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 27-MAR-2024, entry version 200. 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=a ganglioside GM3 (d18:1(4E)) + UDP-N-acetyl-alpha-D- CC galactosamine = a 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=a ganglioside GM3 + UDP-N-acetyl-alpha-D-galactosamine = a 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=a ganglioside GD3 + UDP-N-acetyl-alpha-D-galactosamine = a 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=a ganglioside GD3 (d18:1(4E)) + UDP-N-acetyl-alpha-D- CC galactosamine = a 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 = a 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=a ganglioside GD1a + UDP-N-acetyl-alpha-D-galactosamine = a 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=a ganglioside GT3 (d18:1(4E)) + UDP-N-acetyl-alpha-D- CC galactosamine = a 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=a beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + CC UDP-N-acetyl-alpha-D-galactosamine = a ganglioside GA2 + H(+) + UDP; CC Xref=Rhea:RHEA:62516, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:67138, ChEBI:CHEBI:79208, ChEBI:CHEBI:90085; CC 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=a neolactoside IV(3)-alpha-NeuGc-nLc4Cer + UDP-N-acetyl-alpha- CC D-galactosamine = a neolactoside IV(4)-beta-GalNAc-IV(3)-alpha-NeuGc- CC nLc4Cer + H(+) + 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"; 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; 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. DR AlphaFoldDB; Q00973; -. DR BioGRID; 108856; 30. DR IntAct; Q00973; 5. DR STRING; 9606.ENSP00000341562; -. DR SwissLipids; SLP:000000771; -. DR SwissLipids; SLP:000001406; -. DR CAZy; GT12; Glycosyltransferase Family 12. DR GlyCosmos; Q00973; 3 sites, No reported glycans. 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; 9606-ENSP00000341562; -. DR PeptideAtlas; Q00973; -. DR ProteomicsDB; 3917; -. DR ProteomicsDB; 57885; -. [Q00973-1] DR ProteomicsDB; 72129; -. DR Pumba; Q00973; -. DR Antibodypedia; 2458; 286 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 AGR; HGNC:4117; -. 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; REYQAFQ; -. DR OrthoDB; 3831416at2759; -. DR PhylomeDB; Q00973; -. DR TreeFam; TF332297; -. DR BioCyc; MetaCyc:HS06011-MONOMER; -. DR BRENDA; 2.4.1.92; 2681. DR PathwayCommons; Q00973; -. DR Reactome; R-HSA-9840309; Glycosphingolipid biosynthesis. DR SignaLink; Q00973; -. DR BioGRID-ORCS; 2583; 30 hits in 1154 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 110 other cell types or tissues. DR ExpressionAtlas; Q00973; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB. 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:0008340; P:determination of adult lifespan; IEA:Ensembl. DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:UniProtKB. DR GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:ProtInc. DR GO; GO:0060173; P:limb development; IEA:Ensembl. DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro. DR GO; GO:0019915; P:lipid storage; IEA:Ensembl. DR GO; GO:0061744; P:motor behavior; IEA:Ensembl. DR GO; GO:0021675; P:nerve development; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0007033; P:vacuole organization; IEA:Ensembl. DR CDD; cd00761; Glyco_tranf_GTA_type; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR011143; GM2_synthase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR15046:SF1; BETA-1,4 N-ACETYLGALACTOSAMINYLTRANSFERASE 1; 1. DR PANTHER; PTHR15046; GLYCO_TRANS_2-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00535; Glycos_transf_2; 1. DR PIRSF; PIRSF000474; GM2_GD2_synthase; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR Genevisible; Q00973; HS. 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 //