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XYLT2
Identifiers
Aliases	XYLT2, PXT-II, XT2, xylT-II, SOS, xylosyltransferase 2
External IDs	OMIM: 608125; MGI: 2444797; HomoloGene: 23349; GeneCards: XYLT2; OMA:XYLT2 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17q21.33 Start 50,346,126 bp End 50,363,138 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 D Start 94,554,677 bp End 94,568,341 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of stomach fundus stromal cell of endometrium left testis apex of heart right testis right uterine tube right ovary granulocyte prostate Top expressed in right kidney lip tail of embryo primary visual cortex neural layer of retina ventricular zone superior frontal gyrus dentate gyrus of hippocampal formation granule cell stroma of bone marrow genital tubercle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity acetylglucosaminyltransferase activity glycosyltransferase activity protein xylosyltransferase activity magnesium ion binding manganese ion binding metal ion binding Cellular component integral component of membrane Golgi apparatus endoplasmic reticulum membrane endoplasmic reticulum membrane Golgi membrane cellular component extracellular space extracellular region Biological process chondroitin sulfate biosynthetic process chondroitin sulfate proteoglycan biosynthetic process heparan sulfate proteoglycan biosynthetic process heparin biosynthetic process glycosaminoglycan biosynthetic process proteoglycan biosynthetic process glycosaminoglycan metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 64132 217119 Ensembl ENSG00000015532 ENSMUSG00000020868 UniProt Q9H1B5 Q9EPL0 RefSeq (mRNA) NM_022167 NM_145828 RefSeq (protein) NP_071450 NP_665827 Location (UCSC) Chr 17: 50.35 – 50.36 Mb Chr 11: 94.55 – 94.57 Mb PubMed search
Wikidata
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Xylosyltransferase 2 is an enzyme that in humans is encoded by the XYLT2 gene.

Function

The protein encoded by this gene is an isoform of xylosyltransferase, which belongs to a family of glycosyltransferases. This enzyme transfers xylose from UDP-xylose to specific serine residues of the core protein and initiates the biosynthesis of glycosaminoglycan chains in proteoglycans including chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate.

Clinical significance

The enzyme activity, which is increased in scleroderma patients, is a diagnostic marker for the determination of sclerotic activity in systemic sclerosis.

Mutations in this gene have been shown to be the cause of the spondylo-ocular syndrome. It has also been implicated as cofactor in pseudoxanthoma elasticum.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000015532 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000020868 – 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. Götting C, Kuhn J, Zahn R, Brinkmann T, Kleesiek K (Dec 2000). "Molecular cloning and expression of human UDP-d-Xylose:proteoglycan core protein beta-d-xylosyltransferase and its first isoform XT-II". Journal of Molecular Biology. 304 (4): 517–28. doi:10.1006/jmbi.2000.4261. PMID 11099377.
6. ^ "Entrez Gene: XYLT2 xylosyltransferase II".
7. Taylan F, Costantini A, Coles N, Pekkinen M, Héon E, Şıklar Z, Berberoğlu M, Kämpe A, Kıykım E, Grigelioniene G, Tüysüz B, Mäkitie O (Mar 2016). "Spondyloocular Syndrome - Novel Mutations in XYLT2 Gene and Expansion of the Phenotypic Spectrum". Journal of Bone and Mineral Research. 31 (8): 1577–1585. doi:10.1002/jbmr.2834. PMID 26987875.

Further reading

• Götting C, Kuhn J, Brinkmann T, Kleesiek K (Apr 1998). "Xylosylation of alternatively spliced isoforms of Alzheimer APP by xylosyltransferase". Journal of Protein Chemistry. 17 (3): 295–302. doi:10.1023/A:1022549121672. PMID 9588955. S2CID 39212266.
• Götting C, Sollberg S, Kuhn J, Weilke C, Huerkamp C, Brinkmann T, Krieg T, Kleesiek K (Jun 1999). "Serum xylosyltransferase: a new biochemical marker of the sclerotic process in systemic sclerosis". The Journal of Investigative Dermatology. 112 (6): 919–24. doi:10.1046/j.1523-1747.1999.00590.x. PMID 10383739.
• Kuhn J, Götting C, Schnölzer M, Kempf T, Brinkmann T, Kleesiek K (Feb 2001). "First isolation of human UDP-D-xylose: proteoglycan core protein beta-D-xylosyltransferase secreted from cultured JAR choriocarcinoma cells". The Journal of Biological Chemistry. 276 (7): 4940–7. doi:10.1074/jbc.M005111200. PMID 11087729.
• Götting C, Kuhn J, Brinkmann T, Kleesiek K (Mar 2002). "Xylosyltransferase activity in seminal plasma of infertile men". Clinica Chimica Acta; International Journal of Clinical Chemistry. 317 (1–2): 199–202. doi:10.1016/S0009-8981(01)00793-8. PMID 11814476.
• Schön S, Prante C, Müller S, Schöttler M, Tarnow L, Kuhn J, Kleesiek K, Götting C (Oct 2005). "Impact of polymorphisms in the genes encoding xylosyltransferase I and a homologue in type 1 diabetic patients with and without nephropathy". Kidney International. 68 (4): 1483–90. doi:10.1111/j.1523-1755.2005.00561.x. PMID 16164625.
• Schön S, Prante C, Bahr C, Kuhn J, Kleesiek K, Götting C (May 2006). "Cloning and recombinant expression of active full-length xylosyltransferase I (XT-I) and characterization of subcellular localization of XT-I and XT-II". The Journal of Biological Chemistry. 281 (20): 14224–31. doi:10.1074/jbc.M510690200. PMID 16569644.
• Voglmeir J, Voglauer R, Wilson IB (Mar 2007). "XT-II, the second isoform of human peptide-O-xylosyltransferase, displays enzymatic activity". The Journal of Biological Chemistry. 282 (9): 5984–90. doi:10.1074/jbc.M608087200. PMC 2850172. PMID 17194707.

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