ALG11

Asparagine-linked glycosylation protein 11 is an enzyme encoded by the ALG11 gene.[5]

ALG11
Identifiers
Aliases	ALG11, CDG1P, GT8, alpha-1,2-mannosyltransferase, ALG11 alpha-1,2-mannosyltransferase
External IDs	OMIM: 613666 MGI: 2142632 HomoloGene: 68893 GeneCards: ALG11
Gene location (Human) Chr. Chromosome 13 (human)[1] Band 13q14.3 Start 52,012,398 bp[1] End 52,033,600 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8|8 A2 Start 22,060,721 bp[2] End 22,071,627 bp[2]
Gene ontology Molecular function • transferase activity • transferase activity, transferring glycosyl groups • GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity Cellular component • integral component of membrane • endoplasmic reticulum • membrane • endoplasmic reticulum membrane Biological process • mannosylation • oligosaccharide-lipid intermediate biosynthetic process • protein glycosylation in endoplasmic reticulum • protein N-linked glycosylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	440138	207958
Ensembl	ENSG00000253710	ENSMUSG00000063362
UniProt	Q2TAA5	Q3TZM9
RefSeq (mRNA)	NM_001004127	NM_001243161 NM_183142
RefSeq (protein)	NP_001004127	NP_001230090 NP_898965
Location (UCSC)	Chr 13: 52.01 – 52.03 Mb	Chr 8: 22.06 – 22.07 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

See also

• Congenital disorder of glycosylation

[6]

[7]

References

1. GRCh38: Ensembl release 89: ENSG00000253710 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000063362 - 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. "Entrez Gene: asparagine-linked glycosylation 11".
6. Cipollo, JF; Trimble, RB; Chi, JH; Yan, Q; Dean, N (2001). "The yeast ALG11 gene specifies addition of the terminal alpha 1,2-Man to the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the cytosolic side of the endoplasmic reticulum". J. Biol. Chem. 276 (24): 21828–40. doi:10.1074/jbc.m010896200. PMID 11278778.
7. Gao, XD; Nishikawa, A; Dean, N. (Jun 2004). "Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum. 2004". Glycobiology. 14 (6): 559–70. CiteSeerX 10.1.1.572.6611. doi:10.1093/glycob/cwh072. PMID 15044395.

External links

• Human ALG11 genome location and ALG11 gene details page in the UCSC Genome Browser.

Further reading

• Rohozinski J, Lamb DJ, Bishop CE (2006). "UTP14c is a recently acquired retrogene associated with spermatogenesis and fertility in man". Biol. Reprod. 74 (4): 644–51. doi:10.1095/biolreprod.105.046698. PMID 16354793.
• Rind N, Schmeiser V, Thiel C, et al. (2010). "A severe human metabolic disease caused by deficiency of the endoplasmatic mannosyltransferase hALG11 leads to congenital disorder of glycosylation-Ip". Hum. Mol. Genet. 19 (8): 1413–24. doi:10.1093/hmg/ddq016. PMID 20080937.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Cipollo JF, Trimble RB, Chi JH, Yan Q, Dean N (June 2001). "The yeast ALG11 gene specifies addition of the terminal alpha 1,2-Man to the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the cytosolic side of the endoplasmic reticulum". J. Biol. Chem. 276 (24): 21828–40. doi:10.1074/jbc.M010896200. PMID 11278778.