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Protein

Xylosyltransferase 2

Gene

XYLT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the formation of heparan sulfate and chondroitin sulfate proteoglycans (PubMed:26027496). Probably catalyzes the first step in biosynthesis of glycosaminoglycan. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Initial enzyme in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans in fibroblasts and chondrocytes (By similarity). Its enzyme activity has not been demonstrated.By similarity1 Publication

Catalytic activityi

Transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxy group of an acceptor protein substrate.

Cofactori

Pathwayi: chondroitin sulfate biosynthesis

This protein is involved in the pathway chondroitin sulfate biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway chondroitin sulfate biosynthesis and in Glycan metabolism.

Pathwayi: heparan sulfate biosynthesis

This protein is involved in the pathway heparan sulfate biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway heparan sulfate biosynthesis and in Glycan metabolism.

GO - Molecular functioni

  • acetylglucosaminyltransferase activity Source: InterPro
  • protein xylosyltransferase activity Source: UniProtKB

GO - Biological processi

  • chondroitin sulfate biosynthetic process Source: UniProtKB-UniPathway
  • chondroitin sulfate proteoglycan biosynthetic process Source: UniProtKB
  • glycosaminoglycan biosynthetic process Source: UniProtKB
  • heparan sulfate proteoglycan biosynthetic process Source: UniProtKB
  • heparin biosynthetic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS00371-MONOMER.
BRENDAi2.4.2.26. 2681.
SignaLinkiQ9H1B5.
UniPathwayiUPA00755.
UPA00756.

Protein family/group databases

CAZyiGT14. Glycosyltransferase Family 14.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylosyltransferase 2 (EC:2.4.2.26)
Alternative name(s):
Peptide O-xylosyltransferase 1
Xylosyltransferase II
Short name:
XT-II
Short name:
XylT-II
Gene namesi
Name:XYLT2
Synonyms:XT2
ORF Names:UNQ3058/PRO9878
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:15517. XYLT2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515CytoplasmicSequence analysisAdd
BLAST
Transmembranei16 – 3621Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini37 – 865829LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Spondyloocular syndrome (SOS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by cataract, loss of vision due to retinal detachment, facial dysmorphism, facial hypotonia, normal height with disproportional short trunk, osteoporosis, immobile spine with thoracic kyphosis and reduced lumbal lordosis.
See also OMIM:605822
Pseudoxanthoma elasticum (PXE)1 Publication
The gene represented in this entry acts as a disease modifier. PXE patients carrying causative ABCC6 mutations, manifest a more severe disease course characterized by earlier onset, frequent skin lesions and higher organ involvement, in the presence of XYLT2 variants.1 Publication
Disease descriptionA multisystem disorder characterized by accumulation of mineralized and fragmented elastic fibers in the skin, vascular walls, and Burch membrane in the eye. Clinically, patients exhibit characteristic lesions of the posterior segment of the eye including peau d'orange, angioid streaks, and choroidal neovascularizations, of the skin including soft, ivory colored papules in a reticular pattern that predominantly affect the neck and large flexor surfaces, and of the cardiovascular system with peripheral and coronary arterial occlusive disease as well as gastrointestinal bleedings.
See also OMIM:264800
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti801 – 8011T → R in PXE; acts as a modifier of disease severity; more frequent in patients with a severe disease course. 1 Publication
Corresponds to variant rs6504649 [ dbSNP | Ensembl ].
VAR_022454

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiXYLT2.
MIMi264800. phenotype.
605822. phenotype.
PharmGKBiPA37974.

Polymorphism and mutation databases

BioMutaiXYLT2.
DMDMi126302616.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 865865Xylosyltransferase 2PRO_0000191406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence analysis
Glycosylationi327 – 3271N-linked (GlcNAc...)Sequence analysis
Glycosylationi683 – 6831N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Contains disulfide bonds.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9H1B5.
MaxQBiQ9H1B5.
PaxDbiQ9H1B5.
PeptideAtlasiQ9H1B5.
PRIDEiQ9H1B5.

PTM databases

iPTMnetiQ9H1B5.
PhosphoSiteiQ9H1B5.

Expressioni

Tissue specificityi

Widely expressed. Expressed at higher level in kidney and pancreas.1 Publication

Gene expression databases

BgeeiQ9H1B5.
CleanExiHS_XYLT2.
ExpressionAtlasiQ9H1B5. baseline and differential.
GenevisibleiQ9H1B5. HS.

Organism-specific databases

HPAiHPA016456.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi122081. 12 interactions.
STRINGi9606.ENSP00000017003.

Structurei

3D structure databases

ProteinModelPortaliQ9H1B5.
SMRiQ9H1B5. Positions 234-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0799. Eukaryota.
ENOG410XQ7M. LUCA.
GeneTreeiENSGT00760000119183.
HOGENOMiHOG000070086.
HOVERGENiHBG059443.
InParanoidiQ9H1B5.
KOiK00771.
OMAiVPRHCQL.
OrthoDBiEOG7D85VR.
PhylomeDBiQ9H1B5.
TreeFamiTF315534.

Family and domain databases

InterProiIPR003406. Glyco_trans_14.
IPR024448. XylT.
[Graphical view]
PfamiPF02485. Branch. 1 hit.
PF12529. Xylo_C. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H1B5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVASARVQKL VRRYKLAIAT ALAILLLQGL VVWSFSGLEE DEAGEKGRQR
60 70 80 90 100
KPRPLDPGEG SKDTDSSAGR RGSTGRRHGR WRGRAESPGV PVAKVVRAVT
110 120 130 140 150
SRQRASRRVP PAPPPEAPGR QNLSGAAAGE ALVGAAGFPP HGDTGSVEGA
160 170 180 190 200
PQPTDNGFTP KCEIVGKDAL SALARASTKQ CQQEIANVVC LHQAGSLMPK
210 220 230 240 250
AVPRHCQLTG KMSPGIQWDE SQAQQPMDGP PVRIAYMLVV HGRAIRQLKR
260 270 280 290 300
LLKAVYHEQH FFYIHVDKRS DYLHREVVEL AQGYDNVRVT PWRMVTIWGG
310 320 330 340 350
ASLLRMYLRS MRDLLEVPGW AWDFFINLSA TDYPTRTNEE LVAFLSKNRD
360 370 380 390 400
KNFLKSHGRD NSRFIKKQGL DRLFHECDSH MWRLGERQIP AGIVVDGGSD
410 420 430 440 450
WFVLTRSFVE YVVYTDDPLV AQLRQFYTYT LLPAESFFHT VLENSLACET
460 470 480 490 500
LVDNNLRVTN WNRKLGCKCQ YKHIVDWCGC SPNDFKPQDF LRLQQVSRPT
510 520 530 540 550
FFARKFESTV NQEVLEILDF HLYGSYPPGT PALKAYWENT YDAADGPSGL
560 570 580 590 600
SDVMLTAYTA FARLSLHHAA TAAPPMGTPL CRFEPRGLPS SVHLYFYDDH
610 620 630 640 650
FQGYLVTQAV QPSAQGPAET LEMWLMPQGS LKLLGRSDQA SRLQSLEVGT
660 670 680 690 700
DWDPKERLFR NFGGLLGPLD EPVAVQRWAR GPNLTATVVW IDPTYVVATS
710 720 730 740 750
YDITVDTETE VTQYKPPLSR PLRPGPWTVR LLQFWEPLGE TRFLVLPLTF
760 770 780 790 800
NRKLPLRKDD ASWLHAGPPH NEYMEQSFQG LSSILNLPQP ELAEEAAQRH
810 820 830 840 850
TQLTGPALEA WTDRELSSFW SVAGLCAIGP SPCPSLEPCR LTSWSSLSPD
860
PKSELGPVKA DGRLR
Length:865
Mass (Da):96,767
Last modified:February 20, 2007 - v2
Checksum:iEF477B7C3C1B964B
GO
Isoform 2 (identifier: Q9H1B5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     583-638: FEPRGLPSSV...GSLKLLGRSD → LALIGTPKSV...PMWWPHLMTS
     639-865: Missing.

Note: No experimental confirmation available.
Show »
Length:638
Mass (Da):71,115
Checksum:i0E8F1F0B3ED470CF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti56 – 561D → N.1 Publication
Corresponds to variant rs113835371 [ dbSNP | Ensembl ].
VAR_071276
Natural varianti60 – 601G → R.
Corresponds to variant rs739990 [ dbSNP | Ensembl ].
VAR_049328
Natural varianti115 – 1151P → L.1 Publication
Corresponds to variant rs748114111 [ dbSNP | Ensembl ].
VAR_071277
Natural varianti305 – 3051R → T.3 Publications
Corresponds to variant rs12451299 [ dbSNP | Ensembl ].
VAR_022453
Natural varianti418 – 4181P → L.1 Publication
Corresponds to variant rs72832454 [ dbSNP | Ensembl ].
VAR_071278
Natural varianti801 – 8011T → R in PXE; acts as a modifier of disease severity; more frequent in patients with a severe disease course. 1 Publication
Corresponds to variant rs6504649 [ dbSNP | Ensembl ].
VAR_022454

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei583 – 63856FEPRG…LGRSD → LALIGTPKSVFSGTLGGYWG RWTSLWPCSAGPGAPTSQPQ WSGSTQPMWWPHLMTS in isoform 2. 1 PublicationVSP_013758Add
BLAST
Alternative sequencei639 – 865227Missing in isoform 2. 1 PublicationVSP_013759Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ277442 mRNA. Translation: CAC16788.1.
AY358090 mRNA. Translation: AAQ88457.1.
BC052262 mRNA. Translation: AAH52262.2.
CCDSiCCDS11563.1. [Q9H1B5-1]
RefSeqiNP_071450.2. NM_022167.3. [Q9H1B5-1]
UniGeneiHs.463416.
Hs.718822.

Genome annotation databases

EnsembliENST00000017003; ENSP00000017003; ENSG00000015532. [Q9H1B5-1]
GeneIDi64132.
KEGGihsa:64132.
UCSCiuc002iqo.5. human. [Q9H1B5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ277442 mRNA. Translation: CAC16788.1.
AY358090 mRNA. Translation: AAQ88457.1.
BC052262 mRNA. Translation: AAH52262.2.
CCDSiCCDS11563.1. [Q9H1B5-1]
RefSeqiNP_071450.2. NM_022167.3. [Q9H1B5-1]
UniGeneiHs.463416.
Hs.718822.

3D structure databases

ProteinModelPortaliQ9H1B5.
SMRiQ9H1B5. Positions 234-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122081. 12 interactions.
STRINGi9606.ENSP00000017003.

Protein family/group databases

CAZyiGT14. Glycosyltransferase Family 14.

PTM databases

iPTMnetiQ9H1B5.
PhosphoSiteiQ9H1B5.

Polymorphism and mutation databases

BioMutaiXYLT2.
DMDMi126302616.

Proteomic databases

EPDiQ9H1B5.
MaxQBiQ9H1B5.
PaxDbiQ9H1B5.
PeptideAtlasiQ9H1B5.
PRIDEiQ9H1B5.

Protocols and materials databases

DNASUi64132.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000017003; ENSP00000017003; ENSG00000015532. [Q9H1B5-1]
GeneIDi64132.
KEGGihsa:64132.
UCSCiuc002iqo.5. human. [Q9H1B5-1]

Organism-specific databases

CTDi64132.
GeneCardsiXYLT2.
H-InvDBHIX0013973.
HGNCiHGNC:15517. XYLT2.
HPAiHPA016456.
MalaCardsiXYLT2.
MIMi264800. phenotype.
605822. phenotype.
608125. gene.
neXtProtiNX_Q9H1B5.
PharmGKBiPA37974.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0799. Eukaryota.
ENOG410XQ7M. LUCA.
GeneTreeiENSGT00760000119183.
HOGENOMiHOG000070086.
HOVERGENiHBG059443.
InParanoidiQ9H1B5.
KOiK00771.
OMAiVPRHCQL.
OrthoDBiEOG7D85VR.
PhylomeDBiQ9H1B5.
TreeFamiTF315534.

Enzyme and pathway databases

UniPathwayiUPA00755.
UPA00756.
BioCyciMetaCyc:HS00371-MONOMER.
BRENDAi2.4.2.26. 2681.
SignaLinkiQ9H1B5.

Miscellaneous databases

GeneWikiiXYLT2.
GenomeRNAii64132.
PROiQ9H1B5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H1B5.
CleanExiHS_XYLT2.
ExpressionAtlasiQ9H1B5. baseline and differential.
GenevisibleiQ9H1B5. HS.

Family and domain databases

InterProiIPR003406. Glyco_trans_14.
IPR024448. XylT.
[Graphical view]
PfamiPF02485. Branch. 1 hit.
PF12529. Xylo_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of human UDP-D-xylose:proteoglycan core protein beta-D-xylosyltransferase and its first isoform XT-II."
    Goetting C., Kuhn J., Zahn R., Brinkmann T., Kleesiek K.
    J. Mol. Biol. 304:517-528(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-305, TISSUE SPECIFICITY.
    Tissue: Chondrosarcoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-305.
    Tissue: Pancreas.
  4. "Polymorphisms in the xylosyltransferase genes cause higher serum XT-I activity in patients with pseudoxanthoma elasticum (PXE) and are involved in a severe disease course."
    Schon S., Schulz V., Prante C., Hendig D., Szliska C., Kuhn J., Kleesiek K., Gotting C.
    J. Med. Genet. 43:745-749(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PXE, VARIANT PXE ARG-801, VARIANTS ASN-56; LEU-115; THR-305 AND LEU-418.
  5. "Homozygosity for frameshift mutations in XYLT2 result in a spondylo-ocular syndrome with bone fragility, cataracts, and hearing defects."
    Munns C.F., Fahiminiya S., Poudel N., Munteanu M.C., Majewski J., Sillence D.O., Metcalf J.P., Biggin A., Glorieux F., Fassier F., Rauch F., Hinsdale M.E.
    Am. J. Hum. Genet. 96:971-978(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INVOLVEMENT IN SOS.

Entry informationi

Entry nameiXYLT2_HUMAN
AccessioniPrimary (citable) accession number: Q9H1B5
Secondary accession number(s): Q6UY41, Q86V00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: February 20, 2007
Last modified: July 6, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.