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Q00973 (B4GN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-1,4 N-acetylgalactosaminyltransferase 1

EC=2.4.1.92
Alternative name(s):
(N-acetylneuraminyl)-galactosylglucosylceramide
GM2/GD2 synthase
GalNAc-T
Gene names
Name:B4GALNT1
Synonyms:GALGT, SIAT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of gangliosides GM2, GD2 and GA2.

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + O-(N-acetyl-alpha-neuraminyl)-(2->3)-O-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranosyl-(1<->1)-ceramide = UDP + O-2-(acetylamino)-2-deoxy-beta-D-galactopyranosyl-(1->4)-O-(N-acetyl-alpha-neuraminyl-(2->3))-O-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranosyl-(1<->1)-ceramide.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Homodimer; disulfide-linked. Ref.6

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein.

Involvement in disease

Spastic paraplegia 26, autosomal recessive (SPG26) [MIM:609195]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG26 is a complicated form characterized by onset in the first 2 decades of life of gait abnormalities due to lower limb spasticity and muscle weakness. Some patients have upper limb involvement. Additional features include intellectual disability, peripheral neuropathy, dysarthria, cerebellar signs, extrapyramidal signs, and cortical atrophy. The disorder is slowly progressive.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q00973-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q00973-2)

The sequence of this isoform differs from the canonical sequence as follows:
     74-128: Missing.
Isoform 3 (identifier: Q00973-3)

The sequence of this isoform differs from the canonical sequence as follows:
     238-328: VRFSTEGHEA...RVSGPYVEHY → GARPGWRDGQ...TVGGPRKRLV
     329-533: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 533533Beta-1,4 N-acetylgalactosaminyltransferase 1
PRO_0000059100

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2518Helical; Signal-anchor for type II membrane protein; Potential
Topological domain26 – 533508Lumenal Potential

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Disulfide bond80Interchain (with C-412) Ref.6
Disulfide bond82Interchain (with C-529) Ref.6
Disulfide bond412Interchain (with C-80) Ref.6
Disulfide bond429 ↔ 476 Ref.6
Disulfide bond529Interchain (with C-82) Ref.6

Natural variations

Alternative sequence74 – 12855Missing in isoform 2.
VSP_055039
Alternative sequence238 – 32891VRFST…YVEHY → GARPGWRDGQAGQTEKNQKG WSGQMAEGMGGIWAMARAVQ PHNGCFNWTSRARGRKGAFV HLGLEQARGKPEPWVCLPFR PTVGGPRKRLV in isoform 3.
VSP_055040
Alternative sequence329 – 533205Missing in isoform 3.
VSP_055041
Natural variant351L → V.
Corresponds to variant rs774896 [ dbSNP | Ensembl ].
VAR_012052
Natural variant1721G → R.
Corresponds to variant rs810205 [ dbSNP | Ensembl ].
VAR_012053
Natural variant3001R → C in SPG26. Ref.7
VAR_070235
Natural variant4331D → A in SPG26. Ref.7
VAR_070236
Natural variant5161A → V.
Corresponds to variant rs17454674 [ dbSNP | Ensembl ].
VAR_049237

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 533946E05E2A102B

FASTA53358,882
        10         20         30         40         50         60 
MWLGRRALCA LVLLLACASL GLLYASTRDA PGLRLPLAPW APPQSPRRPE LPDLAPEPRY 

        70         80         90        100        110        120 
AHIPVRIKEQ VVGLLAWNNC SCESSGGGLP LPFQKQVRAI DLTKAFDPAE LRAASATREQ 

       130        140        150        160        170        180 
EFQAFLSRSQ SPADQLLIAP ANSPLQYPLQ GVEVQPLRSI LVPGLSLQAA SGQEVYQVNL 

       190        200        210        220        230        240 
TASLGTWDVA GEVTGVTLTG EGQADLTLVS PGLDQLNRQL QLVTYSSRSY QTNTADTVRF 

       250        260        270        280        290        300 
STEGHEAAFT IRIRHPPNPR LYPPGSLPQG AQYNISALVT IATKTFLRYD RLRALITSIR 

       310        320        330        340        350        360 
RFYPTVTVVI ADDSDKPERV SGPYVEHYLM PFGKGWFAGR NLAVSQVTTK YVLWVDDDFV 

       370        380        390        400        410        420 
FTARTRLERL VDVLERTPLD LVGGAVREIS GFATTYRQLL SVEPGAPGLG NCLRQRRGFH 

       430        440        450        460        470        480 
HELVGFPGCV VTDGVVNFFL ARTDKVREVG FDPRLSRVAH LEFFLDGLGS LRVGSCSDVV 

       490        500        510        520        530 
VDHASKLKLP WTSRDAGAET YARYRYPGSL DESQMAKHRL LFFKHRLQCM TSQ 

« Hide

Isoform 2 [UniParc].

Checksum: 6C41F497A0E2E255
Show »

FASTA47852,860
Isoform 3 [UniParc].

Checksum: 451A27EC0E75259C
Show »

FASTA32835,471

References

« Hide 'large scale' references
[1]"Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase cDNAs that determine the expression of GM2 and GD2 gangliosides."
Nagata Y., Yamashiro S., Yodoi J., Lloyd K.O., Shiku H., Furukawa K.
J. Biol. Chem. 267:12082-12089(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase cDNAs that determine the expression of GM2 and GD2 gangliosides."
Nagata Y., Yamashiro S., Yodoi J., Lloyd K.O., Shiku H., Furukawa K.
J. Biol. Chem. 269:7045-7045(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 412-533.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[6]"Disulfide bonds of GM2 synthase homodimers. Antiparallel orientation of the catalytic domains."
Li J., Yen T.Y., Allende M.L., Joshi R.K., Cai J., Pierce W.M., Jaskiewicz E., Darling D.S., Macher B.A., Young W.W. Jr.
J. Biol. Chem. 275:41476-41486(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[7]"Alteration of ganglioside biosynthesis responsible for complex hereditary spastic paraplegia."
Boukhris A., Schule R., Loureiro J.L., Lourenco C.M., Mundwiller E., Gonzalez M.A., Charles P., Gauthier J., Rekik I., Acosta Lebrigio R.F., Gaussen M., Speziani F., Ferbert A., Feki I., Caballero-Oteyza A., Dionne-Laporte A., Amri M., Noreau A. expand/collapse author list , Forlani S., Cruz V.T., Mochel F., Coutinho P., Dion P., Mhiri C., Schols L., Pouget J., Darios F., Rouleau G.A., Marques W. Jr., Brice A., Durr A., Zuchner S., Stevanin G.
Am. J. Hum. Genet. 93:118-123(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG26 CYS-300 AND ALA-433.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta-1,4 N-acetylgalactosaminyltransferase 1

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83651 mRNA. Translation: AAA35516.1.
AK293432 mRNA. Translation: BAG56937.1.
AC025165 Genomic DNA. No translation available.
BC029828 mRNA. Translation: AAH29828.1.
CCDSCCDS8950.1.
PIRA44128.
A54379.
RefSeqNP_001263397.1. NM_001276468.1.
NP_001469.1. NM_001478.4.
UniGeneHs.159481.

3D structure databases

ProteinModelPortalQ00973.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108856. 2 interactions.
STRING9606.ENSP00000341562.

Protein family/group databases

CAZyGT12. Glycosyltransferase Family 12.

PTM databases

PhosphoSiteQ00973.

Polymorphism databases

DMDM1168736.

Proteomic databases

MaxQBQ00973.
PaxDbQ00973.
PRIDEQ00973.

Protocols and materials databases

DNASU2583.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341156; ENSP00000341562; ENSG00000135454.
ENST00000418555; ENSP00000401601; ENSG00000135454.
ENST00000550764; ENSP00000450303; ENSG00000135454.
ENST00000552350; ENSP00000448500; ENSG00000135454.
GeneID2583.
KEGGhsa:2583.
UCSCuc001spg.2. human.

Organism-specific databases

CTD2583.
GeneCardsGC12M058019.
HGNCHGNC:4117. B4GALNT1.
HPAHPA008968.
HPA015128.
MIM601873. gene.
609195. phenotype.
neXtProtNX_Q00973.
Orphanet101006. Autosomal recessive spastic paraplegia type 26.
PharmGKBPA28532.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40821.
HOGENOMHOG000220853.
HOVERGENHBG004812.
InParanoidQ00973.
KOK00725.
OMAIEHYLMP.
OrthoDBEOG7R2BJS.
PhylomeDBQ00973.
TreeFamTF332297.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ00973.
BgeeQ00973.
CleanExHS_B4GALNT1.
GenevestigatorQ00973.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR011143. GM2_synthase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
PIRSFPIRSF000474. GM2_GD2_synthase. 1 hit.
SUPFAMSSF53448. SSF53448. 1 hit.
ProtoNetSearch...

Other

GeneWikiB4GALNT1.
GenomeRNAi2583.
NextBio10219.
PROQ00973.
SOURCESearch...

Entry information

Entry nameB4GN1_HUMAN
AccessionPrimary (citable) accession number: Q00973
Secondary accession number(s): B4DE26, Q8N636
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM