Xylt2

Functionⁱ

Involved in the formation of heparan sulfate and chondroitin sulfate proteoglycans (By similarity). 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).By similarity

Catalytic activityⁱ

UDP-alpha-D-xylose + [protein]-L-serine = UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine.

Cofactorⁱ

a divalent metal cationBy similarity

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-EC

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

chondroitin sulfate biosynthetic process Source: UniProtKB-UniPathway
chondroitin sulfate proteoglycan biosynthetic process Source: UniProtKB
glycosaminoglycan biosynthetic process
Source: MGI
Inferred from mutant phenotypeⁱ
- 17517600
heparan sulfate proteoglycan biosynthetic process Source: UniProtKB
heparin biosynthetic process
Source: MGI
Inferred from mutant phenotypeⁱ
- 17517600
proteoglycan biosynthetic process
Source: MGI
Inferred from mutant phenotypeⁱ
- 17517600

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosyltransferase, Transferase

Molecular function

Glycosyltransferase, Transferase

Enzyme and pathway databases

Reactomeⁱ	R-MMU-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
UniPathwayⁱ	UPA00755. UPA00756.

Protein family/group databases

Carbohydrate-Active enZymes More...CAZyⁱ	GT14. Glycosyltransferase Family 14.

CAZyⁱ

GT14. Glycosyltransferase Family 14.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Xylosyltransferase 2 (EC:2.4.2.26) Alternative name(s): Peptide O-xylosyltransferase 2 Xylosyltransferase II
Gene namesⁱ	Name:Xylt2
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 11

Organism-specific databases

MGIⁱ	MGI:2444797. Xylt2.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 15	CytoplasmicSequence analysisAdd BLAST	15
Transmembraneⁱ	16 – 36	Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST	21
Topological domainⁱ	37 – 865	LumenalSequence analysisAdd BLAST	829

Keywords - Cellular componentⁱ

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000191407	1 – 865	Xylosyltransferase 2Add BLAST		865

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	122	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	327	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	683	N-linked (GlcNAc...) asparagineSequence analysis	1

Post-translational modificationⁱ

Contains disulfide bonds.By similarity

Keywords - PTMⁱ

Disulfide bond, Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9EPL0.
PaxDbⁱ	Q9EPL0.
PRIDEⁱ	Q9EPL0.

PTM databases

iPTMnetⁱ	Q9EPL0.
PhosphoSitePlusⁱ	Q9EPL0.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000020868.
CleanExⁱ	MM_XYLT2.
ExpressionAtlasⁱ	Q9EPL0. baseline and differential.
Genevisibleⁱ	Q9EPL0. MM.

Interactionⁱ

Subunit structureⁱ

Monomer.By similarity

Protein-protein interaction databases

IntActⁱ	Q9EPL0. 1 interactor.
STRINGⁱ	10090.ENSMUSP00000112052.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q9EPL0.
SMRⁱ	Q9EPL0.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the glycosyltransferase 14 family. XylT subfamily.Curated

Keywords - Domainⁱ

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG0799. Eukaryota. ENOG410XQ7M. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119183.
HOGENOMⁱ	HOG000070086.
HOVERGENⁱ	HBG059443.
InParanoidⁱ	Q9EPL0.
KEGG Orthology (KO) More...KOⁱ	K00771.
OMAⁱ	WRMVTIW.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G020K.
PhylomeDBⁱ	Q9EPL0.
TreeFamⁱ	TF315534.

Family and domain databases

InterProⁱ	View protein in InterPro IPR003406. Glyco_trans_14. IPR024448. XylT.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02485. Branch. 1 hit. PF12529. Xylo_C. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q9EPL0-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MVASARVQKL VRRYKLAIAT ALAILLLQGL VVWSFSGLEE DEPGEKGRQR 
        60         70         80         90        100
KPRPLDPGEG SKDTDSSAGR RGSAGRRHGR WRGRAESPGV PVAKVVRAVT 
       110        120        130        140        150
SRQRASRRVP PAPPPEAPGR QNLSGAAAGE ALIGAPGFPQ HGDTGSVEGA 
       160        170        180        190        200
PQPTDNTFTP KCEIVGKDAL SALARASTKQ CQQEIANVVC LHQAGNLMPK 
       210        220        230        240        250
SVPRHCQLAG KMSPGVQWEE IRAQQPVGGP PVRIAYMLVV HGRAIRQLKR 
       260        270        280        290        300
LLKAVYHEQH FFYIHVDKRS NYLYREVVEL AQHYENVRVT PWRMVTIWGG 
       310        320        330        340        350
ASLLRMYLRS MKDLLEIPGW TWDFFINLSA TDYPTRTNEE LVAFLSKNRD 
       360        370        380        390        400
KNFLKSHGRD NSRFIKKQGL DRLFHECDSH MWRLGERQIP AGIVVDGGSD 
       410        420        430        440        450
WFVLTRSFVE YVVYTDDPLV AQLRQFYTYT LLPAESFFHT VLENSPACAS 
       460        470        480        490        500
LVDNNLRVTN WNRKLGCKCQ YKHIVDWCGC SPNDFKPQDF LRLQQVSRPT 
       510        520        530        540        550
FFARKFESTV NQEVLEILDF HLYGSYPPST PALKAYWENI YDVADGPGGL 
       560        570        580        590        600
SDVLLTAYTA FARLSLRHAA TAVSPLATAV CRFEPRGLPS SVHLYFYDDH 
       610        620        630        640        650
FQGYLVTQAV QPSAQGPAET LEMWLMPQRS LKLLGHSDQA SRLQSLEVGT 
       660        670        680        690        700
EWDPKERLFR NFGGLLGPLD EPVAMQRWAR GPNLTATVVW IDPTYVVATS 
       710        720        730        740        750
YDITVDADTE VTQYKPPLSL PLRPGAWTVR LLQFWEPLGE TRFLVLPLTF 
       760        770        780        790        800
NRKLPLRKDD ASWLHAGPPH NEYMEQSFQG LSGILNLPQA EALEEAARRH 
       810        820        830        840        850
TELTGSALEA WTDGELSNFW SVAGLCAIGP SACPSLELCR LTSWSSLSPD 
       860 
PKSELGPVKA DGRLR

Length:865

Mass (Da):96,811

Last modified:May 10, 2005 - v3

Checksum:ⁱDA30B77B9807A797

GO

Sequence cautionⁱ

The sequence AAH34082 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	94	K → N in CAC18567 (Ref. 1) Curated	1
Sequence conflictⁱ	460	N → K in CAC18567 (Ref. 1) Curated	1
Sequence conflictⁱ	466 – 467	GC → AG in CAC18567 (Ref. 1) Curated	2
Sequence conflictⁱ	478	C → S in CAC18567 (Ref. 1) Curated	1
Sequence conflictⁱ	483	N → K in CAC18567 (Ref. 1) Curated	1
Sequence conflictⁱ	487	P → R in CAC18567 (Ref. 1) Curated	1
Sequence conflictⁱ	504 – 506	RKF → GKL in CAC18567 (Ref. 1) Curated	3
Sequence conflictⁱ	515	L → V in CAC18567 (Ref. 1) Curated	1
Sequence conflictⁱ	666	L → V in CAC18567 (Ref. 1) Curated	1
Sequence conflictⁱ	672	P → A in CAC18567 (Ref. 1) Curated	1
Sequence conflictⁱ	675 – 676	MQ → LR in CAC18567 (Ref. 1) Curated	2
Sequence conflictⁱ	685	T → R in CAC18567 (Ref. 1) Curated	1
Sequence conflictⁱ	768 – 770	PPH → QPQ in CAC18567 (Ref. 1) Curated	3
Sequence conflictⁱ	780	G → V in CAC18567 (Ref. 1) Curated	1
Sequence conflictⁱ	788	P → S in CAC18567 (Ref. 1) Curated	1
Sequence conflictⁱ	799	R → Q in CAC18567 (Ref. 1) Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AJ291751 mRNA. Translation: CAC18567.2. AL645764 Genomic DNA. No translation available. BC034082 mRNA. Translation: AAH34082.1. Different initiation.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS48888.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_665827.2. NM_145828.3.
UniGeneⁱ	Mm.100638.

Genome annotation databases

Ensemblⁱ	ENSMUST00000116349; ENSMUSP00000112052; ENSMUSG00000020868.
GeneIDⁱ	217119.
KEGGⁱ	mmu:217119.
UCSC genome browser More...UCSCⁱ	uc007kzi.2. mouse.

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q9EPL0	Q3TZ69	Mus musculus (Mouse)	865	UniRef100_Q9EPL0	Cluster: Xylosyltransferase 2	2

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q9EPL0	Q9H1B5 UPI000703C2DE UPI000C29F157 UPI00075F812A UPI0005F4C838 UPI000813782A UPI00064357B7 UPI000BB4B078 A0A1U8CBH6 A0A0D9QZ82 +121	Homo sapiens (Human) Tupaia chinensis (Chinese tree shrew) Piliocolobus tephrosceles (Ugandan red Colobus) Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Macaca nemestrina (Pig-tailed macaque) Manis javanica (Malayan pangolin) (Sunda pangolin) Microcebus murinus (Lesser mouse lemur) (Gray Mouse Lemur) Enhydra lutris kenyoni Mesocricetus auratus (Golden hamster) Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus) And more	865	UniRef90_Q9H1B5	Cluster: Xylosyltransferase 2	132

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q9EPL0	Q9H1B5 UPI000703C2DE UPI00075F812A UPI0005F4C838 UPI000C29F157 UPI000813782A UPI00064357B7 A0A1U8CBH6 UPI000BB4B078 G3T3A7 +365	Homo sapiens (Human) Tupaia chinensis (Chinese tree shrew) Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Macaca nemestrina (Pig-tailed macaque) Piliocolobus tephrosceles (Ugandan red Colobus) Manis javanica (Malayan pangolin) (Sunda pangolin) Microcebus murinus (Lesser mouse lemur) (Gray Mouse Lemur) Mesocricetus auratus (Golden hamster) Enhydra lutris kenyoni Loxodonta africana (African elephant) And more	865	UniRef50_Q9H1B5	Cluster: Xylosyltransferase 2	376

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AJ291751 mRNA. Translation: CAC18567.2. AL645764 Genomic DNA. No translation available. BC034082 mRNA. Translation: AAH34082.1. Different initiation.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS48888.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_665827.2. NM_145828.3.
UniGeneⁱ	Mm.100638.

3D structure databases

ProteinModelPortalⁱ	Q9EPL0.
SMRⁱ	Q9EPL0.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	Q9EPL0. 1 interactor.
STRINGⁱ	10090.ENSMUSP00000112052.

Protein family/group databases

Carbohydrate-Active enZymes More...CAZyⁱ	GT14. Glycosyltransferase Family 14.

CAZyⁱ

GT14. Glycosyltransferase Family 14.

PTM databases

iPTMnetⁱ	Q9EPL0.
PhosphoSitePlusⁱ	Q9EPL0.

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9EPL0.
PaxDbⁱ	Q9EPL0.
PRIDEⁱ	Q9EPL0.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000116349; ENSMUSP00000112052; ENSMUSG00000020868.
GeneIDⁱ	217119.
KEGGⁱ	mmu:217119.
UCSC genome browser More...UCSCⁱ	uc007kzi.2. mouse.

Organism-specific databases

CTDⁱ	64132.
MGIⁱ	MGI:2444797. Xylt2.

Phylogenomic databases

eggNOGⁱ	KOG0799. Eukaryota. ENOG410XQ7M. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119183.
HOGENOMⁱ	HOG000070086.
HOVERGENⁱ	HBG059443.
InParanoidⁱ	Q9EPL0.
KEGG Orthology (KO) More...KOⁱ	K00771.
OMAⁱ	WRMVTIW.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G020K.
PhylomeDBⁱ	Q9EPL0.
TreeFamⁱ	TF315534.

Enzyme and pathway databases

UniPathwayⁱ	UPA00755. UPA00756.
Reactomeⁱ	R-MMU-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.

Miscellaneous databases

ChiTaRSⁱ	Xylt2. mouse.
Protein Ontology More...PROⁱ	PR:Q9EPL0.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000020868.
CleanExⁱ	MM_XYLT2.
ExpressionAtlasⁱ	Q9EPL0. baseline and differential.
Genevisibleⁱ	Q9EPL0. MM.

Family and domain databases

InterProⁱ	View protein in InterPro IPR003406. Glyco_trans_14. IPR024448. XylT.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02485. Branch. 1 hit. PF12529. Xylo_C. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	XYLT2_MOUSE
Accessionⁱ	Q9EPL0Primary (citable) accession number: Q9EPL0 Secondary accession number(s): Q5SUY1, Q8K060
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
	Last sequence update:	May 10, 2005
	Last modified:	March 28, 2018
	This is version 118 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9EPL0 (XYLT2_MOUSE)

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Xylosyltransferase 2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: chondroitin sulfate biosynthesis

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: heparan sulfate biosynthesis

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Golgi apparatus

Endoplasmic reticulum

Endoplasmic reticulum

Golgi apparatus

Other locations

Topology

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

Pathwayⁱ: chondroitin sulfate biosynthesis

Pathwayⁱ: heparan sulfate biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ