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 27-MAR-2024, entry version 146. 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; CC Note=N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_548"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSP00000419411; -. DR CAZy; GT14; Glycosyltransferase Family 14. DR GlyCosmos; Q8N0V5; 1 site, No reported glycans. 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 PaxDb; 9606-ENSP00000368917; -. DR PeptideAtlas; Q8N0V5; -. DR ProteomicsDB; 58445; -. DR ProteomicsDB; 71468; -. [Q8N0V5-1] DR ProteomicsDB; 73347; -. DR Antibodypedia; 10005; 268 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; ENST00000643503.2; ENSP00000493918.1; ENSG00000285222.3. [Q8N0V5-2] DR Ensembl; ENST00000644083.4; 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 AGR; HGNC:4204; -. 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; KTPVFLW; -. DR OrthoDB; 5403607at2759; -. DR PhylomeDB; Q8N0V5; -. DR TreeFam; TF315534; -. DR BioCyc; MetaCyc:HS03475-MONOMER; -. DR BRENDA; 2.4.1.150; 2681. DR PathwayCommons; Q8N0V5; -. DR SignaLink; Q8N0V5; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 2651; 18 hits in 1150 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 primordial germ cell in gonad and 108 other cell types or tissues. DR ExpressionAtlas; Q8N0V5; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. 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 phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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 PANTHER; PTHR19297; GLYCOSYLTRANSFERASE 14 FAMILY MEMBER; 1. DR PANTHER; PTHR19297:SF188; N-ACETYLLACTOSAMINIDE BETA-1,6-N-ACETYLGLUCOSAMINYL-TRANSFERASE; 1. DR Pfam; PF02485; Branch; 1. DR Genevisible; Q8N0V5; HS. 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; uncertain significance; FT 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; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28839118" FT /id="VAR_084818" FT VARIANT 385 FT /note="R -> H (in CTRCT13; uncertain significance; FT 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 //