Q8GUI6 (JMJ14_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable lysine-specific demethylase JMJ14
EC=1.14.11.-

Alternative name(s):
Jumonji domain-containing protein 14
Jumonji domain-containing protein 4
Lysine-specific histone demethylase JMJ14
Protein JUMONJI 14

Gene names

Name:	JMJ14
Synonyms:	JMJ4, PKDM7B
Ordered Locus Names:	At4g20400
ORF Names:	F9F13.50

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	954 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a higher activity for H3K4me3 and H3K4me2 than H3K4me1. No activity on H3K9me3/2, H3K36me3/2 and H3K27me3/2. Represses FT and TSF expression to inhibit the floral transition. Binds around the transcription start site of the FT locus. Involved in the DRM2-mediated maintenance of DNA methylation, but not required for the de novo DNA methylation. Required for demethylating histone H3K4me3 at the target of RNA silencing. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Cofactor	Fe2+. Ref.10
Subcellular location	Nucleus › nucleoplasm. Note: Not detected in the nucleolus and the chromocenters. Ref.6 Ref.7 Ref.8
Tissue specificity	Expressed in shoot apex, primary root tip, trichomes of young leaves, leaf vascular tissues, anther filaments and styles. Detected in inflorescences, leaves, stems, roots and siliques. Ref.5 Ref.6 Ref.10
Disruption phenotype	Early flowering, but normal development of all organs. Partially redundant with ELF6. Ref.6 Ref.7 Ref.10
Sequence similarities	Belongs to the JARID1 histone demethylase family. Contains 1 FYR C-terminal domain. Contains 1 FYR N-terminal domain. Contains 1 JmjC domain. Contains 1 JmjN domain.
Sequence caution	The sequence CAB45806.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB79040.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Iron
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	maintenance of DNA methylation Inferred from mutant phenotype Ref.8. Source: TAIR negative regulation of flower development Inferred from mutant phenotype Ref.10. Source: TAIR photoperiodism, flowering Inferred from mutant phenotype Ref.7. Source: TAIR transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	histone demethylase activity (H3-K4 specific) Inferred from direct assay Ref.7Ref.10. Source: TAIR oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Inferred from sequence or structural similarity PubMed 11118137. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8GUI6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8GUI6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-64: MDQLASLAESVAMEEDSEKQSIKGESSLEPDSTPSSPKITARWNPSEACRPLVDDAPIFYPTNE → MILLHGQ

Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 954	954	Probable lysine-specific demethylase JMJ14		PRO_0000412633
Regions
	Domain	56 – 97	42	JmjN
	Domain	263 – 429	167	JmjC
	Domain	726 – 784	59	FYR N-terminal
	Domain	786 – 876	91	FYR C-terminal
Natural variations
	Alternative sequence	1 – 64	64	MDQLA…YPTNE → MILLHGQ in isoform 2.		VSP_041728
Experimental info
	Mutagenesis	387	1	E → K in jmj14-3; loss of transgenic photobleaching phenotype due to RNA silencing. Ref.9
	Mutagenesis	397	1	H → A: Loss of demethylation activity. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 551B17E4D6FF336A	FASTA	954	108,156
	10 20 30 40 50 60 MDQLASLAES VAMEEDSEKQ SIKGESSLEP DSTPSSPKIT ARWNPSEACR PLVDDAPIFY 70 80 90 100 110 120 PTNEDFDDPL GYIEKLRSKA ESYGICRIVP PVAWRPPCPL KEKKIWENSK FPTRIQFIDL 130 140 150 160 170 180 LQNREPIKKS TKTKKRKRRR ISKIGYTRRK RDSGCDTASS GSSDSEGKFG FQTGPDFTLE 190 200 210 220 230 240 EFQKYDEYFK ECYFQSEDHP GSKASENKKF KPKVKDLEGE YWRIVEQATD EVEVYYGADL 250 260 270 280 290 300 ETKKFGSGFP KYKPGYPISE ADQYSQCGWN LNNLSRLPGS VLAFESCDIS GVIVPWLYVG 310 320 330 340 350 360 MCFSTFCWHV EDHHLYSMNY LHTGDPKVWY GIPGNHAESF ENVMKKRLPD LFEEQPDLLH 370 380 390 400 410 420 QLVTQLSPRI LKEEGVPVYR AVQRSGEFIL TFPKAYHSGF NCGFNCAEAV NVAPVDWLVH 430 440 450 460 470 480 GQNAVEGYSK QRRKSSLSHD KLLLGAAMEA TYCLWELSLS KKKTPVIARW KRVCSEDGLL 490 500 510 520 530 540 TKAVKKRVQM EEERLNHLQD GFSLRKMEGD FDNKRERECF LCFYDLHMSA SSCKCSPNRF 550 560 570 580 590 600 ACLIHAKDLC SCESKDRYIL IRHTLDELWA LVRALEGDLD AIDLWASKCR DQYPSQHPRA 610 620 630 640 650 660 REYAYLKSAP CIKSRGSSKV QQREQNNLQL VSERLQSDLT SNKEVQLKQD GDSDVNRHGH 670 680 690 700 710 720 ESERNHVHGI TDKSAVTDVK LGVGGKFDEK KISVESQNPH SVSDVGCSEL AKKVDGCLGG 730 740 750 760 770 780 KDQNAATNRL SLSVELLSSG SLVVKKLWCS KQAIYPKGFK SRVKFLSVLD PTNLTNYISE 790 800 810 820 830 840 VLDAGLLGPL FRVSVEDYPT ENFSNVSAEK CWQMVTQRLK LEIIKKCDQP VSSLTSLQPL 850 860 870 880 890 900 ESINGLEMFG FLSPHVIKVV EALDPKHQLE EYWNQKAVKL FGAEPIKEGE KDDTEKGGAS 910 920 930 940 950 DPSLDRDTRL LRGLLKKATP EELVMMHGLL CGETRNTELK EELSTLVDKM EISP
	Isoform 2 [UniParc]. Checksum: 167CE43E2EDFEDE6	FASTA	897	101,969
	10 20 30 40 50 60 MILLHGQDFD DPLGYIEKLR SKAESYGICR IVPPVAWRPP CPLKEKKIWE NSKFPTRIQF 70 80 90 100 110 120 IDLLQNREPI KKSTKTKKRK RRRISKIGYT RRKRDSGCDT ASSGSSDSEG KFGFQTGPDF 130 140 150 160 170 180 TLEEFQKYDE YFKECYFQSE DHPGSKASEN KKFKPKVKDL EGEYWRIVEQ ATDEVEVYYG 190 200 210 220 230 240 ADLETKKFGS GFPKYKPGYP ISEADQYSQC GWNLNNLSRL PGSVLAFESC DISGVIVPWL 250 260 270 280 290 300 YVGMCFSTFC WHVEDHHLYS MNYLHTGDPK VWYGIPGNHA ESFENVMKKR LPDLFEEQPD 310 320 330 340 350 360 LLHQLVTQLS PRILKEEGVP VYRAVQRSGE FILTFPKAYH SGFNCGFNCA EAVNVAPVDW 370 380 390 400 410 420 LVHGQNAVEG YSKQRRKSSL SHDKLLLGAA MEATYCLWEL SLSKKKTPVI ARWKRVCSED 430 440 450 460 470 480 GLLTKAVKKR VQMEEERLNH LQDGFSLRKM EGDFDNKRER ECFLCFYDLH MSASSCKCSP 490 500 510 520 530 540 NRFACLIHAK DLCSCESKDR YILIRHTLDE LWALVRALEG DLDAIDLWAS KCRDQYPSQH 550 560 570 580 590 600 PRAREYAYLK SAPCIKSRGS SKVQQREQNN LQLVSERLQS DLTSNKEVQL KQDGDSDVNR 610 620 630 640 650 660 HGHESERNHV HGITDKSAVT DVKLGVGGKF DEKKISVESQ NPHSVSDVGC SELAKKVDGC 670 680 690 700 710 720 LGGKDQNAAT NRLSLSVELL SSGSLVVKKL WCSKQAIYPK GFKSRVKFLS VLDPTNLTNY 730 740 750 760 770 780 ISEVLDAGLL GPLFRVSVED YPTENFSNVS AEKCWQMVTQ RLKLEIIKKC DQPVSSLTSL 790 800 810 820 830 840 QPLESINGLE MFGFLSPHVI KVVEALDPKH QLEEYWNQKA VKLFGAEPIK EGEKDDTEKG 850 860 870 880 890 GASDPSLDRD TRLLRGLLKK ATPEELVMMH GLLCGETRNT ELKEELSTLV DKMEISP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
[4]	"Evolutionary history of histone demethylase families: distinct evolutionary patterns suggest functional divergence." Zhou X., Ma H. BMC Evol. Biol. 8:294-294(2008) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[5]	"Comparative analysis of JmjC domain-containing proteins reveals the potential histone demethylases in Arabidopsis and rice." Lu F., Li G., Cui X., Liu C., Wang X.J., Cao X. J. Integr. Plant Biol. 50:886-896(2008) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY.
[6]	"Repression of FLOWERING LOCUS T chromatin by functionally redundant histone H3 lysine 4 demethylases in Arabidopsis." Jeong J.H., Song H.R., Ko J.H., Jeong Y.M., Kwon Y.E., Seol J.H., Amasino R.M., Noh B., Noh Y.S. PLoS ONE 4:E8033-E8033(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[7]	"JMJ14 is an H3K4 demethylase regulating flowering time in Arabidopsis." Lu F., Cui X., Zhang S., Liu C., Cao X. Cell Res. 20:387-390(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF HIS-397, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[8]	"Involvement of a Jumonji-C domain-containing histone demethylase in DRM2-mediated maintenance of DNA methylation." Deleris A., Greenberg M.V., Ausin I., Law R.W., Moissiard G., Schubert D., Jacobsen S.E. EMBO Rep. 11:950-955(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"JMJ14, a JmjC domain protein, is required for RNA silencing and cell-to-cell movement of an RNA silencing signal in Arabidopsis." Searle I.R., Pontes O., Melnyk C.W., Smith L.M., Baulcombe D.C. Genes Dev. 24:986-991(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-387.
[10]	"A plant-specific histone H3 lysine 4 demethylase represses the floral transition in Arabidopsis." Yang W., Jiang D., Jiang J., He Y. Plant J. 62:663-673(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL080253 Genomic DNA. Translation: CAB45806.1. Sequence problems. AL161553 Genomic DNA. Translation: CAB79040.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE84324.1. CP002687 Genomic DNA. Translation: AEE84325.1. BT002486 mRNA. Translation: AAO00846.1. BT010548 mRNA. Translation: AAQ65171.1.
IPI	IPI00516310. IPI00656704.
PIR	T10582.
RefSeq	NP_001031681.1. NM_001036604.1. NP_193773.2. NM_118159.2.
UniGene	At.43482.
3D structure databases
ProteinModelPortal	Q8GUI6.
SMR	Q8GUI6. Positions 59-425.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8GUI6. 1 interaction.
Proteomic databases
PaxDb	Q8GUI6.
PRIDE	Q8GUI6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G20400.1; AT4G20400.1; AT4G20400.
GeneID	827788.
KEGG	ath:AT4G20400.
Organism-specific databases
TAIR	At4g20400.
Phylogenomic databases
eggNOG	NOG327026.
HOGENOM	HOG000241335.
InParanoid	Q8GUI6.
KO	K11446.
OMA	VQRSGEF.
PhylomeDB	Q8GUI6.
ProtClustDB	CLSN2679960.
Gene expression databases
ArrayExpress	Q8GUI6.
Genevestigator	Q8GUI6.
Family and domain databases
InterPro	IPR003889. FYrich_C. IPR003888. FYrich_N. IPR003347. JmjC_dom. IPR003349. TF_JmjN. IPR004198. Znf_C5HC2. [Graphical view]
Pfam	PF05965. FYRC. 1 hit. PF05964. FYRN. 1 hit. PF02373. JmjC. 1 hit. PF02375. JmjN. 1 hit. PF02928. zf-C5HC2. 1 hit. [Graphical view]
SMART	SM00542. FYRC. 1 hit. SM00541. FYRN. 1 hit. SM00558. JmjC. 1 hit. SM00545. JmjN. 1 hit. [Graphical view]
PROSITE	PS51543. FYRC. 1 hit. PS51542. FYRN. 1 hit. PS51184. JMJC. 1 hit. PS51183. JMJN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

JMJ14_ARATH

Accession

Primary (citable) accession number: Q8GUI6
Secondary accession number(s): F4JUW8, Q9SUN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program