Version 5.4
Mus musculus Gene: Galnt7
Summary
InnateDB Gene IDBG-156288.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Galnt7
Gene Name UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase 7
Synonyms AI225872
Species Mus musculus
Ensembl Gene ENSMUSG00000031608
Encoded Proteins
IDBP-156290
UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase 7
IDBP-260530
UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase 7
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 ENSG00000109586:
This gene encodes GalNAc transferase 7, a member of the GalNAc-transferase family. The enzyme encoded by this gene controls the initiation step of mucin-type O-linked protein glycosylation and transfer of N-acetylgalactosamine to serine and threonine amino acid residues. This enzyme is a type II transmembrane protein and shares common sequence motifs with other family members. Unlike other family members, this enzyme shows exclusive specificity for partially GalNAc-glycosylated acceptor substrates and shows no activity with non-glycosylated peptides. This protein may function as a follow-up enzyme in the initiation step of O-glycosylation. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 8:57523828-57653032
Strand Reverse strand
Band B2
Transcripts
ENSMUST00000034021 ENSMUSP00000034021
ENSMUST00000110316 ENSMUSP00000105945
ENSMUST00000139417
ENSMUST00000156907
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 3 experimentally validated interaction(s) in this database.
They are also associated with 2 interaction(s) predicted by orthology.
Experimentally validated
Total 3 [view]
Protein-Protein 2 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004653 polypeptide N-acetylgalactosaminyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006493 protein O-linked glycosylation
Cellular Component
GO:0000139 Golgi membrane
GO:0016020 membrane
GO:0016021 integral component of membrane
Orthologs
Species
Homo sapiens
Bos taurus
Gene ID
Gene Order
ENSG00000109586
View Gene Order
ENSBTAG00000016845
Not yet available
Pathways
NETPATH
REACTOME
REACT_198517
O-linked glycosylation of mucins pathway
REACT_247926
Metabolism of proteins pathway
REACT_236283
Post-translational protein modification pathway
REACT_204003
O-linked glycosylation pathway
KEGG
mmu00512
Mucin type O-Glycan biosynthesis pathway
INOH
PID NCI
Pathway Predictions based on Human Orthology Data
NETPATH
REACTOME
REACT_115606
O-linked glycosylation of mucins pathway
REACT_22161
Post-translational protein modification pathway
REACT_200727
O-linked glycosylation pathway
REACT_17015
Metabolism of proteins pathway
KEGG
hsa00512
Mucin type O-Glycan biosynthesis pathway
INOH
PID NCI
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene
UniGene Mm.408510 Mm.445855 Mm.460157 Mm.62886
RefSeq NM_001167981 NM_144731
OMIM
CCDS CCDS22317 CCDS52552
HPRD
IMGT
MGI ID
MGI Symbol
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