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Protein

Glucoside xylosyltransferase 2

Gene

GXYLT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Glycosyltransferase which elongates the O-linked glucose attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of xylose.1 Publication

Catalytic activityi

UDP-alpha-D-xylose + beta-D-glucosyl-R = UDP + alpha-D-xylose-(1->3)-beta-D-glucosyl-R.

GO - Molecular functioni

  • UDP-xylosyltransferase activity Source: UniProtKB

GO - Biological processi

  • O-glycan processing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-HSA-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
SIGNORiA0PJZ3.

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucoside xylosyltransferase 2 (EC:2.4.2.n2)
Alternative name(s):
Glycosyltransferase 8 domain-containing protein 4
Gene namesi
Name:GXYLT2
Synonyms:GLT8D4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:33383. GXYLT2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence analysis
Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini26 – 443418LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165697418.

Polymorphism and mutation databases

BioMutaiGXYLT2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Glucoside xylosyltransferase 2PRO_0000288539Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence analysis
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiA0PJZ3.
PaxDbiA0PJZ3.
PeptideAtlasiA0PJZ3.
PRIDEiA0PJZ3.

PTM databases

iPTMnetiA0PJZ3.
PhosphoSiteiA0PJZ3.

Expressioni

Gene expression databases

BgeeiA0PJZ3.
CleanExiHS_GLT8D4.
ExpressionAtlasiA0PJZ3. baseline and differential.
GenevisibleiA0PJZ3. HS.

Interactioni

Protein-protein interaction databases

BioGridi608376. 9 interactions.
STRINGi9606.ENSP00000374268.

Structurei

3D structure databases

ProteinModelPortaliA0PJZ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi68 – 9831Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 8 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3765. Eukaryota.
ENOG410XRNY. LUCA.
GeneTreeiENSGT00510000046589.
HOGENOMiHOG000264229.
HOVERGENiHBG059879.
InParanoidiA0PJZ3.
KOiK13676.
OMAiAQFKNSM.
OrthoDBiEOG7W6WMC.
PhylomeDBiA0PJZ3.
TreeFamiTF323210.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

A0PJZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLRSKAAAL LLLALAALLL ALLSLRAGRA EPPALPARPA SAPQRHPAPV
60 70 80 90 100
PARWPGPGAL PGASPGVRRR RPPRPRPRAG RRGAARLEKL ARRPGEPRSF
110 120 130 140 150
QAVLPPELWI HLAVVACGNR LEETLVMLKS AVLFSHRKIQ FHIFTEDSLK
160 170 180 190 200
PEFDKQLRQW PDSYTKKFEH RIYPITFSVG NPQEWKKLFK PCAAQRLFLP
210 220 230 240 250
VILKDVDSLL YVDTDVLFLR PVDDIWKLLR LFNSTQLAAM APEHEIPKIG
260 270 280 290 300
WYSRFARHPF YGSAGVNSGV MLMNLTRIRS TQFKNSMIPT GLAWEDMLYP
310 320 330 340 350
LYQKYKNAIT WGDQDLLNII FYFNPECLYV FPCQWNYRPD HCMYGSNCRE
360 370 380 390 400
AEHEGVSVLH GNRGVYHDDK QPTFRALYEA IRDFPFQDNL FQSMYYPLQL
410 420 430 440
KFLETVHTLC GRIPQVFLKQ IEKTMKRAYE KHVIIHVGPN QMH
Length:443
Mass (Da):51,056
Last modified:May 29, 2007 - v2
Checksum:iA53878D061AA27D9
GO

Sequence cautioni

The sequence AAI27734.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC098481 Genomic DNA. No translation available.
AC114876 Genomic DNA. No translation available.
BC127733 mRNA. Translation: AAI27734.1. Different initiation.
CCDSiCCDS46870.1.
RefSeqiNP_001073862.1. NM_001080393.1.
XP_011532370.1. XM_011534068.1.
UniGeneiHs.710275.

Genome annotation databases

EnsembliENST00000389617; ENSP00000374268; ENSG00000172986.
GeneIDi727936.
KEGGihsa:727936.
UCSCiuc003dpg.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC098481 Genomic DNA. No translation available.
AC114876 Genomic DNA. No translation available.
BC127733 mRNA. Translation: AAI27734.1. Different initiation.
CCDSiCCDS46870.1.
RefSeqiNP_001073862.1. NM_001080393.1.
XP_011532370.1. XM_011534068.1.
UniGeneiHs.710275.

3D structure databases

ProteinModelPortaliA0PJZ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi608376. 9 interactions.
STRINGi9606.ENSP00000374268.

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

PTM databases

iPTMnetiA0PJZ3.
PhosphoSiteiA0PJZ3.

Polymorphism and mutation databases

BioMutaiGXYLT2.

Proteomic databases

MaxQBiA0PJZ3.
PaxDbiA0PJZ3.
PeptideAtlasiA0PJZ3.
PRIDEiA0PJZ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389617; ENSP00000374268; ENSG00000172986.
GeneIDi727936.
KEGGihsa:727936.
UCSCiuc003dpg.4. human.

Organism-specific databases

CTDi727936.
GeneCardsiGXYLT2.
HGNCiHGNC:33383. GXYLT2.
MIMi613322. gene.
neXtProtiNX_A0PJZ3.
PharmGKBiPA165697418.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3765. Eukaryota.
ENOG410XRNY. LUCA.
GeneTreeiENSGT00510000046589.
HOGENOMiHOG000264229.
HOVERGENiHBG059879.
InParanoidiA0PJZ3.
KOiK13676.
OMAiAQFKNSM.
OrthoDBiEOG7W6WMC.
PhylomeDBiA0PJZ3.
TreeFamiTF323210.

Enzyme and pathway databases

ReactomeiR-HSA-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
SIGNORiA0PJZ3.

Miscellaneous databases

GenomeRNAii727936.
PROiA0PJZ3.
SOURCEiSearch...

Gene expression databases

BgeeiA0PJZ3.
CleanExiHS_GLT8D4.
ExpressionAtlasiA0PJZ3. baseline and differential.
GenevisibleiA0PJZ3. HS.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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] OF 119-443.
  3. "Identification of glycosyltransferase 8 family members as xylosyltransferases acting on o-glucosylated notch epidermal growth factor repeats."
    Sethi M.K., Buettner F.F., Krylov V.B., Takeuchi H., Nifantiev N.E., Haltiwanger R.S., Gerardy-Schahn R., Bakker H.
    J. Biol. Chem. 285:1582-1586(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiGXLT2_HUMAN
AccessioniPrimary (citable) accession number: A0PJZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: July 6, 2016
This is version 73 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.