Any feedback?
Please rate this page
(sequences.php)
(0/150)

BRENDA support

Sequence of SIAT1_RAT

EC Number:2.4.3.1

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
beta-galactoside alpha-(2,6)-sialyltransferase
P13721
Rattus norvegicus
403
46754
Reaction
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-R
Other sequences found for EC No. 2.4.3.1

General information:

Sequence
show sequence in fasta format
  0 MIHTNLKKKF SLFILVFLLF AVICVWKKGS DYEALTLQAK EFQMPKSQEK VAMGSASQVV
 60 FSNSKQDPKE DIPILSYHRV TAKVKPQPSF QVWDKDSTYS KLNPRLLKIW RNYLNMNKYK
120 VSYKGPGPGV KFSVEALRCH LRDHVNVSMI EATDFPFNTT EWEGYLPKEN FRTKVGPWQR
180 CAVVSSAGSL KNSQLGREID NHDAVLRFNG APTDNFQQDV GSKTTIRLMN SQLVTTEKRF
240 LKDSLYTEGI LIVWDPSVYH ADIPKWYQKP DYNFFETYKS YRRLNPSQPF YILKPQMPWE
300 LWDIIQEISA DLIQPNPPSS GMLGIIIMMT LCDQVDIYEF LPSKRKTDVC YYHQKFFDSA
360 CTMGAYHPLL FEKNMVKHLN EGTDEDIYLF GKATLSGFRN IRC
Download this sequence
in fasta format
Download all sequences for 2.4.3.1
in fasta format
in csv (Excel, OpenOffice) format
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
358623
Weinstein J.,Lee E.U.,McEntee K.,Lai P.-H.,Paulson J.C.
Primary structure of beta-galactoside alpha 2,6-sialyltransferase. Conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor.
J. Biol. Chem.
262
17735-17743
1987
358624
Wen D.X.,Svensson E.C.,Paulson J.C.
Tissue-specific alternative splicing of the beta-galactoside alpha 2,6-sialyltransferase gene.
J. Biol. Chem.
267
2512-2518
1992
358625
Gibbs R.A.,Weinstock G.M.,Metzker M.L.,Muzny D.M.,Sodergren E.J.,Scherer S.,Scott G.,Steffen D.,Worley K.C.,Burch P.E.,Okwuonu G.,Hines S.,Lewis L.,Deramo C.,Delgado O.,Dugan-Rocha S.,Miner G.,Morgan M.,Hawes A.,Gill R.,Holt R.A.,Adams M.D.,Amanatides P.G.,Baden-Tillson H.,Barnstead M.,Chin S.,Evans C.A.,Ferriera S.,Fosler C.,Glodek A.,Gu Z.,Jennings D.,Kraft C.L.,Nguyen T.,Pfannkoch C.M.,Sitter C.,Sutton G.G.,Venter J.C.,Woodage T.,Smith D.,Lee H.-M.,Gustafson E.,Cahill P.,Kana A.,Doucette-Stamm L.,Weinstock K.,Fechtel K.,Weiss R.B.,Dunn D.M.,Green E.D.,Blakesley R.W.,Bouffard G.G.,De Jong P.J.,Osoegawa K.,Zhu B.,Marra M.,Schein J.,Bosdet I.,Fjell C.,Jones S.,Krzywinski M.,Mathewson C.,Siddiqui A.,Wye N.,McPherson J.,Zhao S.,Fraser C.M.,Shetty J.,Shatsman S.,Geer K.,Chen Y.,Abramzon S.,Nierman W.C.,Havlak P.H.,Chen R.,Durbin K.J.,Egan A.,Ren Y.,Song X.-Z.,Li B.,Liu Y.,Qin X.,Cawley S.,Cooney A.J.,D'Souza L.M.,Martin K.,Wu J.Q.,Gonzalez-Garay M.L.,Jackson A.R.,Kalafus K.J.,McLeod M.P.,Milosavljevic A.,Virk D.,Volkov A.,Wheeler D.A.,Zhang Z.,Bailey J.A.,Eichler E.E.,Tuzun E.,Birney E.,Mongin E.,Ureta-Vidal A.,Woodwark C.,Zdobnov E.,Bork P.,Suyama M.,Torrents D.,Alexandersson M.,Trask B.J.,Young J.M.,Huang H.,Wang H.,Xing H.,Daniels S.,Gietzen D.,Schmidt J.,Stevens K.,Vitt U.,Wingrove J.,Camara F.,Mar Alba M.,Abril J.F.,Guigo R.,Smit A.,Dubchak I.,Rubin E.M.,Couronne O.,Poliakov A.,Huebner N.,Ganten D.,Goesele C.,Hummel O.,Kreitler T.,Lee Y.-A.,Monti J.,Schulz H.,Zimdahl H.,Himmelbauer H.,Lehrach H.,Jacob H.J.,Bromberg S.,Gullings-Handley J.,Jensen-Seaman M.I.,Kwitek A.E.,Lazar J.,Pasko D.,Tonellato P.J.,Twigger S.,Ponting C.P.,Duarte J.M.,Rice S.,Goodstadt L.,Beatson S.A.,Emes R.D.,Winter E.E.,Webber C.,Brandt P.,Nyakatura G.,Adetobi M.,Chiaromonte F.,Elnitski L.,Eswara P.,Hardison R.C.,Hou M.,Kolbe D.,Makova K.,Miller W.,Nekrutenko A.,Riemer C.,Schwartz S.,Taylor J.,Yang S.,Zhang Y.,Lindpaintner K.,Andrews T.D.,Caccamo M.,Clamp M.,Clarke L.,Curwen V.,Durbin R.M.,Eyras E.,Searle S.M.,Cooper G.M.,Batzoglou S.,Brudno M.,Sidow A.,Stone E.A.,Payseur B.A.,Bourque G.,Lopez-Otin C.,Puente X.S.,Chakrabarti K.,Chatterji S.,Dewey C.,Pachter L.,Bray N.,Yap V.B.,Caspi A.,Tesler G.,Pevzner P.A.,Haussler D.,Roskin K.M.,Baertsch R.,Clawson H.,Furey T.S.,Hinrichs A.S.,Karolchik D.,Kent W.J.,Rosenbloom K.R.,Trumbower H.,Weirauch M.,Cooper D.N.,Stenson P.D.,Ma B.,Brent M.,Arumugam M.,Shteynberg D.,Copley R.R.,Taylor M.S.,Riethman H.,Mudunuri U.,Peterson J.,Guyer M.,Felsenfeld A.,Old S.,Mockrin S.,Collins F.S.
Genome sequence of the Brown Norway rat yields insights into mammalian evolution.
Nature
428
493-521
2004
358627
Wang X.,O'Hanlon T.P.,Young R.F.,Lau J.T.Y.
Rat beta-galactoside alpha 2,6-sialyltransferase genomic organization: alternate promoters direct the synthesis of liver and kidney transcripts.
Glycobiology
1
25-31
1990
358628
O'Hanlon T.P.,Lau K.M.,Wang X.,Lau J.T.Y.
Tissue-specific expression of beta-galactoside alpha-2,6-sialyltransferase. Transcript heterogeneity predicts a divergent polypeptide.
J. Biol. Chem.
264
17389-17394
1989
358629
Datta A.K.,Chammas R.,Paulson J.C.
Conserved cysteines in the sialyltransferase sialylmotifs form an essential disulfide bond.
J. Biol. Chem.
276
15200-15207
2001
358630
Meng L.,Forouhar F.,Thieker D.,Gao Z.,Ramiah A.,Moniz H.,Xiang Y.,Seetharaman J.,Milaninia S.,Su M.,Bridger R.,Veillon L.,Azadi P.,Kornhaber G.,Wells L.,Montelione G.T.,Woods R.J.,Tong L.,Moremen K.W.
Enzymatic basis for N-glycan sialylation: structure of rat alpha2,6-sialyltransferase (ST6GAL1) reveals conserved and unique features for glycan sialylation.
J. Biol. Chem.
288
34680-34698
2013