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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Xylosyltransferase 2''' is an [[enzyme]] that in humans is encoded by the ''XYLT2'' [[gene]].<ref name="pmid11099377">{{cite journal | vauthors = Götting C, Kuhn J, Zahn R, Brinkmann T, Kleesiek K | title = Molecular cloning and expression of human UDP-d-Xylose:proteoglycan core protein beta-d-xylosyltransferase and its first isoform XT-II | journal = Journal of Molecular Biology | volume = 304 | issue = 4 | pages = 517–28 | date = Dec 2000 | pmid = 11099377 | pmc =  | doi = 10.1006/jmbi.2000.4261 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: XYLT2 xylosyltransferase II| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64132| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Xylosyltransferase II
| HGNCid = 15517
| Symbol = XYLT2
| AltSymbols =; XT-II; XT2; xylT-II
| OMIM = 608125
| ECnumber = 
| Homologene = 23349
| MGIid = 2444797
| GeneAtlas_image1 = PBB_GE_XYLT2_219401_at_tn.png
| Function = {{GNF_GO|id=GO:0008375 |text = acetylglucosaminyltransferase activity}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0030158 |text = protein xylosyltransferase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006024 |text = glycosaminoglycan biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 64132
    | Hs_Ensembl = ENSG00000015532
    | Hs_RefseqProtein = NP_071450
    | Hs_RefseqmRNA = NM_022167
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 45778392
    | Hs_GenLoc_end = 45793511
    | Hs_Uniprot = Q9H1B5
    | Mm_EntrezGene = 217119
    | Mm_Ensembl = ENSMUSG00000020868
    | Mm_RefseqmRNA = NM_145828
    | Mm_RefseqProtein = NP_665827
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 94479889
    | Mm_GenLoc_end = 94493550
    | Mm_Uniprot = Q3TZ69
  }}
}}


{{CMG}}
The protein encoded by this gene is an isoform of xylosyltransferase, which belongs to a family of [[glycosyltransferases]]. This enzyme transfers xylose from [[Uridine diphosphate|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]].<ref name="entrez"/>


== Clinical significance ==


The enzyme activity, which is increased in [[scleroderma]] patients, is a diagnostic marker for the determination of sclerotic activity in systemic sclerosis.<ref name="entrez">{{cite web | title = Entrez Gene: XYLT2 xylosyltransferase II| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64132| accessdate = }}</ref>


'''Xylosyltransferase II''', also known as '''XYLT2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: XYLT2 xylosyltransferase II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64132| accessdate = }}</ref>
Mutations in this gene have been shown to be the cause of the [[spondylo-ocular syndrome]].<ref name=Taylan_2016>{{cite journal | vauthors = Taylan F, Costantini A, Coles N, Pekkinen M, Héon E, Şıklar Z, Berberoğlu M, Kämpe A, Kıykım E, Grigelioniene G, Tüysüz B, Mäkitie O | title = Spondyloocular Syndrome - Novel Mutations in XYLT2 Gene and Expansion of the Phenotypic Spectrum | journal = Journal of Bone and Mineral Research | date = Mar 2016 | pmid = 26987875 | doi = 10.1002/jbmr.2834 }}</ref> It has also been implicated as  cofactor in [[pseudoxanthoma elasticum]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== References ==
{{PBB_Summary
{{reflist}}
| section_title =  
| summary_text = 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. The enzyme activity, which is increased in scleroderma patients, is a diagnostic marker for the determination of sclerotic activity in systemic sclerosis.<ref name="entrez">{{cite web | title = Entrez Gene: XYLT2 xylosyltransferase II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64132| accessdate = }}</ref>
}}


==References==
== Further reading ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Götting C, Kuhn J, Brinkmann T, Kleesiek K | title = Xylosylation of alternatively spliced isoforms of Alzheimer APP by xylosyltransferase | journal = Journal of Protein Chemistry | volume = 17 | issue = 3 | pages = 295–302 | date = Apr 1998 | pmid = 9588955 | doi = 10.1023/A:1022549121672 }}
| citations =
* {{cite journal | vauthors = Götting C, Sollberg S, Kuhn J, Weilke C, Huerkamp C, Brinkmann T, Krieg T, Kleesiek K | title = Serum xylosyltransferase: a new biochemical marker of the sclerotic process in systemic sclerosis | journal = The Journal of Investigative Dermatology | volume = 112 | issue = 6 | pages = 919–24 | date = Jun 1999 | pmid = 10383739 | doi = 10.1046/j.1523-1747.1999.00590.x }}
*{{cite journal | author=Götting C, Kuhn J, Brinkmann T, Kleesiek K |title=Xylosylation of alternatively spliced isoforms of Alzheimer APP by xylosyltransferase. |journal=J. Protein Chem. |volume=17 |issue= 3 |pages= 295-302 |year= 1998 |pmid= 9588955 |doi= }}
* {{cite journal | vauthors = Kuhn J, Götting C, Schnölzer M, Kempf T, Brinkmann T, Kleesiek K | title = First isolation of human UDP-D-xylose: proteoglycan core protein beta-D-xylosyltransferase secreted from cultured JAR choriocarcinoma cells | journal = The Journal of Biological Chemistry | volume = 276 | issue = 7 | pages = 4940–7 | date = Feb 2001 | pmid = 11087729 | doi = 10.1074/jbc.M005111200 }}
*{{cite journal | author=Götting C, Sollberg S, Kuhn J, ''et al.'' |title=Serum xylosyltransferase: a new biochemical marker of the sclerotic process in systemic sclerosis. |journal=J. Invest. Dermatol. |volume=112 |issue= 6 |pages= 919-24 |year= 1999 |pmid= 10383739 |doi= 10.1046/j.1523-1747.1999.00590.x }}
* {{cite journal | vauthors = Götting C, Kuhn J, Brinkmann T, Kleesiek K | title = Xylosyltransferase activity in seminal plasma of infertile men | journal = Clinica Chimica Acta; International Journal of Clinical Chemistry | volume = 317 | issue = 1-2 | pages = 199–202 | date = Mar 2002 | pmid = 11814476 | doi = 10.1016/S0009-8981(01)00793-8 }}
*{{cite journal | author=Kuhn J, Götting C, Schnölzer M, ''et al.'' |title=First isolation of human UDP-D-xylose: proteoglycan core protein beta-D-xylosyltransferase secreted from cultured JAR choriocarcinoma cells. |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 4940-7 |year= 2001 |pmid= 11087729 |doi= 10.1074/jbc.M005111200 }}
* {{cite journal | vauthors = Schön S, Prante C, Müller S, Schöttler M, Tarnow L, Kuhn J, Kleesiek K, Götting C | title = Impact of polymorphisms in the genes encoding xylosyltransferase I and a homologue in type 1 diabetic patients with and without nephropathy | journal = Kidney International | volume = 68 | issue = 4 | pages = 1483–90 | date = Oct 2005 | pmid = 16164625 | doi = 10.1111/j.1523-1755.2005.00561.x }}
*{{cite journal | author=Götting C, Kuhn J, Zahn R, ''et al.'' |title=Molecular cloning and expression of human UDP-d-Xylose:proteoglycan core protein beta-d-xylosyltransferase and its first isoform XT-II. |journal=J. Mol. Biol. |volume=304 |issue= 4 |pages= 517-28 |year= 2001 |pmid= 11099377 |doi= 10.1006/jmbi.2000.4261 }}
* {{cite journal | vauthors = Schön S, Prante C, Bahr C, Kuhn J, Kleesiek K, Götting C | title = Cloning and recombinant expression of active full-length xylosyltransferase I (XT-I) and characterization of subcellular localization of XT-I and XT-II | journal = The Journal of Biological Chemistry | volume = 281 | issue = 20 | pages = 14224–31 | date = May 2006 | pmid = 16569644 | doi = 10.1074/jbc.M510690200 }}
*{{cite journal  | author=Götting C, Kuhn J, Brinkmann T, Kleesiek K |title=Xylosyltransferase activity in seminal plasma of infertile men. |journal=Clin. Chim. Acta |volume=317 |issue= 1-2 |pages= 199-202 |year= 2002 |pmid= 11814476 |doi=  }}
* {{cite journal | vauthors = Voglmeir J, Voglauer R, Wilson IB | title = XT-II, the second isoform of human peptide-O-xylosyltransferase, displays enzymatic activity | journal = The Journal of Biological Chemistry | volume = 282 | issue = 9 | pages = 5984–90 | date = Mar 2007 | pmid = 17194707 | pmc = 2850172 | doi = 10.1074/jbc.M608087200 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Schön S, Prante C, Müller S, ''et al.'' |title=Impact of polymorphisms in the genes encoding xylosyltransferase I and a homologue in type 1 diabetic patients with and without nephropathy. |journal=Kidney Int. |volume=68 |issue= 4 |pages= 1483-90 |year= 2005 |pmid= 16164625 |doi= 10.1111/j.1523-1755.2005.00561.x }}
*{{cite journal | author=Schön S, Prante C, Bahr C, ''et al.'' |title=Cloning and recombinant expression of active full-length xylosyltransferase I (XT-I) and characterization of subcellular localization of XT-I and XT-II. |journal=J. Biol. Chem. |volume=281 |issue= 20 |pages= 14224-31 |year= 2006 |pmid= 16569644 |doi= 10.1074/jbc.M510690200 }}
*{{cite journal | author=Voglmeir J, Voglauer R, Wilson IB |title=XT-II, the second isoform of human peptide-O-xylosyltransferase, displays enzymatic activity. |journal=J. Biol. Chem. |volume=282 |issue= 9 |pages= 5984-90 |year= 2007 |pmid= 17194707 |doi= 10.1074/jbc.M608087200 }}
}}
{{refend}}
{{refend}}


{{WH}}
{{Glycosyltransferases}}
{{WS}}
{{gene-17-stub}}

Latest revision as of 03:26, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

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Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Xylosyltransferase 2 is an enzyme that in humans is encoded by the XYLT2 gene.[1][2]

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.[2]

Clinical significance

The enzyme activity, which is increased in scleroderma patients, is a diagnostic marker for the determination of sclerotic activity in systemic sclerosis.[2]

Mutations in this gene have been shown to be the cause of the spondylo-ocular syndrome.[3] It has also been implicated as cofactor in pseudoxanthoma elasticum.

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 2.2 "Entrez Gene: XYLT2 xylosyltransferase II".
  3. ↑ 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. 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.
  • 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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