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Reviewed, UniProtKB/Swiss-Prot Q5T0B8 (A3LT2_HUMAN)

Last modified September 2, 2008. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha 1,3-galactosyltransferase 2
      Short name=A3galt2
    EC=2.4.1.87
Alternative name(s):
    Isoglobotriaosylceramide synthase
    iGb3 synthase
      Short name=iGb3S
Gene names
Name: A3GALT2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Transfer of galactose from UDP-galactose to an acceptor molecule (R). Synthesizes the galactose-alpha(1,3)-galactose group, which is the most common carbohydrate containing terminal alpha-galactose. Preferentially glycosylates lipids.

Catalytic activity

UDP-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatusPotential.

Domain

The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis.

Sequence similarities

Belongs to the glycosyltransferase 6 family.

Ontologies

Keywords

   Cellular componentGolgi apparatus
   DomainSignal
   LigandManganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 340307Alpha 1,3-galactosyltransferase 2

Sites

Metal binding1991Manganese By similarity
Metal binding2011Manganese By similarity

Amino acid modifications

Glycosylation581N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5T0B8-1 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 129B673AC0DCE037

FASTA34038,754
        10         20         30         40         50         60 
MALKEGLRAW KRIFWRQILL TLGLLGLFLY GLPKFRHLEA LIPMGVCPSA TMSQLRDNFT 

        70         80         90        100        110        120 
GALRPWARPE VLTCTPWGAP IIWDGSFDPD VAKQEARQQN LTIGLTIFAV GRYLEKYLER 

       130        140        150        160        170        180 
FLETAEQHFM AGQSVMYYVF TELPGAVPRV ALGPGRRLPV ERVARERRWQ DVSMARMRTL 

       190        200        210        220        230        240 
HAALGGLPGR EAHFMFCMDV DQHFSGTFGP EALAESVAQL HSWHYHWPSW LLPFERDAHS 

       250        260        270        280        290        300 
AAAMAWGQGD FYNHAAVFGG SVAALRGLTA HCAGGLDWDR ARGLEARWHD ESHLNKFFWL 

       310        320        330        340 
HKPAKVLSPE FCWSPDIGPR AEIRRPRLLW APKGYRLLRN 

« Hide

References

[1]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AL513327 Genomic DNA. Translation: CAI13954.1. Different initiation.
RefSeqNP_001073907.1.
UniGeneHs.653217

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSG00000184389. Homo sapiens. [Contig view]
GeneID127550.
KEGGhsa:127550.

Organism-specific databases

HGNCHGNC:30005. A3GALT2.
PharmGKBPA142670461.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ5T0B8.
HOVERGENQ5T0B8.

Gene expression databases

ArrayExpressQ5T0B8.
CleanExHS_A3GALT2.

Family and domain databases

InterProIPR005076. Glyco_trans_6.
[Graphical view]
PANTHERPTHR10462. Glyco_trans_6. 1 hit.
PfamPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
ProDomQ5T0B8.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameA3LT2_HUMAN
AccessionPrimary (citable) accession number: Q5T0B8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: September 2, 2008
This is version 24 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents