Version 5.4
Homo sapiens Gene: GALNT9
Summary
InnateDB Gene IDBG-65443.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol GALNT9
Gene Name UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 9 (GalNAc-T9)
Synonyms
Species Homo sapiens
Ensembl Gene ENSG00000182870
Encoded Proteins
IDBP-65445
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 9 (GalNAc-T9)
IDBP-235616
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 9 (GalNAc-T9)
IDBP-385232
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 9 (GalNAc-T9)
IDBP-588866
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 9 (GalNAc-T9)
IDBP-596298
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 9 (GalNAc-T9)
IDBP-589279
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 9 (GalNAc-T9)
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. This gene is expressed specifically in the brain, with highest expression in the cerebellum. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 12:132196372-132329349
Strand Reverse strand
Band q24.33
Transcripts
ENST00000328957 ENSP00000329846
ENST00000397325 ENSP00000380488
ENST00000411988 ENSP00000394446
ENST00000424720
ENST00000541995 ENSP00000440544
ENST00000538356 ENSP00000444709
ENST00000542942 ENSP00000438221
ENST00000535208
ENST00000540493
ENST00000614360
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:0004653 polypeptide N-acetylgalactosaminyltransferase activity
GO:0016740 transferase activity
GO:0016757 transferase activity, transferring glycosyl groups
GO:0046872 metal ion binding
Biological Process
GO:0006486 protein glycosylation
GO:0006493 protein O-linked glycosylation
GO:0008152 metabolic process
GO:0016266 O-glycan processing
GO:0043687 post-translational protein modification
GO:0044267 cellular protein metabolic process
Cellular Component
GO:0000139 Golgi membrane
GO:0005794 Golgi apparatus
GO:0016021 integral component of membrane
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000033316
View Gene Order
ENSBTAG00000005644
Not yet available
Pathways
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
RefSeq NM_001122636 NM_021808
HUGO
OMIM
CCDS CCDS41866
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