Q9NPZ5 (B3GA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
EC=2.4.1.135

Alternative name(s):
Beta-1,3-glucuronyltransferase 2
GlcAT-D
UDP-glucuronosyltransferase S
Short name=GlcAT-S
Short name=Glucuronosyltransferase S

Gene names

Name:	B3GAT2
Synonyms:	GLCATS, KIAA1963

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins By similarity.
Catalytic activity	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.
Cofactor	Manganese.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Homodimer Potential.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein.
Tissue specificity	Expressed in the trachea, retina, spinal cord, hippocampus and other brain regions, and, at lower levels, in testis and ovary.
Sequence similarities	Belongs to the glycosyltransferase 43 family.
Sequence caution	The sequence BAB70889.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB85549.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Manganese Metal-binding
Molecular function	Transferase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome chondroitin sulfate metabolic process Traceable author statement. Source: Reactome protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 323

323

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2

PRO_0000195172

Regions

Topological domain

1 – 2

2

Cytoplasmic Potential

Transmembrane

3 – 23

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

24 – 323

300

Lumenal Potential

Nucleotide binding

87 – 89

3

UDP-glucuronate binding By similarity

Nucleotide binding

185 – 187

3

UDP-glucuronate binding By similarity

Nucleotide binding

300 – 302

3

UDP-glucuronate binding By similarity

Region

234 – 243

10

Interaction with galactose moiety of substrate glycoprotein By similarity

Sites

Active site

273

1

Proton donor/acceptor By similarity

Metal binding

187

1

Manganese By similarity

Binding site

118

1

UDP-glucuronate By similarity

Binding site

155

1

UDP-glucuronate By similarity

Binding site

160

1

UDP-glucuronate By similarity

Site

218

1

Interaction with galactose moiety of substrate glycoprotein By similarity

Site

310

1

Interaction with galactose moiety of substrate glycoprotein By similarity

Amino acid modifications

Glycosylation

67

1

N-linked (GlcNAc...) Potential

Glycosylation

292

1

N-linked (GlcNAc...) Potential

Secondary structure

1

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323

Helix Strand Turn

Details...

Beta strand

82 – 88

7

Helix

94 – 105

12

Beta strand

111 – 121

11

Helix

124 – 132

9

Beta strand

137 – 141

5

Helix

157 – 170

14

Beta strand

173 – 175

3

Beta strand

180 – 183

4

Helix

193 – 198

6

Beta strand

202 – 206

5

Beta strand

209 – 212

4

Beta strand

215 – 223

9

Beta strand

226 – 231

6

Helix

244 – 246

3

Beta strand

247 – 250

4

Helix

251 – 256

6

Beta strand

266 – 268

3

Helix

269 – 271

3

Helix

272 – 278

7

Helix

283 – 285

3

Helix

290 – 293

4

Beta strand

313 – 315

3

Sequences

	Sequence		Length	Mass (Da)
	Q9NPZ5 [UniParc]. Last modified June 1, 2001. Version 2. Checksum: 85058D52D2D28463	FASTA	323	36,919
	10 20 30 40 50 60 MKSALFTRFF ILLPWILIVI IMLDVDTRRP VPPLTPRPYF SPYAVGRGGA RLPLRRGGPA 70 80 90 100 110 120 HGTQKRNQSR PQPQPEPQLP TIYAITPTYS RPVQKAELTR LANTFRQVAQ LHWILVEDAA 130 140 150 160 170 180 ARSELVSRFL ARAGLPSTHL HVPTPRRYKR PGLPRATEQR NAGLAWLRQR HQHQRAQPGV 190 200 210 220 230 240 LFFADDDNTY SLELFQEMRT TRKVSVWPVG LVGGRRYERP LVENGKVVGW YTGWRADRPF 250 260 270 280 290 300 AIDMAGFAVS LQVILSNPKA VFKRRGSQPG MQESDFLKQI TTVEELEPKA NNCTKVLVWH 310 320 TRTEKVNLAN EPKYHLDTVK IEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, characterization, and chromosome mapping of the human GlcAT-S gene." Marcos I., Galan J.J., Borrego S., Antinolo G. J. Hum. Genet. 47:677-680(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins." Nagase T., Kikuno R., Ohara O. DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-323. Tissue: Fetal brain.
[5]	"Crystal structure of GlcAT-S, a human glucuronyltransferase, involved in the biosynthesis of the HNK-1 carbohydrate epitope." Shiba T., Kakuda S., Ishiguro M., Morita I., Oka S., Kawasaki T., Wakatsuki S., Kato R. Proteins 65:499-508(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 78-323.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY070019 mRNA. Translation: AAL57718.1.
AY070110, AY070108, AY070109 Genomic DNA. Translation: AAL58977.1.
AB075843 mRNA. Translation: BAB85549.1. Different initiation.
AL121961, AL450320 Genomic DNA. Translation: CAI42145.1.
AL450320, AL121961 Genomic DNA. Translation: CAI39582.1.
AK055248 mRNA. Translation: BAB70889.1. Different initiation.

IPI

IPI00221205.

RefSeq

NP_542780.1. NM_080742.2.

UniGene

Hs.713609.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D0J	X-ray	2.00	A/B/C/D	78-323	[»]

ProteinModelPortal

Q9NPZ5.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000230053.

Protein family/group databases

CAZy

GT43. Glycosyltransferase Family 43.

Polymorphism databases

DMDM

14285363.

Proteomic databases

PaxDb

Q9NPZ5.

PRIDE

Q9NPZ5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000230053; ENSP00000230053; ENSG00000112309.

GeneID

135152.

KEGG

hsa:135152.

UCSC

uc003pfv.3. human.

Organism-specific databases

CTD

135152.

GeneCards

GC06M071566.

HGNC

HGNC:922. B3GAT2.

HPA

HPA012059.

MIM

607497. gene.

neXtProt

NX_Q9NPZ5.

PharmGKB

PA25216.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG292627.

HOGENOM

HOG000261693.

HOVERGEN

HBG050650.

InParanoid

Q9NPZ5.

KO

K10157.

OMA

FILLPWV.

OrthoDB

EOG4CRM0N.

PhylomeDB

Q9NPZ5.

Enzyme and pathway databases

BioCyc

MetaCyc:HS03557-MONOMER.

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.

UniPathway

UPA00378.

Gene expression databases

ArrayExpress

Q9NPZ5.

Bgee

Q9NPZ5.

CleanEx

HS_B3GAT2.

Genevestigator

Q9NPZ5.

GermOnline

ENSG00000112309. Homo sapiens.

Family and domain databases

InterPro

IPR005027. Glyco_trans_43.
[Graphical view]

PANTHER

PTHR10896. PTHR10896. 1 hit.

Pfam

PF03360. Glyco_transf_43. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5209.

EvolutionaryTrace

Q9NPZ5.

GenomeRNAi

135152.

NextBio

83461.

SOURCE

Search...

Entry information

Entry name

B3GA2_HUMAN

Accession

Primary (citable) accession number: Q9NPZ5
Secondary accession number(s): Q5JS09, Q8TF38, Q96NK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.