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Sequence of UBP36_DROME

EC Number:3.4.19.12

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
ubiquitinyl hydrolase 1
Q9VRP5
Drosophila melanogaster
1038
114088
Reaction
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal)
Other sequences found for EC No. 3.4.19.12

General information:

Sequence
show sequence in fasta format
   0 MPVSMAVCET ANVVNAALRE SLGGNSSAGS STDQAKSGED TNGSLQNHIV ANAKRILMAK
  60 IEYEEVPNYH ESVLENLKSK YIVIKPGNPG AINGFSGKNN TGKLVGANGH DNNGARKQAE
 120 HPNNQSHHIN HHNHQHPTSN PNELPKPKRV LYPRENIRIG WKQSERKWQV GTGMINVGNT
 180 CYLNSTLQAL LHIPALANWL VSEQAHLADC NVAEPGSGCI ICAMTKTLLA TQSNQSAVRP
 240 FLIYSKLKQI CKHMVVGRQE DAHEFLRFLV EAMERAYLMR FRNYKELDQL VKETTPLGQI
 300 FGGYLRSEVR CLSCNHVSIT FQHFQDLLLD IRKADSLEDA FEGHFSRERL EDMGYKCEGC
 360 KKKVSATKQF SLERAPITLC IQLKRFSMIG NKLTKQISFK SRIDLSKYAA RSQAAQAQPL
 420 TYRLVSMVTH LGASQHCGHY TAIGSTDTGS FYNFDDSYVR PIAMHSVCNT NAYIMFFELD
 480 LSQAASPAAN RPNGVRLTNG HSTTPVPAAT VSSPSPTRFI GPQLPAGGAN GYTNGNAQKT
 540 AIQFKQQNQQ SPQNGLQLGT GKFQDTAKPP LVGAHAKGEA TSAPTANGNK SSSPSSNSSS
 600 NHKSINQQQY LPISSDDEDI EDEMKPRPTT AQLPSMPNMT ENHTEPKAKS PVKIQVKTPV
 660 KTPLKSLVPY ESASEEEEAP LPNPRKRPSG EDSSESDQES GQTNGHSKTN GSHTNGSASS
 720 SVHVNNSKQK TDAIDEIFKS LKKSADSDED DDEEEPSIQL TNGWHPQKQS QSQSKAPPSP
 780 KTPPSPAVIK SKTGIWKVTR NDEVDAIEDD VDVVVVEGSP VKIPTPNKNH RNPFSSSKPS
 840 TDSPATPGAK RQKLLNGSAL KSHQQPRVGN GYQSNATSNG STINELLKQS YRGYGSPVLS
 900 WNGKPAELEK ELLVDAREQR QRDIDDDEEN EMDRGRQRKV KSGSAKGNNA SNSTPGYNPF
 960 QEYEGQKRWN KNGGGGGFPR FYNQNYRQNF QQRNKFKFNR FGGPGSAKFQ QQRALQRHLS
1020 AGGGFSRRQP SAQQQQQT
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
114331
Adams M.D.,Celniker S.E.,Holt R.A.,Evans C.A.,Gocayne J.D.,Amanatides P.G.,Scherer S.E.,Li P.W.,Hoskins R.A.,Galle R.F.,George R.A.,Lewis S.E.,Richards S.,Ashburner M.,Henderson S.N.,Sutton G.G.,Wortman J.R.,Yandell M.D.,Zhang Q.,Chen L.X.,Brandon R.C.,Rogers Y.-H.C.,Blazej R.G.,Champe M.,Pfeiffer B.D.,Wan K.H.,Doyle C.,Baxter E.G.,Helt G.,Nelson C.R.,Miklos G.L.G.,Abril J.F.,Agbayani A.,An H.-J.,Andrews-Pfannkoch C.,Baldwin D.,Ballew R.M.,Basu A.,Baxendale J.,Bayraktaroglu L.,Beasley E.M.,Beeson K.Y.,Benos P.V.,Berman B.P.,Bhandari D.,Bolshakov S.,Borkova D.,Botchan M.R.,Bouck J.,Brokstein P.,Brottier P.,Burtis K.C.,Busam D.A.,Butler H.,Cadieu E.,Center A.,Chandra I.,Cherry J.M.,Cawley S.,Dahlke C.,Davenport L.B.,Davies P.,de Pablos B.,Delcher A.,Deng Z.,Mays A.D.,Dew I.,Dietz S.M.,Dodson K.,Doup L.E.,Downes M.,Dugan-Rocha S.,Dunkov B.C.,Dunn P.,Durbin K.J.,Evangelista C.C.,Ferraz C.,Ferriera S.,Fleischmann W.,Fosler C.,Gabrielian A.E.,Garg N.S.,Gelbart W.M.,Glasser K.,Glodek A.,Gong F.,Gorrell J.H.,Gu Z.,Guan P.,Harris M.,Harris N.L.,Harvey D.A.,Heiman T.J.,Hernandez J.R.,Houck J.,Hostin D.,Houston K.A.,Howland T.J.,Wei M.-H.,Ibegwam C.,Jalali M.,Kalush F.,Karpen G.H.,Ke Z.,Kennison J.A.,Ketchum K.A.,Kimmel B.E.,Kodira C.D.,Kraft C.L.,Kravitz S.,Kulp D.,Lai Z.,Lasko P.,Lei Y.,Levitsky A.A.,Li J.H.,Li Z.,Liang Y.,Lin X.,Liu X.,Mattei B.,McIntosh T.C.,McLeod M.P.,McPherson D.,Merkulov G.,Milshina N.V.,Mobarry C.,Morris J.,Moshrefi A.,Mount S.M.,Moy M.,Murphy B.,Murphy L.,Muzny D.M.,Nelson D.L.,Nelson D.R.,Nelson K.A.,Nixon K.,Nusskern D.R.,Pacleb J.M.,Palazzolo M.,Pittman G.S.,Pan S.,Pollard J.,Puri V.,Reese M.G.,Reinert K.,Remington K.,Saunders R.D.C.,Scheeler F.,Shen H.,Shue B.C.,Siden-Kiamos I.,Simpson M.,Skupski M.P.,Smith T.J.,Spier E.,Spradling A.C.,Stapleton M.,Strong R.,Sun E.,Svirskas R.,Tector C.,Turner R.,Venter E.,Wang A.H.,Wang X.,Wang Z.-Y.,Wassarman D.A.,Weinstock G.M.,Weissenbach J.,Williams S.M.,Woodage T.,Worley K.C.,Wu D.,Yang S.,Yao Q.A.,Ye J.,Yeh R.-F.,Zaveri J.S.,Zhan M.,Zhang G.,Zhao Q.,Zheng L.,Zheng X.H.,Zhong F.N.,Zhong W.,Zhou X.,Zhu S.C.,Zhu X.,Smith H.O.,Gibbs R.A.,Myers E.W.,Rubin G.M.,Venter J.C.
The genome sequence of Drosophila melanogaster.
Science
287
2185-2195
2000
114332
Misra S.,Crosby M.A.,Mungall C.J.,Matthews B.B.,Campbell K.S.,Hradecky P.,Huang Y.,Kaminker J.S.,Millburn G.H.,Prochnik S.E.,Smith C.D.,Tupy J.L.,Whitfield E.J.,Bayraktaroglu L.,Berman B.P.,Bettencourt B.R.,Celniker S.E.,de Grey A.D.N.J.,Drysdale R.A.,Harris N.L.,Richter J.,Russo S.,Schroeder A.J.,Shu S.Q.,Stapleton M.,Yamada C.,Ashburner M.,Gelbart W.M.,Rubin G.M.,Lewis S.E.
Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.
Genome Biol.
3
0-0
2002
114333
Stapleton M.,Carlson J.W.,Brokstein P.,Yu C.,Champe M.,George R.A.,Guarin H.,Kronmiller B.,Pacleb J.M.,Park S.,Wan K.H.,Rubin G.M.,Celniker S.E.
A Drosophila full-length cDNA resource.
Genome Biol.
3
0-0
2002
114335
Zhai B.,Villen J.,Beausoleil S.A.,Mintseris J.,Gygi S.P.
Phosphoproteome analysis of Drosophila melanogaster embryos.
J. Proteome Res.
7
1675-1682
2008
114336
Thevenon D.,Engel E.,Avet-Rochex A.,Gottar M.,Bergeret E.,Tricoire H.,Benaud C.,Baudier J.,Taillebourg E.,Fauvarque M.O.
The Drosophila ubiquitin-specific protease dUSP36/Scny targets IMD to prevent constitutive immune signaling.
Cell Host Microbe
6
309-320
2009
114337
Buszczak M.,Paterno S.,Spradling A.C.
Drosophila stem cells share a common requirement for the histone H2B ubiquitin protease scrawny.
Science
323
248-251
2009
114338
Taillebourg E.,Gregoire I.,Viargues P.,Jacomin A.C.,Thevenon D.,Faure M.,Fauvarque M.O.
The deubiquitinating enzyme USP36 controls selective autophagy activation by ubiquitinated proteins.
Autophagy
8
767-779
2012
114339
Engel E.,Viargues P.,Mortier M.,Taillebourg E.,Coute Y.,Thevenon D.,Fauvarque M.O.
Identifying USPs regulating immune signals in Drosophila: USP2 deubiquitinates Imd and promotes its degradation by interacting with the proteasome.
Cell Commun. Signal.
12
41-41
2014