B3GL2_HUMAN
ID B3GL2_HUMAN Reviewed; 500 AA.
AC Q8NCR0; Q59GR3; Q5TCI3; Q96AL7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2;
DE Short=Beta-1,3-GalNAc-T2;
DE EC=2.4.1.313 {ECO:0000269|PubMed:23929950};
DE AltName: Full=Beta-1,3-N-acetylgalactosaminyltransferase II;
GN Name=B3GALNT2;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 74-500 (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=14724282; DOI=10.1074/jbc.m310614200;
RA Hiruma T., Togayachi A., Okamura K., Sato T., Kikuchi N., Kwon Y.D.,
RA Nakamura A., Fujimura K., Gotoh M., Tachibana K., Ishizuka Y., Noce T.,
RA Nakanishi H., Narimatsu H.;
RT "A novel human beta1,3-N-acetylgalactosaminyltransferase that synthesizes a
RT unique carbohydrate structure, GalNAcbeta1-3GlcNAc.";
RL J. Biol. Chem. 279:14087-14095(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, VARIANTS MDDGA11 GLU-247; GLY-252; MET-268
RP AND PRO-292, AND CHARACTERIZATION OF VARIANTS MDDGA11 GLU-247; MET-268 AND
RP PRO-292.
RX PubMed=23453667; DOI=10.1016/j.ajhg.2013.01.016;
RG UK10K Consortium;
RA Stevens E., Carss K.J., Cirak S., Foley A.R., Torelli S., Willer T.,
RA Tambunan D.E., Yau S., Brodd L., Sewry C.A., Feng L., Haliloglu G.,
RA Orhan D., Dobyns W.B., Enns G.M., Manning M., Krause A., Salih M.A.,
RA Walsh C.A., Hurles M., Campbell K.P., Manzini M.C., Stemple D., Lin Y.Y.,
RA Muntoni F.;
RT "Mutations in B3GALNT2 cause congenital muscular dystrophy and
RT hypoglycosylation of alpha-dystroglycan.";
RL Am. J. Hum. Genet. 92:354-365(2013).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23929950; DOI=10.1126/science.1239951;
RA Yoshida-Moriguchi T., Willer T., Anderson M.E., Venzke D., Whyte T.,
RA Muntoni F., Lee H., Nelson S.F., Yu L., Campbell K.P.;
RT "SGK196 is a glycosylation-specific O-mannose kinase required for
RT dystroglycan function.";
RL Science 341:896-899(2013).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] SER-203.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a
CC unique carbohydrate structure, GalNAc-beta-1-3GlcNAc, on N- and O-
CC glycans. Has no galactose nor galactosaminyl transferase activity
CC toward any acceptor substrate. Involved in alpha-dystroglycan (DAG1)
CC glycosylation: acts coordinately with GTDC2/POMGnT2 to synthesize a
CC GalNAc-beta3-GlcNAc-beta-terminus at the 4-position of protein O-
CC mannose in the biosynthesis of the phosphorylated O-mannosyl
CC trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-
CC (phosphate-6-)mannose), a carbohydrate structure present in alpha-
CC dystroglycan, which is required for binding laminin G-like domain-
CC containing extracellular proteins with high affinity.
CC {ECO:0000269|PubMed:14724282, ECO:0000269|PubMed:23453667,
CC ECO:0000269|PubMed:23929950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl)-L-
CC threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[beta-
CC D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-alpha-D-Man]-L-Thr-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:37667, Rhea:RHEA-COMP:13308, Rhea:RHEA-
CC COMP:13618, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:136709, ChEBI:CHEBI:137540; EC=2.4.1.313;
CC Evidence={ECO:0000269|PubMed:23929950};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 uM for UDP-GalNAc {ECO:0000269|PubMed:14724282};
CC KM=11 mM for GlcNAc-beta-Bn {ECO:0000269|PubMed:14724282};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q8NCR0; Q969X1: TMBIM1; NbExp=3; IntAct=EBI-12934759, EBI-2820569;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:23453667}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NCR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NCR0-2; Sequence=VSP_020250, VSP_020251, VSP_020252;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, but at highest
CC levels in testis, adipose tissue, skeletal muscle and ovary.
CC {ECO:0000269|PubMed:14724282}.
CC -!- PTM: N-glycosylated. {ECO:0000305|PubMed:14724282}.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain
CC and eye anomalies A11 (MDDGA11) [MIM:615181]: An autosomal recessive
CC disorder characterized by congenital muscular dystrophy associated with
CC cobblestone lissencephaly and other brain anomalies, eye malformations,
CC profound intellectual disability, and death usually in the first years
CC of life. Included diseases are the more severe Walker-Warburg syndrome
CC and the slightly less severe muscle-eye-brain disease.
CC {ECO:0000269|PubMed:23453667}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16974.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL135928; CAI21727.1; -; Genomic_DNA.
DR EMBL; AL135928; CAI21728.1; -; Genomic_DNA.
DR EMBL; BC016974; AAH16974.1; ALT_INIT; mRNA.
DR EMBL; BC029564; AAH29564.1; -; mRNA.
DR EMBL; AB209046; BAD92283.1; -; mRNA.
DR CCDS; CCDS1606.1; -. [Q8NCR0-1]
DR CCDS; CCDS60453.1; -. [Q8NCR0-2]
DR RefSeq; NP_001264084.1; NM_001277155.2. [Q8NCR0-2]
DR RefSeq; NP_689703.1; NM_152490.4. [Q8NCR0-1]
DR AlphaFoldDB; Q8NCR0; -.
DR SMR; Q8NCR0; -.
DR BioGRID; 127169; 61.
DR IntAct; Q8NCR0; 9.
DR STRING; 9606.ENSP00000355559; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q8NCR0; 2 sites.
DR iPTMnet; Q8NCR0; -.
DR PhosphoSitePlus; Q8NCR0; -.
DR BioMuta; B3GALNT2; -.
DR DMDM; 74751196; -.
DR EPD; Q8NCR0; -.
DR jPOST; Q8NCR0; -.
DR MassIVE; Q8NCR0; -.
DR MaxQB; Q8NCR0; -.
DR PaxDb; Q8NCR0; -.
DR PeptideAtlas; Q8NCR0; -.
DR PRIDE; Q8NCR0; -.
DR ProteomicsDB; 72925; -. [Q8NCR0-1]
DR ProteomicsDB; 72926; -. [Q8NCR0-2]
DR TopDownProteomics; Q8NCR0-2; -. [Q8NCR0-2]
DR Antibodypedia; 1593; 119 antibodies from 22 providers.
DR DNASU; 148789; -.
DR Ensembl; ENST00000313984.3; ENSP00000315678.3; ENSG00000162885.14. [Q8NCR0-2]
DR Ensembl; ENST00000366600.8; ENSP00000355559.3; ENSG00000162885.14. [Q8NCR0-1]
DR Ensembl; ENST00000635244.1; ENSP00000489219.1; ENSG00000282880.4. [Q8NCR0-2]
DR Ensembl; ENST00000635453.2; ENSP00000489342.1; ENSG00000282880.4. [Q8NCR0-1]
DR GeneID; 148789; -.
DR KEGG; hsa:148789; -.
DR MANE-Select; ENST00000366600.8; ENSP00000355559.3; NM_152490.5; NP_689703.1.
DR UCSC; uc001hxc.4; human. [Q8NCR0-1]
DR CTD; 148789; -.
DR DisGeNET; 148789; -.
DR GeneCards; B3GALNT2; -.
DR HGNC; HGNC:28596; B3GALNT2.
DR HPA; ENSG00000162885; Low tissue specificity.
DR MalaCards; B3GALNT2; -.
DR MIM; 610194; gene.
DR MIM; 615181; phenotype.
DR neXtProt; NX_Q8NCR0; -.
DR OpenTargets; ENSG00000162885; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR Orphanet; 588; Muscle-eye-brain disease.
DR Orphanet; 899; Walker-Warburg syndrome.
DR PharmGKB; PA142672567; -.
DR VEuPathDB; HostDB:ENSG00000162885; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000156562; -.
DR HOGENOM; CLU_591287_0_0_1; -.
DR InParanoid; Q8NCR0; -.
DR OrthoDB; 640360at2759; -.
DR PhylomeDB; Q8NCR0; -.
DR TreeFam; TF314311; -.
DR BioCyc; MetaCyc:ENSG00000162885-MON; -.
DR BRENDA; 2.4.1.313; 2681.
DR PathwayCommons; Q8NCR0; -.
DR Reactome; R-HSA-5173105; O-linked glycosylation.
DR SABIO-RK; Q8NCR0; -.
DR SignaLink; Q8NCR0; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 148789; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; B3GALNT2; human.
DR GenomeRNAi; 148789; -.
DR Pharos; Q8NCR0; Tbio.
DR PRO; PR:Q8NCR0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8NCR0; protein.
DR Bgee; ENSG00000162885; Expressed in body of pancreas and 105 other tissues.
DR ExpressionAtlas; Q8NCR0; baseline and differential.
DR Genevisible; Q8NCR0; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IMP:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Congenital muscular dystrophy; Disease variant;
KW Dystroglycanopathy; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Lissencephaly; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..500
FT /note="UDP-GalNAc:beta-1,3-N-
FT acetylgalactosaminyltransferase 2"
FT /id="PRO_0000248362"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..500
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 37
FT /note="A -> AGGVSLLLPRLECNGAVSAHPNLHLPGSRDSPASASQVAGIT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020250"
FT VAR_SEQ 281..285
FT /note="EGDAL -> GKFAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020251"
FT VAR_SEQ 286..500
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020252"
FT VARIANT 203
FT /note="N -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035860"
FT VARIANT 247
FT /note="G -> E (in MDDGA11; affects subcellular
FT localization; dbSNP:rs367543072)"
FT /evidence="ECO:0000269|PubMed:23453667"
FT /id="VAR_069638"
FT VARIANT 252
FT /note="V -> G (in MDDGA11; dbSNP:rs367543073)"
FT /evidence="ECO:0000269|PubMed:23453667"
FT /id="VAR_069639"
FT VARIANT 268
FT /note="V -> M (in MDDGA11; affects subcellular
FT localization; dbSNP:rs367543074)"
FT /evidence="ECO:0000269|PubMed:23453667"
FT /id="VAR_069640"
FT VARIANT 292
FT /note="R -> P (in MDDGA11; does not affect subcellular
FT localization; dbSNP:rs367543076)"
FT /evidence="ECO:0000269|PubMed:23453667"
FT /id="VAR_069641"
SQ SEQUENCE 500 AA; 56704 MW; F346C95857886026 CRC64;
MRNWLVLLCP CVLGAALHLW LRLRSPPPAC ASGAGPADQL ALFPQWKSTH YDVVVGVLSA
RNNHELRNVI RSTWMRHLLQ HPTLSQRVLV KFIIGAHGCE VPVEDREDPY SCKLLNITNP
VLNQEIEAFS LSEDTSSGLP EDRVVSVSFR VLYPIVITSL GVFYDANDVG FQRNITVKLY
QAEQEEALFI ARFSPPSCGV QVNKLWYKPV EQFILPESFE GTIVWESQDL HGLVSRNLHK
VTVNDGGGVL RVITAGEGAL PHEFLEGVEG VAGGFIYTIQ EGDALLHNLH SRPQRLIDHI
RNLHEEDALL KEESSIYDDI VFVDVVDTYR NVPAKLLNFY RWTVETTSFN LLLKTDDDCY
IDLEAVFNRI VQKNLDGPNF WWGNFRLNWA VDRTGKWQEL EYPSPAYPAF ACGSGYVISK
DIVKWLASNS GRLKTYQGED VSMGIWMAAI GPKRYQDSLW LCEKTCETGM LSSPQYSPWE
LTELWKLKER CGDPCRCQAR
