POMT2

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Identifiers
Aliases|
External IDs| GeneCards: [1]
Orthologs
Species| Human| Mouse
Entrez| |

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Ensembl| |

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UniProt| |

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RefSeq (mRNA)| |

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RefSeq (protein)| |

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Location (UCSC)| n/a| n/a
PubMed search| n/a| n/a
Wikidata
| View/Edit Human|

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Protein O-mannosyl-transferase 2 is an enzyme that in humans is encoded by the POMT2 gene.[1][2][3]

## Contents

* 1 Function
* 2 References
* 3 Further reading
* 4 External links

## Function

[edit | edit source]

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][3]

## References

[edit | edit source]

1. ↑ 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.
2. ↑ 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.
3. ↑ 3.0 3.1 "Entrez Gene: POMT2 protein-O-mannosyltransferase 2".

## Further reading

[edit | edit source]

* 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". 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.

## External links

[edit | edit source]

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

* v
* t
* e

Transferases: glycosyltransferases (EC 2.4)

2.4.1: Hexosyl-
transferases|

| Glucosyl-|

* Phosphorylase
* Starch
* Glycogen
* Myo-
* Glycogen synthase
* Debranching enzyme
* Branching enzyme
* 1,3-Beta-glucan synthase
* Ceramide glucosyltransferase
* N-glycosyltransferase

|

Galactosyl-|

* Lactose synthase
* B-N-acetylglucosaminyl-glycopeptide b-1,4-galactosyltransferase
* Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase (C1GALT1)

Glucuronosyl-|

* B3GAT1
* B3GAT2
* B3GAT3

* UGT1A1
* UGT1A3
* UGT1A4
* UGT1A5
* UGT1A6
* UGT1A7
* UGT1A8
* UGT1A9
* UGT1A10

* UGT2A1
* UGT2A2
* UGT2A3
* UGT2B4
* UGT2B7
* UGT2B10
* UGT2B11
* UGT2B15
* UGT2B17
* UGT2B28

* Hyaluronan synthase: HAS1
* HAS2
* HAS3

Fucosyl-|

* POFUT1
* POFUT2
* FUT1
* FUT2
* FUT3
* FUT4
* FUT5
* FUT6
* FUT7
* FUT8
* FUT9
* FUT10
* FUT11

Mannosyl-|

* Dolichyl-phosphate-mannose-protein mannosyltransferase
* POMT1
* POMT2
* DPM1
* DPM3

* ALG1
* ALG2
* ALG3
* ALG6
* ALG8
* ALG9
* ALG12

2.4.2: Pentosyl-
transferases|

| Ribose|

| ADP-ribosyltransferase|

* NAD+:diphthamide ADP-ribosyltransferase
* Diphtheria toxin

* NAD(P)+:arginine ADP-ribosyltransferase
* Pertussis toxin
* Cholera toxin

* Poly ADP ribose polymerase

* Sirtuin

|

Phosphoribosyltransferase|

* Adenine phosphoribosyltransferase
* Hypoxanthine-guanine phosphoribosyltransferase
* Uracil phosphoribosyltransferase
* Amidophosphoribosyltransferase

Other|

* Purine nucleoside phosphorylase: Thymidine phosphorylase
* ECGF1

Other|

* Xylosyltransferase
* XYLT1
* XYLT2
* Arabinosyltransferase
* Indolylacetylinositol arabinosyltransferase

2.4.99: Sialyl
transferases|

* Beta-galactoside alpha-2,6-sialyltransferase
* Monosialoganglioside sialyltransferase
* ST8SIA4

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