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Protein

Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase

Gene

ST8SIA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of sialic acid from a CMP-linked sialic acid donor onto the terminal sialic acid of an acceptor through alpha-2,8-linkages. Is active with alpha-2,3-linked, alpha-2,6-linked and alpha-2,8-linked sialic acid of N-linked oligosaccharides of glycoproteins and glycolipids. Displays preference for substrates with alpha-2,3-linked terminal sialic acid. It can form polysialic acid in vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid.3 Publications

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei190 – 1901Substrate1 Publication
Active sitei354 – 3541Proton donor/acceptor1 Publication

GO - Molecular functioni

  • alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity Source: BHF-UCL
  • sialic acid binding Source: BHF-UCL
  • sialyltransferase activity Source: UniProtKB

GO - Biological processi

  • ganglioside biosynthetic process Source: BHF-UCL
  • glycoprotein metabolic process Source: BHF-UCL
  • glycosphingolipid biosynthetic process Source: ProtInc
  • N-glycan processing Source: UniProtKB
  • oligosaccharide metabolic process Source: BHF-UCL
  • protein glycosylation Source: BHF-UCL
  • protein sialylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-HSA-4085001. Sialic acid metabolism.
R-HSA-975577. N-Glycan antennae elongation.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Names & Taxonomyi

Protein namesi
Recommended name:
Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase (EC:2.4.99.-1 Publication)
Alternative name(s):
Alpha-2,8-sialyltransferase 8C
Alpha-2,8-sialyltransferase III
ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3
Sialyltransferase 8C
Short name:
SIAT8-C
Sialyltransferase St8Sia III1 Publication
Short name:
ST8SiaIII1 Publication
Gene namesi
Name:ST8SIA3
Synonyms:SIAT8C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:14269. ST8SIA3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence analysis
Transmembranei10 – 3324Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini34 – 380347LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi354 – 3541H → A: Abolishes enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA37864.

Polymorphism and mutation databases

BioMutaiST8SIA3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferasePRO_0000149289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence analysis1 Publication
Glycosylationi113 – 1131N-linked (GlcNAc...)1 Publication
Glycosylationi160 – 1601N-linked (GlcNAc...)1 Publication
Disulfide bondi162 ↔ 313Combined sources1 Publication
Disulfide bondi176 ↔ 379Combined sources1 Publication
Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence analysis1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO43173.
PRIDEiO43173.

PTM databases

iPTMnetiO43173.
PhosphoSiteiO43173.

Expressioni

Tissue specificityi

Expressed in fetal and adult brain and fetal liver.1 Publication

Gene expression databases

BgeeiO43173.
CleanExiHS_ST8SIA3.
ExpressionAtlasiO43173. baseline and differential.
GenevisibleiO43173. HS.

Organism-specific databases

HPAiHPA063398.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi119243. 11 interactions.
DIPiDIP-61706N.
STRINGi9606.ENSP00000320431.

Structurei

Secondary structure

1
380
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi94 – 10714Combined sources
Helixi110 – 1134Combined sources
Helixi118 – 1203Combined sources
Helixi142 – 1465Combined sources
Turni153 – 1564Combined sources
Beta strandi159 – 1657Combined sources
Helixi169 – 1713Combined sources
Helixi177 – 1815Combined sources
Beta strandi183 – 1897Combined sources
Helixi195 – 1973Combined sources
Helixi198 – 2014Combined sources
Beta strandi206 – 2094Combined sources
Helixi214 – 2185Combined sources
Helixi220 – 2223Combined sources
Helixi225 – 23612Combined sources
Turni237 – 2404Combined sources
Beta strandi242 – 2443Combined sources
Helixi251 – 2533Combined sources
Helixi254 – 26613Combined sources
Turni267 – 2693Combined sources
Beta strandi274 – 2763Combined sources
Helixi282 – 29110Combined sources
Helixi301 – 31212Combined sources
Beta strandi313 – 3208Combined sources
Beta strandi324 – 3263Combined sources
Turni328 – 3303Combined sources
Beta strandi351 – 3533Combined sources
Helixi356 – 36813Combined sources
Beta strandi371 – 3744Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5BO6X-ray2.07A/B81-380[»]
5BO7X-ray1.85A/B81-380[»]
5BO8X-ray2.70A/B61-380[»]
5BO9X-ray2.30A/B81-380[»]
ProteinModelPortaliO43173.
SMRiO43173. Positions 90-380.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni211 – 2133Substrate binding1 Publication
Regioni300 – 3023Substrate binding1 Publication
Regioni336 – 3372Substrate binding1 Publication

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00550000074407.
HOVERGENiHBG056466.
InParanoidiO43173.
KOiK06613.
OMAiHELQEKP.
OrthoDBiEOG7VQJD1.
PhylomeDBiO43173.
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.

O43173-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNCKMARVA SVLGLVMLSV ALLILSLISY VSLKKENIFT TPKYASPGAP
60 70 80 90 100
RMYMFHAGFR SQFALKFLDP SFVPITNSLT QELQEKPSKW KFNRTAFLHQ
110 120 130 140 150
RQEILQHVDV IKNFSLTKNS VRIGQLMHYD YSSHKYVFSI SNNFRSLLPD
160 170 180 190 200
VSPIMNKHYN ICAVVGNSGI LTGSQCGQEI DKSDFVFRCN FAPTEAFQRD
210 220 230 240 250
VGRKTNLTTF NPSILEKYYN NLLTIQDRNN FFLSLKKLDG AILWIPAFFF
260 270 280 290 300
HTSATVTRTL VDFFVEHRGQ LKVQLAWPGN IMQHVNRYWK NKHLSPKRLS
310 320 330 340 350
TGILMYTLAS AICEEIHLYG FWPFGFDPNT REDLPYHYYD KKGTKFTTKW
360 370 380
QESHQLPAEF QLLYRMHGEG LTKLTLSHCA
Length:380
Mass (Da):43,970
Last modified:October 17, 2006 - v3
Checksum:i70D782A2CAD2666A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1742GS → FI in AAB87642 (PubMed:9826427).Curated
Sequence conflicti178 – 1781Q → R in AAB87642 (PubMed:9826427).Curated
Sequence conflicti194 – 1941T → S in AAB87642 (PubMed:9826427).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911K → T.
Corresponds to variant rs3745060 [ dbSNP | Ensembl ].
VAR_020249

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004668 mRNA. Translation: AAB87642.1.
AF003092 mRNA. Translation: AAC15901.2.
AK289517 mRNA. Translation: BAF82206.1.
AK313047 mRNA. Translation: BAG35879.1.
BC074909 mRNA. Translation: AAH74909.1.
CCDSiCCDS32834.1.
RefSeqiNP_056963.2. NM_015879.2.
UniGeneiHs.23172.

Genome annotation databases

EnsembliENST00000324000; ENSP00000320431; ENSG00000177511.
GeneIDi51046.
KEGGihsa:51046.
UCSCiuc002lgn.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST8Sia III

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004668 mRNA. Translation: AAB87642.1.
AF003092 mRNA. Translation: AAC15901.2.
AK289517 mRNA. Translation: BAF82206.1.
AK313047 mRNA. Translation: BAG35879.1.
BC074909 mRNA. Translation: AAH74909.1.
CCDSiCCDS32834.1.
RefSeqiNP_056963.2. NM_015879.2.
UniGeneiHs.23172.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5BO6X-ray2.07A/B81-380[»]
5BO7X-ray1.85A/B81-380[»]
5BO8X-ray2.70A/B61-380[»]
5BO9X-ray2.30A/B81-380[»]
ProteinModelPortaliO43173.
SMRiO43173. Positions 90-380.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119243. 11 interactions.
DIPiDIP-61706N.
STRINGi9606.ENSP00000320431.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

PTM databases

iPTMnetiO43173.
PhosphoSiteiO43173.

Polymorphism and mutation databases

BioMutaiST8SIA3.

Proteomic databases

PaxDbiO43173.
PRIDEiO43173.

Protocols and materials databases

DNASUi51046.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324000; ENSP00000320431; ENSG00000177511.
GeneIDi51046.
KEGGihsa:51046.
UCSCiuc002lgn.4. human.

Organism-specific databases

CTDi51046.
GeneCardsiST8SIA3.
HGNCiHGNC:14269. ST8SIA3.
HPAiHPA063398.
MIMi609478. gene.
neXtProtiNX_O43173.
PharmGKBiPA37864.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00550000074407.
HOVERGENiHBG056466.
InParanoidiO43173.
KOiK06613.
OMAiHELQEKP.
OrthoDBiEOG7VQJD1.
PhylomeDBiO43173.
TreeFamiTF323961.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-HSA-4085001. Sialic acid metabolism.
R-HSA-975577. N-Glycan antennae elongation.

Miscellaneous databases

ChiTaRSiST8SIA3. human.
GenomeRNAii51046.
PROiO43173.
SOURCEiSearch...

Gene expression databases

BgeeiO43173.
CleanExiHS_ST8SIA3.
ExpressionAtlasiO43173. baseline and differential.
GenevisibleiO43173. HS.

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. "Cloning and expression of cDNA for a human Sia alpha 2,3Gal beta 1,4GlcNA:alpha 2,8-sialyltransferase (hST8Sia III)."
    Lee Y.-C., Kim Y.-J., Lee K.-Y., Kim K.-S., Kim B.-U., Kim H.-N., Kim C.-H., Do S.-I.
    Arch. Biochem. Biophys. 360:41-46(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Differential biosynthesis of polysialic acid on neural cell adhesion molecule (NCAM) and oligosaccharide acceptors by three distinct alpha2,8-Sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III."
    Angata K., Suzuki M., McAuliffe J., Ding Y., Hindsgaul O., Fukuda M.
    J. Biol. Chem. 275:18594-18601(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Fetal brain.
  3. Angata K., Fukuda M.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 19; 241 AND 296.
  4. "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.
    , 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].
    Tissue: Brain and Cerebellum.
  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].
  6. "Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation."
    Volkers G., Worrall L.J., Kwan D.H., Yu C.C., Baumann L., Lameignere E., Wasney G.A., Scott N.E., Wakarchuk W., Foster L.J., Withers S.G., Strynadka N.C.
    Nat. Struct. Mol. Biol. 22:627-635(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 81-380 IN COMPLEXES WITH CDP; CTP AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF HIS-354, SUBUNIT, PATHWAY, DISULFIDE BONDS, GLYCOSYLATION AT ASN-93; ASN-113; ASN-160 AND ASN-206, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSIA8C_HUMAN
AccessioniPrimary (citable) accession number: O43173
Secondary accession number(s): A8K0F2, Q6B085, Q9NS41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: October 17, 2006
Last modified: June 8, 2016
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.