B4GN1_HUMAN
ID B4GN1_HUMAN Reviewed; 533 AA.
AC Q00973; B4DE26; Q8N636;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Beta-1,4 N-acetylgalactosaminyltransferase 1 {ECO:0000305};
DE EC=2.4.1.92 {ECO:0000269|PubMed:1601877, ECO:0000269|PubMed:7487055, ECO:0000269|PubMed:7890749};
DE AltName: Full=(N-acetylneuraminyl)-galactosylglucosylceramide;
DE AltName: Full=GM2/GD2 synthase;
DE AltName: Full=GalNAc-T;
GN Name=B4GALNT1 {ECO:0000312|HGNC:HGNC:4117}; Synonyms=GALGT, SIAT2;
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 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=1601877; DOI=10.1016/s0021-9258(19)49809-8;
RA Nagata Y., Yamashiro S., Yodoi J., Lloyd K.O., Shiku H., Furukawa K.;
RT "Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase cDNAs
RT that determine the expression of GM2 and GD2 gangliosides.";
RL J. Biol. Chem. 267:12082-12089(1992).
RN [2]
RP SEQUENCE REVISION TO 412-533.
RX PubMed=8120069; DOI=10.1016/s0021-9258(17)37480-x;
RA Nagata Y., Yamashiro S., Yodoi J., Lloyd K.O., Shiku H., Furukawa K.;
RT "Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase cDNAs
RT that determine the expression of GM2 and GD2 gangliosides.";
RL J. Biol. Chem. 269:7045-7045(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7487055; DOI=10.1006/abbi.1995.0003;
RA Ruan S., Raj B.K., Furukawa K., Lloyd K.O.;
RT "Analysis of melanoma cells stably transfected with beta 1,4GalNAc
RT transferase (GM2/GD2 synthase) cDNA: relative glycosyltransferase levels
RT play a dominant role in determining ganglioside expression.";
RL Arch. Biochem. Biophys. 323:11-18(1995).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7890749; DOI=10.1074/jbc.270.11.6149;
RA Yamashiro S., Haraguchi M., Furukawa K., Takamiya K., Yamamoto A.,
RA Nagata Y., Lloyd K.O., Shiku H., Furukawa K.;
RT "Substrate specificity of beta 1,4-N-acetylgalactosaminyltransferase in
RT vitro and in cDNA-transfected cells. GM2/GD2 synthase efficiently generates
RT asialo-GM2 in certain cells.";
RL J. Biol. Chem. 270:6149-6155(1995).
RN [8]
RP DISULFIDE BONDS.
RX PubMed=11018043; DOI=10.1074/jbc.m007480200;
RA Li J., Yen T.Y., Allende M.L., Joshi R.K., Cai J., Pierce W.M.,
RA Jaskiewicz E., Darling D.S., Macher B.A., Young W.W. Jr.;
RT "Disulfide bonds of GM2 synthase homodimers. Antiparallel orientation of
RT the catalytic domains.";
RL J. Biol. Chem. 275:41476-41486(2000).
RN [9]
RP VARIANTS SPG26 CYS-300 AND ALA-433.
RX PubMed=23746551; DOI=10.1016/j.ajhg.2013.05.006;
RA Boukhris A., Schule R., Loureiro J.L., Lourenco C.M., Mundwiller E.,
RA Gonzalez M.A., Charles P., Gauthier J., Rekik I., Acosta Lebrigio R.F.,
RA Gaussen M., Speziani F., Ferbert A., Feki I., Caballero-Oteyza A.,
RA Dionne-Laporte A., Amri M., Noreau A., Forlani S., Cruz V.T., Mochel F.,
RA Coutinho P., Dion P., Mhiri C., Schols L., Pouget J., Darios F.,
RA Rouleau G.A., Marques W. Jr., Brice A., Durr A., Zuchner S., Stevanin G.;
RT "Alteration of ganglioside biosynthesis responsible for complex hereditary
RT spastic paraplegia.";
RL Am. J. Hum. Genet. 93:118-123(2013).
CC -!- FUNCTION: Involved in the biosynthesis of gangliosides GM2, GD2, GT2
CC and GA2 from GM3, GD3, GT3 and GA3, respectively.
CC {ECO:0000269|PubMed:1601877, ECO:0000269|PubMed:7487055,
CC ECO:0000269|PubMed:7890749}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC galactosamine = ganglioside GM2 (d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:12588, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:60065, ChEBI:CHEBI:67138, ChEBI:CHEBI:71502; EC=2.4.1.92;
CC Evidence={ECO:0000269|PubMed:1601877, ECO:0000269|PubMed:7890749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12589;
CC Evidence={ECO:0000269|PubMed:1601877, ECO:0000269|PubMed:7890749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM3 + UDP-N-acetyl-alpha-D-galactosamine =
CC ganglioside GM2 + H(+) + UDP; Xref=Rhea:RHEA:43268,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:79210, ChEBI:CHEBI:79218;
CC Evidence={ECO:0000269|PubMed:7487055, ECO:0000269|PubMed:7890749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43269;
CC Evidence={ECO:0000269|PubMed:7487055, ECO:0000269|PubMed:7890749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD3 + UDP-N-acetyl-alpha-D-galactosamine =
CC ganglioside GD2 + H(+) + UDP; Xref=Rhea:RHEA:43272,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:79214, ChEBI:CHEBI:79220;
CC Evidence={ECO:0000269|PubMed:7487055, ECO:0000269|PubMed:7890749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43273;
CC Evidence={ECO:0000269|PubMed:7487055, ECO:0000269|PubMed:7890749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC galactosamine = ganglioside GD2 (d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:41816, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:78436, ChEBI:CHEBI:78542;
CC Evidence={ECO:0000269|PubMed:7890749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41817;
CC Evidence={ECO:0000269|PubMed:7890749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-N-
CC acetyl-alpha-D-galactosamine = ganglioside GA2 (d18:1(4E)) + H(+) +
CC UDP; Xref=Rhea:RHEA:47564, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950,
CC ChEBI:CHEBI:27731, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138;
CC Evidence={ECO:0000305|PubMed:7890749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47565;
CC Evidence={ECO:0000305|PubMed:7890749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD1a + UDP-N-acetyl-alpha-D-galactosamine =
CC ganglioside GalNAc-GD1a + H(+) + UDP; Xref=Rhea:RHEA:43276,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:82637, ChEBI:CHEBI:82945;
CC Evidence={ECO:0000250|UniProtKB:Q10468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43277;
CC Evidence={ECO:0000250|UniProtKB:Q10468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GT3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC galactosamine = ganglioside GT2 (d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:47580, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:78438, ChEBI:CHEBI:87788;
CC Evidence={ECO:0000250|UniProtKB:Q10468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47581;
CC Evidence={ECO:0000250|UniProtKB:Q10468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide +
CC UDP-N-acetyl-alpha-D-galactosamine = H(+) + N-acetyl-beta-D-
CC galactosaminyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-ceramide + UDP; Xref=Rhea:RHEA:62516, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:79208,
CC ChEBI:CHEBI:90085; Evidence={ECO:0000269|PubMed:7890749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62517;
CC Evidence={ECO:0000269|PubMed:7890749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-N-glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-
CC N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
CC glucosyl-(1<->1')-ceramide + UDP-N-acetyl-alpha-D-galactosamine =
CC H(+) + N-acetyl-beta-D-galactosaminyl-(1->4)-[alpha-N-
CC glycoloylneuraminosyl-(2->3)]-beta-D-galactosyl-(1->4)-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-ceramide + UDP; Xref=Rhea:RHEA:43300, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:82950,
CC ChEBI:CHEBI:82951; Evidence={ECO:0000250|UniProtKB:Q10468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43301;
CC Evidence={ECO:0000250|UniProtKB:Q10468};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=500 uM for GM3 {ECO:0000269|PubMed:7890749};
CC KM=40 uM for lactosylceramide {ECO:0000269|PubMed:7890749};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:1601877,
CC ECO:0000269|PubMed:7487055, ECO:0000269|PubMed:7890749}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:11018043}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q10468}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q00973-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q00973-2; Sequence=VSP_055039;
CC Name=3;
CC IsoId=Q00973-3; Sequence=VSP_055040, VSP_055041;
CC -!- DISEASE: Spastic paraplegia 26, autosomal recessive (SPG26)
CC [MIM:609195]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body. SPG26 is a complicated
CC form characterized by onset in the first 2 decades of life of gait
CC abnormalities due to lower limb spasticity and muscle weakness. Some
CC patients have upper limb involvement. Additional features include
CC intellectual disability, peripheral neuropathy, dysarthria, cerebellar
CC signs, extrapyramidal signs, and cortical atrophy. The disorder is
CC slowly progressive. {ECO:0000269|PubMed:23746551}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,4
CC N-acetylgalactosaminyltransferase 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_480";
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DR EMBL; M83651; AAA35516.1; -; mRNA.
DR EMBL; AK293432; BAG56937.1; -; mRNA.
DR EMBL; AC025165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029828; AAH29828.1; -; mRNA.
DR CCDS; CCDS61170.1; -. [Q00973-2]
DR CCDS; CCDS61171.1; -. [Q00973-3]
DR CCDS; CCDS8950.1; -. [Q00973-1]
DR PIR; A44128; A44128.
DR PIR; A54379; A54379.
DR RefSeq; NP_001263397.1; NM_001276468.1. [Q00973-2]
DR RefSeq; NP_001263398.1; NM_001276469.1. [Q00973-3]
DR RefSeq; NP_001469.1; NM_001478.4. [Q00973-1]
DR RefSeq; XP_016874631.1; XM_017019142.1. [Q00973-1]
DR AlphaFoldDB; Q00973; -.
DR BioGRID; 108856; 29.
DR IntAct; Q00973; 5.
DR STRING; 9606.ENSP00000341562; -.
DR SwissLipids; SLP:000000771; -.
DR SwissLipids; SLP:000001406; -.
DR CAZy; GT12; Glycosyltransferase Family 12.
DR GlyGen; Q00973; 3 sites.
DR iPTMnet; Q00973; -.
DR PhosphoSitePlus; Q00973; -.
DR SwissPalm; Q00973; -.
DR BioMuta; B4GALNT1; -.
DR DMDM; 1168736; -.
DR EPD; Q00973; -.
DR jPOST; Q00973; -.
DR MassIVE; Q00973; -.
DR MaxQB; Q00973; -.
DR PaxDb; Q00973; -.
DR PeptideAtlas; Q00973; -.
DR PRIDE; Q00973; -.
DR ProteomicsDB; 3917; -.
DR ProteomicsDB; 57885; -. [Q00973-1]
DR ProteomicsDB; 72129; -.
DR Antibodypedia; 2458; 258 antibodies from 30 providers.
DR DNASU; 2583; -.
DR Ensembl; ENST00000341156.9; ENSP00000341562.4; ENSG00000135454.14. [Q00973-1]
DR Ensembl; ENST00000418555.6; ENSP00000401601.2; ENSG00000135454.14. [Q00973-2]
DR Ensembl; ENST00000550764.5; ENSP00000450303.1; ENSG00000135454.14. [Q00973-3]
DR Ensembl; ENST00000552350.5; ENSP00000448500.1; ENSG00000135454.14. [Q00973-3]
DR GeneID; 2583; -.
DR KEGG; hsa:2583; -.
DR MANE-Select; ENST00000341156.9; ENSP00000341562.4; NM_001478.5; NP_001469.1.
DR UCSC; uc001spg.3; human. [Q00973-1]
DR CTD; 2583; -.
DR DisGeNET; 2583; -.
DR GeneCards; B4GALNT1; -.
DR HGNC; HGNC:4117; B4GALNT1.
DR HPA; ENSG00000135454; Tissue enriched (brain).
DR MalaCards; B4GALNT1; -.
DR MIM; 601873; gene.
DR MIM; 609195; phenotype.
DR neXtProt; NX_Q00973; -.
DR OpenTargets; ENSG00000135454; -.
DR Orphanet; 101006; Autosomal recessive spastic paraplegia type 26.
DR PharmGKB; PA28532; -.
DR VEuPathDB; HostDB:ENSG00000135454; -.
DR eggNOG; ENOG502QTK7; Eukaryota.
DR GeneTree; ENSGT00390000006679; -.
DR HOGENOM; CLU_036051_0_0_1; -.
DR InParanoid; Q00973; -.
DR OMA; RRFYPTI; -.
DR OrthoDB; 363090at2759; -.
DR PhylomeDB; Q00973; -.
DR TreeFam; TF332297; -.
DR BioCyc; MetaCyc:HS06011-MON; -.
DR BRENDA; 2.4.1.92; 2681.
DR PathwayCommons; Q00973; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR SignaLink; Q00973; -.
DR BioGRID-ORCS; 2583; 17 hits in 1076 CRISPR screens.
DR GeneWiki; B4GALNT1; -.
DR GenomeRNAi; 2583; -.
DR Pharos; Q00973; Tbio.
DR PRO; PR:Q00973; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q00973; protein.
DR Bgee; ENSG00000135454; Expressed in right hemisphere of cerebellum and 109 other tissues.
DR ExpressionAtlas; Q00973; baseline and differential.
DR Genevisible; Q00973; HS.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0030173; C:integral component of Golgi membrane; IEA:InterPro.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0003947; F:(N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:ProtInc.
DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR GO; GO:0019915; P:lipid storage; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR011143; GM2_synthase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR PIRSF; PIRSF000474; GM2_GD2_synthase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Hereditary spastic paraplegia;
KW Lipid metabolism; Membrane; Neurodegeneration; Reference proteome;
KW Signal-anchor; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..533
FT /note="Beta-1,4 N-acetylgalactosaminyltransferase 1"
FT /id="PRO_0000059100"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..533
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80
FT /note="Interchain (with C-412)"
FT /evidence="ECO:0000269|PubMed:11018043"
FT DISULFID 82
FT /note="Interchain (with C-529)"
FT /evidence="ECO:0000269|PubMed:11018043"
FT DISULFID 412
FT /note="Interchain (with C-80)"
FT /evidence="ECO:0000269|PubMed:11018043"
FT DISULFID 429..476
FT /evidence="ECO:0000269|PubMed:11018043"
FT DISULFID 529
FT /note="Interchain (with C-82)"
FT /evidence="ECO:0000269|PubMed:11018043"
FT VAR_SEQ 74..128
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055039"
FT VAR_SEQ 238..328
FT /note="VRFSTEGHEAAFTIRIRHPPNPRLYPPGSLPQGAQYNISALVTIATKTFLRY
FT DRLRALITSIRRFYPTVTVVIADDSDKPERVSGPYVEHY -> GARPGWRDGQAGQTEK
FT NQKGWSGQMAEGMGGIWAMARAVQPHNGCFNWTSRARGRKGAFVHLGLEQARGKPEPWV
FT CLPFRPTVGGPRKRLV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055040"
FT VAR_SEQ 329..533
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055041"
FT VARIANT 35
FT /note="L -> V (in dbSNP:rs774896)"
FT /id="VAR_012052"
FT VARIANT 172
FT /note="G -> R (in dbSNP:rs810205)"
FT /id="VAR_012053"
FT VARIANT 300
FT /note="R -> C (in SPG26; dbSNP:rs756710480)"
FT /evidence="ECO:0000269|PubMed:23746551"
FT /id="VAR_070235"
FT VARIANT 433
FT /note="D -> A (in SPG26; dbSNP:rs879255242)"
FT /evidence="ECO:0000269|PubMed:23746551"
FT /id="VAR_070236"
FT VARIANT 516
FT /note="A -> V (in dbSNP:rs17454674)"
FT /id="VAR_049237"
SQ SEQUENCE 533 AA; 58882 MW; 533946E05E2A102B CRC64;
MWLGRRALCA LVLLLACASL GLLYASTRDA PGLRLPLAPW APPQSPRRPE LPDLAPEPRY
AHIPVRIKEQ VVGLLAWNNC SCESSGGGLP LPFQKQVRAI DLTKAFDPAE LRAASATREQ
EFQAFLSRSQ SPADQLLIAP ANSPLQYPLQ GVEVQPLRSI LVPGLSLQAA SGQEVYQVNL
TASLGTWDVA GEVTGVTLTG EGQADLTLVS PGLDQLNRQL QLVTYSSRSY QTNTADTVRF
STEGHEAAFT IRIRHPPNPR LYPPGSLPQG AQYNISALVT IATKTFLRYD RLRALITSIR
RFYPTVTVVI ADDSDKPERV SGPYVEHYLM PFGKGWFAGR NLAVSQVTTK YVLWVDDDFV
FTARTRLERL VDVLERTPLD LVGGAVREIS GFATTYRQLL SVEPGAPGLG NCLRQRRGFH
HELVGFPGCV VTDGVVNFFL ARTDKVREVG FDPRLSRVAH LEFFLDGLGS LRVGSCSDVV
VDHASKLKLP WTSRDAGAET YARYRYPGSL DESQMAKHRL LFFKHRLQCM TSQ
