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Protein

Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase

Gene

St8sia1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the production of gangliosides GD3 and GT3 from GM3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid.1 Publication

Catalytic activityi

CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-R = CMP + alpha-N-acetylneuraminyl-(2->8)-alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-R.1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Pathwayi: sphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway sphingolipid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei165 – 1651SubstrateBy similarity
Active sitei321 – 3211Proton donor/acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to heat Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • protein glycosylation Source: UniProtKB-UniPathway
  • sphingolipid metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BRENDAi2.4.99.8. 3474.
ReactomeiR-MMU-4085001. Sialic acid metabolism.
UniPathwayiUPA00222.
UPA00378.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase (EC:2.4.99.8)
Alternative name(s):
Alpha-2,8-sialyltransferase 8A
Ganglioside GD3 synthase
Ganglioside GT3 synthase
Sialyltransferase 8A
Short name:
SIAT8-A
Sialyltransferase St8Sia I
Short name:
ST8SiaI
Gene namesi
Name:St8sia1
Synonyms:Siat8, Siat8a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:106011. St8sia1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2828CytoplasmicSequence analysisAdd
BLAST
Transmembranei29 – 4719Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini48 – 355308LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355Alpha-N-acetylneuraminide alpha-2,8-sialyltransferasePRO_0000149283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence analysis
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi137 ↔ 286By similarity
Disulfide bondi151 ↔ 346By similarity
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence analysis
Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ64687.
PaxDbiQ64687.
PRIDEiQ64687.

PTM databases

PhosphoSiteiQ64687.

Expressioni

Gene expression databases

BgeeiQ64687.
GenevisibleiQ64687. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032421.

Structurei

3D structure databases

ProteinModelPortaliQ64687.
SMRiQ64687. Positions 67-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni187 – 1893Substrate bindingBy similarity
Regioni273 – 2753Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00550000074407.
HOGENOMiHOG000090201.
HOVERGENiHBG106106.
InParanoidiQ64687.
KOiK03371.
OMAiWHLHKSG.
OrthoDBiEOG7SV0V9.
TreeFamiTF323961.

Family and domain databases

InterProiIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamiPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFiPIRSF005557. Sialyl_trans. 1 hit.

Sequencei

Sequence statusi: Complete.

Q64687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPCGRALHT SRGAMAMLAR KFPRTRLPVG ASALCVVVLC WLYIFPVYRL
60 70 80 90 100
PNEKEIVQGV LAQRTAWRTN QTSASLFRRQ MEDCCDPAHL FAMTKMNSPM
110 120 130 140 150
GKSLWYDGEL LYSFTIDNST YSLFPQATPF QLPLKKCAVV GNGGILKMSG
160 170 180 190 200
CGRQIDEANF VMRCNLPPLS SEYTRDVGSK TQLVTANPSI IRQRFENLLW
210 220 230 240 250
SRKKFVDNMK IYNHSYIYMP AFSMKTGTEP SLRVYYTLKD VGANQTVLFA
260 270 280 290 300
NPNFLRNIGK FWKSRGIHAK RLSTGLFLVS AALGLCEEVS IYGFWPFSVN
310 320 330 340 350
MQGDPISHHY YDNVLPFSGY HAMPEEFLQL WYLHKIGALR MQLDPCEEPS

PQPTS
Length:355
Mass (Da):40,324
Last modified:July 27, 2011 - v2
Checksum:i220BD56BBEE6E6C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501L → P in CAA59014 (PubMed:8910600).Curated
Sequence conflicti64 – 641R → S in CAA59014 (PubMed:8910600).Curated
Sequence conflicti294 – 2941F → S in CAA59014 (PubMed:8910600).Curated
Sequence conflicti318 – 3181S → T in CAA59014 (PubMed:8910600).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84235 mRNA. Translation: CAA59014.1.
CH466572 Genomic DNA. Translation: EDL10653.1.
BC024821 mRNA. Translation: AAH24821.1.
CCDSiCCDS20689.1.
RefSeqiNP_035504.2. NM_011374.2.
UniGeneiMm.260838.

Genome annotation databases

EnsembliENSMUST00000032421; ENSMUSP00000032421; ENSMUSG00000030283.
GeneIDi20449.
KEGGimmu:20449.
UCSCiuc009epv.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

ST8Sia I

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84235 mRNA. Translation: CAA59014.1.
CH466572 Genomic DNA. Translation: EDL10653.1.
BC024821 mRNA. Translation: AAH24821.1.
CCDSiCCDS20689.1.
RefSeqiNP_035504.2. NM_011374.2.
UniGeneiMm.260838.

3D structure databases

ProteinModelPortaliQ64687.
SMRiQ64687. Positions 67-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032421.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSiteiQ64687.

Proteomic databases

MaxQBiQ64687.
PaxDbiQ64687.
PRIDEiQ64687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032421; ENSMUSP00000032421; ENSMUSG00000030283.
GeneIDi20449.
KEGGimmu:20449.
UCSCiuc009epv.1. mouse.

Organism-specific databases

CTDi6489.
MGIiMGI:106011. St8sia1.

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00550000074407.
HOGENOMiHOG000090201.
HOVERGENiHBG106106.
InParanoidiQ64687.
KOiK03371.
OMAiWHLHKSG.
OrthoDBiEOG7SV0V9.
TreeFamiTF323961.

Enzyme and pathway databases

UniPathwayiUPA00222.
UPA00378.
BRENDAi2.4.99.8. 3474.
ReactomeiR-MMU-4085001. Sialic acid metabolism.

Miscellaneous databases

ChiTaRSiSt8sia1. mouse.
NextBioi298514.
PROiQ64687.
SOURCEiSearch...

Gene expression databases

BgeeiQ64687.
GenevisibleiQ64687. MM.

Family and domain databases

InterProiIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamiPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFiPIRSF005557. Sialyl_trans. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of a fifth type of alpha2,8-sialyltransferase (ST8Sia V). Its substrate specificity is similar to that of SAT-V/III, which synthesize GD1c, GT1a, GQ1b and GT3."
    Kono M., Yoshida Y., Kojima N., Tsuji S.
    J. Biol. Chem. 271:29366-29371(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
    Tissue: Brain.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Eye.
  4. "The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach."
    Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R.
    Glycobiology 15:805-817(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney.

Entry informationi

Entry nameiSIA8A_MOUSE
AccessioniPrimary (citable) accession number: Q64687
Secondary accession number(s): Q8K1C1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: December 9, 2015
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.