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Q8GUI6

- JMJ14_ARATH

UniProt

Q8GUI6 - JMJ14_ARATH

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Protein

Probable lysine-specific demethylase JMJ14

Gene

JMJ14

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.5 Publications

Cofactori

Protein has several cofactor binding sites:
  • 2-oxoglutarate1 Publication
  • Fe2+1 PublicationNote: Binds 1 Fe(2+) ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi309 – 3091Iron; catalyticPROSITE-ProRule annotation
Metal bindingi311 – 3111Iron; catalyticPROSITE-ProRule annotation
Metal bindingi397 – 3971Iron; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. dioxygenase activity Source: UniProtKB-KW
  2. histone demethylase activity (H3-K4 specific) Source: TAIR
  3. metal ion binding Source: UniProtKB-KW
  4. sequence-specific DNA binding transcription factor activity Source: TAIR

GO - Biological processi

  1. histone H3-K4 demethylation Source: TAIR
  2. maintenance of DNA methylation Source: TAIR
  3. negative regulation of flower development Source: TAIR
  4. photoperiodism, flowering Source: TAIR
  5. regulation of transcription, DNA-templated Source: TAIR
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:JMJ14
Synonyms:JMJ4, PKDM7B
Ordered Locus Names:At4g20400
ORF Names:F9F13.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G20400.

Subcellular locationi

Nucleusnucleoplasm 3 Publications
Note: Not detected in the nucleolus and the chromocenters.

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Early flowering, but normal development of all organs. Partially redundant with ELF6.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi387 – 3871E → K in jmj14-3; loss of transgenic photobleaching phenotype due to RNA silencing. 1 Publication
Mutagenesisi397 – 3971H → A: Loss of demethylation activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 954954Probable lysine-specific demethylase JMJ14PRO_0000412633Add
BLAST

Proteomic databases

PaxDbiQ8GUI6.
PRIDEiQ8GUI6.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

GenevestigatoriQ8GUI6.

Interactioni

Protein-protein interaction databases

BioGridi13079. 1 interaction.
IntActiQ8GUI6. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8GUI6.
SMRiQ8GUI6. Positions 41-413.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 9742JmjNPROSITE-ProRule annotationAdd
BLAST
Domaini263 – 429167JmjCPROSITE-ProRule annotationAdd
BLAST
Domaini726 – 78459FYR N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini786 – 87691FYR C-terminalPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the JARID1 histone demethylase family.Curated
Contains 1 FYR C-terminal domain.PROSITE-ProRule annotation
Contains 1 FYR N-terminal domain.PROSITE-ProRule annotation
Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 1 JmjN domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG327026.
HOGENOMiHOG000241335.
InParanoidiQ8GUI6.
KOiK11446.
OMAiGHESERN.
PhylomeDBiQ8GUI6.

Family and domain databases

InterProiIPR003889. FYrich_C.
IPR003888. FYrich_N.
IPR003347. JmjC_dom.
IPR003349. TF_JmjN.
IPR004198. Znf_C5HC2.
[Graphical view]
PfamiPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view]
SMARTiSM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
[Graphical view]
PROSITEiPS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8GUI6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDQLASLAES VAMEEDSEKQ SIKGESSLEP DSTPSSPKIT ARWNPSEACR
60 70 80 90 100
PLVDDAPIFY PTNEDFDDPL GYIEKLRSKA ESYGICRIVP PVAWRPPCPL
110 120 130 140 150
KEKKIWENSK FPTRIQFIDL LQNREPIKKS TKTKKRKRRR ISKIGYTRRK
160 170 180 190 200
RDSGCDTASS GSSDSEGKFG FQTGPDFTLE EFQKYDEYFK ECYFQSEDHP
210 220 230 240 250
GSKASENKKF KPKVKDLEGE YWRIVEQATD EVEVYYGADL ETKKFGSGFP
260 270 280 290 300
KYKPGYPISE ADQYSQCGWN LNNLSRLPGS VLAFESCDIS GVIVPWLYVG
310 320 330 340 350
MCFSTFCWHV EDHHLYSMNY LHTGDPKVWY GIPGNHAESF ENVMKKRLPD
360 370 380 390 400
LFEEQPDLLH QLVTQLSPRI LKEEGVPVYR AVQRSGEFIL TFPKAYHSGF
410 420 430 440 450
NCGFNCAEAV NVAPVDWLVH GQNAVEGYSK QRRKSSLSHD KLLLGAAMEA
460 470 480 490 500
TYCLWELSLS KKKTPVIARW KRVCSEDGLL TKAVKKRVQM EEERLNHLQD
510 520 530 540 550
GFSLRKMEGD FDNKRERECF LCFYDLHMSA SSCKCSPNRF ACLIHAKDLC
560 570 580 590 600
SCESKDRYIL IRHTLDELWA LVRALEGDLD AIDLWASKCR DQYPSQHPRA
610 620 630 640 650
REYAYLKSAP CIKSRGSSKV QQREQNNLQL VSERLQSDLT SNKEVQLKQD
660 670 680 690 700
GDSDVNRHGH ESERNHVHGI TDKSAVTDVK LGVGGKFDEK KISVESQNPH
710 720 730 740 750
SVSDVGCSEL AKKVDGCLGG KDQNAATNRL SLSVELLSSG SLVVKKLWCS
760 770 780 790 800
KQAIYPKGFK SRVKFLSVLD PTNLTNYISE VLDAGLLGPL FRVSVEDYPT
810 820 830 840 850
ENFSNVSAEK CWQMVTQRLK LEIIKKCDQP VSSLTSLQPL ESINGLEMFG
860 870 880 890 900
FLSPHVIKVV EALDPKHQLE EYWNQKAVKL FGAEPIKEGE KDDTEKGGAS
910 920 930 940 950
DPSLDRDTRL LRGLLKKATP EELVMMHGLL CGETRNTELK EELSTLVDKM

EISP
Length:954
Mass (Da):108,156
Last modified:March 1, 2003 - v1
Checksum:i551B17E4D6FF336A
GO
Isoform 2 (identifier: Q8GUI6-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:897
Mass (Da):101,969
Checksum:i167CE43E2EDFEDE6
GO

Sequence cautioni

The sequence CAB45806.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB79040.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6464MDQLA…YPTNE → MILLHGQ in isoform 2. CuratedVSP_041728Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT10582.
RefSeqiNP_001031681.1. NM_001036604.1. [Q8GUI6-2]
NP_193773.2. NM_118159.2. [Q8GUI6-1]
UniGeneiAt.43482.

Genome annotation databases

EnsemblPlantsiAT4G20400.1; AT4G20400.1; AT4G20400. [Q8GUI6-1]
GeneIDi827788.
KEGGiath:AT4G20400.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi T10582.
RefSeqi NP_001031681.1. NM_001036604.1. [Q8GUI6-2 ]
NP_193773.2. NM_118159.2. [Q8GUI6-1 ]
UniGenei At.43482.

3D structure databases

ProteinModelPortali Q8GUI6.
SMRi Q8GUI6. Positions 41-413.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 13079. 1 interaction.
IntActi Q8GUI6. 1 interaction.

Proteomic databases

PaxDbi Q8GUI6.
PRIDEi Q8GUI6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G20400.1 ; AT4G20400.1 ; AT4G20400 . [Q8GUI6-1 ]
GeneIDi 827788.
KEGGi ath:AT4G20400.

Organism-specific databases

TAIRi AT4G20400.

Phylogenomic databases

eggNOGi NOG327026.
HOGENOMi HOG000241335.
InParanoidi Q8GUI6.
KOi K11446.
OMAi GHESERN.
PhylomeDBi Q8GUI6.

Gene expression databases

Genevestigatori Q8GUI6.

Family and domain databases

InterProi IPR003889. FYrich_C.
IPR003888. FYrich_N.
IPR003347. JmjC_dom.
IPR003349. TF_JmjN.
IPR004198. Znf_C5HC2.
[Graphical view ]
Pfami PF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view ]
SMARTi SM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
[Graphical view ]
PROSITEi PS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiJMJ14_ARATH
AccessioniPrimary (citable) accession number: Q8GUI6
Secondary accession number(s): F4JUW8, Q9SUN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3