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Protein

Beta-1,3-galactosyltransferase 6

Gene

B3galt6

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

Functioni

Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-linked galactose residue. Has a preference for galactose-beta-1,4-xylose that is found in the linker region of glycosaminoglycans, such as heparan sulfate and chondroitin sulfate. Has no activity towards substrates with terminal glucosamine or galactosamine residues (By similarity).By similarity

Catalytic activityi

UDP-alpha-D-galactose + 4-beta-D-galactosyl-O-beta-D-xylosyl-[protein] = UDP + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosyl-[protein].

Cofactori

Mn2+By 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese

Enzyme and pathway databases

ReactomeiR-MMU-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
UniPathwayiUPA00755.
UPA00756.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-galactosyltransferase 6 (EC:2.4.1.134)
Short name:
Beta-1,3-GalTase 6
Short name:
Beta3Gal-T6
Short name:
Beta3GalT6
Alternative name(s):
GAG GalTII
Galactosyltransferase II
Galactosylxylosylprotein 3-beta-galactosyltransferase
UDP-Gal:betaGal beta 1,3-galactosyltransferase polypeptide 6
Gene namesi
Name:B3galt6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2152819. B3galt6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence analysisAdd
BLAST
Transmembranei12 – 3019Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini31 – 325295LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • Golgi medial cisterna Source: MGI
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 325325Beta-1,3-galactosyltransferase 6PRO_0000219169Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ91Z92.
MaxQBiQ91Z92.
PaxDbiQ91Z92.
PRIDEiQ91Z92.

PTM databases

PhosphoSiteiQ91Z92.

Expressioni

Gene expression databases

BgeeiQ91Z92.
GenevisibleiQ91Z92. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000057521.

Structurei

3D structure databases

ProteinModelPortaliQ91Z92.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2288. Eukaryota.
ENOG410XV5H. LUCA.
GeneTreeiENSGT00530000063810.
HOGENOMiHOG000230579.
HOVERGENiHBG050652.
InParanoidiQ91Z92.
KOiK00734.
OMAiKYTERRS.
OrthoDBiEOG7XH6Q3.
PhylomeDBiQ91Z92.
TreeFamiTF314311.

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.

Q91Z92-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVFRRAWRH RVALGLGGLA FCGTTLLYLA RCASEGETPS ASGAARPRAK
60 70 80 90 100
AFLAVLVASA PRAVERRTAV RSTWLAPERR GGPEDVWARF AVGTGGLGSE
110 120 130 140 150
ERRALELEQA QHGDLLLLPA LRDAYENLTA KVLAMLTWLD ERVDFEFVLK
160 170 180 190 200
ADDDSFARLD AILVDLRARE PARRRRLYWG FFSGRGRVKP GGRWREAAWQ
210 220 230 240 250
LCDYYLPYAL GGGYVLSADL VHYLRLSREY LRAWHSEDVS LGTWLAPVDV
260 270 280 290 300
QREHDPRFDT EYKSRGCNNQ YLVTHKQSPE DMLEKQQMLL HEGRLCKHEV
310 320
QLRLSYVYDW SAPPSQCCQR KEGVP
Length:325
Mass (Da):37,021
Last modified:December 1, 2001 - v1
Checksum:i971D2C00528169A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY050569 mRNA. Translation: AAL11441.1.
AK033608 mRNA. Translation: BAC28387.1.
AK078083 mRNA. Translation: BAC37119.1.
AK090344 mRNA. Translation: BAC41178.1.
BC082998 mRNA. Translation: AAH82998.1.
CCDSiCCDS19053.1.
RefSeqiNP_536693.1. NM_080445.4.
UniGeneiMm.440185.

Genome annotation databases

EnsembliENSMUST00000052185; ENSMUSP00000057521; ENSMUSG00000050796.
GeneIDi117592.
KEGGimmu:117592.
UCSCiuc008wfq.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

b3GalT6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY050569 mRNA. Translation: AAL11441.1.
AK033608 mRNA. Translation: BAC28387.1.
AK078083 mRNA. Translation: BAC37119.1.
AK090344 mRNA. Translation: BAC41178.1.
BC082998 mRNA. Translation: AAH82998.1.
CCDSiCCDS19053.1.
RefSeqiNP_536693.1. NM_080445.4.
UniGeneiMm.440185.

3D structure databases

ProteinModelPortaliQ91Z92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000057521.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSiteiQ91Z92.

Proteomic databases

EPDiQ91Z92.
MaxQBiQ91Z92.
PaxDbiQ91Z92.
PRIDEiQ91Z92.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052185; ENSMUSP00000057521; ENSMUSG00000050796.
GeneIDi117592.
KEGGimmu:117592.
UCSCiuc008wfq.1. mouse.

Organism-specific databases

CTDi126792.
MGIiMGI:2152819. B3galt6.

Phylogenomic databases

eggNOGiKOG2288. Eukaryota.
ENOG410XV5H. LUCA.
GeneTreeiENSGT00530000063810.
HOGENOMiHOG000230579.
HOVERGENiHBG050652.
InParanoidiQ91Z92.
KOiK00734.
OMAiKYTERRS.
OrthoDBiEOG7XH6Q3.
PhylomeDBiQ91Z92.
TreeFamiTF314311.

Enzyme and pathway databases

UniPathwayiUPA00755.
UPA00756.
ReactomeiR-MMU-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.

Miscellaneous databases

NextBioi369698.
PROiQ91Z92.
SOURCEiSearch...

Gene expression databases

BgeeiQ91Z92.
GenevisibleiQ91Z92. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Biosynthesis of the linkage region of glycosaminoglycans: cloning and activity of galactosyltransferase II, the sixth member of the beta 1,3-galactosyltransferase family (beta 3GalT6)."
    Bai X., Zhou D., Brown J.R., Crawford B.E., Hennet T., Esko J.D.
    J. Biol. Chem. 276:48189-48195(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
  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].
    Strain: C57BL/6J.
    Tissue: Cecum.
  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].
    Strain: FVB/N-3.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiB3GT6_MOUSE
AccessioniPrimary (citable) accession number: Q91Z92
Secondary accession number(s): Q8CC93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: December 1, 2001
Last modified: March 16, 2016
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

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 one 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.