SIAT1_HUMAN
ID SIAT1_HUMAN Reviewed; 406 AA.
AC P15907; A8KA14; B2R513; D3DNV3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Beta-galactoside alpha-2,6-sialyltransferase 1;
DE Short=Alpha 2,6-ST 1;
DE EC=2.4.99.1 {ECO:0000269|PubMed:21081508, ECO:0000269|PubMed:23999306};
DE AltName: Full=B-cell antigen CD75;
DE AltName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1;
DE AltName: Full=ST6Gal I;
DE Short=ST6GalI;
DE AltName: Full=Sialyltransferase 1;
GN Name=ST6GAL1; Synonyms=SIAT1;
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).
RC TISSUE=Placenta;
RX PubMed=2408023; DOI=10.1093/nar/18.3.667;
RA Grundmann U.G., Nerlich C., Rein T., Zettlmeissl G.;
RT "Complete cDNA sequence encoding human beta-galactoside alpha-2,6-
RT sialyltransferase.";
RL Nucleic Acids Res. 18:667-667(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2373995; DOI=10.1084/jem.172.2.641;
RA Stamenkovic I., Asheim H.C., Deggerdal A., Blomhoff H.K., Smeland E.B.,
RA Funderud S.;
RT "The B cell antigen CD75 is a cell surface sialyltransferase.";
RL J. Exp. Med. 172:641-643(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=1730763; DOI=10.1083/jcb.116.2.423;
RA Bast B.J.E.G., Zhou L.J., Freeman G.J., Colley K.J., Ernst T.J.,
RA Munro J.M., Tedder T.F.;
RT "The HB-6, CDw75, and CD76 differentiation antigens are unique cell-surface
RT carbohydrate determinants generated by the beta-galactoside alpha 2,6-
RT sialyltransferase.";
RL J. Cell Biol. 116:423-435(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Thymus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph, and Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-406 (ISOFORM 1).
RX PubMed=2803295; DOI=10.1016/0006-291x(89)91706-3;
RA Lance P., Lau K.M., Lau J.T.Y.;
RT "Isolation and characterization of a partial cDNA for a human
RT sialyltransferase.";
RL Biochem. Biophys. Res. Commun. 164:225-232(1989).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-149 AND ASN-161.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-369, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF CYS-24.
RX PubMed=20378551; DOI=10.1074/jbc.m110.103184;
RA Hassinen A., Rivinoja A., Kauppila A., Kellokumpu S.;
RT "Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme
RT complexes in live cells.";
RL J. Biol. Chem. 285:17771-17777(2010).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21081508; DOI=10.1093/glycob/cwq187;
RA Wu Z.L., Ethen C.M., Prather B., Machacek M., Jiang W.;
RT "Universal phosphatase-coupled glycosyltransferase assay.";
RL Glycobiology 21:727-733(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 89-406 IN COMPLEXES WITH CMP;
RP CYTIDINE AND PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-149, AND
RP DISULFIDE BONDS.
RX PubMed=23999306; DOI=10.1107/s0907444913015412;
RA Kuhn B., Benz J., Greif M., Engel A.M., Sobek H., Rudolph M.G.;
RT "The structure of human alpha-2,6-sialyltransferase reveals the binding
RT mode of complex glycans.";
RL Acta Crystallogr. D 69:1826-1838(2013).
CC -!- FUNCTION: Transfers sialic acid from CMP-sialic acid to galactose-
CC containing acceptor substrates. {ECO:0000269|PubMed:21081508,
CC ECO:0000269|PubMed:23999306}.
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:21081508,
CC ECO:0000269|PubMed:23999306};
CC -!- ACTIVITY REGULATION: Inhibited by CTP. {ECO:0000269|PubMed:23999306}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=530 uM for CMP-NeuAc {ECO:0000269|PubMed:21081508};
CC Vmax=1.074 pmol/min/ug enzyme {ECO:0000269|PubMed:21081508};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:20378551}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:20378551}; Single-pass type II membrane protein
CC {ECO:0000305}. Secreted. Note=Membrane-bound form in trans cisternae of
CC Golgi. Secreted into the body fluid.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P15907-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15907-2; Sequence=VSP_056076;
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000250|UniProtKB:P13721}.
CC -!- PTM: The HB-6, CDW75, and CD76 differentiation antigens are cell-
CC surface carbohydrate determinants generated by this enzyme.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:23999306}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6Gal I;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_628";
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DR EMBL; X17247; CAA35111.1; -; mRNA.
DR EMBL; X54363; CAA38246.1; -; mRNA.
DR EMBL; X62822; CAA44634.1; -; mRNA.
DR EMBL; AK292879; BAF85568.1; -; mRNA.
DR EMBL; AK312023; BAG34960.1; -; mRNA.
DR EMBL; AC007488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78160.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78161.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78162.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78164.1; -; Genomic_DNA.
DR EMBL; BC031476; AAH31476.1; -; mRNA.
DR EMBL; BC040009; AAH40009.1; -; mRNA.
DR CCDS; CCDS3285.1; -. [P15907-1]
DR CCDS; CCDS46973.1; -. [P15907-2]
DR PIR; A41734; A41734.
DR RefSeq; NP_003023.1; NM_003032.2. [P15907-1]
DR RefSeq; NP_775323.1; NM_173216.2. [P15907-1]
DR RefSeq; NP_775324.1; NM_173217.2. [P15907-2]
DR RefSeq; XP_005247776.1; XM_005247719.1.
DR RefSeq; XP_005247777.1; XM_005247720.1.
DR RefSeq; XP_006713797.1; XM_006713734.1.
DR RefSeq; XP_011511387.1; XM_011513085.1.
DR RefSeq; XP_011511388.1; XM_011513086.1.
DR RefSeq; XP_016862554.1; XM_017007065.1.
DR RefSeq; XP_016862555.1; XM_017007066.1.
DR RefSeq; XP_016862556.1; XM_017007067.1.
DR RefSeq; XP_016862557.1; XM_017007068.1.
DR PDB; 4JS1; X-ray; 2.09 A; A=89-406.
DR PDB; 4JS2; X-ray; 2.30 A; A=89-406.
DR PDB; 6QVS; X-ray; 1.60 A; A/B=132-406.
DR PDB; 6QVT; X-ray; 1.70 A; A/B=132-406.
DR PDBsum; 4JS1; -.
DR PDBsum; 4JS2; -.
DR PDBsum; 6QVS; -.
DR PDBsum; 6QVT; -.
DR AlphaFoldDB; P15907; -.
DR SMR; P15907; -.
DR BioGRID; 112374; 22.
DR IntAct; P15907; 19.
DR STRING; 9606.ENSP00000169298; -.
DR BindingDB; P15907; -.
DR ChEMBL; CHEMBL3596075; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; P15907; 2 sites.
DR iPTMnet; P15907; -.
DR PhosphoSitePlus; P15907; -.
DR BioMuta; ST6GAL1; -.
DR DMDM; 115445; -.
DR EPD; P15907; -.
DR jPOST; P15907; -.
DR MassIVE; P15907; -.
DR MaxQB; P15907; -.
DR PaxDb; P15907; -.
DR PeptideAtlas; P15907; -.
DR PRIDE; P15907; -.
DR ProteomicsDB; 3411; -.
DR ProteomicsDB; 53240; -. [P15907-1]
DR Antibodypedia; 4243; 574 antibodies from 38 providers.
DR DNASU; 6480; -.
DR Ensembl; ENST00000169298.8; ENSP00000169298.3; ENSG00000073849.16. [P15907-1]
DR Ensembl; ENST00000416235.6; ENSP00000414504.2; ENSG00000073849.16. [P15907-1]
DR Ensembl; ENST00000448044.5; ENSP00000389337.1; ENSG00000073849.16. [P15907-1]
DR Ensembl; ENST00000457772.6; ENSP00000412221.2; ENSG00000073849.16. [P15907-2]
DR Ensembl; ENST00000676633.1; ENSP00000504448.1; ENSG00000073849.16. [P15907-1]
DR Ensembl; ENST00000677292.1; ENSP00000503457.1; ENSG00000073849.16. [P15907-1]
DR GeneID; 6480; -.
DR KEGG; hsa:6480; -.
DR MANE-Select; ENST00000169298.8; ENSP00000169298.3; NM_173216.2; NP_775323.1.
DR UCSC; uc003frb.4; human. [P15907-1]
DR CTD; 6480; -.
DR DisGeNET; 6480; -.
DR GeneCards; ST6GAL1; -.
DR HGNC; HGNC:10860; ST6GAL1.
DR HPA; ENSG00000073849; Group enriched (liver, lymphoid tissue).
DR MIM; 109675; gene.
DR neXtProt; NX_P15907; -.
DR OpenTargets; ENSG00000073849; -.
DR PharmGKB; PA35762; -.
DR VEuPathDB; HostDB:ENSG00000073849; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000157053; -.
DR HOGENOM; CLU_038334_0_0_1; -.
DR InParanoid; P15907; -.
DR OMA; ICVWKER; -.
DR OrthoDB; 494294at2759; -.
DR PhylomeDB; P15907; -.
DR TreeFam; TF323961; -.
DR BioCyc; MetaCyc:HS01118-MON; -.
DR BRENDA; 2.4.99.1; 2681.
DR PathwayCommons; P15907; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-9683673; Maturation of protein 3a.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-9694719; Maturation of protein 3a.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
DR SignaLink; P15907; -.
DR SIGNOR; P15907; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 6480; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; ST6GAL1; human.
DR GeneWiki; ST6GAL1; -.
DR GenomeRNAi; 6480; -.
DR Pharos; P15907; Tchem.
DR PRO; PR:P15907; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P15907; protein.
DR Bgee; ENSG00000073849; Expressed in liver and 206 other tissues.
DR ExpressionAtlas; P15907; baseline and differential.
DR Genevisible; P15907; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005797; C:Golgi medial cisterna; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0000138; C:Golgi trans cisterna; IEA:Ensembl.
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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; IDA:UniProtKB.
DR GO; GO:0050922; P:negative regulation of chemotaxis; IEA:Ensembl.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; IEA:Ensembl.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; IEA:Ensembl.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR GO; GO:1990743; P:protein sialylation; IEA:Ensembl.
DR GO; GO:1900024; P:regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0097503; P:sialylation; IDA:UniProtKB.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Secreted; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..406
FT /note="Beta-galactoside alpha-2,6-sialyltransferase 1"
FT /id="PRO_0000149249"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT TRANSMEM 10..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..406
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23999306,
FT ECO:0007744|PDB:4JS1"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23999306"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23999306"
FT BINDING 322..324
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23999306,
FT ECO:0007744|PDB:4JS1"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23999306,
FT ECO:0007744|PDB:4JS1"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23999306,
FT ECO:0007744|PDB:4JS1"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23999306,
FT ECO:0007744|PDB:4JS1, ECO:0007744|PDB:4JS2"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23999306"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23999306,
FT ECO:0007744|PDB:4JS2"
FT MOD_RES 369
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:23999306, ECO:0007744|PDB:4JS1"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 142..406
FT /evidence="ECO:0000269|PubMed:23999306,
FT ECO:0007744|PDB:4JS2"
FT DISULFID 184..335
FT /evidence="ECO:0000269|PubMed:23999306,
FT ECO:0007744|PDB:4JS1, ECO:0007744|PDB:4JS2"
FT DISULFID 353..364
FT /evidence="ECO:0000269|PubMed:23999306,
FT ECO:0007744|PDB:4JS1, ECO:0007744|PDB:4JS2"
FT VAR_SEQ 1..231
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056076"
FT MUTAGEN 24
FT /note="C->G: No effect on dimerization and on location at
FT the Golgi stack."
FT /evidence="ECO:0000269|PubMed:20378551"
FT CONFLICT 27
FT /note="K -> L (in Ref. 2; CAA38246)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..73
FT /note="HR -> T (in Ref. 2; CAA38246)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="L -> P (in Ref. 2; CAA38246)"
FT /evidence="ECO:0000305"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4JS1"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:4JS1"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:6QVS"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6QVS"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:6QVS"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:6QVS"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:6QVS"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:6QVS"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:6QVS"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:6QVS"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:6QVS"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:6QVS"
FT STRAND 335..344
FT /evidence="ECO:0007829|PDB:6QVS"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:4JS1"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:4JS1"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:4JS1"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 387..393
FT /evidence="ECO:0007829|PDB:6QVS"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:6QVS"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:6QVS"
SQ SEQUENCE 406 AA; 46605 MW; AC1E24A3875CF00F CRC64;
MIHTNLKKKF SCCVLVFLLF AVICVWKEKK KGSYYDSFKL QTKEFQVLKS LGKLAMGSDS
QSVSSSSTQD PHRGRQTLGS LRGLAKAKPE ASFQVWNKDS SSKNLIPRLQ KIWKNYLSMN
KYKVSYKGPG PGIKFSAEAL RCHLRDHVNV SMVEVTDFPF NTSEWEGYLP KESIRTKAGP
WGRCAVVSSA GSLKSSQLGR EIDDHDAVLR FNGAPTANFQ QDVGTKTTIR LMNSQLVTTE
KRFLKDSLYN EGILIVWDPS VYHSDIPKWY QNPDYNFFNN YKTYRKLHPN QPFYILKPQM
PWELWDILQE ISPEEIQPNP PSSGMLGIII MMTLCDQVDI YEFLPSKRKT DVCYYYQKFF
DSACTMGAYH PLLYEKNLVK HLNQGTDEDI YLLGKATLPG FRTIHC
