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Beta-galactoside alpha-2,6-sialyltransferase 1 (Alpha 2,6-ST 1) (EC 2.4.99.1) (B-cell antigen CD75) (CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1) (ST6Gal I) (ST6GalI) (Sialyltransferase 1)

 SIAT1_HUMAN             Reviewed;         406 AA.
P15907; A8KA14; B2R513; D3DNV3;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
28-MAR-2018, entry version 187.
RecName: Full=Beta-galactoside alpha-2,6-sialyltransferase 1;
Short=Alpha 2,6-ST 1;
EC=2.4.99.1 {ECO:0000269|PubMed:21081508, ECO:0000269|PubMed:23999306};
AltName: Full=B-cell antigen CD75;
AltName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1;
AltName: Full=ST6Gal I;
Short=ST6GalI;
AltName: Full=Sialyltransferase 1;
Name=ST6GAL1; Synonyms=SIAT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=2408023; DOI=10.1093/nar/18.3.667;
Grundmann U.G., Nerlich C., Rein T., Zettlmeissl G.;
"Complete cDNA sequence encoding human beta-galactoside alpha-2,6-
sialyltransferase.";
Nucleic Acids Res. 18:667-667(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2373995; DOI=10.1084/jem.172.2.641;
Stamenkovic I., Asheim H.C., Deggerdal A., Blomhoff H.K.,
Smeland E.B., Funderud S.;
"The B cell antigen CD75 is a cell surface sialyltransferase.";
J. Exp. Med. 172:641-643(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Spleen;
PubMed=1730763; DOI=10.1083/jcb.116.2.423;
Bast B.J.E.G., Zhou L.J., Freeman G.J., Colley K.J., Ernst T.J.,
Munro J.M., Tedder T.F.;
"The HB-6, CDw75, and CD76 differentiation antigens are unique cell-
surface carbohydrate determinants generated by the beta-galactoside
alpha 2,6-sialyltransferase.";
J. Cell Biol. 116:423-435(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Thymus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 74-406 (ISOFORM 1).
PubMed=2803295; DOI=10.1016/0006-291X(89)91706-3;
Lance P., Lau K.M., Lau J.T.Y.;
"Isolation and characterization of a partial cDNA for a human
sialyltransferase.";
Biochem. Biophys. Res. Commun. 164:225-232(1989).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-149 AND ASN-161.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-369, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=21081508; DOI=10.1093/glycob/cwq187;
Wu Z.L., Ethen C.M., Prather B., Machacek M., Jiang W.;
"Universal phosphatase-coupled glycosyltransferase assay.";
Glycobiology 21:727-733(2011).
[12]
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 89-406 IN COMPLEXES WITH
CMP; CYTIDINE AND PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT
ASN-149, AND DISULFIDE BONDS.
PubMed=23999306; DOI=10.1107/S0907444913015412;
Kuhn B., Benz J., Greif M., Engel A.M., Sobek H., Rudolph M.G.;
"The structure of human alpha-2,6-sialyltransferase reveals the
binding mode of complex glycans.";
Acta Crystallogr. D 69:1826-1838(2013).
-!- FUNCTION: Transfers sialic acid from CMP-sialic acid to galactose-
containing acceptor substrates. {ECO:0000269|PubMed:21081508,
ECO:0000269|PubMed:23999306}.
-!- CATALYTIC ACTIVITY: CMP-N-acetyl-beta-neuraminate + beta-D-
galactosyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-
galactosyl-R. {ECO:0000269|PubMed:21081508,
ECO:0000269|PubMed:23999306}.
-!- ENZYME REGULATION: Inhibited by CTP.
{ECO:0000269|PubMed:23999306}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=530 uM for CMP-NeuAc {ECO:0000269|PubMed:21081508};
Vmax=1.074 pmol/min/ug enzyme {ECO:0000269|PubMed:21081508};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane;
Single-pass type II membrane protein. Secreted. Note=Membrane-
bound form in trans cisternae of Golgi. Secreted into the body
fluid.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P15907-1; Sequence=Displayed;
Name=2;
IsoId=P15907-2; Sequence=VSP_056076;
Note=No experimental confirmation available.;
-!- PTM: The soluble form derives from the membrane form by
proteolytic processing.
-!- PTM: The HB-6, CDW75, and CD76 differentiation antigens are cell-
surface carbohydrate determinants generated by this enzyme.
-!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=ST6Gal I;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_628";
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EMBL; X17247; CAA35111.1; -; mRNA.
EMBL; X54363; CAA38246.1; -; mRNA.
EMBL; X62822; CAA44634.1; -; mRNA.
EMBL; AK292879; BAF85568.1; -; mRNA.
EMBL; AK312023; BAG34960.1; -; mRNA.
EMBL; AC007488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78160.1; -; Genomic_DNA.
EMBL; CH471052; EAW78161.1; -; Genomic_DNA.
EMBL; CH471052; EAW78162.1; -; Genomic_DNA.
EMBL; CH471052; EAW78164.1; -; Genomic_DNA.
EMBL; BC031476; AAH31476.1; -; mRNA.
EMBL; BC040009; AAH40009.1; -; mRNA.
CCDS; CCDS3285.1; -. [P15907-1]
CCDS; CCDS46973.1; -. [P15907-2]
PIR; A41734; A41734.
RefSeq; NP_003023.1; NM_003032.2. [P15907-1]
RefSeq; NP_775323.1; NM_173216.2. [P15907-1]
RefSeq; NP_775324.1; NM_173217.2. [P15907-2]
RefSeq; XP_005247776.1; XM_005247719.1. [P15907-1]
RefSeq; XP_005247777.1; XM_005247720.1. [P15907-1]
RefSeq; XP_006713797.1; XM_006713734.1. [P15907-1]
RefSeq; XP_011511387.1; XM_011513085.1. [P15907-1]
RefSeq; XP_011511388.1; XM_011513086.1. [P15907-1]
RefSeq; XP_016862554.1; XM_017007065.1. [P15907-1]
RefSeq; XP_016862555.1; XM_017007066.1. [P15907-1]
RefSeq; XP_016862556.1; XM_017007067.1. [P15907-1]
RefSeq; XP_016862557.1; XM_017007068.1. [P15907-1]
UniGene; Hs.207459; -.
PDB; 4JS1; X-ray; 2.09 A; A=89-406.
PDB; 4JS2; X-ray; 2.30 A; A=89-406.
PDBsum; 4JS1; -.
PDBsum; 4JS2; -.
ProteinModelPortal; P15907; -.
SMR; P15907; -.
BioGrid; 112374; 20.
IntAct; P15907; 2.
STRING; 9606.ENSP00000169298; -.
BindingDB; P15907; -.
ChEMBL; CHEMBL3596075; -.
CAZy; GT29; Glycosyltransferase Family 29.
iPTMnet; P15907; -.
PhosphoSitePlus; P15907; -.
BioMuta; ST6GAL1; -.
DMDM; 115445; -.
EPD; P15907; -.
MaxQB; P15907; -.
PaxDb; P15907; -.
PeptideAtlas; P15907; -.
PRIDE; P15907; -.
DNASU; 6480; -.
Ensembl; ENST00000169298; ENSP00000169298; ENSG00000073849. [P15907-1]
Ensembl; ENST00000448044; ENSP00000389337; ENSG00000073849. [P15907-1]
Ensembl; ENST00000457772; ENSP00000412221; ENSG00000073849. [P15907-2]
GeneID; 6480; -.
KEGG; hsa:6480; -.
UCSC; uc003frb.4; human. [P15907-1]
CTD; 6480; -.
DisGeNET; 6480; -.
EuPathDB; HostDB:ENSG00000073849.14; -.
GeneCards; ST6GAL1; -.
HGNC; HGNC:10860; ST6GAL1.
HPA; CAB015018; -.
HPA; CAB016122; -.
MIM; 109675; gene.
neXtProt; NX_P15907; -.
OpenTargets; ENSG00000073849; -.
PharmGKB; PA35762; -.
eggNOG; KOG2692; Eukaryota.
eggNOG; ENOG410XT8P; LUCA.
GeneTree; ENSGT00550000074444; -.
HOGENOM; HOG000013206; -.
HOVERGEN; HBG052853; -.
InParanoid; P15907; -.
KO; K00778; -.
OMA; SFQVWNK; -.
OrthoDB; EOG091G07C7; -.
PhylomeDB; P15907; -.
TreeFam; TF323961; -.
BioCyc; MetaCyc:HS01118-MONOMER; -.
BRENDA; 2.4.99.1; 2681.
Reactome; R-HSA-4085001; Sialic acid metabolism.
Reactome; R-HSA-975577; N-Glycan antennae elongation.
Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
UniPathway; UPA00378; -.
ChiTaRS; ST6GAL1; human.
GeneWiki; ST6GAL1; -.
GenomeRNAi; 6480; -.
PRO; PR:P15907; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000073849; -.
CleanEx; HS_ST6GAL1; -.
ExpressionAtlas; P15907; baseline and differential.
Genevisible; P15907; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0003835; F:beta-galactoside alpha-2,6-sialyltransferase activity; IDA:UniProtKB.
GO; GO:0008373; F:sialyltransferase activity; IDA:UniProtKB.
GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
GO; GO:0006054; P:N-acetylneuraminate metabolic process; IDA:UniProtKB.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
GO; GO:0097503; P:sialylation; IDA:UniProtKB.
Gene3D; 3.90.1480.20; -; 1.
InterPro; IPR001675; Glyco_trans_29.
InterPro; IPR038578; GT29-like_sf.
InterPro; IPR012163; Sialyl_trans.
Pfam; PF00777; Glyco_transf_29; 1.
PIRSF; PIRSF005557; Sialyl_trans; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
Phosphoprotein; Reference proteome; Secreted; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 406 Beta-galactoside alpha-2,6-
sialyltransferase 1.
/FTId=PRO_0000149249.
TOPO_DOM 1 9 Cytoplasmic.
TRANSMEM 10 26 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 27 406 Lumenal. {ECO:0000255}.
REGION 322 324 Substrate binding.
BINDING 189 189 Substrate; via amide nitrogen.
BINDING 212 212 Substrate.
BINDING 233 233 Substrate.
BINDING 353 353 Substrate; via carbonyl oxygen.
BINDING 354 354 Substrate.
BINDING 365 365 Substrate.
BINDING 369 369 Substrate. {ECO:0000305}.
BINDING 370 370 Substrate.
BINDING 376 376 Substrate.
MOD_RES 369 369 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
CARBOHYD 149 149 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:23999306}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 142 406 {ECO:0000269|PubMed:23999306}.
DISULFID 184 335 {ECO:0000269|PubMed:23999306}.
DISULFID 353 364 {ECO:0000269|PubMed:23999306}.
VAR_SEQ 1 231 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056076.
CONFLICT 27 27 K -> L (in Ref. 2; CAA38246).
{ECO:0000305}.
CONFLICT 72 73 HR -> T (in Ref. 2; CAA38246).
{ECO:0000305}.
CONFLICT 144 144 L -> P (in Ref. 2; CAA38246).
{ECO:0000305}.
HELIX 102 104 {ECO:0000244|PDB:4JS1}.
HELIX 107 118 {ECO:0000244|PDB:4JS1}.
HELIX 137 147 {ECO:0000244|PDB:4JS1}.
TURN 158 161 {ECO:0000244|PDB:4JS1}.
HELIX 163 165 {ECO:0000244|PDB:4JS1}.
TURN 166 168 {ECO:0000244|PDB:4JS1}.
HELIX 174 177 {ECO:0000244|PDB:4JS1}.
STRAND 181 187 {ECO:0000244|PDB:4JS1}.
HELIX 191 193 {ECO:0000244|PDB:4JS1}.
HELIX 199 202 {ECO:0000244|PDB:4JS1}.
STRAND 205 211 {ECO:0000244|PDB:4JS1}.
HELIX 220 223 {ECO:0000244|PDB:4JS1}.
STRAND 228 233 {ECO:0000244|PDB:4JS1}.
HELIX 234 239 {ECO:0000244|PDB:4JS1}.
HELIX 241 244 {ECO:0000244|PDB:4JS1}.
HELIX 247 250 {ECO:0000244|PDB:4JS1}.
STRAND 251 257 {ECO:0000244|PDB:4JS1}.
HELIX 266 271 {ECO:0000244|PDB:4JS1}.
HELIX 278 287 {ECO:0000244|PDB:4JS1}.
STRAND 293 296 {ECO:0000244|PDB:4JS1}.
HELIX 299 311 {ECO:0000244|PDB:4JS1}.
STRAND 312 314 {ECO:0000244|PDB:4JS1}.
HELIX 323 334 {ECO:0000244|PDB:4JS1}.
STRAND 335 344 {ECO:0000244|PDB:4JS1}.
STRAND 354 356 {ECO:0000244|PDB:4JS1}.
HELIX 363 366 {ECO:0000244|PDB:4JS1}.
STRAND 368 370 {ECO:0000244|PDB:4JS1}.
HELIX 372 382 {ECO:0000244|PDB:4JS1}.
HELIX 387 393 {ECO:0000244|PDB:4JS1}.
STRAND 395 399 {ECO:0000244|PDB:4JS1}.
HELIX 401 403 {ECO:0000244|PDB:4JS1}.
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


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EIAAB38432 Alpha 2,6-ST 2,Beta-galactoside alpha-2,6-sialyltransferase 2,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2,Rat,Rattus norvegicus,Sialyltransferase 2,ST6Gal II,St6gal2,ST6Ga
EIAAB38433 Alpha 2,6-ST 2,Beta-galactoside alpha-2,6-sialyltransferase 2,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2,Kiaa1877,Mouse,Mus musculus,Sialyltransferase 2,ST6Gal II,St6gal2
EIAAB38429 Alpha 2,6-ST 1,Beta-galactoside alpha-2,6-sialyltransferase 1,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1,Mouse,Mus musculus,Sialyltransferase 1,Siat1,ST6Gal I,St6gal1,ST6
EIAAB38435 Alpha 2,6-ST 2,Beta-galactoside alpha-2,6-sialyltransferase 2,Bos taurus,Bovine,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2,Sialyltransferase 2,ST6Gal II,ST6GAL2,ST6GalII
EIAAB38434 Alpha 2,6-ST 2,Beta-galactoside alpha-2,6-sialyltransferase 2,Chicken,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2,Gallus gallus,Sialyltransferase 2,ST6Gal II,ST6GAL2,ST6Ga
EIAAB38428 Alpha 2,6-ST 1,Beta-galactoside alpha-2,6-sialyltransferase 1,Chicken,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1,Gallus gallus,Sialyltransferase 1,SIAT1,ST6Gal I,ST6GAL1,
EIAAB38431 Alpha 2,6-ST 2,Beta-galactoside alpha-2,6-sialyltransferase 2,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2,Homo sapiens,hST6Gal II,Human,KIAA1877,Sialyltransferase 2,SIAT2,
EIAAB38376 Alpha 2,3-ST 1,Beta-galactoside alpha-2,3-sialyltransferase 1,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gal-NAc6S,Mouse,M
EIAAB38379 Alpha 2,3-ST 1,Beta-galactoside alpha-2,3-sialyltransferase 1,Chicken,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gallus ga
EIAAB38377 Alpha 2,3-ST 1,Beta-galactoside alpha-2,3-sialyltransferase 1,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gal-NAc6S,Homo sa
EIAAB38381 Alpha 2,3-ST 2,Beta-galactoside alpha-2,3-sialyltransferase 2,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gal-NAc6S,Mouse,M
EIAAB38382 Alpha 2,3-ST 2,Beta-galactoside alpha-2,3-sialyltransferase 2,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gal-NAc6S,Homo sa
EIAAB38383 Alpha 2,3-sialyltransferase IV,Alpha 2,3-ST 4,Beta-galactoside alpha-2,3-sialyltransferase 4,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4,Gal-beta-1,4-GalNAc-alpha-2,3-sial
EIAAB38384 Alpha 2,3-sialyltransferase IV,Alpha 2,3-ST 4,Beta-galactoside alpha-2,3-sialyltransferase 4,CGS23,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4,Gal-beta-1,4-GalNAc-alpha-2,
EIAAB38385 Alpha 2,3-sialyltransferase IV,Alpha 2,3-ST 4,Beta-galactoside alpha-2,3-sialyltransferase 4,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4,Gal-beta-1,4-GalNAc-alpha-2,3-sial
EIAAB38380 Alpha 2,3-ST 2,Beta-galactoside alpha-2,3-sialyltransferase 2,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gal-NAc6S,Rat,Rat
EIAAB38378 Alpha 2,3-ST 1,Beta-galactoside alpha-2,3-sialyltransferase 1,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gal-NAc6S,Pig,Sia
EIAAB38438 Alpha 2,3-ST 3,Beta-galactoside alpha-2,3-sialyltransferase 3,CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase,Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase,Mouse,Mus musc
EIAAB38437 Alpha 2,3-ST 3,Beta-galactoside alpha-2,3-sialyltransferase 3,CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase,Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase,Homo sapiens,H
EIAAB38436 Alpha 2,3-ST 3,Beta-galactoside alpha-2,3-sialyltransferase 3,CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase,Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase,N-acetyllactos
EIAAB38372 CMP-NeuAc beta-galactoside alpha-2,3-sialyltransferase VI,Mouse,Mus musculus,Sialyltransferase 10,Siat10,ST3Gal VI,St3gal6,ST3GalVI,Type 2 lactosamine alpha-2,3-sialyltransferase
EIAAB38373 CMP-NeuAc beta-galactoside alpha-2,3-sialyltransferase VI,Rat,Rattus norvegicus,Sialyltransferase 10,Siat10,ST3Gal VI,St3gal6,ST3GalVI,Type 2 lactosamine alpha-2,3-sialyltransferase
EIAAB38371 Bos taurus,Bovine,CMP-NeuAc beta-galactoside alpha-2,3-sialyltransferase VI,Sialyltransferase 10,SIAT10,ST3Gal VI,ST3GAL6,ST3GalVI,Type 2 lactosamine alpha-2,3-sialyltransferase


 

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