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
RING-type E3 ubiquitin transferase
P40318
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1319
151455
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 normal format
>P40318|RING-type E3 ubiquitin transferase|EC 2.3.2.27|Saccharomyces cerevisiae (strain ATCC 204508 / S288c)|Swiss-Prot
MDVDSDVNVSRLRDELHKVANEETDTATFNDDAPSGATCRICRGEATEDNPLFHPCKCRG
SIKYMHESCLLEWVASKNIDISKPGADVKCDICHYPIQFKTIYAENMPEKIPFSLLLSKS
ILTFFEKARLALTIGLAAVLYIIGVPLVWNMFGKLYTMMLDGSSPYPGDFLKSLIYGYDQ
SATPELTTRAIFYQLLQNHSFTSLQFIMIVILHIALYFQYDMIVREDVFSKMVFHKIGPR
LSPKDLKSRLKERFPMMDDRMVEYLAREMRAHDENRQEQGHDRLNMPAAAADNNNNVINP
RNDNVPPQDPNDHRNFENLRHVDELDHDEATEEHENNDSDNSLPSGDDSSRILPGSSSDN
EEDEEAEGQQQQQQPEEEADYRDHIEPNPIDMWANRRAQNEFDDLIAAQQNAINRPNAPV
FIPPPAQNRAGNVDQDEQDFGAAVGVPPAQANPDDQGQGPLVINLKLKLLNVIAYFIIAV
VFTAIYLAISYLFPTFIGFGLLKIYFGIFKVILRGLCHLYYLSGAHIAYNGLTKLVPKVD
VAMSWISDHLIHDIIYLYNGYTENTMKHSIFIRALPALTTYLTSVSIVCASSNLVSRGYG
RENGMSNPTRRLIFQILFALKCTFKVFTLFFIELAGFPILAGVMLDFSLFCPILASNSRM
LWVPSICAIWPPFSLFVYWTIGTLYMYWFAKYIGMIRKNIIRPGVLFFIRSPEDPNIKIL
HDSLIHPMSIQLSRLCLSMFIYAIFIVLGFGFHTRIFFPFMLKSNLLSVPEAYKPTSIIS
WKFNTILLTLYFTKRILESSSYVKPLLERYWKTIFKLCSRKLRLSSFILGKDTPTERGHI
VYRNLFYKYIAAKNAEWSNQELFTKPKTLEQAEELFGQVRDVHAYFVPDGVLMRVPSSDI
VSRNYVQTMFVPVTKDDKLLKPLDLERIKERNKRAAGEFGYLDEQNTEYDQYYIVYVPPD
FRLRYMTLLGLVWLFASILMLGVTFISQALINFVCSFGFLPVVKLLLGERNKVYVAWKEL
SDISYSYLNIYYVCVGSVCLSKIAKDILHFTEGQNTLDEHAVDENEVEEVEHDIPERDIN
NAPVNNINNVEEGQGIFMAIFNSIFDSMLVKYNLMVFIAIMIAVIRTMVSWVVLTDGILA
CYNYLTIRVFGNSSYTIGNSKWFKYDESLLFVVWIISSMVNFGTGYKSLKLFFRNRNTSK
LNFLKTMALELFKQGFLHMVIYVLPIIILSLVFLRDVSTKQIIDISHGSRSFTLSLNESF
PTWTRMQDIYFGLLIALESFTFFFQATVLFIQWFKSTVQNVKDEVYTKGRALENLPDES
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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
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
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
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
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
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
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
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
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
26642
Deng M.,Hochstrasser M.
Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase.
Nature
443
827-831
2006
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
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
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
26646
Hwang C.S.,Shemorry A.,Varshavsky A.
N-terminal acetylation of cellular proteins creates specific degradation signals.
Science
327
973-977
2010
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
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
