PMM1

PMM1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2FUC, 2FUE
Identifiers
Aliases	PMM1 , Sec53, phosphomannomutase 1, PMMH-22, PMM 1
External IDs	OMIM: 601786; MGI: 1353418; HomoloGene: 90898; GeneCards: PMM1; OMA:PMM1 - orthologs
Gene location (Human) Chr. Chromosome 22 (human) [1] Band 22q13.2 Start 41,576,900 bp [1] End 41,589,871 bp [1]
Gene location (Mouse) Chr. Chromosome 15 (mouse) [2] Band 15|15 E1 Start 81,835,309 bp [2] End 81,845,131 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon body of stomach right lobe of liver nucleus accumbens right frontal lobe right adrenal gland right lung left adrenal gland right adrenal cortex cingulate gyrus Top expressed in morula morula neural layer of retina dentate gyrus of hippocampal formation granule cell superior frontal gyrus cerebellar cortex primary visual cortex lateral hypothalamus lateral geniculate nucleus hippocampus proper More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phosphomannomutase activity isomerase activity protein binding metal ion binding Cellular component cytoplasm soma cytosol Biological process mannose metabolic process protein N-linked glycosylation protein targeting to ER GDP-mannose biosynthetic process cellular response to leukemia inhibitory factor Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5372 29858 Ensembl ENSG00000100417 ENSMUSG00000022474 UniProt Q92871 O35621 RefSeq (mRNA) NM_002676 NM_001282040 NM_001282041 NM_013872 RefSeq (protein) NP_002667 NP_001268969 NP_001268970 NP_038900 Location (UCSC) Chr 22: 41.58 – 41.59 Mb Chr 15: 81.84 – 81.85 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Phosphomannomutase 1 is an enzyme that in humans is encoded by the PMM1 gene. ^{[5] [6] [7]}

Phosphomannomutase catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for synthesis of dolichol-phosphate-mannose, which is essential for N-linked glycosylation and thus the secretion of several glycoproteins as well as for the synthesis of Glycosylphosphatidylinositol (GPI) anchored proteins. ^[7]

This enzyme has been extracted from the venom of the wasp species Polistes major major . ^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000100417 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022474 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Matthijs G, Schollen E, Pirard M, Budarf ML, Van Schaftingen E, Cassiman JJ (Jun 1997). "PMM (PMM1), the human homologue of SEC53 or yeast phosphomannomutase, is localized on chromosome 22q13". Genomics. 40 (1): 41–7. doi: 10.1006/geno.1996.4536 . PMID   9070917.
6. Pirard M, Collet JF, Matthijs G, Van Schaftingen E (Sep 1997). "Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells". FEBS Lett. 411 (2–3): 251–4. doi: 10.1016/S0014-5793(97)00704-7 . PMID   9271215.
7. "Entrez Gene: PMM1 phosphomannomutase 1".
8. ČeŘovský V (2007). "Identification of three novel peptides isolated from the venom of the neotropical social wasp Polistes major major". Journal of Peptide Science. 13 (7): 445–450. doi:10.1002/psc.860. PMID   17559065. S2CID   41958134.

Further reading

• Wada Y, Sakamoto M (1997). "Isolation of the human phosphomannomutase gene (PMM1) and assignment to chromosome 22q13". Genomics. 39 (3): 416–7. doi:10.1006/geno.1996.4487. PMID   9119384.
• Hansen SH, Frank SR, Casanova JE (1997). "Cloning and characterization of human phosphomannomutase, a mammalian homologue of yeast SEC53". Glycobiology. 7 (6): 829–34. doi: 10.1093/glycob/7.6.829 . PMID   9376685.
• Collet JF, Stroobant V, Pirard M, et al. (1998). "A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif". J. Biol. Chem. 273 (23): 14107–12. doi: 10.1074/jbc.273.23.14107 . PMID   9603909.
• Pirard M, Achouri Y, Collet JF, et al. (1999). "Kinetic properties and tissular distribution of mammalian phosphomannomutase isozymes". Biochem. J. 339 (1): 201–7. doi:10.1042/0264-6021:3390201. PMC   1220145 . PMID   10085245.
• Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi: 10.1038/990031 . PMID   10591208.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Jensen H, Kjaergaard S, Klie F, Moller HU (2003). "Ophthalmic manifestations of congenital disorder of glycosylation type 1a". Ophthalmic Genet. 24 (2): 81–8. doi:10.1076/opge.24.2.81.13994. PMID   12789572. S2CID   29341185.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi: 10.1186/gb-2004-5-10-r84 . PMC   545604 . PMID   15461802.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• Silvaggi NR, Zhang C, Lu Z, et al. (2006). "The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a". J. Biol. Chem. 281 (21): 14918–26. doi: 10.1074/jbc.M601505200 . PMID   16540464.
• Baumbusch LO, Myhre S, Langerød A, et al. (2006). "Expression of full-length p53 and its isoform Deltap53 in breast carcinomas in relation to mutation status and clinical parameters". Mol. Cancer. 5: 47. doi: 10.1186/1476-4598-5-47 . PMC   1636663 . PMID   17054774.
• Barone R, Sturiale L, Fiumara A, et al. (2007). "Borderline mental development in a congenital disorder of glycosylation (CDG) type Ia patient with multisystemic involvement (intermediate phenotype)". J. Inherit. Metab. Dis. 30 (1): 107. doi:10.1007/s10545-006-0486-6. PMID   17186415. S2CID   12016939.