Q8N0V5 (GNT2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 402	402	N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase, isoform A		PRO_0000395119
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 23	16	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	24 – 400	377	Lumenal Potential
Amino acid modifications
	Glycosylation	41	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (IGNTA) (IGNT1) [UniParc]. Last modified October 1, 2002. Version 1. Checksum: FCA6AE905D78D7D5	FASTA	402	45,873
	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
	Isoform B (IGNTB) (IGNT2) [UniParc]. See Q06430.		–	–
	Isoform C (IGNTC) (IGNT3) [UniParc]. See Q8NFS9.		–	–

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
IPI	IPI00166086.
RefSeq	NP_663624.1. NM_145649.4.
UniGene	Hs.519884.
3D structure databases
ProteinModelPortal	Q8N0V5.
SMR	Q8N0V5. Positions 74-389.
ModBase	Search...
Protein family/group databases
CAZy	GT14. Glycosyltransferase Family 14.
Polymorphism databases
DMDM	74714686.
Proteomic databases
PaxDb	Q8N0V5.
PRIDE	Q8N0V5.
Protocols and materials databases
DNASU	2651.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379597; ENSP00000368917; ENSG00000111846. ENST00000495262; ENSP00000419411; ENSG00000111846.
GeneID	2651.
KEGG	hsa:2651.
UCSC	uc003mzc.4. human.
Organism-specific databases
CTD	2651.
GeneCards	GC06P010492.
HGNC	HGNC:4204. GCNT2.
MIM	110800. phenotype. 600429. gene.
neXtProt	NX_Q8N0V5.
PharmGKB	PA169.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG253565.
HOGENOM	HOG000293251.
HOVERGEN	HBG051711.
KO	K00742.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q8N0V5.
Bgee	Q8N0V5.
Family and domain databases
InterPro	IPR003406. Glyco_trans_14. [Graphical view]
Pfam	PF02485. Branch. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GCNT2. human.
GenomeRNAi	2651.
NextBio	10472.
SOURCE	Search...

Entry information

Entry name

GNT2A_HUMAN

Accession

Primary (citable) accession number: Q8N0V5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.