SIA8B_HUMAN
ID SIA8B_HUMAN Reviewed; 375 AA.
AC Q92186; Q4VAZ0; Q92470; Q92746;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Alpha-2,8-sialyltransferase 8B;
DE EC=2.4.99.-;
DE AltName: Full=Sialyltransferase 8B;
DE Short=SIAT8-B;
DE AltName: Full=Sialyltransferase St8Sia II;
DE Short=ST8SiaII;
DE AltName: Full=Sialyltransferase X;
DE Short=STX;
GN Name=ST8SIA2; Synonyms=SIAT8B, STX;
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].
RX PubMed=7559389; DOI=10.1074/jbc.270.39.22685;
RA Scheidegger E.P., Sternberg L.R., Roth J., Lowe J.B.;
RT "A human STX cDNA confers polysialic acid expression in mammalian cells.";
RL J. Biol. Chem. 270:22685-22688(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9054414; DOI=10.1074/jbc.272.11.7182;
RA Angata K., Nakayama J., Fredette B., Chong K., Ranscht B., Fukuda M.;
RT "Human STX polysialyltransferase forms the embryonic form of the neural
RT cell adhesion molecule. Tissue-specific expression, neurite outgrowth, and
RT chromosomal localization in comparison with another polysialyltransferase,
RT PST.";
RL J. Biol. Chem. 272:7182-7190(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 154-375.
RC TISSUE=Fetal brain;
RX PubMed=8027041; DOI=10.1016/s0021-9258(17)32390-6;
RA Kitagawa H., Paulson J.C.;
RT "Differential expression of five sialyltransferase genes in human
RT tissues.";
RL J. Biol. Chem. 269:17872-17878(1994).
CC -!- FUNCTION: May transfer sialic acid through alpha-2,8-linkages to the
CC alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked
CC oligosaccharides of glycoproteins and may be involved in PSA
CC (polysialic acid) expression.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal brain, kidney and heart
CC and to a much lesser extent in adult heart and thymus.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia
CC II;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_637";
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DR EMBL; U33551; AAC24458.1; -; mRNA.
DR EMBL; U82762; AAB51242.1; -; mRNA.
DR EMBL; BC069584; AAH69584.1; -; mRNA.
DR EMBL; BC096203; AAH96203.1; -; mRNA.
DR EMBL; BC096204; AAH96204.1; -; mRNA.
DR EMBL; L29556; AAA36613.1; -; mRNA.
DR CCDS; CCDS10372.1; -.
DR PIR; B54898; B54898.
DR PIR; I39169; I39169.
DR RefSeq; NP_006002.1; NM_006011.3.
DR AlphaFoldDB; Q92186; -.
DR SMR; Q92186; -.
DR BioGRID; 113793; 14.
DR STRING; 9606.ENSP00000268164; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q92186; 6 sites.
DR iPTMnet; Q92186; -.
DR PhosphoSitePlus; Q92186; -.
DR BioMuta; ST8SIA2; -.
DR DMDM; 2494831; -.
DR MassIVE; Q92186; -.
DR PaxDb; Q92186; -.
DR PeptideAtlas; Q92186; -.
DR PRIDE; Q92186; -.
DR ABCD; Q92186; 1 sequenced antibody.
DR Antibodypedia; 29022; 132 antibodies from 30 providers.
DR DNASU; 8128; -.
DR Ensembl; ENST00000268164.8; ENSP00000268164.3; ENSG00000140557.12.
DR GeneID; 8128; -.
DR KEGG; hsa:8128; -.
DR MANE-Select; ENST00000268164.8; ENSP00000268164.3; NM_006011.4; NP_006002.1.
DR UCSC; uc002bra.4; human.
DR CTD; 8128; -.
DR DisGeNET; 8128; -.
DR GeneCards; ST8SIA2; -.
DR HGNC; HGNC:10870; ST8SIA2.
DR HPA; ENSG00000140557; Tissue enhanced (brain, heart muscle).
DR MIM; 602546; gene.
DR neXtProt; NX_Q92186; -.
DR OpenTargets; ENSG00000140557; -.
DR PharmGKB; PA35771; -.
DR VEuPathDB; HostDB:ENSG00000140557; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR InParanoid; Q92186; -.
DR OMA; TWRHNQT; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; Q92186; -.
DR TreeFam; TF352820; -.
DR BRENDA; 2.4.99.8; 2681.
DR PathwayCommons; Q92186; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR SignaLink; Q92186; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 8128; 6 hits in 1054 CRISPR screens.
DR ChiTaRS; ST8SIA2; human.
DR GeneWiki; ST8SIA2; -.
DR GenomeRNAi; 8128; -.
DR Pharos; Q92186; Tbio.
DR PRO; PR:Q92186; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q92186; protein.
DR Bgee; ENSG00000140557; Expressed in cortical plate and 71 other tissues.
DR ExpressionAtlas; Q92186; baseline and differential.
DR Genevisible; Q92186; HS.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0033691; F:sialic acid binding; IC:BHF-UCL.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0006491; P:N-glycan processing; IDA:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA:BHF-UCL.
DR GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; IDA:BHF-UCL.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR InterPro; IPR012163; Sialyl_trans.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR PIRSF; PIRSF005557; Sialyl_trans; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..375
FT /note="Alpha-2,8-sialyltransferase 8B"
FT /id="PRO_0000149285"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..375
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 346
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 294..296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 329..330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 157..307
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 171..371
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CONFLICT 155
FT /note="G -> Q (in Ref. 2; AAA36613)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="C -> Y (in Ref. 2; AAA36613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 42430 MW; 42F0BC5B33D62325 CRC64;
MQLQFRSWML AALTLLVVFL IFADISEIEE EIGNSGGRGT IRSAVNSLHS KSNRAEVVIN
GSSSPAVVDR SNESIKHNIQ PASSKWRHNQ TLSLRIRKQI LKFLDAEKDI SVLKGTLKPG
DIIHYIFDRD STMNVSQNLY ELLPRTSPLK NKHFGTCAIV GNSGVLLNSG CGQEIDAHSF
VIRCNLAPVQ EYARDVGLKT DLVTMNPSVI QRAFEDLVNA TWREKLLQRL HSLNGSILWI
PAFMARGGKE RVEWVNELIL KHHVNVRTAY PSLRLLHAVR GYWLTNKVHI KRPTTGLLMY
TLATRFCKQI YLYGFWPFPL DQNQNPVKYH YYDSLKYGYT SQASPHTMPL EFKALKSLHE
QGALKLTVGQ CDGAT
