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Q8GUI6 (JMJ14_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length954 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Nucleusnucleoplasm. 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 954954Probable lysine-specific demethylase JMJ14
PRO_0000412633

Regions

Domain56 – 9742JmjN
Domain263 – 429167JmjC
Domain726 – 78459FYR N-terminal
Domain786 – 87691FYR C-terminal

Natural variations

Alternative sequence1 – 6464MDQLA…YPTNE → MILLHGQ in isoform 2.
VSP_041728

Experimental info

Mutagenesis3871E → K in jmj14-3; loss of transgenic photobleaching phenotype due to RNA silencing. Ref.9
Mutagenesis3971H → A: Loss of demethylation activity. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 551B17E4D6FF336A

FASTA954108,156
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 167CE43E2EDFEDE6
Show »

FASTA897101,969

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
PIRT10582.
RefSeqNP_001031681.1. NM_001036604.1.
NP_193773.2. NM_118159.2.
UniGeneAt.43482.

3D structure databases

ProteinModelPortalQ8GUI6.
SMRQ8GUI6. Positions 41-455, 729-873.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13079. 1 interaction.
IntActQ8GUI6. 1 interaction.

Proteomic databases

PaxDbQ8GUI6.
PRIDEQ8GUI6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G20400.1; AT4G20400.1; AT4G20400. [Q8GUI6-1]
GeneID827788.
KEGGath:AT4G20400.

Organism-specific databases

TAIRAT4G20400.

Phylogenomic databases

eggNOGNOG327026.
HOGENOMHOG000241335.
InParanoidQ8GUI6.
KOK11446.
OMAGHESERN.
PhylomeDBQ8GUI6.
ProtClustDBCLSN2679960.

Gene expression databases

GenevestigatorQ8GUI6.

Family and domain databases

InterProIPR003889. FYrich_C.
IPR003888. FYrich_N.
IPR003347. JmjC_dom.
IPR003349. TF_JmjN.
IPR004198. Znf_C5HC2.
[Graphical view]
PfamPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view]
SMARTSM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
[Graphical view]
PROSITEPS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameJMJ14_ARATH
AccessionPrimary (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: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names