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Q9NY97 (B3GN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2

Short name=BGnT-2
Short name=Beta-1,3-Gn-T2
Short name=Beta-1,3-N-acetylglucosaminyltransferase 2
Short name=Beta3Gn-T2
EC=2.4.1.-
Alternative name(s):
Beta-1,3-N-acetylglucosaminyltransferase 1
Short name=BGnT-1
Short name=Beta-1,3-Gn-T1
Short name=Beta3Gn-T1
Beta-1,3-galactosyltransferase 7
Short name=Beta-1,3-GalTase 7
Short name=Beta3Gal-T7
Short name=Beta3GalT7
Short name=b3Gal-T7
Beta-3-Gx-T7
UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7
UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7
Gene names
Name:B3GNT2
Synonyms:B3GALT7, B3GNT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains. Ref.1

Cofactor

Manganese. Ref.1

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts with B3GNT8; this interaction greatly increases B3GNT2 catalytic activity, independently of B3GNT8 enzymatic activity. Ref.13

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Potential.

Tissue specificity

Ubiquitous. Ref.5

Sequence similarities

Belongs to the glycosyltransferase 31 family.

Caution

Was indicated as B3Gal-T6 in submitted DNA entries.

Sequence caution

The sequence BAA92031.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NY97-1)

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.
Isoform 2 (identifier: Q9NY97-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MSVGRRRIKLL → MVSRSLV
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2
PRO_0000219170

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 397369Lumenal Potential

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Ref.12
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 1111MSVGRRRIKLL → MVSRSLV in isoform 2.
VSP_001791

Experimental info

Mutagenesis2451D → A: Loss of enzymatic activity, no loss of B3GNT8-binding. Ref.13
Sequence conflict111L → LL in CAB91546. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 11, 2003. Version 2.
Checksum: B104ECCAE26DC4AC

FASTA39746,022
        10         20         30         40         50         60 
MSVGRRRIKL LGILMMANVF IYFIMEVSKS SSQEKNGKGE VIIPKEKFWK ISTPPEAYWN 

        70         80         90        100        110        120 
REQEKLNRQY NPILSMLTNQ TGEAGRLSNI SHLNYCEPDL RVTSVVTGFN NLPDRFKDFL 

       130        140        150        160        170        180 
LYLRCRNYSL LIDQPDKCAK KPFLLLAIKS LTPHFARRQA IRESWGQESN AGNQTVVRVF 

       190        200        210        220        230        240 
LLGQTPPEDN HPDLSDMLKF ESEKHQDILM WNYRDTFFNL SLKEVLFLRW VSTSCPDTEF 

       250        260        270        280        290        300 
VFKGDDDVFV NTHHILNYLN SLSKTKAKDL FIGDVIHNAG PHRDKKLKYY IPEVVYSGLY 

       310        320        330        340        350        360 
PPYAGGGGFL YSGHLALRLY HITDQVHLYP IDDVYTGMCL QKLGLVPEKH KGFRTFDIEE 

       370        380        390 
KNKNNICSYV DLMLVHSRKP QEMIDIWSQL QSAHLKC 

« Hide

Isoform 2 [UniParc].

Checksum: DA6ECD0416167FEF
Show »

FASTA39345,484

References

« Hide 'large scale' references
[1]"A beta-1,3-N-acetylglucosaminyltransferase with poly-N-acetyllactosamine synthase activity is structurally related to beta-1,3-galactosyltransferases."
Zhou D., Dinter A., Gutierrez Gallego R., Kamerling J.P., Vliegenthart J.F.G., Berger E.G., Hennet T.
Proc. Natl. Acad. Sci. U.S.A. 96:406-411(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COFACTOR.
Tissue: Brain.
[2]Zhou D., Berger E.G., Hennet T.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Cloning and expression of two beta-1,3-galactosyltransferases: beta3gal-T5 and beta3gal-T6."
Amado M., Carneiro F., Clausen H.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"A novel member of beta-1,3-galactosyltransferase family is down regulated during bladder TCC progression."
Gromova I., Gromov P., Celis J.E.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Urinary bladder.
[5]"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] (ISOFORM 1), CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Brain and Testis.
[9]"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. expand/collapse author list , 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] OF 25-397.
Tissue: Placenta.
[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.
[11]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[12]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79.
Tissue: Plasma.
[13]"Activation of beta1,3-N-acetylglucosaminyltransferase-2 (beta3Gn-T2) by beta3Gn-T8. Possible involvement of beta3Gn-T8 in increasing poly-N-acetyllactosamine chains in differentiated HL-60 cells."
Seko A., Yamashita K.
J. Biol. Chem. 283:33094-33100(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH B3GNT8, MUTAGENESIS OF ASP-245.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF092051 mRNA. Translation: AAD09764.2.
AJ006077 mRNA. Translation: CAB91546.1.
AF288208 mRNA. Translation: AAF97253.1.
AF288209 mRNA. Translation: AAF97254.1.
AB049584 mRNA. Translation: BAB21530.1.
BC030579 mRNA. Translation: AAH30579.1.
AC093401 Genomic DNA. Translation: AAX93271.1.
CH471053 Genomic DNA. Translation: EAW99977.1.
CH471053 Genomic DNA. Translation: EAW99978.1.
CH471053 Genomic DNA. Translation: EAW99979.1.
BC047933 mRNA. Translation: AAH47933.1.
AK002009 mRNA. Translation: BAA92031.1. Different initiation.
CCDSCCDS1870.1. [Q9NY97-1]
RefSeqNP_006568.2. NM_006577.5. [Q9NY97-1]
UniGeneHs.173203.

3D structure databases

ProteinModelPortalQ9NY97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115919. 2 interactions.
IntActQ9NY97. 1 interaction.
STRING9606.ENSP00000305595.

Protein family/group databases

CAZyGT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSiteQ9NY97.

Proteomic databases

MaxQBQ9NY97.
PaxDbQ9NY97.
PRIDEQ9NY97.

Protocols and materials databases

DNASU10678.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301998; ENSP00000305595; ENSG00000170340. [Q9NY97-1]
ENST00000405767; ENSP00000384692; ENSG00000170340. [Q9NY97-1]
GeneID10678.
KEGGhsa:10678.
UCSCuc002sbs.3. human. [Q9NY97-1]

Organism-specific databases

CTD10678.
GeneCardsGC02P062423.
HGNCHGNC:15629. B3GNT2.
HPAHPA005997.
MIM605581. gene.
neXtProtNX_Q9NY97.
PharmGKBPA25218.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262849.
HOGENOMHOG000232195.
HOVERGENHBG050653.
InParanoidQ9NY97.
KOK00741.
OMARNNICSY.
OrthoDBEOG7BGHKT.
PhylomeDBQ9NY97.
TreeFamTF318639.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

BgeeQ9NY97.
CleanExHS_B3GNT1.
HS_B3GNT2.
GenevestigatorQ9NY97.

Family and domain databases

InterProIPR002659. Glyco_trans_31.
[Graphical view]
PANTHERPTHR11214. PTHR11214. 1 hit.
PfamPF01762. Galactosyl_T. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSB3GNT2. human.
GeneWikiB3GNT2.
GenomeRNAi10678.
NextBio40601.
PROQ9NY97.
SOURCESearch...

Entry information

Entry nameB3GN2_HUMAN
AccessionPrimary (citable) accession number: Q9NY97
Secondary accession number(s): Q54AC1 expand/collapse secondary AC list , Q9NQQ9, Q9NQR0, Q9NUT9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: April 11, 2003
Last modified: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM