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Q8GUI6

- JMJ14_ARATH

UniProt

Q8GUI6 - JMJ14_ARATH

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
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    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

    Fe2+.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. 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

    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. nucleoplasm Source: UniProtKB-SubCell

    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

    MDQLASLAES VAMEEDSEKQ SIKGESSLEP DSTPSSPKIT ARWNPSEACR    50
    PLVDDAPIFY PTNEDFDDPL GYIEKLRSKA ESYGICRIVP PVAWRPPCPL 100
    KEKKIWENSK FPTRIQFIDL LQNREPIKKS TKTKKRKRRR ISKIGYTRRK 150
    RDSGCDTASS GSSDSEGKFG FQTGPDFTLE EFQKYDEYFK ECYFQSEDHP 200
    GSKASENKKF KPKVKDLEGE YWRIVEQATD EVEVYYGADL ETKKFGSGFP 250
    KYKPGYPISE ADQYSQCGWN LNNLSRLPGS VLAFESCDIS GVIVPWLYVG 300
    MCFSTFCWHV EDHHLYSMNY LHTGDPKVWY GIPGNHAESF ENVMKKRLPD 350
    LFEEQPDLLH QLVTQLSPRI LKEEGVPVYR AVQRSGEFIL TFPKAYHSGF 400
    NCGFNCAEAV NVAPVDWLVH GQNAVEGYSK QRRKSSLSHD KLLLGAAMEA 450
    TYCLWELSLS KKKTPVIARW KRVCSEDGLL TKAVKKRVQM EEERLNHLQD 500
    GFSLRKMEGD FDNKRERECF LCFYDLHMSA SSCKCSPNRF ACLIHAKDLC 550
    SCESKDRYIL IRHTLDELWA LVRALEGDLD AIDLWASKCR DQYPSQHPRA 600
    REYAYLKSAP CIKSRGSSKV QQREQNNLQL VSERLQSDLT SNKEVQLKQD 650
    GDSDVNRHGH ESERNHVHGI TDKSAVTDVK LGVGGKFDEK KISVESQNPH 700
    SVSDVGCSEL AKKVDGCLGG KDQNAATNRL SLSVELLSSG SLVVKKLWCS 750
    KQAIYPKGFK SRVKFLSVLD PTNLTNYISE VLDAGLLGPL FRVSVEDYPT 800
    ENFSNVSAEK CWQMVTQRLK LEIIKKCDQP VSSLTSLQPL ESINGLEMFG 850
    FLSPHVIKVV EALDPKHQLE EYWNQKAVKL FGAEPIKEGE KDDTEKGGAS 900
    DPSLDRDTRL LRGLLKKATP EELVMMHGLL CGETRNTELK EELSTLVDKM 950
    EISP 954
    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.
    The sequence CAB79040.1 differs from that shown. Reason: Erroneous gene model prediction.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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

    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: October 1, 2014
    This is version 88 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