Sequence of JMJ25_ARATH
EC Number:1.14.11.65
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
a [histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2 = a [histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
Other sequences found for EC No. 1.14.11.65
General information:
Sequence
0 MDSVEEEGVV RVEEENGRGG LRRHRRVSTK LANYVDPPTD DEEDGGPKRK GKRGGNRAPK
60 KTPKKDEEMQ KNEIDEANRV TGLVKEKRAA TKILNRKDSI IEVGEASGSM PKEVKGIRIG
120 KRKGEIDGEI PTKPGKKPKT TVDPRIIGYR PDNMCHQCQK SDRIVERCQT CNSKRYCHPC
180 LDTWYPLIAK EDVAKKCMFC SSTCNCRACL RLDTKLKGIN SNLIVSEEEK VQASKFILQS
240 LLPHLKGIND EQVAEKEVEA KIYGLKFEEV RPQDAKAFPD ERLYCDICKT SIYDLHRNCK
300 SCSFDICLSC CLEIRNGKAL ACKEDVSWNY INRGLEYEHG QEGKVIEKPA NKLDDKLKDK
360 LDGKPDDKPK GKPKGRPKGK PDDKPKGKLK GKQDDKPDDK PDEKPVNTDH MKYPSLWKAN
420 EAGIITCCCG AGELVLKRLL PDGWISELVN RVEKTAEAGE LLNLPETVLE RCPCSNSDRH
480 IDIDSCNLLK AACREGSEDN YLYSPSVWDV QQDDLKHFQH HWVKGEPVIV RNVLEATSGL
540 SWEPMVMHRA CRQISHVQHG SLKDVVAVDC LDFCEVKVNL HEFFTGYTDG RYDRMGWPLV
600 LKLKDWPPAK VFKDNLPRHA EEFLCSLPLK HYTHPVNGPL NLAVKLPQNC LKPDMGPKTY
660 VASGFAQELG RGDSVTKLHC DMSDAVNILT HISEVPNMQP GIGNLKKKHA EQDLKELYSS
720 VANKEEMMEI LENSRQQVQN VETDDGALWD IFRREDIPKL ESYIEKHHKE FRHLYCCPVS
780 QVVHPIHDQN FYLTRYHIMK LKEEYGIEPW TFNQKLGDAV LIPVGCPHQV RNLKSCNKVA
840 LDFVSPENVS ECLRLTKQYR LLPPNHFAKE DKLGVKKMIV HAVDKALRDL SGEKSPEPEE
900 KKQNMRGPKK GAAKAVAKAL KDLSPSEKKS SEAAEEEISN GIVNAIDKGL KDLPPSEEKS
960 SEAKVEISNG IVSAMDKDLE HISSSEKKST EEEGVKRPNI VRTYERRKKL GSEVTNAYID
1020 RLEMEKM
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
560049
Salanoubat M.,Lemcke K.,Rieger M.,Ansorge W.,Unseld M.,Fartmann B.,Valle G.,Bloecker H.,Perez-Alonso M.,Obermaier B.,Delseny M.,Boutry M.,Grivell L.A.,Mache R.,Puigdomenech P.,De Simone V.,Choisne N.,Artiguenave F.,Robert C.,Brottier P.,Wincker P.,Cattolico L.,Weissenbach J.,Saurin W.,Quetier F.,Schaefer M.,Mueller-Auer S.,Gabel C.,Fuchs M.,Benes V.,Wurmbach E.,Drzonek H.,Erfle H.,Jordan N.,Bangert S.,Wiedelmann R.,Kranz H.,Voss H.,Holland R.,Brandt P.,Nyakatura G.,Vezzi A.,D'Angelo M.,Pallavicini A.,Toppo S.,Simionati B.,Conrad A.,Hornischer K.,Kauer G.,Loehnert T.-H.,Nordsiek G.,Reichelt J.,Scharfe M.,Schoen O.,Bargues M.,Terol J.,Climent J.,Navarro P.,Collado C.,Perez-Perez A.,Ottenwaelder B.,Duchemin D.,Cooke R.,Laudie M.,Berger-Llauro C.,Purnelle B.,Masuy D.,de Haan M.,Maarse A.C.,Alcaraz J.-P.,Cottet A.,Casacuberta E.,Monfort A.,Argiriou A.,Flores M.,Liguori R.,Vitale D.,Mannhaupt G.,Haase D.,Schoof H.,Rudd S.,Zaccaria P.,Mewes H.-W.,Mayer K.F.X.,Kaul S.,Town C.D.,Koo H.L.,Tallon L.J.,Jenkins J.,Rooney T.,Rizzo M.,Walts A.,Utterback T.,Fujii C.Y.,Shea T.P.,Creasy T.H.,Haas B.,Maiti R.,Wu D.,Peterson J.,Van Aken S.,Pai G.,Militscher J.,Sellers P.,Gill J.E.,Feldblyum T.V.,Preuss D.,Lin X.,Nierman W.C.,Salzberg S.L.,White O.,Venter J.C.,Fraser C.M.,Kaneko T.,Nakamura Y.,Sato S.,Kato T.,Asamizu E.,Sasamoto S.,Kimura T.,Idesawa K.,Kawashima K.,Kishida Y.,Kiyokawa C.,Kohara M.,Matsumoto M.,Matsuno A.,Muraki A.,Nakayama S.,Nakazaki N.,Shinpo S.,Takeuchi C.,Wada T.,Watanabe A.,Yamada M.,Yasuda M.,Tabata S.
Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.
Nature
408
820-822
2000
560050
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
560051
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
560052
Saze H.,Shiraishi A.,Miura A.,Kakutani T.
Control of genic DNA methylation by a jmjC domain-containing protein in Arabidopsis thaliana.
Science
319
462-465
2008
560053
Miura A.,Nakamura M.,Inagaki S.,Kobayashi A.,Saze H.,Kakutani T.
An Arabidopsis jmjC domain protein protects transcribed genes from DNA methylation at CHG sites.
EMBO J.
28
1078-1086
2009
560054
Inagaki S.,Miura-Kamio A.,Nakamura Y.,Lu F.,Cui X.,Cao X.,Kimura H.,Saze H.,Kakutani T.
Autocatalytic differentiation of epigenetic modifications within the Arabidopsis genome.
EMBO J.
29
3496-3506
2010
560055
Rigal M.,Kevei Z.,Pelissier T.,Mathieu O.
DNA methylation in an intron of the IBM1 histone demethylase gene stabilizes chromatin modification patterns.
EMBO J.
31
2981-2993
2012
560056
Fan D.,Dai Y.,Wang X.,Wang Z.,He H.,Yang H.,Cao Y.,Deng X.W.,Ma L.
IBM1, a JmjC domain-containing histone demethylase, is involved in the regulation of RNA-directed DNA methylation through the epigenetic control of RDR2 and DCL3 expression in Arabidopsis.
Nucleic Acids Res.
40
8905-8916
2012
560057
Wang X.,Duan C.-G.,Tang K.,Wang B.,Zhang H.,Lei M.,Lu K.,Mangrauthia S.K.,Wang P.,Zhu G.,Zhao Y.,Zhu J.-K.
RNA-binding protein regulates plant DNA methylation by controlling mRNA processing at the intronic heterochromatin-containing gene IBM1.
Proc. Natl. Acad. Sci. U.S.A.
110
15467-15472
2013
560058
Coustham V.,Vlad D.,Deremetz A.,Gy I.,Cubillos F.A.,Kerdaffrec E.,Loudet O.,Bouche N.
SHOOT GROWTH1 maintains Arabidopsis epigenomes by regulating IBM1.
PLoS ONE
9
0-0
2014
560059
Wang Y.,Xue X.,Zhu J.-K.,Dong J.
Demethylation of ERECTA receptor genes by IBM1 histone demethylase affects stomatal development.
Development
143
4452-4461
2016
560060
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
560061
Butel N.,Yu A.,Le Masson I.,Borges F.,Elmayan T.,Taochy C.,Gursanscky N.R.,Cao J.,Bi S.,Sawyer A.,Carroll B.J.,Vaucheret H.
Contrasting epigenetic control of transgenes and endogenous genes promotes post-transcriptional transgene silencing in Arabidopsis.
Nat. Commun.
12
2787-2787
2021
