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Protein

Beta-1,3-galactosyltransferase 2

Gene

B3GALT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 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-N-acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. Inactive towards substrates with terminal alpha-N-acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine (alpha-GalNAc) residues.2 Publications

Cofactori

Mn2+By similarity

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

  • UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity Source: ProtInc

GO - Biological processi

  • oligosaccharide biosynthetic process Source: Ensembl
  • protein glycosylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese

Enzyme and pathway databases

BRENDAi2.4.1.62. 2681.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Chemistry

SwissLipidsiSLP:000000773.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-galactosyltransferase 2 (EC:2.4.1.-)
Short name:
Beta-1,3-GalTase 2
Short name:
Beta3Gal-T2
Short name:
Beta3GalT2
Alternative name(s):
UDP-galactose:2-acetamido-2-deoxy-D-glucose 3beta-galactosyltransferase 2
Gene namesi
Name:B3GALT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:917. B3GALT2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2424CytoplasmicSequence analysisAdd
BLAST
Transmembranei25 – 4521Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini46 – 422377LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25210.

Polymorphism and mutation databases

BioMutaiB3GALT2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Beta-1,3-galactosyltransferase 2PRO_0000219150Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence analysis
Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence analysis
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence analysis
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO43825.
PRIDEiO43825.

PTM databases

PhosphoSiteiO43825.

Expressioni

Tissue specificityi

Detected in heart and brain.2 Publications

Gene expression databases

BgeeiO43825.
CleanExiHS_B3GALT2.
GenevisibleiO43825. HS.

Organism-specific databases

HPAiHPA055372.

Interactioni

Protein-protein interaction databases

BioGridi114250. 10 interactions.
IntActiO43825. 1 interaction.
STRINGi9606.ENSP00000356404.

Structurei

3D structure databases

ProteinModelPortaliO43825.
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.
GeneTreeiENSGT00760000118879.
HOGENOMiHOG000059604.
HOVERGENiHBG101354.
InParanoidiO43825.
KOiK07820.
OMAiYTIRGFR.
OrthoDBiEOG7C2R1D.
PhylomeDBiO43825.
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.

O43825-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQWRRRHCC FAKMTWNAKR SLFRTHLIGV LSLVFLFAMF LFFNHHDWLP
60 70 80 90 100
GRAGFKENPV TYTFRGFRST KSETNHSSLR NIWKETVPQT LRPQTATNSN
110 120 130 140 150
NTDLSPQGVT GLENTLSANG SIYNEKGTGH PNSYHFKYII NEPEKCQEKS
160 170 180 190 200
PFLILLIAAE PGQIEARRAI RQTWGNESLA PGIQITRIFL LGLSIKLNGY
210 220 230 240 250
LQRAILEESR QYHDIIQQEY LDTYYNLTIK TLMGMNWVAT YCPHIPYVMK
260 270 280 290 300
TDSDMFVNTE YLINKLLKPD LPPRHNYFTG YLMRGYAPNR NKDSKWYMPP
310 320 330 340 350
DLYPSERYPV FCSGTGYVFS GDLAEKIFKV SLGIRRLHLE DVYVGICLAK
360 370 380 390 400
LRIDPVPPPN EFVFNHWRVS YSSCKYSHLI TSHQFQPSEL IKYWNHLQQN
410 420
KHNACANAAK EKAGRYRHRK LH
Length:422
Mass (Da):49,213
Last modified:June 1, 1998 - v1
Checksum:iBA62942D6AFB4B0C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721Q → R in AAG60610 (PubMed:11318611).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15014 mRNA. Translation: CAA75245.1.
Y15060 mRNA. Translation: CAA75344.1.
AF288390 mRNA. Translation: AAG60610.1.
AK314116 mRNA. Translation: BAG36808.1.
AL390863 Genomic DNA. Translation: CAH71590.1.
CH471067 Genomic DNA. Translation: EAW91251.1.
BC022507 mRNA. Translation: AAH22507.1.
CCDSiCCDS1383.1.
RefSeqiNP_003774.1. NM_003783.3.
UniGeneiHs.518834.

Genome annotation databases

EnsembliENST00000367434; ENSP00000356404; ENSG00000162630.
GeneIDi8707.
KEGGihsa:8707.
UCSCiuc001gtc.5. human.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta-1,3-galactosyltransferase 2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15014 mRNA. Translation: CAA75245.1.
Y15060 mRNA. Translation: CAA75344.1.
AF288390 mRNA. Translation: AAG60610.1.
AK314116 mRNA. Translation: BAG36808.1.
AL390863 Genomic DNA. Translation: CAH71590.1.
CH471067 Genomic DNA. Translation: EAW91251.1.
BC022507 mRNA. Translation: AAH22507.1.
CCDSiCCDS1383.1.
RefSeqiNP_003774.1. NM_003783.3.
UniGeneiHs.518834.

3D structure databases

ProteinModelPortaliO43825.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114250. 10 interactions.
IntActiO43825. 1 interaction.
STRINGi9606.ENSP00000356404.

Chemistry

SwissLipidsiSLP:000000773.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSiteiO43825.

Polymorphism and mutation databases

BioMutaiB3GALT2.

Proteomic databases

PaxDbiO43825.
PRIDEiO43825.

Protocols and materials databases

DNASUi8707.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367434; ENSP00000356404; ENSG00000162630.
GeneIDi8707.
KEGGihsa:8707.
UCSCiuc001gtc.5. human.

Organism-specific databases

CTDi8707.
GeneCardsiB3GALT2.
HGNCiHGNC:917. B3GALT2.
HPAiHPA055372.
MIMi603018. gene.
neXtProtiNX_O43825.
PharmGKBiPA25210.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2287. Eukaryota.
ENOG410ZZ1B. LUCA.
GeneTreeiENSGT00760000118879.
HOGENOMiHOG000059604.
HOVERGENiHBG101354.
InParanoidiO43825.
KOiK07820.
OMAiYTIRGFR.
OrthoDBiEOG7C2R1D.
PhylomeDBiO43825.
TreeFamiTF318639.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.62. 2681.

Miscellaneous databases

GenomeRNAii8707.
NextBioi32657.
PROiO43825.
SOURCEiSearch...

Gene expression databases

BgeeiO43825.
CleanExiHS_B3GALT2.
GenevisibleiO43825. HS.

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. "Cloning of a human UDP-galactose:2-acetamido-2-deoxy-D-glucose 3beta-galactosyltransferase catalyzing the formation of type 1 chains."
    Kolbinger F., Streiff M.B., Katopodis A.G.
    J. Biol. Chem. 273:433-440(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "A family of human beta3-galactosyltransferases. Characterization of four members of a UDP-galactose:beta-N-acetyl-glucosamine/beta-nacetyl-galactosamine beta-1,3-galactosyltransferase family."
    Amado M., Almeida R., Carneiro F., Levery S.B., Holmes E.H., Nomoto M., Hollingsworth M.A., Hassan H., Schwientek T., Nielsen P.A., Bennett E.P., Clausen H.
    J. Biol. Chem. 273:12770-12778(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  3. "Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus."
    Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M., Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H., Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M., Carpten J.D.
    Genomics 73:211-222(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Amygdala.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Brain.

Entry informationi

Entry nameiB3GT2_HUMAN
AccessioniPrimary (citable) accession number: O43825
Secondary accession number(s): B2RAB1, Q9BZQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: June 1, 1998
Last modified: March 16, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.