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
  8. 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. 2007 Nov 2;282(44):31844-51. Epub 2007 Sep 5. [PubMed:17804405 ]