Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2

Gene

B3galnt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAc-beta-1-3GlcNAc, on N- and O-glycans. Has no galactose nor galactosaminyl transferase activity toward any acceptor substrate. Involved in alpha-dystroglycan (DAG1) glycosylation: acts coordinately with GTDC2/POMGnT2 to synthesize a GalNAc-beta3-GlcNAc-beta-terminus at the 4-position of protein O-mannose in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan, which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity).By similarity

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + N-acetyl-beta-D-glucosaminyl-(1->4)-O-alpha-D-mannosylprotein = UDP + N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-O-alpha-D-mannosylprotein.

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2 (EC:2.4.1.-)
Short name:
Beta-1,3-GalNAc-T2
Alternative name(s):
Beta-1,3-N-acetylgalactosaminyltransferase II
Gene namesi
Name:B3galnt2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2145517. B3galnt2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33CytoplasmicSequence analysis
Transmembranei4 – 2421Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini25 – 504480LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2PRO_0000248363Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence analysis
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8BG28.
PRIDEiQ8BG28.

PTM databases

iPTMnetiQ8BG28.
PhosphoSiteiQ8BG28.

Expressioni

Tissue specificityi

Present in testis (at protein level). In testis, it is mainly detected in the middle layers of seminiferous tubules at stages XII to II. Strongly expressed in primary and secondary spermatocytes and early round spermatids, but not in spermatogonia, elongating or elongated spermatids, or in Leydig or Sertoli cells.1 Publication

Gene expression databases

BgeeiQ8BG28.
GenevisibleiQ8BG28. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000097336.

Structurei

3D structure databases

ProteinModelPortaliQ8BG28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2287. Eukaryota.
ENOG410ZZ1B. LUCA.
GeneTreeiENSGT00530000063810.
HOGENOMiHOG000293391.
HOVERGENiHBG080884.
InParanoidiQ8BG28.
KOiK09654.
OMAiFYRWTVE.
OrthoDBiEOG7PK8Z9.
PhylomeDBiQ8BG28.
TreeFamiTF314311.

Family and domain databases

InterProiIPR002659. Glyco_trans_31.
[Graphical view]
PANTHERiPTHR11214. PTHR11214. 2 hits.
PfamiPF01762. Galactosyl_T. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BG28-1) [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
MRNWLVLLCP CVLGAALHLW HLWLRSPPDP HNTGPSAADQ SALFPHWKFS
60 70 80 90 100
HYDVVVGVLS ARNNHELRNV IRNTWLKNLL HHPTLSQRVL VKFIIGARGC
110 120 130 140 150
EVPVEDREDP YSCRLLNITN PVLNQEIEAF SFPEDASSSR LSEDRVVSVS
160 170 180 190 200
FRVLYPIVIT SLGVFYDASD VGFQRNITVK LYQTEQEEAL FIARFSPPSC
210 220 230 240 250
GVQVNKLWYK PVEQFILPES FEGTIVWESQ DLHGLVSRNL HRVTVNDGGG
260 270 280 290 300
VLRVLAAGEG ALPHEFMEGV EGVAGGFIYT VQEGDALLRS LYSRPQRLAD
310 320 330 340 350
HIQDLQVEDA LLQEESSVHD DIVFVDVVDT YRNVPAKLLN FYRWTVESTS
360 370 380 390 400
FDLLLKTDDD CYIDLEAVFN RIAQKNLDGP NFWWGNFRLN WAVDRTGKWQ
410 420 430 440 450
ELEYPSPAYP AFACGSGYVI SKDIVDWLAG NSRRLKTYQG EDVSMGIWMA
460 470 480 490 500
AIGPKRHQDS LWLCEKTCET GMLSSPQYSP EELSKLWELK ELCGDPCQCE

AKVR
Length:504
Mass (Da):57,219
Last modified:March 1, 2003 - v1
Checksum:iCF23C733C84AC6C0
GO
Isoform 2 (identifier: Q8BG28-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     188-209: EALFIARFSPPSCGVQVNKLWY → VCTGMDRIFLLLKQLFFVVPID
     210-504: Missing.

Note: No experimental confirmation available.
Show »
Length:209
Mass (Da):23,895
Checksum:iA9B2B2AEB33BD7E8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601S → P in AAH85110 (PubMed:15489334).Curated
Sequence conflicti406 – 4061S → G in AAH85110 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei188 – 20922EALFI…NKLWY → VCTGMDRIFLLLKQLFFVVP ID in isoform 2. 1 PublicationVSP_020253Add
BLAST
Alternative sequencei210 – 504295Missing in isoform 2. 1 PublicationVSP_020254Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB116655 mRNA. Translation: BAD13421.1.
AK035259 mRNA. Translation: BAC29004.1.
AK041022 mRNA. Translation: BAC30784.1.
AK044785 mRNA. Translation: BAC32091.1.
AK084275 mRNA. Translation: BAC39153.1.
AK151677 mRNA. Translation: BAE30602.1.
AK153362 mRNA. Translation: BAE31934.1.
AK167635 mRNA. Translation: BAE39686.1.
BC085110 mRNA. Translation: AAH85110.1.
CCDSiCCDS26246.1. [Q8BG28-1]
RefSeqiNP_848755.1. NM_178640.2. [Q8BG28-1]
UniGeneiMm.21686.

Genome annotation databases

EnsembliENSMUST00000099747; ENSMUSP00000097336; ENSMUSG00000039242. [Q8BG28-1]
GeneIDi97884.
KEGGimmu:97884.
UCSCiuc007pmm.1. mouse. [Q8BG28-2]
uc007pmn.1. mouse. [Q8BG28-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB116655 mRNA. Translation: BAD13421.1.
AK035259 mRNA. Translation: BAC29004.1.
AK041022 mRNA. Translation: BAC30784.1.
AK044785 mRNA. Translation: BAC32091.1.
AK084275 mRNA. Translation: BAC39153.1.
AK151677 mRNA. Translation: BAE30602.1.
AK153362 mRNA. Translation: BAE31934.1.
AK167635 mRNA. Translation: BAE39686.1.
BC085110 mRNA. Translation: AAH85110.1.
CCDSiCCDS26246.1. [Q8BG28-1]
RefSeqiNP_848755.1. NM_178640.2. [Q8BG28-1]
UniGeneiMm.21686.

3D structure databases

ProteinModelPortaliQ8BG28.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000097336.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

PTM databases

iPTMnetiQ8BG28.
PhosphoSiteiQ8BG28.

Proteomic databases

PaxDbiQ8BG28.
PRIDEiQ8BG28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000099747; ENSMUSP00000097336; ENSMUSG00000039242. [Q8BG28-1]
GeneIDi97884.
KEGGimmu:97884.
UCSCiuc007pmm.1. mouse. [Q8BG28-2]
uc007pmn.1. mouse. [Q8BG28-1]

Organism-specific databases

CTDi148789.
MGIiMGI:2145517. B3galnt2.

Phylogenomic databases

eggNOGiKOG2287. Eukaryota.
ENOG410ZZ1B. LUCA.
GeneTreeiENSGT00530000063810.
HOGENOMiHOG000293391.
HOVERGENiHBG080884.
InParanoidiQ8BG28.
KOiK09654.
OMAiFYRWTVE.
OrthoDBiEOG7PK8Z9.
PhylomeDBiQ8BG28.
TreeFamiTF314311.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi353158.
PROiQ8BG28.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BG28.
GenevisibleiQ8BG28. MM.

Family and domain databases

InterProiIPR002659. Glyco_trans_31.
[Graphical view]
PANTHERiPTHR11214. PTHR11214. 2 hits.
PfamiPF01762. Galactosyl_T. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel human beta1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAcbeta1-3GlcNAc."
    Hiruma T., Togayachi A., Okamura K., Sato T., Kikuchi N., Kwon Y.D., Nakamura A., Fujimura K., Gotoh M., Tachibana K., Ishizuka Y., Noce T., Nakanishi H., Narimatsu H.
    J. Biol. Chem. 279:14087-14095(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  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: Aorta, Bone marrow, Eye, Placenta, Retina, Urinary bladder and Vein.
  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).
    Tissue: Trophoblast stem cell.

Entry informationi

Entry nameiB3GL2_MOUSE
AccessioniPrimary (citable) accession number: Q8BG28
Secondary accession number(s): Q5U4F9, Q8BXL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: March 1, 2003
Last modified: January 20, 2016
This is version 88 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.