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

BRENDA support

Sequence of DOA10_YEAST

EC Number:2.3.2.27

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
2.3.2.27
RING-type E3 ubiquitin transferase
P40318
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1319
151455
Swiss-Prot
Reaction
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
Other sequences found for EC No. 2.3.2.27

General information:

Sequence
show sequence in fasta format
   0 MDVDSDVNVS RLRDELHKVA NEETDTATFN DDAPSGATCR ICRGEATEDN PLFHPCKCRG
  60 SIKYMHESCL LEWVASKNID ISKPGADVKC DICHYPIQFK TIYAENMPEK IPFSLLLSKS
 120 ILTFFEKARL ALTIGLAAVL YIIGVPLVWN MFGKLYTMML DGSSPYPGDF LKSLIYGYDQ
 180 SATPELTTRA IFYQLLQNHS FTSLQFIMIV ILHIALYFQY DMIVREDVFS KMVFHKIGPR
 240 LSPKDLKSRL KERFPMMDDR MVEYLAREMR AHDENRQEQG HDRLNMPAAA ADNNNNVINP
 300 RNDNVPPQDP NDHRNFENLR HVDELDHDEA TEEHENNDSD NSLPSGDDSS RILPGSSSDN
 360 EEDEEAEGQQ QQQQPEEEAD YRDHIEPNPI DMWANRRAQN EFDDLIAAQQ NAINRPNAPV
 420 FIPPPAQNRA GNVDQDEQDF GAAVGVPPAQ ANPDDQGQGP LVINLKLKLL NVIAYFIIAV
 480 VFTAIYLAIS YLFPTFIGFG LLKIYFGIFK VILRGLCHLY YLSGAHIAYN GLTKLVPKVD
 540 VAMSWISDHL IHDIIYLYNG YTENTMKHSI FIRALPALTT YLTSVSIVCA SSNLVSRGYG
 600 RENGMSNPTR RLIFQILFAL KCTFKVFTLF FIELAGFPIL AGVMLDFSLF CPILASNSRM
 660 LWVPSICAIW PPFSLFVYWT IGTLYMYWFA KYIGMIRKNI IRPGVLFFIR SPEDPNIKIL
 720 HDSLIHPMSI QLSRLCLSMF IYAIFIVLGF GFHTRIFFPF MLKSNLLSVP EAYKPTSIIS
 780 WKFNTILLTL YFTKRILESS SYVKPLLERY WKTIFKLCSR KLRLSSFILG KDTPTERGHI
 840 VYRNLFYKYI AAKNAEWSNQ ELFTKPKTLE QAEELFGQVR DVHAYFVPDG VLMRVPSSDI
 900 VSRNYVQTMF VPVTKDDKLL KPLDLERIKE RNKRAAGEFG YLDEQNTEYD QYYIVYVPPD
 960 FRLRYMTLLG LVWLFASILM LGVTFISQAL INFVCSFGFL PVVKLLLGER NKVYVAWKEL
1020 SDISYSYLNI YYVCVGSVCL SKIAKDILHF TEGQNTLDEH AVDENEVEEV EHDIPERDIN
1080 NAPVNNINNV EEGQGIFMAI FNSIFDSMLV KYNLMVFIAI MIAVIRTMVS WVVLTDGILA
1140 CYNYLTIRVF GNSSYTIGNS KWFKYDESLL FVVWIISSMV NFGTGYKSLK LFFRNRNTSK
1200 LNFLKTMALE LFKQGFLHMV IYVLPIIILS LVFLRDVSTK QIIDISHGSR SFTLSLNESF
1260 PTWTRMQDIY FGLLIALESF TFFFQATVLF IQWFKSTVQN VKDEVYTKGR ALENLPDES
Download this sequence
in fasta format
Download all sequences for 2.3.2.27
in fasta format
in csv (Excel, OpenOffice) format
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
26633
Mandart E.,Dufour M.-E.,Lacroute F.
Inactivation of SSM4, a new Saccharomyces cerevisiae gene, suppresses mRNA instability due to RNA14 mutations.
Mol. Gen. Genet.
245
323-333
1994
7816042
26634
Churcher C.M.,Bowman S.,Badcock K.,Bankier A.T.,Brown D.,Chillingworth T.,Connor R.,Devlin K.,Gentles S.,Hamlin N.,Harris D.E.,Horsnell T.,Hunt S.,Jagels K.,Jones M.,Lye G.,Moule S.,Odell C.,Pearson D.,Rajandream M.A.,Rice P.,Rowley N.,Skelton J.,Smith V.,Walsh S.V.,Whitehead S.,Barrell B.G.
The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.
Nature
387
84-87
1997
9169870
26635
Engel S.R.,Dietrich F.S.,Fisk D.G.,Binkley G.,Balakrishnan R.,Costanzo M.C.,Dwight S.S.,Hitz B.C.,Karra K.,Nash R.S.,Weng S.,Wong E.D.,Lloyd P.,Skrzypek M.S.,Miyasato S.R.,Simison M.,Cherry J.M.
The reference genome sequence of Saccharomyces cerevisiae: Then and now.
G3 (Bethesda)
4
389-398
2014
24374639
26636
Swanson R.,Locher M.,Hochstrasser M.
A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation.
Genes Dev.
15
2660-2674
2001
11641273
26637
Neuber O.,Jarosch E.,Volkwein C.,Walter J.,Sommer T.
Ubx2 links the Cdc48 complex to ER-associated protein degradation.
Nat. Cell Biol.
7
993-998
2005
16179953
26638
Schuberth C.,Buchberger A.
Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation.
Nat. Cell Biol.
7
999-1006
2005
16179952
26639
Carvalho P.,Goder V.,Rapoport T.A.
Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins.
Cell
126
361-373
2006
16873066
26640
Ravid T.,Kreft S.G.,Hochstrasser M.
Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways.
EMBO J.
25
533-543
2006
16437165
26641
Kreft S.G.,Wang L.,Hochstrasser M.
Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI).
J. Biol. Chem.
281
4646-4653
2006
16373356
26642
Deng M.,Hochstrasser M.
Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase.
Nature
443
827-831
2006
17051211
26643
Metzger M.B.,Maurer M.J.,Dancy B.M.,Michaelis S.
Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.
J. Biol. Chem.
283
32302-32316
2008
18812321
26644
Holt L.J.,Tuch B.B.,Villen J.,Johnson A.D.,Gygi S.P.,Morgan D.O.
Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.
Science
325
1682-1686
2009
19779198
26645
Liu C.,van Dyk D.,Xu P.,Choe V.,Pan H.,Peng J.,Andrews B.,Rao H.
Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates.
J. Biol. Chem.
285
10265-10272
2010
20159987
26646
Hwang C.S.,Shemorry A.,Varshavsky A.
N-terminal acetylation of cellular proteins creates specific degradation signals.
Science
327
973-977
2010
20110468
26647
Van Damme P.,Lasa M.,Polevoda B.,Gazquez C.,Elosegui-Artola A.,Kim D.S.,De Juan-Pardo E.,Demeyer K.,Hole K.,Larrea E.,Timmerman E.,Prieto J.,Arnesen T.,Sherman F.,Gevaert K.,Aldabe R.
N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
Proc. Natl. Acad. Sci. U.S.A.
109
12449-12454
2012
22814378
26648
Matsumoto S.,Nakatsukasa K.,Kakuta C.,Tamura Y.,Esaki M.,Endo T.
Msp1 clears mistargeted proteins by facilitating their transfer from mitochondria to the ER.
Mol. Cell
76
191-205
2019
31445887