POMT2

POMT2
Identifiers
Aliases	POMT2 , LGMD2N, MDDGA2, MDDGB2, MDDGC2, protein O-mannosyltransferase 2, LGMDR14
External IDs	OMIM: 607439 MGI: 2444430 HomoloGene: 5297 GeneCards: POMT2
Gene location (Human) Chr. Chromosome 14 (human) [1] Band 14q24.3 Start 77,274,956 bp [1] End 77,320,883 bp [1]
Gene location (Mouse) Chr. Chromosome 12 (mouse) [2] Band 12|12 D2 Start 87,106,861 bp [2] End 87,147,968 bp [2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • glycosyltransferase activity • dolichyl-phosphate-mannose-protein mannosyltransferase activity • transferase activity • mannosyltransferase activity • metal ion binding Cellular component • integral component of membrane • endoplasmic reticulum • membrane • endoplasmic reticulum membrane Biological process • protein O-linked glycosylation • protein O-linked mannosylation • ER-associated misfolded protein catabolic process • mannosylation • positive regulation of protein O-linked glycosylation • protein glycosylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	29954	217734
Ensembl	ENSG00000009830	ENSMUSG00000034126
UniProt	Q9UKY4	Q8BGQ4
RefSeq (mRNA)	NM_013382	NM_153415
RefSeq (protein)	NP_037514	NP_700464
Location (UCSC)	Chr 14: 77.27 – 77.32 Mb	Chr 12: 87.11 – 87.15 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Protein O-mannosyl-transferase 2 is an enzyme that in humans is encoded by the POMT2 gene. ^{[5] [6] [7]}

Function

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] ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000009830 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000034126 - 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. Fukuda S, Sumii M, Masuda Y, Takahashi M, Koike N, Teishima J, Yasumoto H, Itamoto T, Asahara T, Dohi K, Kamiya K (Feb 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.
6. Willer T, Amselgruber W, Deutzmann R, Strahl S (Dec 2002). "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. doi: 10.1093/glycob/cwf086 . PMID   12460945.
7. "Entrez Gene: POMT2 protein-O-mannosyltransferase 2".

Further reading

• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi: 10.1101/gr.6.9.791 . PMID   8889548.
• 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 . PMC   139241 . 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 . PMC   327176 . 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. PMC   528928 . PMID   15489334.
• van Reeuwijk J, Janssen M, van den Elzen C, et al. (2006). "POMT2 mutations cause α-dystroglycan hypoglycosylation and Walker-Warburg syndrome". J. Med. Genet. 42 (12): 907–12. doi:10.1136/jmg.2005.031963. PMC   1735967 . 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. PMC   1356129 . 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" (PDF). Neurology. 69 (12): 1254–60. doi:10.1212/01.wnl.0000268489.60809.c4. PMID   17634419. S2CID   26108950.
• 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.

External links

• GeneReviews/NCBI/NIH/UW entry on Congenital Muscular Dystrophy Overview