Version 5.4
Bos taurus Gene: MGAT2
Summary
InnateDB Gene IDBG-648580.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol MGAT2
Gene Name Uncharacterized protein
Synonyms
Species Bos taurus
Ensembl Gene ENSBTAG00000033891
Encoded Proteins
IDBP-701316
mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary This gene does not have any Entrez summary - the following is the summary from its human ortholog ENSG00000168282:
The product of this gene is a Golgi enzyme catalyzing an essential step in the conversion of oligomannose to complex N-glycans. The enzyme has the typical glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. Mutations in this gene may lead to carbohydrate-deficient glycoprotein syndrome, type II. The coding region of this gene is intronless. Transcript variants with a spliced 5' UTR may exist, but their biological validity has not been determined. [provided by RefSeq, Jul 2008]
The product of this gene is a Golgi enzyme catalyzing an essential step in the conversion of oligomannose to complex N-glycans. The enzyme has the typical glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. Mutations in this gene may lead to carbohydrate-deficient glycoprotein syndrome, type II. The coding region of this gene is intronless. Transcript variants with a spliced 5\' UTR may exist, but their biological validity has not been determined. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 10:42701307-42702665
Strand Forward strand
Band
Transcripts
ENSBTAT00000048092 ENSBTAP00000045192
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0008455 alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity
Biological Process
GO:0009312 oligosaccharide biosynthetic process
GO:0018279 protein N-linked glycosylation via asparagine
Cellular Component
GO:0005795 Golgi stack
GO:0016020 membrane
GO:0016021 integral component of membrane
Orthologs
Species
Homo sapiens
Mus musculus
Gene ID
Gene Order
ENSG00000168282
View Gene Order
ENSMUSG00000043998
View Gene Order
Pathway Predictions based on Human Orthology Data
NETPATH
REACTOME
REACT_25302
Reactions specific to the complex N-glycan synthesis pathway pathway
REACT_25046
Transport to the Golgi and subsequent modification pathway
REACT_22426
Asparagine N-linked glycosylation pathway
REACT_22161
Post-translational protein modification pathway
REACT_25208
N-glycan antennae elongation in the medial/trans-Golgi pathway
REACT_17015
Metabolism of proteins pathway
REACT_198566
N-glycan antennae elongation in the medial/trans-Golgi pathway
REACT_206143
Transport to the Golgi and subsequent modification pathway
REACT_198568
Reactions specific to the complex N-glycan synthesis pathway pathway
REACT_247926
Metabolism of proteins pathway
REACT_236283
Post-translational protein modification pathway
REACT_237472
Asparagine N-linked glycosylation pathway
KEGG
hsa00510
N-Glycan biosynthesis pathway
mmu00510
N-Glycan biosynthesis pathway
INOH
PID NCI
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene
UniGene
RefSeq XM_005193645 XM_005211733
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL
GenPept
RNA Seq Atlas

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca