SIAT2_HUMAN
ID SIAT2_HUMAN Reviewed; 529 AA.
AC Q96JF0; D3DVK3; Q53QP4; Q86Y44; Q8IUG7; Q96HE4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Beta-galactoside alpha-2,6-sialyltransferase 2;
DE Short=Alpha 2,6-ST 2;
DE EC=2.4.99.1 {ECO:0000269|PubMed:12235148, ECO:0000269|PubMed:12603328, ECO:0000269|PubMed:16439063};
DE AltName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2;
DE AltName: Full=ST6Gal II;
DE Short=ST6GalII;
DE Short=hST6Gal II;
DE AltName: Full=Sialyltransferase 2;
GN Name=ST6GAL2; Synonyms=KIAA1877, SIAT2;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=12235148; DOI=10.1074/jbc.m206808200;
RA Takashima S., Tsuji S., Tsujimoto M.;
RT "Characterization of the second type of human beta-galactoside alpha2,6-
RT sialyltransferase (ST6Gal II) that sialylates Galbeta1,4GlcNAc structures
RT on oligosaccharides preferentially.";
RL J. Biol. Chem. 277:45719-45728(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 315-529 (ISOFORM 1), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=12603328; DOI=10.1046/j.1432-1033.2003.03458.x;
RA Krzewinski-Recchi M.-A., Julien S., Juliant S., Teintenier-Lelievre M.,
RA Samyn-Petit B., Montiel M.-D., Mir A.-M., Cerutti M., Harduin-Lepers A.,
RA Delannoy P.;
RT "Identification and functional expression of a second human beta-
RT galactoside alpha2,6-sialyltransferase, ST6Gal II.";
RL Eur. J. Biochem. 270:950-961(2003).
RN [7]
RP ENZYME ACTIVITY.
RX PubMed=16439063; DOI=10.1016/j.bbagen.2005.12.012;
RA Rohfritsch P.F., Joosten J.A.F., Krzewinski-Recchi M.-A.,
RA Harduin-Lepers A., Laporte B., Juliant S., Cerutti M., Delannoy P.,
RA Vliegenthart J.F.G., Kamerling J.P.;
RT "Probing the substrate specificity of four different sialyltransferases
RT using synthetic beta-D-Galp-(1-->4)-beta-D-GlcpNAc-(1-->2)-alpha-D-Manp-
RT (1-->O) (CH(2))7CH3 analogues general activating effect of replacing N-
RT acetylglucosamine by N-propionylglucosamine.";
RL Biochim. Biophys. Acta 1760:685-692(2006).
RN [8]
RP INDUCTION.
RX PubMed=17944600; DOI=10.1042/bj20070958;
RA Groux-Degroote S., Krzewinski-Recchi M.-A., Cazet A., Vincent A.,
RA Lehoux S., Lafitte J.-J., van Seuningen I., Delannoy P.;
RT "IL-6 and IL-8 increase the expression of glycosyltransferases and
RT sulfotransferases involved in the biosynthesis of sialylated and/or
RT sulfated Lewis x epitopes in the human bronchial mucosa.";
RL Biochem. J. 410:213-223(2008).
RN [9]
RP GLYCOSYLATION AT SER-69, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
CC -!- FUNCTION: Transfers sialic acid from the donor of substrate CMP-sialic
CC acid to galactose containing acceptor substrates. Has alpha-2,6-
CC sialyltransferase activity toward oligosaccharides that have the Gal-
CC beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate
CC groups, but it has weak or no activities toward glycoproteins and
CC glycolipids. {ECO:0000269|PubMed:12235148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N-
CC acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP +
CC H(+); Xref=Rhea:RHEA:52104, ChEBI:CHEBI:15378, ChEBI:CHEBI:28034,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:136398;
CC EC=2.4.99.1; Evidence={ECO:0000269|PubMed:12235148,
CC ECO:0000269|PubMed:12603328, ECO:0000269|PubMed:16439063};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.74 mM for Gal-beta-1,4-GlcNAc-beta-O-octyl
CC {ECO:0000269|PubMed:12235148, ECO:0000269|PubMed:12603328};
CC KM=0.71 mM for Gal-beta-1,4-GlcNAc {ECO:0000269|PubMed:12235148,
CC ECO:0000269|PubMed:12603328};
CC KM=0.48 mM for lacto-N-neotetraose {ECO:0000269|PubMed:12235148,
CC ECO:0000269|PubMed:12603328};
CC -!- INTERACTION:
CC Q96JF0-2; Q13520: AQP6; NbExp=3; IntAct=EBI-12908338, EBI-13059134;
CC Q96JF0-2; P19397: CD53; NbExp=3; IntAct=EBI-12908338, EBI-6657396;
CC Q96JF0-2; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-12908338, EBI-12142257;
CC Q96JF0-2; Q8TF64: GIPC3; NbExp=3; IntAct=EBI-12908338, EBI-12372489;
CC Q96JF0-2; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-12908338, EBI-712073;
CC Q96JF0-2; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12908338, EBI-11721746;
CC Q96JF0-2; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-12908338, EBI-18053395;
CC Q96JF0-2; O15173: PGRMC2; NbExp=3; IntAct=EBI-12908338, EBI-1050125;
CC Q96JF0-2; Q9H2B4-2: SLC26A1; NbExp=3; IntAct=EBI-12908338, EBI-12908340;
CC Q96JF0-2; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-12908338, EBI-12898013;
CC Q96JF0-2; P30825: SLC7A1; NbExp=3; IntAct=EBI-12908338, EBI-4289564;
CC Q96JF0-2; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-12908338, EBI-6268651;
CC Q96JF0-2; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-12908338, EBI-8638294;
CC Q96JF0-2; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-12908338, EBI-10982110;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96JF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JF0-2; Sequence=VSP_030356;
CC -!- TISSUE SPECIFICITY: Weakly expressed in some tissues, such as small
CC intestine, colon and fetal brain. {ECO:0000269|PubMed:12235148,
CC ECO:0000269|PubMed:12603328}.
CC -!- INDUCTION: By IL6/interleukin-6 and IL8//interleukin-8.
CC {ECO:0000269|PubMed:17944600}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08680.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB47506.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB059555; BAC24793.1; -; mRNA.
DR EMBL; AB058780; BAB47506.1; ALT_INIT; mRNA.
DR EMBL; AC016994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108049; AAY15022.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01742.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01743.1; -; Genomic_DNA.
DR EMBL; BC008680; AAH08680.1; ALT_INIT; mRNA.
DR EMBL; AJ512141; CAD54408.1; -; mRNA.
DR CCDS; CCDS2073.1; -. [Q96JF0-1]
DR CCDS; CCDS46380.1; -. [Q96JF0-2]
DR RefSeq; NP_001135823.1; NM_001142351.1. [Q96JF0-1]
DR RefSeq; NP_001135824.1; NM_001142352.1. [Q96JF0-2]
DR RefSeq; NP_001309291.1; NM_001322362.1. [Q96JF0-1]
DR RefSeq; NP_115917.1; NM_032528.2. [Q96JF0-1]
DR RefSeq; XP_006712865.1; XM_006712802.1. [Q96JF0-1]
DR RefSeq; XP_011510301.1; XM_011511999.2. [Q96JF0-1]
DR RefSeq; XP_011510303.1; XM_011512001.2. [Q96JF0-2]
DR AlphaFoldDB; Q96JF0; -.
DR SMR; Q96JF0; -.
DR BioGRID; 124151; 17.
DR IntAct; Q96JF0; 15.
DR STRING; 9606.ENSP00000386942; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q96JF0; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q96JF0; -.
DR PhosphoSitePlus; Q96JF0; -.
DR BioMuta; ST6GAL2; -.
DR DMDM; 166219772; -.
DR jPOST; Q96JF0; -.
DR MassIVE; Q96JF0; -.
DR PaxDb; Q96JF0; -.
DR PeptideAtlas; Q96JF0; -.
DR PRIDE; Q96JF0; -.
DR Antibodypedia; 2496; 84 antibodies from 18 providers.
DR DNASU; 84620; -.
DR Ensembl; ENST00000361686.8; ENSP00000355273.4; ENSG00000144057.16. [Q96JF0-1]
DR Ensembl; ENST00000409087.3; ENSP00000387332.3; ENSG00000144057.16. [Q96JF0-2]
DR Ensembl; ENST00000409382.8; ENSP00000386942.3; ENSG00000144057.16. [Q96JF0-1]
DR GeneID; 84620; -.
DR KEGG; hsa:84620; -.
DR MANE-Select; ENST00000409382.8; ENSP00000386942.3; NM_001142351.2; NP_001135823.1.
DR UCSC; uc002tdq.4; human. [Q96JF0-1]
DR CTD; 84620; -.
DR DisGeNET; 84620; -.
DR GeneCards; ST6GAL2; -.
DR HGNC; HGNC:10861; ST6GAL2.
DR HPA; ENSG00000144057; Tissue enhanced (brain, thyroid gland).
DR MIM; 608472; gene.
DR neXtProt; NX_Q96JF0; -.
DR OpenTargets; ENSG00000144057; -.
DR PharmGKB; PA35763; -.
DR VEuPathDB; HostDB:ENSG00000144057; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000158714; -.
DR HOGENOM; CLU_038334_1_0_1; -.
DR InParanoid; Q96JF0; -.
DR OMA; WRQRMLC; -.
DR OrthoDB; 494294at2759; -.
DR PhylomeDB; Q96JF0; -.
DR TreeFam; TF323961; -.
DR BRENDA; 2.4.99.1; 2681.
DR PathwayCommons; Q96JF0; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR SignaLink; Q96JF0; -.
DR BioGRID-ORCS; 84620; 7 hits in 1064 CRISPR screens.
DR ChiTaRS; ST6GAL2; human.
DR GenomeRNAi; 84620; -.
DR Pharos; Q96JF0; Tbio.
DR PRO; PR:Q96JF0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96JF0; protein.
DR Bgee; ENSG00000144057; Expressed in cortical plate and 128 other tissues.
DR ExpressionAtlas; Q96JF0; baseline and differential.
DR Genevisible; Q96JF0; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003835; F:beta-galactoside alpha-2,6-sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0097503; P:sialylation; IBA:GO_Central.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..529
FT /note="Beta-galactoside alpha-2,6-sialyltransferase 2"
FT /id="PRO_0000314785"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..529
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 253..519
FT /evidence="ECO:0000250"
FT DISULFID 296..448
FT /evidence="ECO:0000250"
FT DISULFID 466..477
FT /evidence="ECO:0000250"
FT VAR_SEQ 441..529
FT /note="ILIMMSMCREVHVYEYIPSVRQTELCHYHELYYDAACTLGAYHPLLYEKLLV
FT QRLNMGTQGDLHRKGKVVLPGFQAVHCPAPSPVIPHS -> SFVKIGHIRACSEPRSRD
FT CTPAWTTE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030356"
FT VARIANT 154
FT /note="G -> R (in dbSNP:rs3796110)"
FT /id="VAR_038046"
FT VARIANT 341
FT /note="I -> V (in dbSNP:rs12615112)"
FT /id="VAR_038047"
SQ SEQUENCE 529 AA; 60158 MW; C3647E6DC0A9EFE3 CRC64;
MKPHLKQWRQ RMLFGIFAWG LLFLLIFIYF TDSNPAEPVP SSLSFLETRR LLPVQGKQRA
IMGAAHEPSP PGGLDARQAL PRAHPAGSFH AGPGDLQKWA QSQDGFEHKE FFSSQVGRKS
QSAFYPEDDD YFFAAGQPGW HSHTQGTLGF PSPGEPGPRE GAFPAAQVQR RRVKKRHRRQ
RRSHVLEEGD DGDRLYSSMS RAFLYRLWKG NVSSKMLNPR LQKAMKDYLT ANKHGVRFRG
KREAGLSRAQ LLCQLRSRAR VRTLDGTEAP FSALGWRRLV PAVPLSQLHP RGLRSCAVVM
SAGAILNSSL GEEIDSHDAV LRFNSAPTRG YEKDVGNKTT IRIINSQILT NPSHHFIDSS
LYKDVILVAW DPAPYSANLN LWYKKPDYNL FTPYIQHRQR NPNQPFYILH PKFIWQLWDI
IQENTKEKIQ PNPPSSGFIG ILIMMSMCRE VHVYEYIPSV RQTELCHYHE LYYDAACTLG
AYHPLLYEKL LVQRLNMGTQ GDLHRKGKVV LPGFQAVHCP APSPVIPHS
