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P59270

- B3GA2_MOUSE

UniProt

P59270 - B3GA2_MOUSE

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Protein

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2

Gene

B3gat2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins.

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 sitei119 – 1191UDP-glucuronateBy similarity
Binding sitei156 – 1561UDP-glucuronateBy similarity
Binding sitei161 – 1611UDP-glucuronateBy similarity
Metal bindingi188 – 1881ManganeseBy similarity
Sitei219 – 2191Interaction with galactose moiety of substrate glycoproteinBy similarity
Active sitei274 – 2741Proton donor/acceptorBy similarity
Sitei311 – 3111Interaction with galactose moiety of substrate glycoproteinBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 903UDP-glucuronate bindingBy similarity
Nucleotide bindingi186 – 1883UDP-glucuronate bindingBy similarity
Nucleotide bindingi301 – 3033UDP-glucuronate bindingBy similarity

GO - Molecular functioni

  1. galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity Source: UniProtKB
  2. glucuronosyltransferase activity Source: MGI
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196489. 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 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 namesi
Name:B3gat2
Synonyms:Glcats
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:2389490. B3gat2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22CytoplasmicSequence Analysis
Transmembranei3 – 2321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini24 – 324301LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2PRO_0000195173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP59270.
PRIDEiP59270.

Expressioni

Tissue specificityi

Expressed in brain, but not in liver and kidney.

Gene expression databases

BgeeiP59270.
ExpressionAtlasiP59270. baseline and differential.
GenevestigatoriP59270.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

MINTiMINT-4996887.

Structurei

3D structure databases

ProteinModelPortaliP59270.
SMRiP59270. Positions 79-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni235 – 24410Interaction with galactose moiety of substrate glycoproteinBy similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 43 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292627.
GeneTreeiENSGT00390000017640.
HOVERGENiHBG050650.
InParanoidiP59270.
KOiK10157.
OMAiFILLPWV.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P59270-1) [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
MKSALCSRFF ILLPWILIVI IMLDVDPRRP APQLTSRPYF SPHAVGCGGS
60 70 80 90 100
RVPLRRSSPG RDAAEKRNES RPQLQPEPRL PTIYAITPTY SRPVQKAELT
110 120 130 140 150
RLANTFRQVA QLHWILVEDR ATRSELVSSF LARAGLPNTH LHVPTPRRYK
160 170 180 190 200
RPWLPRATEQ RNAGLAWLRQ RHQHQSAQPG VLFFADDDNT YSLELFQEMR
210 220 230 240 250
TTRKVSVWPV GLVGGRRYER PLVKNGKVVG WYTGWREDRP FAIDMAGFAV
260 270 280 290 300
SLQVILSNPK AVFKRRGSQP GMQESDFLKQ ITTVEELEPK ASNCTKVLVW
310 320
HTRTEKVNLA NEPKYHLDTV NIEV
Length:324
Mass (Da):37,132
Last modified:February 1, 2003 - v1
Checksum:i675C549D3787B957
GO
Isoform 2 (identifier: P59270-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     248-302: FAVSLQVILS...NCTKVLVWHT → EQNAWDICPC...VQVEVDFRSG
     303-324: Missing.

Note: No experimental confirmation available.

Show »
Length:302
Mass (Da):34,808
Checksum:i1DFD4FA45506B311
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti291 – 2911A → V in BAC20343. (PubMed:12383500)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei248 – 30255FAVSL…LVWHT → EQNAWDICPCRMGPRRNWER PIFIKPLSVLHSSEEILIFK IGSLMVQVEVDFRSG in isoform 2. 1 PublicationVSP_001796Add
BLAST
Alternative sequencei303 – 32422Missing in isoform 2. 1 PublicationVSP_001797Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB055902 mRNA. Translation: BAC20343.1.
AK048146 mRNA. Translation: BAC33257.1.
AK052640 mRNA. Translation: BAC35075.1.
BC056368 mRNA. Translation: AAH56368.1.
BC058082 mRNA. Translation: AAH58082.1.
CCDSiCCDS14850.1. [P59270-1]
RefSeqiNP_742122.2. NM_172124.2. [P59270-1]
UniGeneiMm.471661.

Genome annotation databases

EnsembliENSMUST00000063663; ENSMUSP00000066582; ENSMUSG00000026156. [P59270-1]
ENSMUST00000140583; ENSMUSP00000117089; ENSMUSG00000026156. [P59270-2]
GeneIDi280645.
KEGGimmu:280645.
UCSCiuc007amd.1. mouse. [P59270-2]
uc007ame.1. mouse. [P59270-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB055902 mRNA. Translation: BAC20343.1 .
AK048146 mRNA. Translation: BAC33257.1 .
AK052640 mRNA. Translation: BAC35075.1 .
BC056368 mRNA. Translation: AAH56368.1 .
BC058082 mRNA. Translation: AAH58082.1 .
CCDSi CCDS14850.1. [P59270-1 ]
RefSeqi NP_742122.2. NM_172124.2. [P59270-1 ]
UniGenei Mm.471661.

3D structure databases

ProteinModelPortali P59270.
SMRi P59270. Positions 79-324.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4996887.

Protein family/group databases

CAZyi GT43. Glycosyltransferase Family 43.

Proteomic databases

MaxQBi P59270.
PRIDEi P59270.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000063663 ; ENSMUSP00000066582 ; ENSMUSG00000026156 . [P59270-1 ]
ENSMUST00000140583 ; ENSMUSP00000117089 ; ENSMUSG00000026156 . [P59270-2 ]
GeneIDi 280645.
KEGGi mmu:280645.
UCSCi uc007amd.1. mouse. [P59270-2 ]
uc007ame.1. mouse. [P59270-1 ]

Organism-specific databases

CTDi 135152.
MGIi MGI:2389490. B3gat2.

Phylogenomic databases

eggNOGi NOG292627.
GeneTreei ENSGT00390000017640.
HOVERGENi HBG050650.
InParanoidi P59270.
KOi K10157.
OMAi FILLPWV.
TreeFami TF313522.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_196489. A tetrasaccharide linker sequence is required for GAG synthesis.

Miscellaneous databases

NextBioi 394065.
PROi P59270.
SOURCEi Search...

Gene expression databases

Bgeei P59270.
ExpressionAtlasi P59270. baseline and differential.
Genevestigatori P59270.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR005027. Glyco_trans_43.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR10896. PTHR10896. 1 hit.
Pfami PF03360. Glyco_transf_43. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, genomic structure and chromosomal mapping of the mouse glucuronyltransferase-S involved in the biosynthesis of the HNK-1 carbohydrate epitope."
    Imiya K., Ishizaki T., Seiki T., Saito F., Inazawa J., Oka S., Kawasaki T.
    Gene 296:29-36(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/c.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Embryonic head and Kidney.
  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).
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiB3GA2_MOUSE
AccessioniPrimary (citable) accession number: P59270
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: February 1, 2003
Last modified: November 26, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3