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Q8N0V5 (GNT2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. 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:
N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase, isoform A

Short name=N-acetylglucosaminyltransferase
EC=2.4.1.150
Alternative name(s):
I-branching enzyme
IGNT
Gene names
Name:GCNT2
Synonyms:GCNT5, II, NACGT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Branching enzyme that converts linear into branched poly-N-acetyllactosaminoglycans. Introduces the blood group I antigen during embryonic development. It is closely associated with the development and maturation of erythroid cells. The expression of the blood group I antigen in erythrocytes is determined by isoform C.

Catalytic activity

UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

Isoform B is expressed in lens epithelium cells. Isoform C is expressed in reticulocytes. Ref.1

Polymorphism

GCNT2 is involved in determining the blood group I system (Ii) [MIM:110800]. The i (fetal) and I (adult) antigens are determined by linear and branched poly-N-acetyllactosaminoglycans, respectively. A replacement during development of i by I is dependent on the appearance of a beta-1,6-N-acetylglucosaminyltransferase, the I-branching enzyme. The expression of the blood group I antigen in erythrocytes is determined by isoform C of GCNT2.

Sequence similarities

Belongs to the glycosyltransferase 14 family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmaintenance of lens transparency

Inferred from mutant phenotype Ref.1. Source: UniProt

negative regulation of cell-substrate adhesion

Inferred from mutant phenotype PubMed 21750175. Source: UniProt

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype PubMed 21750175. Source: UniProt

positive regulation of cell migration

Inferred from mutant phenotype PubMed 21750175. Source: UniProt

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProt

positive regulation of epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 21750175. Source: UniProt

positive regulation of heterotypic cell-cell adhesion

Inferred from mutant phenotype PubMed 21750175. Source: UniProt

positive regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 21750175. Source: UniProt

posttranscriptional regulation of gene expression

Inferred from mutant phenotype PubMed 21750175. Source: UniProt

protein glycosylation

Inferred from mutant phenotype Ref.1. Source: UniProt

transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype PubMed 21750175. Source: UniProt

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionN-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity

Inferred from mutant phenotype Ref.1. Source: UniProt

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoforms A, B and C have different exons 1, but identical exons 2 and 3.
Isoform A (identifier: Q8N0V5-1)

Also known as: IGNTA; IGNT1;

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 B (identifier: Q06430-1)

Also known as: IGNTB; IGNT2;

The sequence of this isoform can be found in the external entry Q06430.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Expressed in lens epithelium cells.
Isoform C (identifier: Q8NFS9-1)

Also known as: IGNTC; IGNT3;

The sequence of this isoform can be found in the external entry Q8NFS9.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Expressed in reticulocytes. This isoform determines the expression of the blood group I antigen in erythrocytes.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 402402N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase, isoform A
PRO_0000395119

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2316Helical; Signal-anchor for type II membrane protein; Potential
Topological domain24 – 400377Lumenal Potential

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Isoform A (IGNTA) (IGNT1) [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: FCA6AE905D78D7D5

FASTA40245,873
        10         20         30         40         50         60 
MMGSWKHCLF SASLISALIF VFVYNTELWE NKRFLRAALS NASLLAEACH QIFEGKVFYP 

        70         80         90        100        110        120 
TENALKTTLD EATCYEYMVR SHYVTETLSE EEAGFPLAYT VTIHKDFGTF ERLFRAIYMP 

       130        140        150        160        170        180 
QNVYCVHLDQ KATDAFKGAV KQLLSCFPNA FLASKKESVV YGGISRLQAD LNCLEDLVAS 

       190        200        210        220        230        240 
EVPWKYVINT CGQDFPLKTN REIVQYLKGF KGKNITPGVL PPDHAVGRTK YVHQELLNHK 

       250        260        270        280        290        300 
NSYVIKTTKL KTPPPHDMVI YFGTAYVALT RDFANFVLQD QLALDLLSWS KDTYSPDEHF 

       310        320        330        340        350        360 
WVTLNRIPGV PGSMPNASWT GNLRAIKWSD MEDRHGGCHG HYVHGICIYG NGDLKWLVNS 

       370        380        390        400 
PSLFANKFEL NTYPLTVECL ELRHRERTLN QSETAIQPSW YF 

« Hide

Isoform B (IGNTB) (IGNT2) [UniParc].

See Q06430.

Isoform C (IGNTC) (IGNT3) [UniParc].

See Q8NFS9.

References

« Hide 'large scale' references
[1]"The molecular genetics of the human I locus and molecular background explain the partial association of the adult i phenotype with congenital cataracts."
Yu L.C., Twu Y.C., Chou M.L., Reid M.E., Gray A.R., Moulds J.M., Chang C.Y., Lin M.
Blood 101:2081-2088(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
Tissue: Prostate.
[2]"Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation."
Zhang T., Haws P., Wu Q.
Genome Res. 14:79-89(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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].
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Tissue: Brain.
[5]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF458024 mRNA. Translation: AAM73864.1.
AY435145 mRNA. Translation: AAR95646.1.
AK090483 mRNA. Translation: BAC03464.1.
AK291767 mRNA. Translation: BAF84456.1.
AL139039, AL358777 Genomic DNA. Translation: CAQ52588.1.
AL358777, AL139039 Genomic DNA. Translation: CAQ52597.1.
CH471087 Genomic DNA. Translation: EAW55262.1.
CCDSCCDS34338.1. [Q8N0V5-1]
RefSeqNP_663624.1. NM_145649.4. [Q8N0V5-1]
XP_006715115.1. XM_006715052.1. [Q8N0V5-1]
UniGeneHs.519884.

3D structure databases

ProteinModelPortalQ8N0V5.
SMRQ8N0V5. Positions 74-389.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108921. 1 interaction.

Protein family/group databases

CAZyGT14. Glycosyltransferase Family 14.

Proteomic databases

PaxDbQ8N0V5.
PRIDEQ8N0V5.

Protocols and materials databases

DNASU2651.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379597; ENSP00000368917; ENSG00000111846. [Q8N0V5-1]
ENST00000495262; ENSP00000419411; ENSG00000111846. [Q8N0V5-1]
GeneID2651.
KEGGhsa:2651.
UCSCuc003mzc.4. human. [Q8N0V5-1]

Organism-specific databases

CTD2651.
GeneCardsGC06P010492.
HGNCHGNC:4204. GCNT2.
MIM110800. phenotype.
600429. gene.
neXtProtNX_Q8N0V5.
PharmGKBPA169.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253565.
HOGENOMHOG000293251.
HOVERGENHBG051711.
KOK00742.
OMAGKSIDEF.
PhylomeDBQ8N0V5.
TreeFamTF315534.

Enzyme and pathway databases

SignaLinkQ8N0V5.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ8N0V5.
BgeeQ8N0V5.

Family and domain databases

InterProIPR003406. Glyco_trans_14.
[Graphical view]
PfamPF02485. Branch. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGCNT2. human.
GenomeRNAi2651.
NextBio10472.
SOURCESearch...

Entry information

Entry nameGNT2A_HUMAN
AccessionPrimary (citable) accession number: Q8N0V5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 81 of the entry and version 1 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 6

Human chromosome 6: entries, gene names and cross-references to MIM