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Q5JCS9

- B3GN3_MOUSE

UniProt

Q5JCS9 - B3GN3_MOUSE

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Protein

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3

Gene

B3gnt3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Has a beta-1,3-N-acetylglucosaminyltransferase activity for type 2 oligosaccharides.

Catalytic activityi

UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-(1->3)-(N-acetyl-D-glucosaminyl-(1->6))-N-acetyl-D-galactosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-(N-acetyl-D-glucosaminyl-(1->6))-N-acetyl-D-galactosaminyl-R.

Pathwayi

GO - Molecular functioni

  1. beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
  2. galactosyltransferase activity Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_198517. O-linked glycosylation of mucins.
REACT_198578. Keratan sulfate biosynthesis.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3 (EC:2.4.1.146)
Short name:
BGnT-3
Short name:
Beta-1,3-Gn-T3
Short name:
Beta-1,3-N-acetylglucosaminyltransferase 3
Short name:
Beta3Gn-T3
Alternative name(s):
Core 1 extending beta-1,3-N-acetylglucosaminyltransferase
Core1-beta3GlcNAcT
Gene namesi
Name:B3gnt3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:2152535. B3gnt3.

Subcellular locationi

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 – 372372UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3PRO_0000219173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ5JCS9.
PaxDbiQ5JCS9.
PRIDEiQ5JCS9.

PTM databases

PhosphoSiteiQ5JCS9.

Expressioni

Gene expression databases

BgeeiQ5JCS9.
GenevestigatoriQ5JCS9.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034260.

Structurei

3D structure databases

ProteinModelPortaliQ5JCS9.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010CytoplasmicSequence Analysis
Topological domaini32 – 372341LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG293830.
GeneTreeiENSGT00760000118879.
HOGENOMiHOG000232195.
HOVERGENiHBG050653.
InParanoidiQ5JCS9.
KOiK07970.
OMAiCAQPVFL.
OrthoDBiEOG7BGHKT.
PhylomeDBiQ5JCS9.
TreeFamiTF318639.

Family and domain databases

InterProiIPR002659. Glyco_trans_31.
[Graphical view]
PANTHERiPTHR11214. PTHR11214. 1 hit.
PfamiPF01762. Galactosyl_T. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5JCS9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLPRQSPYE ILLLVLVALL VLLLLLTSKS PPSCSAPERS KEPEDNPGWA
60 70 80 90 100
TGHPRTHPAR CRANLSVSSH PDFAGLPLHV RDFLFYRHCR DFPVLREPRV
110 120 130 140 150
TKCAEPVFLL LAIKSSPANY GRRQMLRTTW ARERRVRGAP LRRLFLVGSD
160 170 180 190 200
RDPQQARKYN RLLELEAQKY GDILQWDFHD SFFNLTLKQV LFLEWQLTYC
210 220 230 240 250
TNASFVLNGD DDVFAHTDNM VTYLQDHDPD QHLFVGHLIQ NVGPIRVPWS
260 270 280 290 300
KYFIPALVMA EDRYPPYCGG GGFLLSRFTV AALRRAARVL PMFPIDDVFL
310 320 330 340 350
GMCLQQQGLA PGTHSGVRTA GVFPPSPRVS SFDPCFYRDL LLVHRFLPFE
360 370
MLLMWDALNQ PQLLCGRQSP AY
Length:372
Mass (Da):42,586
Last modified:February 15, 2005 - v1
Checksum:i484771C8054DE265
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561A → T in AAH26418. (PubMed:15489334)Curated
Sequence conflicti283 – 2831L → I1 PublicationCurated
Sequence conflicti283 – 2831L → I(PubMed:16141072)Curated
Sequence conflicti295 – 2951I → V1 PublicationCurated
Sequence conflicti295 – 2951I → V(PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY037785 mRNA. Translation: AAK68855.1.
AY039028 mRNA. Translation: AAK72481.1.
AK008674 mRNA. Translation: BAB25824.1.
BC026418 mRNA. Translation: AAH26418.1.
CCDSiCCDS22405.1.
RefSeqiNP_082465.3. NM_028189.3.
XP_006509815.1. XM_006509752.1.
XP_006509816.1. XM_006509753.1.
UniGeneiMm.290837.

Genome annotation databases

EnsembliENSMUST00000034260; ENSMUSP00000034260; ENSMUSG00000031803.
GeneIDi72297.
KEGGimmu:72297.
UCSCiuc009mer.3. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

beta 3 GlcNAc-T III

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY037785 mRNA. Translation: AAK68855.1 .
AY039028 mRNA. Translation: AAK72481.1 .
AK008674 mRNA. Translation: BAB25824.1 .
BC026418 mRNA. Translation: AAH26418.1 .
CCDSi CCDS22405.1.
RefSeqi NP_082465.3. NM_028189.3.
XP_006509815.1. XM_006509752.1.
XP_006509816.1. XM_006509753.1.
UniGenei Mm.290837.

3D structure databases

ProteinModelPortali Q5JCS9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000034260.

Protein family/group databases

CAZyi GT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSitei Q5JCS9.

Proteomic databases

MaxQBi Q5JCS9.
PaxDbi Q5JCS9.
PRIDEi Q5JCS9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034260 ; ENSMUSP00000034260 ; ENSMUSG00000031803 .
GeneIDi 72297.
KEGGi mmu:72297.
UCSCi uc009mer.3. mouse.

Organism-specific databases

CTDi 10331.
MGIi MGI:2152535. B3gnt3.

Phylogenomic databases

eggNOGi NOG293830.
GeneTreei ENSGT00760000118879.
HOGENOMi HOG000232195.
HOVERGENi HBG050653.
InParanoidi Q5JCS9.
KOi K07970.
OMAi CAQPVFL.
OrthoDBi EOG7BGHKT.
PhylomeDBi Q5JCS9.
TreeFami TF318639.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_198517. O-linked glycosylation of mucins.
REACT_198578. Keratan sulfate biosynthesis.

Miscellaneous databases

NextBioi 335942.
PROi Q5JCS9.
SOURCEi Search...

Gene expression databases

Bgeei Q5JCS9.
Genevestigatori Q5JCS9.

Family and domain databases

InterProi IPR002659. Glyco_trans_31.
[Graphical view ]
PANTHERi PTHR11214. PTHR11214. 1 hit.
Pfami PF01762. Galactosyl_T. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse beta1,3 N-acetylglucosaminyltransferase-3."
    Zhou D., Hennet T.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/Sv.
  2. "Core 1 beta-1,3-N-acetylglucosaminyltransferase (Core1-beta3GlcNAcT)."
    Yeh J.-C., Fukuda M.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
    Strain: C57BL/6J.
    Tissue: Stomach.
  4. "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].
    Strain: FVB/N.
    Tissue: Colon.

Entry informationi

Entry nameiB3GN3_MOUSE
AccessioniPrimary (citable) accession number: Q5JCS9
Secondary accession number(s): Q8R0U2, Q9D7Z2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: February 15, 2005
Last modified: October 29, 2014
This is version 86 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