Sequence of JMJ24_ARATH
EC Number:2.3.2.27
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
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
0 MQVNFDETCD SVIRMNANEQ TRSANGIGNG NGESIPGIPD DLRCKRSDGK QWRCTAMSMA
60 DKTVCEKHYI QAKKRAANSA FRANQKKAKR RSSLGETDTY SEGKMDDFEL PVTSIDHYNN
120 GLASASKSNG RLEKRHNKSL MRYSPETPMM RSFSPRVAVD LNDDLGRDVV MFEEGYRSYR
180 TPPSVAVMDP TRNRSHQSTS PMEYSAASTD VSAESLGEIC HQCQRKDRER IISCLKCNQR
240 AFCHNCLSAR YSEISLEEVE KVCPACRGLC DCKSCLRSDN TIKVRIREIP VLDKLQYLYR
300 LLSAVLPVIK QIHLEQCMEV ELEKRLREVE IDLVRARLKA DEQMCCNVCR IPVVDYYRHC
360 PNCSYDLCLR CCQDLREESS VTISGTNQNV QDRKGAPKLK LNFSYKFPEW EANGDGSIPC
420 PPKEYGGCGS HSLNLARIFK MNWVAKLVKN AEEIVSGCKL SDLLNPDMCD SRFCKFAERE
480 ESGDNYVYSP SLETIKTDGV AKFEQQWAEG RLVTVKMVLD DSSCSRWDPE TIWRDIDELS
540 DEKLREHDPF LKAINCLDGL EVDVRLGEFT RAYKDGKNQE TGLPLLWKLK DWPSPSASEE
600 FIFYQRPEFI RSFPFLEYIH PRLGLLNVAA KLPHYSLQND SGPKIYVSCG TYQEISAGDS
660 LTGIHYNMRD MVYLLVHTSE ETTFERVRKT KPVPEEPDQK MSENESLLSP EQKLRDGELH
720 DLSLGEASME KNEPELALTV NPENLTENGD NMESSCTSSC AGGAQWDVFR RQDVPKLSGY
780 LQRTFQKPDN IQTDFVSRPL YEGLFLNEHH KRQLRDEFGV EPWTFEQHRG EAIFIPAGCP
840 FQITNLQSNI QVALDFLCPE SVGESARLAE EIRCLPNDHE AKLQILEIGK ISLYAASSAI
900 KEVQKLVLDP KFGAELGFED SNLTKAVSHN LDEATKRPQQ NSCT
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
560039
Theologis A.,Ecker J.R.,Palm C.J.,Federspiel N.A.,Kaul S.,White O.,Alonso J.,Altafi H.,Araujo R.,Bowman C.L.,Brooks S.Y.,Buehler E.,Chan A.,Chao Q.,Chen H.,Cheuk R.F.,Chin C.W.,Chung M.K.,Conn L.,Conway A.B.,Conway A.R.,Creasy T.H.,Dewar K.,Dunn P.,Etgu P.,Feldblyum T.V.,Feng J.-D.,Fong B.,Fujii C.Y.,Gill J.E.,Goldsmith A.D.,Haas B.,Hansen N.F.,Hughes B.,Huizar L.,Hunter J.L.,Jenkins J.,Johnson-Hopson C.,Khan S.,Khaykin E.,Kim C.J.,Koo H.L.,Kremenetskaia I.,Kurtz D.B.,Kwan A.,Lam B.,Langin-Hooper S.,Lee A.,Lee J.M.,Lenz C.A.,Li J.H.,Li Y.-P.,Lin X.,Liu S.X.,Liu Z.A.,Luros J.S.,Maiti R.,Marziali A.,Militscher J.,Miranda M.,Nguyen M.,Nierman W.C.,Osborne B.I.,Pai G.,Peterson J.,Pham P.K.,Rizzo M.,Rooney T.,Rowley D.,Sakano H.,Salzberg S.L.,Schwartz J.R.,Shinn P.,Southwick A.M.,Sun H.,Tallon L.J.,Tambunga G.,Toriumi M.J.,Town C.D.,Utterback T.,Van Aken S.,Vaysberg M.,Vysotskaia V.S.,Walker M.,Wu D.,Yu G.,Fraser C.M.,Venter J.C.,Davis R.W.
Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.
Nature
408
816-820
2000
560040
Cheng C.Y.,Krishnakumar V.,Chan A.P.,Thibaud-Nissen F.,Schobel S.,Town C.D.
Araport11: a complete reannotation of the Arabidopsis thaliana reference genome.
Plant J.
89
789-804
2017
560041
Iida K.,Fukami-Kobayashi K.,Toyoda A.,Sakaki Y.,Kobayashi M.,Seki M.,Shinozaki K.
Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs.
DNA Res.
16
155-164
2009
560044
Lu F.,Li G.,Cui X.,Liu C.,Wang X.-J.,Cao X.
Comparative analysis of JmjC domain-containing proteins reveals the potential histone demethylases in Arabidopsis and rice.
J. Integr. Plant Biol.
50
886-896
2008
560045
Deng S.,Xu J.,Liu J.,Kim S.-H.,Shi S.,Chua N.-H.
JMJ24 binds to RDR2 and is required for the basal level transcription of silenced loci in Arabidopsis.
Plant J.
83
770-782
2015
560046
Deng S.,Jang I.-C.,Su L.,Xu J.,Chua N.-H.
JMJ24 targets CHROMOMETHYLASE3 for proteasomal degradation in Arabidopsis.
Genes Dev.
30
251-256
2016
560047
Kabelitz T.,Brzezinka K.,Friedrich T.,Gorka M.,Graf A.,Kappel C.,Baeurle I.
A JUMONJI protein with E3 ligase and histone H3 binding activities affects transposon silencing in Arabidopsis.
Plant Physiol.
171
344-358
2016
560048
Audonnet L.,Shen Y.,Zhou D.-X.
JMJ24 antagonizes histone H3K9 demethylase IBM1/JMJ25 function and interacts with RNAi pathways for gene silencing.
Gene Expr. Patterns
25
1-7
2017
