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Protein

N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3

Gene

B3GNT3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Has activity for type 2 oligosaccharides (PubMed:11042166). Also acts as a core1-1,3-N-acetylglucosaminyltransferase (Core1-beta3GlcNAcT) to form the 6-sulfo sialyl Lewis x on extended core1 O-glycans (PubMed:11439191).2 Publications

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.1 Publication
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R.1 Publication

Pathway: 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

BioCyciMetaCyc:ENSG00000179913-MONOMER.
BRENDAi2.4.1.146. 2681.
ReactomeiREACT_115606. O-linked glycosylation of mucins.
REACT_121120. Keratan sulfate biosynthesis.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3 (EC:2.4.1.1491 Publication)
Alternative name(s):
Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase (EC:2.4.1.1461 Publication)
Beta-1,3-galactosyltransferase 8
Short name:
Beta-1,3-GalTase 8
Short name:
Beta3Gal-T8
Short name:
Beta3GalT8
Short name:
b3Gal-T8
Beta-3-Gx-T8
Core 1 extending beta-1,3-N-acetylglucosaminyltransferase1 Publication
Core1-beta3GlcNAcT1 Publication
Transmembrane protein 3
UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 8
UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3
Short name:
BGnT-3
Short name:
Beta-1,3-Gn-T3
Short name:
Beta-1,3-N-acetylglucosaminyltransferase 3
Short name:
Beta3Gn-T3
UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 8
Gene namesi
Name:B3GNT3
Synonyms:B3GALT8, TMEM3
ORF Names:UNQ637/PRO1266
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:13528. B3GNT3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010CytoplasmicSequence Analysis
Transmembranei11 – 3121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini32 – 372341LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • Golgi membrane Source: Reactome
  • integral component of plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25219.

Polymorphism and mutation databases

BioMutaiB3GNT3.
DMDMi311033352.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3PRO_0000219172Add
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
Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9Y2A9.
PaxDbiQ9Y2A9.
PRIDEiQ9Y2A9.

PTM databases

PhosphoSiteiQ9Y2A9.

Expressioni

Tissue specificityi

Expressed in colon, jejunum, stomach, esophagus, placenta and trachea.1 Publication

Gene expression databases

BgeeiQ9Y2A9.
CleanExiHS_B3GNT3.
ExpressionAtlasiQ9Y2A9. baseline and differential.
GenevisibleiQ9Y2A9. HS.

Organism-specific databases

HPAiHPA024298.

Interactioni

Protein-protein interaction databases

BioGridi115614. 13 interactions.
STRINGi9606.ENSP00000321874.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2A9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG293830.
GeneTreeiENSGT00760000118879.
HOGENOMiHOG000232195.
HOVERGENiHBG050653.
InParanoidiQ9Y2A9.
KOiK07970.
OMAiCAQPVFL.
PhylomeDBiQ9Y2A9.
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.

Q9Y2A9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYLRHRRPN ATLILAIGAF TLLLFSLLVS PPTCKVQEQP PAIPEALAWP
60 70 80 90 100
TPPTRPAPAP CHANTSMVTH PDFATQPQHV QNFLLYRHCR HFPLLQDVPP
110 120 130 140 150
SKCAQPVFLL LVIKSSPSNY VRRELLRRTW GRERKVRGLQ LRLLFLVGTA
160 170 180 190 200
SNPHEARKVN RLLELEAQTH GDILQWDFHD SFFNLTLKQV LFLQWQETRC
210 220 230 240 250
ANASFVLNGD DDVFAHTDNM VFYLQDHDPG RHLFVGQLIQ NVGPIRAFWS
260 270 280 290 300
KYYVPEVVTQ NERYPPYCGG GGFLLSRFTA AALRRAAHVL DIFPIDDVFL
310 320 330 340 350
GMCLELEGLK PASHSGIRTS GVRAPSQRLS SFDPCFYRDL LLVHRFLPYE
360 370
MLLMWDALNQ PNLTCGNQTQ IY
Length:372
Mass (Da):42,534
Last modified:November 2, 2010 - v2
Checksum:iA6E3FE88B2F00F10
GO

Sequence cautioni

The sequence CAC82374.1 differs from that shown. Reason: Frameshift at positions 194, 196, 202, 204, 209 and 215. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891C → Y in AAH66876 (PubMed:15489334).Curated
Sequence conflicti355 – 3551W → R in AAH67423 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti328 – 3281R → H.6 Publications
Corresponds to variant rs36686 [ dbSNP | Ensembl ].
VAR_022644

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015630 mRNA. Translation: BAA76497.1.
AF293973 mRNA. Translation: AAK00849.1.
AB049585 mRNA. Translation: BAB21531.1.
AJ130847 mRNA. Translation: CAC45044.1.
AJ278961 mRNA. Translation: CAC82374.1. Frameshift.
AY358955 mRNA. Translation: AAQ89314.1.
AK314323 mRNA. Translation: BAG36971.1.
AC008761 Genomic DNA. No translation available.
BC066876 mRNA. Translation: AAH66876.1.
BC067423 mRNA. Translation: AAH67423.1.
CCDSiCCDS12364.1.
RefSeqiNP_055071.2. NM_014256.3.
UniGeneiHs.657825.
Hs.69009.

Genome annotation databases

EnsembliENST00000318683; ENSP00000321874; ENSG00000179913.
ENST00000595387; ENSP00000472638; ENSG00000179913.
GeneIDi10331.
KEGGihsa:10331.
UCSCiuc002nhl.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015630 mRNA. Translation: BAA76497.1.
AF293973 mRNA. Translation: AAK00849.1.
AB049585 mRNA. Translation: BAB21531.1.
AJ130847 mRNA. Translation: CAC45044.1.
AJ278961 mRNA. Translation: CAC82374.1. Frameshift.
AY358955 mRNA. Translation: AAQ89314.1.
AK314323 mRNA. Translation: BAG36971.1.
AC008761 Genomic DNA. No translation available.
BC066876 mRNA. Translation: AAH66876.1.
BC067423 mRNA. Translation: AAH67423.1.
CCDSiCCDS12364.1.
RefSeqiNP_055071.2. NM_014256.3.
UniGeneiHs.657825.
Hs.69009.

3D structure databases

ProteinModelPortaliQ9Y2A9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115614. 13 interactions.
STRINGi9606.ENSP00000321874.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSiteiQ9Y2A9.

Polymorphism and mutation databases

BioMutaiB3GNT3.
DMDMi311033352.

Proteomic databases

MaxQBiQ9Y2A9.
PaxDbiQ9Y2A9.
PRIDEiQ9Y2A9.

Protocols and materials databases

DNASUi10331.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318683; ENSP00000321874; ENSG00000179913.
ENST00000595387; ENSP00000472638; ENSG00000179913.
GeneIDi10331.
KEGGihsa:10331.
UCSCiuc002nhl.1. human.

Organism-specific databases

CTDi10331.
GeneCardsiGC19P017905.
HGNCiHGNC:13528. B3GNT3.
HPAiHPA024298.
MIMi605863. gene.
neXtProtiNX_Q9Y2A9.
PharmGKBiPA25219.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG293830.
GeneTreeiENSGT00760000118879.
HOGENOMiHOG000232195.
HOVERGENiHBG050653.
InParanoidiQ9Y2A9.
KOiK07970.
OMAiCAQPVFL.
PhylomeDBiQ9Y2A9.
TreeFamiTF318639.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:ENSG00000179913-MONOMER.
BRENDAi2.4.1.146. 2681.
ReactomeiREACT_115606. O-linked glycosylation of mucins.
REACT_121120. Keratan sulfate biosynthesis.

Miscellaneous databases

GeneWikiiBeta-1,3-N-acetylglucosaminyltransferase_3.
GenomeRNAii10331.
NextBioi39169.
PROiQ9Y2A9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2A9.
CleanExiHS_B3GNT3.
ExpressionAtlasiQ9Y2A9. baseline and differential.
GenevisibleiQ9Y2A9. 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. "Selection of cDNAs encoding putative type II membrane proteins on the cell surface from a human full-length cDNA bank."
    Yokoyama-Kobayashi M., Yamaguchi T., Sekine S., Kato S.
    Gene 228:161-167(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-328.
  2. "Novel sulfated lymphocyte homing receptors and their control by a Core1 extension beta 1,3-N-acetylglucosaminyltransferase."
    Yeh J.-C., Hiraoka N., Petryniak B., Nakayama J., Ellies L.G., Rabuka D., Hindsgaul O., Marth J.D., Lowe J.B., Fukuda M.
    Cell 105:957-969(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, VARIANT HIS-328.
  3. "Identification and characterization of three novel beta 1,3-N-acetylglucosaminyltransferases structurally related to the beta 1,3-galactosyltransferase family."
    Shiraishi N., Natsume A., Togayachi A., Endo T., Akashima T., Yamada Y., Imai N., Nakagawa S., Koizumi S., Sekine S., Narimatsu H., Sasaki K.
    J. Biol. Chem. 276:3498-3507(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.
    Tissue: Gastric mucosa.
  4. "Cloning of a new member of the beta 1,3 galactosyltransferase family, b1,3Gal-T6."
    Jensen M.A., Bennett E.P.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-328.
  5. Bennett E.P.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-328.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-328.
  7. "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: Placenta.
  8. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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], VARIANT HIS-328.
  10. "Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions."
    Amado M., Almeida R., Schwientek T., Clausen H.
    Biochim. Biophys. Acta 1473:35-53(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiB3GN3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2A9
Secondary accession number(s): B2RAS4
, Q6NWU9, Q6NXU9, Q8WWR6, Q9C0J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 2, 2010
Last modified: June 24, 2015
This is version 130 of the entry and version 2 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.