Version 5.4
Homo sapiens Protein: FAM20B
Summary
InnateDB Protein IDBP-389763.4
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol FAM20B
Protein Name family with sequence similarity 20, member B
Synonyms gxk1;
Species Homo sapiens
Ensembl Protein ENSP00000404005
InnateDB Gene IDBG-105087 (FAM20B)
Protein Structure
UniProt Annotation
Function Responsible for the 2-O-phosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature GAG chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG- protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1- O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O-phosphorylation may influence the catalytic activity of B3GAT3 (GlcAT-I) which completes the precursor tetrasaccharide of GAG-protein linkage regions on which the repeating disaccharide region is synthesized. {ECO:0000269PubMed:19473117}.
Subcellular Localization Golgi apparatus membrane {ECO:0000269PubMed:19473117}; Single-pass type II membrane protein {ECO:0000269PubMed:19473117}.
Disease Associations
Tissue Specificity Widely expressed. {ECO:0000269PubMed:15676076}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Protein Structure and Domains
PDB ID
InterPro
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-O75063
TrEMBL X6RH03
UniProt Splice Variant
Entrez Gene 9917
UniGene Hs.740494
RefSeq
HUGO HGNC:23017
OMIM 611063
CCDS
HPRD 13297
IMGT
EMBL AL139132
GenPept

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