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Q62315

- JARD2_MOUSE

UniProt

Q62315 - JARD2_MOUSE

Protein

Protein Jumonji

Gene

Jarid2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Regulator of histone methyltransferase complexes that plays an essential role in embryonic development, including heart and liver development, neural tube fusion process and hematopoiesis. Acts by modulating histone methyltransferase activity and promoting the recruitment of histone methyltransferase complexes to their target genes. Binds DNA and mediates the recruitment of the PRC2 complex to target genes in embryonic stem cells. Does not have histone demethylase activity but regulates activity of various histone methyltransferase complexes. In embryonic stem cells, it associates with the PRC2 complex and inhibits trimethylation of 'Lys-27' of histone H3 (H3K27me3) by the PRC2 complex, thereby playing a key role in differentiation of embryonic stem cells and normal development. In cardiac cells, it is required to repress expression of cyclin-D1 (CCND1) by activating methylation of 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone methyltransferases. Also acts as a transcriptional repressor of ANF via its interaction with GATA4 and NKX2-5. Participates in the negative regulation of cell proliferation signaling.10 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. DNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. liver development Source: MGI
    3. negative regulation of cell proliferation Source: MGI
    4. negative regulation of histone methylation Source: UniProtKB
    5. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    7. positive regulation of histone H3-K9 methylation Source: UniProtKB
    8. regulation of cell proliferation Source: MGI
    9. spleen development Source: MGI
    10. stem cell differentiation Source: UniProtKB
    11. thymus development Source: MGI
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Developmental protein, Repressor

    Keywords - Biological processi

    Differentiation, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_222475. PRC2 methylates histones and DNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein Jumonji
    Alternative name(s):
    Jumonji/ARID domain-containing protein 2
    Gene namesi
    Name:Jarid2
    Synonyms:Jmj
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:104813. Jarid2.

    Subcellular locationi

    Nucleus 4 PublicationsPROSITE-ProRule annotation
    Note: Colocalizes with the PRC2 complex on chromatin.

    GO - Cellular componenti

    1. ESC/E(Z) complex Source: Ensembl
    2. histone methyltransferase complex Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Embryos die before 15.5 dpc and show severe cardiac morphological defects and altered heart-specific gene expression. Some, but not all, of the homozygotes develop an abnormal groove in a region just anterior to the midbrain-hindbrain boundary on the neural plate at 8-8.5 dpc and show a defect in neural tube closure in the midbrain region. Variable phenotypes are observed depending on the genetic backgrounds: mutant mice with a C57BL/6J X 129S1/Sv genetic background die upon birth and show cardiac defects such as ventricular septal defects, double-outlet right ventricle, and thin ventricular wall at later embryonic stages. In addition to the thin ventricular wall, mutant embryos with a pure BALB/c background show deficient cell growth in the liver, thymus, and spleen. In contrast, mutant mice with a C3H/He genetic background die at 11.5 dpc, which exhibit hyperplasia and increased cyclin-D1 (CCND1) expression in the trabecular layer of the ventricle at 10.5 dpc.4 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1072RK → AA: Leads to cytoplasmic relocalization. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12341234Protein JumonjiPRO_0000200592Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei78 – 781PhosphoserineBy similarity
    Modified residuei378 – 3781N6-acetyllysineBy similarity
    Modified residuei449 – 4491PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiQ62315.

    PTM databases

    PhosphoSiteiQ62315.

    Expressioni

    Tissue specificityi

    Widely expressed in embryos. In adults, expressed at high levels in heart, skeletal muscle, brain and thymus.1 Publication

    Gene expression databases

    ArrayExpressiQ62315.
    BgeeiQ62315.
    CleanExiMM_JARID2.
    GenevestigatoriQ62315.

    Interactioni

    Subunit structurei

    Associates with the PRC2 complex, which includes EED, EZH1, EZH2, SUZ12, RBBP4 and AEBP2; JARID2 is probably not a core component of the PRC2 complex and associates to PRC2 via its interaction with SUZ12. Associates with a histone methyltransferase complex containing GLP1/EHMT1 and G9a/EHMT2. Interacts with SUZ12; the interaction is direct. Interacts with GATA4 (via the N-terminal region). Interacts with NKX2-5 (via the C-terminal region). Interacts with RB1. Interacts with ZNF496.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EedQ921E610EBI-493592,EBI-904301
    Ezh1P703514EBI-493592,EBI-2531737
    Ezh2Q6118815EBI-493592,EBI-904311
    Gata4Q083693EBI-493592,EBI-297008
    Nkx2-5P425823EBI-493592,EBI-297021
    Suz12Q80U7012EBI-493592,EBI-2526494
    Znf496Q5SXI56EBI-493592,EBI-7417351

    Protein-protein interaction databases

    BioGridi200866. 18 interactions.
    DIPiDIP-34312N.
    IntActiQ62315. 20 interactions.
    MINTiMINT-4792531.

    Structurei

    Secondary structure

    1
    1234
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi621 – 63515
    Helixi653 – 66210
    Helixi666 – 6716
    Helixi675 – 6817
    Helixi691 – 70010
    Helixi703 – 7086
    Helixi711 – 72616

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RQ5NMR-A615-730[»]
    ProteinModelPortaliQ62315.
    SMRiQ62315. Positions 552-730, 803-1068.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ62315.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini555 – 59642JmjNPROSITE-ProRule annotationAdd
    BLAST
    Domaini619 – 71193ARIDPROSITE-ProRule annotationAdd
    BLAST
    Domaini882 – 1046165JmjCPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi104 – 1107Nuclear localization signal1 Publication
    Motifi872 – 8765GSGFP motif

    Domaini

    The ARID domain is required to target the PRC2 complex to its target genes.
    The GSGFP motif is required for the interaction with SUZ12.

    Sequence similaritiesi

    Belongs to the JARID2 family.Curated
    Contains 1 ARID domain.PROSITE-ProRule annotation
    Contains 1 JmjC domain.PROSITE-ProRule annotation
    Contains 1 JmjN domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG327026.
    GeneTreeiENSGT00530000063118.
    HOGENOMiHOG000013203.
    HOVERGENiHBG052160.
    InParanoidiQ3TPU4.
    KOiK11478.
    OMAiWAAMDEI.
    OrthoDBiEOG76MK7F.
    PhylomeDBiQ62315.
    TreeFamiTF323264.

    Family and domain databases

    Gene3Di1.10.150.60. 1 hit.
    InterProiIPR001606. ARID/BRIGHT_DNA-bd.
    IPR003347. JmjC_dom.
    IPR003349. TF_JmjN.
    IPR004198. Znf_C5HC2.
    [Graphical view]
    PfamiPF01388. ARID. 1 hit.
    PF02373. JmjC. 1 hit.
    PF02375. JmjN. 1 hit.
    PF02928. zf-C5HC2. 1 hit.
    [Graphical view]
    SMARTiSM00501. BRIGHT. 1 hit.
    SM00558. JmjC. 1 hit.
    SM00545. JmjN. 1 hit.
    [Graphical view]
    SUPFAMiSSF46774. SSF46774. 1 hit.
    PROSITEiPS51011. ARID. 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: Q62315-1) [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

    MSKERPKRNI IQKKYDDSDG IPWSEERVVR KVLYLSLKEF KNAQKRQHGE     50
    GLAGSLKAVN GLLGNAQAKA LGPASEQSEN EKDDASQVSS TSNDVSSSDF 100
    EEGPSRKRPR LQAQRKFAQS QPNSPSTTPV KIVEPLLPPP ATQISDLSKR 150
    KPKTEDFLTF LCLRGSPALP NSMVYFGSSQ DEEDVEEEDD ETEDVKATTN 200
    NASSSCQSTP RKGKTHKHVH NGHVFNGSSR SAREKEPAHK HRSKEATPGK 250
    EKHSEPRADS RREQASGAQP TAASAAASSA KGLAANHQPP PSHRSAQDLR 300
    KQVSKVNGVT RMSSLGAGTN SAKKIREVRP SPSKTVKYTA TVTKGTVTYT 350
    KAKRELVKET KPNHHKPSSA VNHTISGKTE SSNAKTRKQV LSLGGASKST 400
    GPAASGLKAS SRLNPKSCTK EVGGRQLREG LRNSKRRLEE AQQVDKPQSP 450
    PKKMKGVAGN AEAPGKKASA ASGEKSLLNG HVKKEVPERS LERNRPKRAA 500
    AGKNMLGKQA HGKTEGTPCE NRSTSQPESS HKPHDPQGKP EKGSGKSGWA 550
    AMDEIPVLRP SAKEFHDPLI YIESVRAQVE KYGMCRVIPP PDWRPECKLN 600
    DEMRFVTQIQ HIHKLGRRWG PNVQRLACIK KHLRSQGITM DELPLIGGCE 650
    LDLACFFRLI NEMGGMQQVT DLKKWNKLAD MLRIPKTAQD RLAKLQEAYC 700
    QYLLSYDSLS PEEHRRLEKE VLMEKEILEK RKGPLEGHTE SDHHKFHSLP 750
    RFEPKNGLVH GVTPRNGFRS KLKEVGRAPL KTGRRRLFAQ EKEVVKEEEE 800
    DKGVLNDFHK CIYKGRSVSL TTFYRTARNI MNMCFSKEPA PAEIEQEYWR 850
    LVEEKDCHVA VHCGKVDTNT HGSGFPVGKS EPFSRHGWNL TVLPNNTGSI 900
    LRHLGAVPGV TIPWLNIGMV FSTSCWSRDQ NHLPYIDYLH TGADCIWYCI 950
    PAEEENKLED VVHTLLQGNG TPGLQMLESN VMISPEVLCK KGIKVHRTVQ 1000
    QSGQFVVCFP GSFVSKVCCG YNVSETVHFA TTQWTSMGFE TAKEMKRRHI 1050
    AKPFSMEKLL YQIAQAEAKK ENGPTLSTIS ALLDELRDTE LRQRRLLFEA 1100
    GLHSSARYGS HDGNSTVADG KKKPRKWLQL ETSERRCQIC QHLCYLSMVV 1150
    QENENVVFCL ECALRHVEKQ KSCRGLKLMY RYDEEQIISL VNQICGKVSG 1200
    KHGGIENCLN KPTPKRGPRK RATVDVPPSR LPSS 1234
    Length:1,234
    Mass (Da):137,445
    Last modified:November 1, 1997 - v1
    Checksum:iB56E172C5E5745B5
    GO
    Isoform 2 (identifier: Q62315-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-60: MSKERPKRNI...GLAGSLKAVN → MAAPRVCQVQFLVAYLEEPGIE

    Show »
    Length:1,196
    Mass (Da):132,938
    Checksum:iDE32BC3F7733C6F5
    GO

    Sequence cautioni

    The sequence BAE27780.1 differs from that shown. Reason: Frameshift at position 11.
    The sequence EDL41007.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti873 – 8731S → G in BAE37641. (PubMed:16141072)Curated
    Sequence conflicti1096 – 10961L → Q in AAH03374. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6060MSKER…LKAVN → MAAPRVCQVQFLVAYLEEPG IE in isoform 2. 1 PublicationVSP_038758Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31967 mRNA. Translation: BAA06736.1.
    AK045214 mRNA. Translation: BAC32264.1.
    AK147226 mRNA. Translation: BAE27780.1. Frameshift.
    AK164134 mRNA. Translation: BAE37641.1.
    CH466546 Genomic DNA. Translation: EDL41007.1. Sequence problems.
    BC003374 mRNA. Translation: AAH03374.1.
    BC052444 mRNA. Translation: AAH52444.1.
    BC060695 mRNA. Translation: AAH60695.1.
    CCDSiCCDS36646.1. [Q62315-1]
    PIRiT30254.
    RefSeqiNP_001191972.1. NM_001205043.1. [Q62315-1]
    NP_001191973.1. NM_001205044.1. [Q62315-1]
    NP_068678.1. NM_021878.3. [Q62315-1]
    XP_006516918.1. XM_006516855.1. [Q62315-1]
    XP_006516919.1. XM_006516856.1. [Q62315-1]
    XP_006516920.1. XM_006516857.1. [Q62315-1]
    XP_006516921.1. XM_006516858.1. [Q62315-2]
    XP_006516922.1. XM_006516859.1.
    XP_006516923.1. XM_006516860.1.
    UniGeneiMm.25059.

    Genome annotation databases

    EnsembliENSMUST00000044608; ENSMUSP00000037774; ENSMUSG00000038518. [Q62315-1]
    ENSMUST00000173246; ENSMUSP00000134205; ENSMUSG00000038518. [Q62315-1]
    ENSMUST00000173704; ENSMUSP00000134675; ENSMUSG00000038518. [Q62315-1]
    GeneIDi16468.
    KEGGimmu:16468.
    UCSCiuc007qgr.2. mouse. [Q62315-1]
    uc007qgv.1. mouse. [Q62315-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31967 mRNA. Translation: BAA06736.1 .
    AK045214 mRNA. Translation: BAC32264.1 .
    AK147226 mRNA. Translation: BAE27780.1 . Frameshift.
    AK164134 mRNA. Translation: BAE37641.1 .
    CH466546 Genomic DNA. Translation: EDL41007.1 . Sequence problems.
    BC003374 mRNA. Translation: AAH03374.1 .
    BC052444 mRNA. Translation: AAH52444.1 .
    BC060695 mRNA. Translation: AAH60695.1 .
    CCDSi CCDS36646.1. [Q62315-1 ]
    PIRi T30254.
    RefSeqi NP_001191972.1. NM_001205043.1. [Q62315-1 ]
    NP_001191973.1. NM_001205044.1. [Q62315-1 ]
    NP_068678.1. NM_021878.3. [Q62315-1 ]
    XP_006516918.1. XM_006516855.1. [Q62315-1 ]
    XP_006516919.1. XM_006516856.1. [Q62315-1 ]
    XP_006516920.1. XM_006516857.1. [Q62315-1 ]
    XP_006516921.1. XM_006516858.1. [Q62315-2 ]
    XP_006516922.1. XM_006516859.1.
    XP_006516923.1. XM_006516860.1.
    UniGenei Mm.25059.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RQ5 NMR - A 615-730 [» ]
    ProteinModelPortali Q62315.
    SMRi Q62315. Positions 552-730, 803-1068.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200866. 18 interactions.
    DIPi DIP-34312N.
    IntActi Q62315. 20 interactions.
    MINTi MINT-4792531.

    PTM databases

    PhosphoSitei Q62315.

    Proteomic databases

    PRIDEi Q62315.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000044608 ; ENSMUSP00000037774 ; ENSMUSG00000038518 . [Q62315-1 ]
    ENSMUST00000173246 ; ENSMUSP00000134205 ; ENSMUSG00000038518 . [Q62315-1 ]
    ENSMUST00000173704 ; ENSMUSP00000134675 ; ENSMUSG00000038518 . [Q62315-1 ]
    GeneIDi 16468.
    KEGGi mmu:16468.
    UCSCi uc007qgr.2. mouse. [Q62315-1 ]
    uc007qgv.1. mouse. [Q62315-2 ]

    Organism-specific databases

    CTDi 3720.
    MGIi MGI:104813. Jarid2.

    Phylogenomic databases

    eggNOGi NOG327026.
    GeneTreei ENSGT00530000063118.
    HOGENOMi HOG000013203.
    HOVERGENi HBG052160.
    InParanoidi Q3TPU4.
    KOi K11478.
    OMAi WAAMDEI.
    OrthoDBi EOG76MK7F.
    PhylomeDBi Q62315.
    TreeFami TF323264.

    Enzyme and pathway databases

    Reactomei REACT_222475. PRC2 methylates histones and DNA.

    Miscellaneous databases

    ChiTaRSi JARID2. mouse.
    EvolutionaryTracei Q62315.
    NextBioi 289745.
    PROi Q62315.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q62315.
    Bgeei Q62315.
    CleanExi MM_JARID2.
    Genevestigatori Q62315.

    Family and domain databases

    Gene3Di 1.10.150.60. 1 hit.
    InterProi IPR001606. ARID/BRIGHT_DNA-bd.
    IPR003347. JmjC_dom.
    IPR003349. TF_JmjN.
    IPR004198. Znf_C5HC2.
    [Graphical view ]
    Pfami PF01388. ARID. 1 hit.
    PF02373. JmjC. 1 hit.
    PF02375. JmjN. 1 hit.
    PF02928. zf-C5HC2. 1 hit.
    [Graphical view ]
    SMARTi SM00501. BRIGHT. 1 hit.
    SM00558. JmjC. 1 hit.
    SM00545. JmjN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46774. SSF46774. 1 hit.
    PROSITEi PS51011. ARID. 1 hit.
    PS51184. JMJC. 1 hit.
    PS51183. JMJN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene trap capture of a novel mouse gene, jumonji, required for neural tube formation."
      Takeuchi T., Yamazaki Y., Katoh-Fukui Y., Tsuchiya R., Kondo S., Motoyama J., Higashinakagawa T.
      Genes Dev. 9:1211-1222(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE.
      Strain: 129/Ola.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1068 (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Embryo, Placenta and Spinal cord.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6 and Czech II.
      Tissue: Brain and Mammary gland.
    5. "Organogenesis of the liver, thymus and spleen is affected in jumonji mutant mice."
      Motoyama J., Kitajima K., Kojima M., Kondo S., Takeuchi T.
      Mech. Dev. 66:27-37(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    6. "jumonji gene is essential for the neurulation and cardiac development of mouse embryos with a C3H/He background."
      Takeuchi T., Kojima M., Nakajima K., Kondo S.
      Mech. Dev. 86:29-38(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    7. "Jumonji is a nuclear protein that participates in the negative regulation of cell growth."
      Toyoda M., Kojima M., Takeuchi T.
      Biochem. Biophys. Res. Commun. 274:332-336(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Jumonji, a nuclear protein that is necessary for normal heart development."
      Lee Y., Song A.J., Baker R., Micales B., Conway S.J., Lyons G.E.
      Circ. Res. 86:932-938(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    9. "jumonji downregulates cardiac cell proliferation by repressing cyclin D1 expression."
      Toyoda M., Shirato H., Nakajima K., Kojima M., Takahashi M., Kubota M., Suzuki-Migishima R., Motegi Y., Yokoyama M., Takeuchi T.
      Dev. Cell 5:85-97(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "JUMONJI, a critical factor for cardiac development, functions as a transcriptional repressor."
      Kim T.-G., Kraus J.C., Chen J., Lee Y.
      J. Biol. Chem. 278:42247-42255(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 106-ARG-LYS-107.
    11. "Jumonji represses atrial natriuretic factor gene expression by inhibiting transcriptional activities of cardiac transcription factors."
      Kim T.-G., Chen J., Sadoshima J., Lee Y.
      Mol. Cell. Biol. 24:10151-10160(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GATA4 AND NKX2-5.
    12. "Characterization of zinc finger protein 496 that interacts with Jumonji/JARID2."
      Mysliwiec M.R., Kim T.G., Lee Y.
      FEBS Lett. 581:2633-2640(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF496.
    13. "Jumonji regulates cardiomyocyte proliferation via interaction with retinoblastoma protein."
      Jung J., Kim T.G., Lyons G.E., Kim H.R., Lee Y.
      J. Biol. Chem. 280:30916-30923(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RB1.
    14. "Jumonji modulates polycomb activity and self-renewal versus differentiation of stem cells."
      Shen X., Kim W., Fujiwara Y., Simon M.D., Liu Y., Mysliwiec M.R., Yuan G.C., Lee Y., Orkin S.H.
      Cell 139:1303-1314(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, LACK OF HISTONE DEMETHYLASE ACTIVITY, SUBCELLULAR LOCATION, ASSOCIATION WITH THE PRC2 COMPLEX.
    15. "Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target gene occupancy in pluripotent cells."
      Peng J.C., Valouev A., Swigut T., Zhang J., Zhao Y., Sidow A., Wysocka J.
      Cell 139:1290-1302(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE PRC2 COMPLEX, DOMAIN GSGFP MOTIF, INTERACTION WITH SUZ12.
    16. "A jumonji (Jarid2) protein complex represses cyclin D1 expression by methylation of histone H3-K9."
      Shirato H., Ogawa S., Nakajima K., Inagawa M., Kojima M., Tachibana M., Shinkai Y., Takeuchi T.
      J. Biol. Chem. 284:733-739(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "JARID2 regulates binding of the Polycomb repressive complex 2 to target genes in ES cells."
      Pasini D., Cloos P.A., Walfridsson J., Olsson L., Bukowski J.P., Johansen J.V., Bak M., Tommerup N., Rappsilber J., Helin K.
      Nature 464:306-310(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, DOMAIN ARID.
    18. "Solution structure of the AT-rich interaction domain of Jumonji/JARID2."
      Kusunoki H., Takeuchi T., Kohno T.
      Proteins 76:1023-1028(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 615-730.

    Entry informationi

    Entry nameiJARD2_MOUSE
    AccessioniPrimary (citable) accession number: Q62315
    Secondary accession number(s): Q3TPU4, Q3UHS7, Q99LD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    'Jumonji' means 'cruciform' in Japanese.

    Caution

    Despite the presence of a JmjC domain, lacks the conserved residues that bind the iron cofactor, explaining the absence of histone methyltransferase activity.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3