GNT2A_HUMAN
ID GNT2A_HUMAN Reviewed; 402 AA.
AC Q8N0V5; Q06430; Q5T4J1; Q5W0E9; Q6T5E5; Q8NFS9;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase {ECO:0000305};
DE Short=N-acetylglucosaminyltransferase;
DE EC=2.4.1.150;
DE AltName: Full=I-branching enzyme;
DE AltName: Full=IGNT;
GN Name=GCNT2; Synonyms=GCNT5, II, NACGT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND FUNCTION.
RC TISSUE=Embryonic carcinoma;
RX PubMed=8449405; DOI=10.1101/gad.7.3.468;
RA Bierhuizen M.F.A., Mattei M.-G., Fukuda M.;
RT "Expression of the developmental I antigen by a cloned human cDNA encoding
RT a member of a beta-1,6-N-acetylglucosaminyltransferase gene family.";
RL Genes Dev. 7:468-478(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B), FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Placenta;
RX PubMed=7579796; DOI=10.1093/glycob/5.4.417;
RA Bierhuizen M.F.A., Maemura K., Kudo S., Fukuda M.;
RT "Genomic organization of core 2 and I branching beta-1,6-N-
RT acetylglucosaminyltransferases. Implication for evolution of the beta-1,6-
RT N-acetylglucosaminyltransferase gene family.";
RL Glycobiology 5:417-425(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), ALTERNATIVE SPLICING,
RP TISSUE SPECIFICITY, AND VARIANTS THR-169 AND GLN-228.
RC TISSUE=Prostate;
RX PubMed=12424189; DOI=10.1182/blood-2002-09-2693;
RA Yu L.C., Twu Y.C., Chou M.L., Reid M.E., Gray A.R., Moulds J.M.,
RA Chang C.Y., Lin M.;
RT "The molecular genetics of the human I locus and molecular background
RT explain the partial association of the adult i phenotype with congenital
RT cataracts.";
RL Blood 101:2081-2088(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), ALTERNATIVE SPLICING, FUNCTION
RP (ISOFORM C), AND TISSUE SPECIFICITY.
RX PubMed=12468428; DOI=10.1182/blood-2002-09-2838;
RA Inaba N., Hiruma T., Togayachi A., Iwasaki H., Wang X.H., Furukawa Y.,
RA Sumi R., Kudo T., Fujimura K., Iwai T., Gotoh M., Nakamura M.,
RA Narimatsu H.;
RT "A novel I-branching beta-1,6-N-acetylglucosaminyltransferase involved in
RT human blood group I antigen expression.";
RL Blood 101:2870-2876(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=14672974; DOI=10.1101/gr.1225204;
RA Zhang T., Haws P., Wu Q.;
RT "Multiple variable first exons: a mechanism for cell- and tissue-specific
RT gene regulation.";
RL Genome Res. 14:79-89(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC TISSUE=Fetal skin;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; B AND C).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP INVOLVEMENT IN CTRCT13, AND VARIANTS CTRCT13 GLU-350 AND HIS-385.
RX PubMed=11739194; DOI=10.1182/blood.v98.13.3840;
RA Yu L.C., Twu Y.C., Chang C.Y., Lin M.;
RT "Molecular basis of the adult i phenotype and the gene responsible for the
RT expression of the human blood group I antigen.";
RL Blood 98:3840-3845(2001).
RN [12]
RP VARIANT CTRCT13 SER-364.
RX PubMed=28839118; DOI=10.1534/g3.117.300109;
RA Javadiyan S., Craig J.E., Souzeau E., Sharma S., Lower K.M., Mackey D.A.,
RA Staffieri S.E., Elder J.E., Taranath D., Straga T., Black J., Pater J.,
RA Casey T., Hewitt A.W., Burdon K.P.;
RT "High-Throughput Genetic Screening of 51 Pediatric Cataract Genes
RT Identifies Causative Mutations in Inherited Pediatric Cataract in South
RT Eastern Australia.";
RL G3 (Bethesda) 7:3257-3268(2017).
RN [13]
RP VARIANTS CTRCT13 GLU-350 AND HIS-385.
RX PubMed=29914532; DOI=10.1186/s13023-018-0828-0;
RA Li J., Leng Y., Han S., Yan L., Lu C., Luo Y., Zhang X., Cao L.;
RT "Clinical and genetic characteristics of Chinese patients with familial or
RT sporadic pediatric cataract.";
RL Orphanet J. Rare Dis. 13:94-94(2018).
CC -!- FUNCTION: Branching enzyme that converts linear into branched poly-N-
CC acetyllactosaminoglycans. Introduces the blood group I antigen during
CC embryonic development. It is closely associated with the development
CC and maturation of erythroid cells. {ECO:0000269|PubMed:7579796,
CC ECO:0000269|PubMed:8449405}.
CC -!- FUNCTION: [Isoform C]: Determines the expression of the blood group I
CC antigen in erythrocytes. {ECO:0000269|PubMed:12468428}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-GlcNAc derivative + UDP-N-acetyl-alpha-D-glucosamine = a beta-
CC D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-[beta-D-GlcNAc-(1->6)]-beta-D-Gal-
CC (1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP;
CC Xref=Rhea:RHEA:54820, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:138371, ChEBI:CHEBI:138372;
CC EC=2.4.1.150;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q8N0V5-3; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-17248158, EBI-12142257;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Isoforms A, B and C have different exons 1, but identical
CC exons 2 and 3.;
CC Name=A; Synonyms=IGnTA, IGNT1;
CC IsoId=Q8N0V5-1; Sequence=Displayed;
CC Name=B; Synonyms=IGnTB, IGNT2;
CC IsoId=Q8N0V5-2; Sequence=VSP_058348;
CC Name=C; Synonyms=IGnTC, IGNT3;
CC IsoId=Q8N0V5-3; Sequence=VSP_058347;
CC -!- TISSUE SPECIFICITY: [Isoform B]: Expressed in lens epithelium cells.
CC {ECO:0000269|PubMed:12424189}.
CC -!- TISSUE SPECIFICITY: [Isoform C]: Expressed in reticulocytes.
CC {ECO:0000269|PubMed:12468428}.
CC -!- DEVELOPMENTAL STAGE: [Isoform B]: Expression increases dramatically
CC during development and oncogenesis. {ECO:0000269|PubMed:7579796}.
CC -!- POLYMORPHISM: GCNT2 is involved in determining the blood group I system
CC (Ii) [MIM:110800]. The i (fetal) and I (adult) antigens are determined
CC by linear and branched poly-N-acetyllactosaminoglycans, respectively. A
CC replacement during development of i by I is dependent on the appearance
CC of a beta-1,6-N-acetylglucosaminyltransferase, the I-branching enzyme.
CC The expression of the blood group I antigen in erythrocytes is
CC determined by isoform C of GCNT2. {ECO:0000269|PubMed:12424189}.
CC -!- DISEASE: Cataract 13, with adult i phenotype (CTRCT13) [MIM:116700]: An
CC opacification of the crystalline lens of the eye that frequently
CC results in visual impairment or blindness. Opacities vary in
CC morphology, are often confined to a portion of the lens, and may be
CC static or progressive. In general, the more posteriorly located and
CC dense an opacity, the greater the impact on visual function. CTRCT13 is
CC associated with the rare adult i phenotype, in which adult red blood
CC cells are rich in i antigen and contain low levels of I antigen.
CC {ECO:0000269|PubMed:11739194, ECO:0000269|PubMed:28839118,
CC ECO:0000269|PubMed:29914532}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=N-
CC acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_548";
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DR EMBL; Z19550; CAA79610.1; -; mRNA.
DR EMBL; L19659; AAA81777.1; -; mRNA.
DR EMBL; L41607; AAA99832.1; -; Genomic_DNA.
DR EMBL; L41605; AAA99832.1; JOINED; Genomic_DNA.
DR EMBL; L41606; AAA99832.1; JOINED; Genomic_DNA.
DR EMBL; AF458024; AAM73864.1; -; mRNA.
DR EMBL; AF458025; AAM73865.1; -; mRNA.
DR EMBL; AF458026; AAM73866.1; -; mRNA.
DR EMBL; AB078433; BAC66782.1; -; mRNA.
DR EMBL; AY435145; AAR95646.1; -; mRNA.
DR EMBL; AY435146; AAR95647.1; -; mRNA.
DR EMBL; AY435147; AAR95648.1; -; mRNA.
DR EMBL; BX647576; CAI46081.1; -; mRNA.
DR EMBL; AK090483; BAC03464.1; -; mRNA.
DR EMBL; AK291767; BAF84456.1; -; mRNA.
DR EMBL; AK313426; BAG36218.1; -; mRNA.
DR EMBL; AK313903; BAG36626.1; -; mRNA.
DR EMBL; AL139039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55259.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55260.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55262.1; -; Genomic_DNA.
DR EMBL; BC074802; AAH74802.1; -; mRNA.
DR EMBL; BC074801; AAH74801.1; -; mRNA.
DR EMBL; BC130524; AAI30525.1; -; mRNA.
DR CCDS; CCDS34338.1; -. [Q8N0V5-1]
DR CCDS; CCDS4512.1; -. [Q8N0V5-2]
DR CCDS; CCDS4513.1; -. [Q8N0V5-3]
DR PIR; A46297; A46297.
DR RefSeq; NP_001482.1; NM_001491.2. [Q8N0V5-2]
DR RefSeq; NP_663624.1; NM_145649.4. [Q8N0V5-1]
DR RefSeq; NP_663630.2; NM_145655.3. [Q8N0V5-3]
DR RefSeq; XP_006715115.1; XM_006715052.3. [Q8N0V5-1]
DR AlphaFoldDB; Q8N0V5; -.
DR SMR; Q8N0V5; -.
DR BioGRID; 108921; 50.
DR IntAct; Q8N0V5; 9.
DR STRING; 9606.ENSP00000368917; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GlyGen; Q8N0V5; 1 site.
DR iPTMnet; Q8N0V5; -.
DR PhosphoSitePlus; Q8N0V5; -.
DR BioMuta; GCNT2; -.
DR DMDM; 543887; -.
DR EPD; Q8N0V5; -.
DR jPOST; Q8N0V5; -.
DR MassIVE; Q8N0V5; -.
DR MaxQB; Q8N0V5; -.
DR PeptideAtlas; Q8N0V5; -.
DR PRIDE; Q8N0V5; -.
DR ProteomicsDB; 58445; -.
DR ProteomicsDB; 71468; -. [Q8N0V5-1]
DR ProteomicsDB; 73347; -.
DR Antibodypedia; 10005; 235 antibodies from 25 providers.
DR DNASU; 2651; -.
DR Ensembl; ENST00000265012.5; ENSP00000265012.4; ENSG00000111846.20. [Q8N0V5-3]
DR Ensembl; ENST00000316170.9; ENSP00000314844.3; ENSG00000111846.20. [Q8N0V5-2]
DR Ensembl; ENST00000379597.7; ENSP00000368917.3; ENSG00000111846.20. [Q8N0V5-1]
DR Ensembl; ENST00000495262.7; ENSP00000419411.2; ENSG00000111846.20. [Q8N0V5-1]
DR Ensembl; ENST00000642698.1; ENSP00000495911.1; ENSG00000285222.3. [Q8N0V5-1]
DR Ensembl; ENST00000643503.1; ENSP00000493918.1; ENSG00000285222.3. [Q8N0V5-2]
DR Ensembl; ENST00000644083.3; ENSP00000494927.1; ENSG00000285222.3. [Q8N0V5-1]
DR GeneID; 2651; -.
DR KEGG; hsa:2651; -.
DR MANE-Select; ENST00000495262.7; ENSP00000419411.2; NM_145649.5; NP_663624.1.
DR UCSC; uc010joo.4; human. [Q8N0V5-1]
DR CTD; 2651; -.
DR DisGeNET; 2651; -.
DR GeneCards; GCNT2; -.
DR HGNC; HGNC:4204; GCNT2.
DR HPA; ENSG00000111846; Tissue enhanced (prostate).
DR MalaCards; GCNT2; -.
DR MIM; 110800; phenotype.
DR MIM; 116700; phenotype.
DR MIM; 600429; gene.
DR neXtProt; NX_Q8N0V5; -.
DR OpenTargets; ENSG00000111846; -.
DR Orphanet; 98994; Total early-onset cataract.
DR PharmGKB; PA169; -.
DR VEuPathDB; HostDB:ENSG00000111846; -.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000156849; -.
DR InParanoid; Q8N0V5; -.
DR OMA; RADLHCM; -.
DR OrthoDB; 791893at2759; -.
DR PhylomeDB; Q8N0V5; -.
DR TreeFam; TF315534; -.
DR BioCyc; MetaCyc:HS03475-MON; -.
DR BRENDA; 2.4.1.150; 2681.
DR PathwayCommons; Q8N0V5; -.
DR SignaLink; Q8N0V5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 2651; 17 hits in 1070 CRISPR screens.
DR ChiTaRS; GCNT2; human.
DR GeneWiki; GCNT2; -.
DR GenomeRNAi; 2651; -.
DR Pharos; Q8N0V5; Tbio.
DR PRO; PR:Q8N0V5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8N0V5; protein.
DR Bgee; ENSG00000111846; Expressed in heart left ventricle and 107 other tissues.
DR ExpressionAtlas; Q8N0V5; baseline and differential.
DR Genevisible; Q8N0V5; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0008109; F:N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity; IMP:UniProtKB.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:ProtInc.
DR GO; GO:0036438; P:maintenance of lens transparency; IMP:UniProtKB.
DR GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:CAFA.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IMP:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR InterPro; IPR003406; Glyco_trans_14.
DR Pfam; PF02485; Branch; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cataract; Disease variant; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..402
FT /note="N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-
FT transferase"
FT /id="PRO_0000395119"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..400
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..308
FT /note="MMGSWKHCLFSASLISALIFVFVYNTELWENKRFLRAALSNASLLAEACHQI
FT FEGKVFYPTENALKTTLDEATCYEYMVRSHYVTETLSEEEAGFPLAYTVTIHKDFGTFE
FT RLFRAIYMPQNVYCVHLDQKATDAFKGAVKQLLSCFPNAFLASKKESVVYGGISRLQAD
FT LNCLEDLVASEVPWKYVINTCGQDFPLKTNREIVQYLKGFKGKNITPGVLPPDHAVGRT
FT KYVHQELLNHKNSYVIKTTKLKTPPPHDMVIYFGTAYVALTRDFANFVLQDQLALDLLS
FT WSKDTYSPDEHFWVTLNRIP -> MNFWRYCFFAFTLLSVVIFVRFYSSQLSPPKSYEK
FT LNSSSERYFRKTACNHALEKMPVFLWENILPSPLRSVPCKDYLTQNHYITSPLSEEEAA
FT FPLAYVMVIHKDFDTFERLFRAIYMPQNVYCVHVDEKAPAEYKESVRQLLSCFQNAFIA
FT SKTESVVYAGISRLQADLNCLKDLVASEVPWKYVINTCGQDFPLKTNREIVQHLKGFKG
FT KNITPGVLPPDHAIKRTKYVHQEHTDKGGFFVKNTNILKTSPPHQLTIYFGTAYVALTR
FT DFVDFVLRDQRAIDLLQWSKDTYSPDEHFWVTLNRVS (in isoform C)"
FT /id="VSP_058347"
FT VAR_SEQ 1..294
FT /note="MMGSWKHCLFSASLISALIFVFVYNTELWENKRFLRAALSNASLLAEACHQI
FT FEGKVFYPTENALKTTLDEATCYEYMVRSHYVTETLSEEEAGFPLAYTVTIHKDFGTFE
FT RLFRAIYMPQNVYCVHLDQKATDAFKGAVKQLLSCFPNAFLASKKESVVYGGISRLQAD
FT LNCLEDLVASEVPWKYVINTCGQDFPLKTNREIVQYLKGFKGKNITPGVLPPDHAVGRT
FT KYVHQELLNHKNSYVIKTTKLKTPPPHDMVIYFGTAYVALTRDFANFVLQDQLALDLLS
FT WSKDTY -> MPLSMRYLFIISVSSVIIFIVFSVFNFGGDPSFQRLNISDPLRLTQVCT
FT SFINGKTRFLWKNKLMIHEKSSCKEYLTQSHYITAPLSKEEADFPLAYIMVIHHHFDTF
FT ARLFRAIYMPQNIYCVHVDEKATTEFKDAVEQLLSCFPNAFLASKMEPVVYGGISRLQA
FT DLNCIRDLSAFEVSWKYVINTCGQDFPLKTNKEIVQYLKGFKGKNITPGVLPPAHAIGR
FT TKYVHQEHLGKELSYVIRTTALKPPPPHNLTIYFGSAYVALSREFANFVLHDPRAVDLL
FT QWSKDTF (in isoform B)"
FT /id="VSP_058348"
FT VARIANT 169
FT /note="A -> T (defines the adult i phenotype;
FT dbSNP:rs137853339)"
FT /evidence="ECO:0000269|PubMed:12424189"
FT /id="VAR_073827"
FT VARIANT 228
FT /note="R -> Q (defines the adult i phenotype;
FT dbSNP:rs137853340)"
FT /evidence="ECO:0000269|PubMed:12424189"
FT /id="VAR_073828"
FT VARIANT 350
FT /note="G -> E (in CTRCT13; unknown pathological
FT significance; dbSNP:rs56141211)"
FT /evidence="ECO:0000269|PubMed:11739194,
FT ECO:0000269|PubMed:29914532"
FT /id="VAR_073829"
FT VARIANT 364
FT /note="F -> S (in CTRCT13; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28839118"
FT /id="VAR_084818"
FT VARIANT 385
FT /note="R -> H (in CTRCT13; unknown pathological
FT significance; dbSNP:rs55940927)"
FT /evidence="ECO:0000269|PubMed:11739194,
FT ECO:0000269|PubMed:29914532"
FT /id="VAR_073830"
FT CONFLICT 272
FT /note="D -> E (in Ref. 3; AAM73866, 4; BAC66782, 6;
FT CAI46081, 7; BAG36218, 9; EAW55259 and 10; AAI30525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 45873 MW; FCA6AE905D78D7D5 CRC64;
MMGSWKHCLF SASLISALIF VFVYNTELWE NKRFLRAALS NASLLAEACH QIFEGKVFYP
TENALKTTLD EATCYEYMVR SHYVTETLSE EEAGFPLAYT VTIHKDFGTF ERLFRAIYMP
QNVYCVHLDQ KATDAFKGAV KQLLSCFPNA FLASKKESVV YGGISRLQAD LNCLEDLVAS
EVPWKYVINT CGQDFPLKTN REIVQYLKGF KGKNITPGVL PPDHAVGRTK YVHQELLNHK
NSYVIKTTKL KTPPPHDMVI YFGTAYVALT RDFANFVLQD QLALDLLSWS KDTYSPDEHF
WVTLNRIPGV PGSMPNASWT GNLRAIKWSD MEDRHGGCHG HYVHGICIYG NGDLKWLVNS
PSLFANKFEL NTYPLTVECL ELRHRERTLN QSETAIQPSW YF
