Q06430 (GNT2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase, isoform B
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	400 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.
Tissue specificity	In the adult, highly expressed in prostate and to a lesser extent in small intestine and colon. Barely detected in heart, brain, kidney and pancreas. No expression in placenta, lung, liver, skeletal muscle, spleen, thymus, testis, ovary and peripheral blood leukocytes. In fetus, highly expressed in brain and to a lesser extent in lung and kidney. Barely detected in liver. Ref.3 Ref.9
Developmental stage	Its expression increases dramatically during development and oncogenesis.
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 Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycosaminoglycan biosynthetic process Traceable author statement Ref.1. Source: ProtInc multicellular organismal development Traceable author statement PubMed 9134435. Source: ProtInc 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 membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity Traceable author statement Ref.1. Source: ProtInc
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 B (identifier: Q06430-1)

Also known as: IGNTB; IGNT2;

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.

Note: Expressed in lens epithelium cells.

Isoform A (identifier: Q8N0V5-1)

Also known as: IGNTA; IGNT1;

The sequence of this isoform can be found in the external entry Q8N0V5.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

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 – 400	400	N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase, isoform B		PRO_0000191397
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 25	19	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	26 – 400	375	Lumenal Potential
Amino acid modifications
	Glycosylation	37	1	N-linked (GlcNAc...) Potential
	Glycosylation	255	1	N-linked (GlcNAc...) Potential
	Glycosylation	314	1	N-linked (GlcNAc...) Potential
	Glycosylation	388	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	85	1	P → R. Corresponds to variant rs17637756 [ dbSNP | Ensembl ].		VAR_049323

Sequences

	Sequence		Length	Mass (Da)
	Isoform B (IGNTB) (IGNT2) [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 1469628690A1F43B	FASTA	400	45,855
	10 20 30 40 50 60 MPLSMRYLFI ISVSSVIIFI VFSVFNFGGD PSFQRLNISD PLRLTQVCTS FINGKTRFLW 70 80 90 100 110 120 KNKLMIHEKS SCKEYLTQSH YITAPLSKEE ADFPLAYIMV IHHHFDTFAR LFRAIYMPQN 130 140 150 160 170 180 IYCVHVDEKA TTEFKDAVEQ LLSCFPNAFL ASKMEPVVYG GISRLQADLN CIRDLSAFEV 190 200 210 220 230 240 SWKYVINTCG QDFPLKTNKE IVQYLKGFKG KNITPGVLPP AHAIGRTKYV HQEHLGKELS 250 260 270 280 290 300 YVIRTTALKP PPPHNLTIYF GSAYVALSRE FANFVLHDPR AVDLLQWSKD TFSPDEHFWV 310 320 330 340 350 360 TLNRIPGVPG SMPNASWTGN LRAIKWSDME DRHGGCHGHY VHGICIYGNG DLKWLVNSPS 370 380 390 400 LFANKFELNT YPLTVECLEL RHRERTLNQS ETAIQPSWYF
	Isoform A (IGNTA) (IGNT1) [UniParc]. See Q8N0V5.		–	–
	Isoform C (IGNTC) (IGNT3) [UniParc]. See Q8NFS9.		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of the developmental I antigen by a cloned human cDNA encoding a member of a beta-1,6-N-acetylglucosaminyltransferase gene family." Bierhuizen M.F.A., Mattei M.-G., Fukuda M. Genes Dev. 7:468-478(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Embryonic carcinoma.
[2]	"Genomic organization of core 2 and I branching beta-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the beta-1,6-N-acetylglucosaminyltransferase gene family." Bierhuizen M.F.A., Maemura K., Kudo S., Fukuda M. Glycobiology 5:417-425(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[3]	"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.
[4]	"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].
[5]	"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].
[6]	"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.
[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. , 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].
[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]. Tissue: Lung.
[9]	"Expression cloning of cDNA encoding a human beta-1,3-N-acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis." Sasaki K., Kurata-Miura K., Ujita M., Angata K., Nakagawa S., Sekine S., Nishi T., Fukuda M. Proc. Natl. Acad. Sci. U.S.A. 94:14294-14299(1997) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	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	L19659 mRNA. Translation: AAA81777.1. L41607, L41605, L41606 Genomic DNA. Translation: AAA99832.1. Z19550 mRNA. Translation: CAA79610.1. AF458025 mRNA. Translation: AAM73865.1. AY435146 mRNA. Translation: AAR95647.1. AK313903 mRNA. Translation: BAG36626.1. AL139039, AL358777 Genomic DNA. Translation: CAH73010.1. AL358777, AL139039 Genomic DNA. Translation: CAI13999.1. CH471087 Genomic DNA. Translation: EAW55260.1. BC074801 mRNA. Translation: AAH74801.1. BC074802 mRNA. Translation: AAH74802.1.
IPI	IPI00030933.
PIR	A46297.
RefSeq	NP_001482.1. NM_001491.2.
UniGene	Hs.519884.
3D structure databases
ProteinModelPortal	Q06430.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000265012.
Protein family/group databases
CAZy	GT14. Glycosyltransferase Family 14.
PTM databases
PhosphoSite	Q06430.
Polymorphism databases
DMDM	543887.
Proteomic databases
PRIDE	Q06430.
Protocols and materials databases
DNASU	2651.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000316170; ENSP00000314844; ENSG00000111846.
GeneID	2651.
KEGG	hsa:2651.
UCSC	uc003mzd.3. human.
Organism-specific databases
CTD	2651.
GeneCards	GC06P010492.
HGNC	HGNC:4204. GCNT2.
MIM	110800. phenotype. 600429. gene.
neXtProt	NX_Q06430.
PharmGKB	PA169.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HOG000293251.
HOVERGEN	HBG051711.
KO	K00742.
Enzyme and pathway databases
SignaLink	Q06430.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q06430.
Bgee	Q06430.
CleanEx	HS_GCNT2.
Genevestigator	Q06430.
GermOnline	ENSG00000111846. Homo sapiens.
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

GNT2B_HUMAN

Accession

Primary (citable) accession number: Q06430
Secondary accession number(s): Q5W0E9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 29, 2013
This is version 115 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.