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Q62315

- JARD2_MOUSE

UniProt

Q62315 - JARD2_MOUSE

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Protein

Protein Jumonji

Gene

Jarid2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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
Complete GO annotation...

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

MaxQBiQ62315.
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

BgeeiQ62315.
CleanExiMM_JARID2.
ExpressionAtlasiQ62315. baseline and differential.
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.
InParanoidiQ62315.
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

        10         20         30         40         50
MSKERPKRNI IQKKYDDSDG IPWSEERVVR KVLYLSLKEF KNAQKRQHGE
60 70 80 90 100
GLAGSLKAVN GLLGNAQAKA LGPASEQSEN EKDDASQVSS TSNDVSSSDF
110 120 130 140 150
EEGPSRKRPR LQAQRKFAQS QPNSPSTTPV KIVEPLLPPP ATQISDLSKR
160 170 180 190 200
KPKTEDFLTF LCLRGSPALP NSMVYFGSSQ DEEDVEEEDD ETEDVKATTN
210 220 230 240 250
NASSSCQSTP RKGKTHKHVH NGHVFNGSSR SAREKEPAHK HRSKEATPGK
260 270 280 290 300
EKHSEPRADS RREQASGAQP TAASAAASSA KGLAANHQPP PSHRSAQDLR
310 320 330 340 350
KQVSKVNGVT RMSSLGAGTN SAKKIREVRP SPSKTVKYTA TVTKGTVTYT
360 370 380 390 400
KAKRELVKET KPNHHKPSSA VNHTISGKTE SSNAKTRKQV LSLGGASKST
410 420 430 440 450
GPAASGLKAS SRLNPKSCTK EVGGRQLREG LRNSKRRLEE AQQVDKPQSP
460 470 480 490 500
PKKMKGVAGN AEAPGKKASA ASGEKSLLNG HVKKEVPERS LERNRPKRAA
510 520 530 540 550
AGKNMLGKQA HGKTEGTPCE NRSTSQPESS HKPHDPQGKP EKGSGKSGWA
560 570 580 590 600
AMDEIPVLRP SAKEFHDPLI YIESVRAQVE KYGMCRVIPP PDWRPECKLN
610 620 630 640 650
DEMRFVTQIQ HIHKLGRRWG PNVQRLACIK KHLRSQGITM DELPLIGGCE
660 670 680 690 700
LDLACFFRLI NEMGGMQQVT DLKKWNKLAD MLRIPKTAQD RLAKLQEAYC
710 720 730 740 750
QYLLSYDSLS PEEHRRLEKE VLMEKEILEK RKGPLEGHTE SDHHKFHSLP
760 770 780 790 800
RFEPKNGLVH GVTPRNGFRS KLKEVGRAPL KTGRRRLFAQ EKEVVKEEEE
810 820 830 840 850
DKGVLNDFHK CIYKGRSVSL TTFYRTARNI MNMCFSKEPA PAEIEQEYWR
860 870 880 890 900
LVEEKDCHVA VHCGKVDTNT HGSGFPVGKS EPFSRHGWNL TVLPNNTGSI
910 920 930 940 950
LRHLGAVPGV TIPWLNIGMV FSTSCWSRDQ NHLPYIDYLH TGADCIWYCI
960 970 980 990 1000
PAEEENKLED VVHTLLQGNG TPGLQMLESN VMISPEVLCK KGIKVHRTVQ
1010 1020 1030 1040 1050
QSGQFVVCFP GSFVSKVCCG YNVSETVHFA TTQWTSMGFE TAKEMKRRHI
1060 1070 1080 1090 1100
AKPFSMEKLL YQIAQAEAKK ENGPTLSTIS ALLDELRDTE LRQRRLLFEA
1110 1120 1130 1140 1150
GLHSSARYGS HDGNSTVADG KKKPRKWLQL ETSERRCQIC QHLCYLSMVV
1160 1170 1180 1190 1200
QENENVVFCL ECALRHVEKQ KSCRGLKLMY RYDEEQIISL VNQICGKVSG
1210 1220 1230
KHGGIENCLN KPTPKRGPRK RATVDVPPSR LPSS
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

MaxQBi Q62315.
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 Q62315.
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

Bgeei Q62315.
CleanExi MM_JARID2.
ExpressionAtlasi Q62315. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 121 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