POMT2

From Wikipedia, the free encyclopedia

Protein-O-mannosyltransferase 2

Identifiers

POMT2; DKFZp686G10254; FLJ22309

External IDs

OMIM: 607439 MGI: 2444430 HomoloGene: 5297

Gene ontology
Molecular Function:	• mannosyltransferase activity • magnesium ion binding • dolichyl-phosphate-mannose-protein mannosyltransferase activity • transferase activity, transferring glycosyl groups
Cellular Component:	• endoplasmic reticulum • membrane • integral to membrane
Biological Process:	• protein amino acid O-linked glycosylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_013382 (mRNA)
NP_037514 (protein)

NM_153415 (mRNA)
NP_700464 (protein)

Location

Chr 14: 76.81 - 76.86 Mb

Chr 12: 88 - 88.04 Mb

Pubmed search

[1]

[2]

Protein-O-mannosyltransferase 2, also known as POMT2, is a human gene.^[1]

POMT2 encodes an integral membrane protein of the endoplasmic reticulum (ER) that shares significant sequence similarity with a family of protein O-mannosyltransferases of S. cerevisiae. For additional background information, see POMT1 (MIM 607423).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: POMT2 protein-O-mannosyltransferase 2.

[edit] Further reading

Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Fukuda S, Sumii M, Masuda Y, et al. (2001). "Murine and human SDF2L1 is an endoplasmic reticulum stress-inducible gene and encodes a new member of the Pmt/rt protein family.". Biochem. Biophys. Res. Commun. 280 (1): 407–14. doi:10.1006/bbrc.2000.4111. PMID 11162531.
Willer T, Amselgruber W, Deutzmann R, Strahl S (2004). "Characterization of POMT2, a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids.". Glycobiology 12 (11): 771–83. PMID 12460945.
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. doi:10.1073/pnas.242603899. PMID 12477932.
Heilig R, Eckenberg R, Petit JL, et al. (2003). "The DNA sequence and analysis of human chromosome 14.". Nature 421 (6923): 601–7. doi:10.1038/nature01348. PMID 12508121.
Manya H, Chiba A, Yoshida A, et al. (2004). "Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity.". Proc. Natl. Acad. Sci. U.S.A. 101 (2): 500–5. doi:10.1073/pnas.0307228101. PMID 14699049.
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.
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. PMID 15489334.
van Reeuwijk J, Janssen M, van den Elzen C, et al. (2006). "POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-Warburg syndrome.". J. Med. Genet. 42 (12): 907–12. doi:10.1136/jmg.2005.031963. PMID 15894594.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.
Akasaka-Manya K, Manya H, Nakajima A, et al. (2006). "Physical and functional association of human protein O-mannosyltransferases 1 and 2.". J. Biol. Chem. 281 (28): 19339–45. doi:10.1074/jbc.M601091200. PMID 16698797.
Yanagisawa A, Bouchet C, Van den Bergh PY, et al. (2007). "New POMT2 mutations causing congenital muscular dystrophy: identification of a founder mutation.". Neurology 69 (12): 1254–60. doi:10.1212/01.wnl.0000268489.60809.c4. PMID 17634419.
Biancheri R, Falace A, Tessa A, et al. (2007). "POMT2 gene mutation in limb-girdle muscular dystrophy with inflammatory changes.". Biochem. Biophys. Res. Commun. 363 (4): 1033–7. doi:10.1016/j.bbrc.2007.09.066. PMID 17923109.