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Protein

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1

Gene

B3GAT1

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

Functioni

Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group (By similarity).By similarity

Catalytic activityi

UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein.

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei122 – 1221UDP-glucuronate
Binding sitei165 – 1651UDP-glucuronate
Binding sitei170 – 1701UDP-glucuronateBy similarity
Metal bindingi197 – 1971ManganeseBy similarity
Sitei228 – 2281Interaction with galactose moiety of substrate glycoprotein
Active sitei284 – 2841Proton donor/acceptor
Sitei321 – 3211Interaction with galactose moiety of substrate glycoproteinBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi91 – 933UDP-glucuronate binding
Nucleotide bindingi195 – 1973UDP-glucuronate binding
Nucleotide bindingi311 – 3133UDP-glucuronate binding

GO - Molecular functioni

  1. galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity Source: Ensembl

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. chondroitin sulfate metabolic process Source: Reactome
  3. glycosaminoglycan metabolic process Source: Reactome
  4. pathogenesis Source: Reactome
  5. protein glycosylation Source: UniProtKB-UniPathway
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS03272-MONOMER.
BRENDAi2.4.1.135. 2681.
ReactomeiREACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT43. Glycosyltransferase Family 43.

Names & Taxonomyi

Protein namesi
Recommended name:
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 (EC:2.4.1.135)
Alternative name(s):
Beta-1,3-glucuronyltransferase 1
Glucuronosyltransferase P
Short name:
GlcAT-P
UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase
Short name:
GlcUAT-P
Gene namesi
Name:B3GAT1
Synonyms:GLCATP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:921. B3GAT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini28 – 334307LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25215.

Polymorphism and mutation databases

BioMutaiB3GAT1.
DMDMi205830910.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1PRO_0000195167Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031PhosphothreonineBy similarity
Modified residuei108 – 1081PhosphothreonineBy similarity
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9P2W7.
PRIDEiQ9P2W7.

PTM databases

PhosphoSiteiQ9P2W7.

Expressioni

Tissue specificityi

Mainly expressed in the brain.

Gene expression databases

BgeeiQ9P2W7.
CleanExiHS_B3GAT1.
ExpressionAtlasiQ9P2W7. baseline and differential.
GenevestigatoriQ9P2W7.

Organism-specific databases

HPAiCAB002500.
CAB010893.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

BioGridi117990. 2 interactions.
IntActiQ9P2W7. 2 interactions.
STRINGi9606.ENSP00000307875.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi85 – 928Combined sources
Helixi98 – 10912Combined sources
Beta strandi112 – 12514Combined sources
Helixi128 – 13710Combined sources
Beta strandi140 – 1456Combined sources
Helixi150 – 1534Combined sources
Helixi167 – 18014Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi198 – 2003Combined sources
Helixi202 – 2098Combined sources
Beta strandi212 – 2165Combined sources
Beta strandi219 – 2213Combined sources
Beta strandi225 – 2328Combined sources
Beta strandi238 – 2425Combined sources
Beta strandi244 – 2463Combined sources
Helixi255 – 2573Combined sources
Beta strandi258 – 2614Combined sources
Helixi262 – 2676Combined sources
Beta strandi275 – 2784Combined sources
Helixi283 – 2919Combined sources
Helixi294 – 2963Combined sources
Beta strandi297 – 2993Combined sources
Helixi301 – 3044Combined sources
Helixi320 – 3223Combined sources
Turni323 – 3253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V82X-ray1.85A/B83-334[»]
1V83X-ray1.90A/B83-334[»]
1V84X-ray1.82A/B83-334[»]
ProteinModelPortaliQ9P2W7.
SMRiQ9P2W7. Positions 83-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P2W7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni245 – 25410Interaction with galactose moiety of substrate glycoprotein

Sequence similaritiesi

Belongs to the glycosyltransferase 43 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG310844.
GeneTreeiENSGT00390000017640.
HOVERGENiHBG050650.
InParanoidiQ9P2W7.
KOiK00735.
OrthoDBiEOG7QG44X.
PhylomeDBiQ9P2W7.
TreeFamiTF313522.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005027. Glyco_trans_43.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10896. PTHR10896. 1 hit.
PfamiPF03360. Glyco_transf_43. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9P2W7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRRDILAI VLIVLPWTLL ITVWHQSTLA PLLAVHKDEG SDPRRETPPG
60 70 80 90 100
ADPREYCTSD RDIVEVVRTE YVYTRPPPWS DTLPTIHVVT PTYSRPVQKA
110 120 130 140 150
ELTRMANTLL HVPNLHWLVV EDAPRRTPLT ARLLRDTGLN YTHLHVETPR
160 170 180 190 200
NYKLRGDARD PRIPRGTMQR NLALRWLRET FPRNSSQPGV VYFADDDNTY
210 220 230 240 250
SLELFEEMRS TRRVSVWPVA FVGGLRYEAP RVNGAGKVVG WKTVFDPHRP
260 270 280 290 300
FAIDMAGFAV NLRLILQRSQ AYFKLRGVKG GYQESSLLRE LVTLNDLEPK
310 320 330
AANCTKILVW HTRTEKPVLV NEGKKGFTDP SVEI
Length:334
Mass (Da):38,256
Last modified:July 22, 2008 - v2
Checksum:i0DF42399D19701B3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti240 – 2401G → R in BAA96077 (PubMed:10783264).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti131 – 1311A → T.
Corresponds to variant rs35434644 [ dbSNP | Ensembl ].
VAR_044538

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029396 mRNA. Translation: BAA96077.1.
CR457098 mRNA. Translation: CAG33379.1.
BC010466 mRNA. Translation: AAH10466.1.
CCDSiCCDS8500.1.
RefSeqiNP_061114.2. NM_018644.3.
NP_473366.1. NM_054025.2.
UniGeneiHs.381050.

Genome annotation databases

EnsembliENST00000312527; ENSP00000307875; ENSG00000109956.
ENST00000392580; ENSP00000376359; ENSG00000109956.
ENST00000524765; ENSP00000433847; ENSG00000109956.
GeneIDi27087.
KEGGihsa:27087.
UCSCiuc001qhq.3. human.

Polymorphism and mutation databases

BioMutaiB3GAT1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029396 mRNA. Translation: BAA96077.1.
CR457098 mRNA. Translation: CAG33379.1.
BC010466 mRNA. Translation: AAH10466.1.
CCDSiCCDS8500.1.
RefSeqiNP_061114.2. NM_018644.3.
NP_473366.1. NM_054025.2.
UniGeneiHs.381050.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V82X-ray1.85A/B83-334[»]
1V83X-ray1.90A/B83-334[»]
1V84X-ray1.82A/B83-334[»]
ProteinModelPortaliQ9P2W7.
SMRiQ9P2W7. Positions 83-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117990. 2 interactions.
IntActiQ9P2W7. 2 interactions.
STRINGi9606.ENSP00000307875.

Protein family/group databases

CAZyiGT43. Glycosyltransferase Family 43.

PTM databases

PhosphoSiteiQ9P2W7.

Polymorphism and mutation databases

BioMutaiB3GAT1.
DMDMi205830910.

Proteomic databases

PaxDbiQ9P2W7.
PRIDEiQ9P2W7.

Protocols and materials databases

DNASUi27087.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312527; ENSP00000307875; ENSG00000109956.
ENST00000392580; ENSP00000376359; ENSG00000109956.
ENST00000524765; ENSP00000433847; ENSG00000109956.
GeneIDi27087.
KEGGihsa:27087.
UCSCiuc001qhq.3. human.

Organism-specific databases

CTDi27087.
GeneCardsiGC11M134248.
H-InvDBHIX0010301.
HGNCiHGNC:921. B3GAT1.
HPAiCAB002500.
CAB010893.
MIMi151290. gene.
neXtProtiNX_Q9P2W7.
PharmGKBiPA25215.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG310844.
GeneTreeiENSGT00390000017640.
HOVERGENiHBG050650.
InParanoidiQ9P2W7.
KOiK00735.
OrthoDBiEOG7QG44X.
PhylomeDBiQ9P2W7.
TreeFamiTF313522.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:HS03272-MONOMER.
BRENDAi2.4.1.135. 2681.
ReactomeiREACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.

Miscellaneous databases

ChiTaRSiB3GAT1. human.
EvolutionaryTraceiQ9P2W7.
GeneWikiiB3GAT1.
GenomeRNAii27087.
NextBioi49699.
PROiQ9P2W7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P2W7.
CleanExiHS_B3GAT1.
ExpressionAtlasiQ9P2W7. baseline and differential.
GenevestigatoriQ9P2W7.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005027. Glyco_trans_43.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10896. PTHR10896. 1 hit.
PfamiPF03360. Glyco_transf_43. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and chromosomal mapping of human glucuronyltransferase involved in biosynthesis of the HNK-1 carbohydrate epitope."
    Mitsumoto Y., Oka S., Sakuma H., Inazawa J., Kawasaki T.
    Genomics 65:166-173(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Tissue: Brain.
  4. "Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1."
    Kakuda S., Shiba T., Ishiguro M., Tagawa H., Oka S., Kajihara Y., Kawasaki T., Wakatsuki S., Kato R.
    J. Biol. Chem. 279:22693-22703(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 83-334 IN COMPLEX WITH UDP-GLUCURONIC ACID AND GALACTOSE MOIETY OF SUBSTRATE GLYCOPROTEIN.

Entry informationi

Entry nameiB3GA1_HUMAN
AccessioniPrimary (citable) accession number: Q9P2W7
Secondary accession number(s): Q96FS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: July 22, 2008
Last modified: April 29, 2015
This is version 142 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.