JARD2_MOUSE
ID JARD2_MOUSE Reviewed; 1234 AA.
AC Q62315; Q3TPU4; Q3UHS7; Q99LD1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Protein Jumonji;
DE AltName: Full=Jumonji/ARID domain-containing protein 2;
GN Name=Jarid2; Synonyms=Jmj;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=129/Ola;
RX PubMed=7758946; DOI=10.1101/gad.9.10.1211;
RA Takeuchi T., Yamazaki Y., Katoh-Fukui Y., Tsuchiya R., Kondo S.,
RA Motoyama J., Higashinakagawa T.;
RT "Gene trap capture of a novel mouse gene, jumonji, required for neural tube
RT formation.";
RL Genes Dev. 9:1211-1222(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1068 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Placenta, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=9376320; DOI=10.1016/s0925-4773(97)00082-8;
RA Motoyama J., Kitajima K., Kojima M., Kondo S., Takeuchi T.;
RT "Organogenesis of the liver, thymus and spleen is affected in jumonji
RT mutant mice.";
RL Mech. Dev. 66:27-37(1997).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=10446263; DOI=10.1016/s0925-4773(99)00100-8;
RA Takeuchi T., Kojima M., Nakajima K., Kondo S.;
RT "jumonji gene is essential for the neurulation and cardiac development of
RT mouse embryos with a C3H/He background.";
RL Mech. Dev. 86:29-38(1999).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10913339; DOI=10.1006/bbrc.2000.3138;
RA Toyoda M., Kojima M., Takeuchi T.;
RT "Jumonji is a nuclear protein that participates in the negative regulation
RT of cell growth.";
RL Biochem. Biophys. Res. Commun. 274:332-336(2000).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10807864; DOI=10.1161/01.res.86.9.932;
RA Lee Y., Song A.J., Baker R., Micales B., Conway S.J., Lyons G.E.;
RT "Jumonji, a nuclear protein that is necessary for normal heart
RT development.";
RL Circ. Res. 86:932-938(2000).
RN [9]
RP FUNCTION.
RX PubMed=12852854; DOI=10.1016/s1534-5807(03)00189-8;
RA Toyoda M., Shirato H., Nakajima K., Kojima M., Takahashi M., Kubota M.,
RA Suzuki-Migishima R., Motegi Y., Yokoyama M., Takeuchi T.;
RT "jumonji downregulates cardiac cell proliferation by repressing cyclin D1
RT expression.";
RL Dev. Cell 5:85-97(2003).
RN [10]
RP FUNCTION, DNA-BINDING, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF
RP 106-ARG-LYS-107.
RX PubMed=12890668; DOI=10.1074/jbc.m307386200;
RA Kim T.-G., Kraus J.C., Chen J., Lee Y.;
RT "JUMONJI, a critical factor for cardiac development, functions as a
RT transcriptional repressor.";
RL J. Biol. Chem. 278:42247-42255(2003).
RN [11]
RP FUNCTION, AND INTERACTION WITH GATA4 AND NKX2-5.
RX PubMed=15542826; DOI=10.1128/mcb.24.23.10151-10160.2004;
RA Kim T.-G., Chen J., Sadoshima J., Lee Y.;
RT "Jumonji represses atrial natriuretic factor gene expression by inhibiting
RT transcriptional activities of cardiac transcription factors.";
RL Mol. Cell. Biol. 24:10151-10160(2004).
RN [12]
RP INTERACTION WITH ZNF496.
RX PubMed=17521633; DOI=10.1016/j.febslet.2007.05.006;
RA Mysliwiec M.R., Kim T.G., Lee Y.;
RT "Characterization of zinc finger protein 496 that interacts with
RT Jumonji/JARID2.";
RL FEBS Lett. 581:2633-2640(2007).
RN [13]
RP FUNCTION, AND INTERACTION WITH RB1.
RX PubMed=15870077; DOI=10.1074/jbc.m414482200;
RA Jung J., Kim T.G., Lyons G.E., Kim H.R., Lee Y.;
RT "Jumonji regulates cardiomyocyte proliferation via interaction with
RT retinoblastoma protein.";
RL J. Biol. Chem. 280:30916-30923(2005).
RN [14]
RP FUNCTION, LACK OF HISTONE DEMETHYLASE ACTIVITY, SUBCELLULAR LOCATION, AND
RP ASSOCIATION WITH THE PRC2 COMPLEX.
RX PubMed=20064376; DOI=10.1016/j.cell.2009.12.003;
RA Shen X., Kim W., Fujiwara Y., Simon M.D., Liu Y., Mysliwiec M.R.,
RA Yuan G.C., Lee Y., Orkin S.H.;
RT "Jumonji modulates polycomb activity and self-renewal versus
RT differentiation of stem cells.";
RL Cell 139:1303-1314(2009).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE PRC2 COMPLEX, DOMAIN
RP GSGFP MOTIF, AND INTERACTION WITH SUZ12.
RX PubMed=20064375; DOI=10.1016/j.cell.2009.12.002;
RA Peng J.C., Valouev A., Swigut T., Zhang J., Zhao Y., Sidow A., Wysocka J.;
RT "Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target
RT gene occupancy in pluripotent cells.";
RL Cell 139:1290-1302(2009).
RN [16]
RP FUNCTION.
RX PubMed=19010785; DOI=10.1074/jbc.m804994200;
RA Shirato H., Ogawa S., Nakajima K., Inagawa M., Kojima M., Tachibana M.,
RA Shinkai Y., Takeuchi T.;
RT "A jumonji (Jarid2) protein complex represses cyclin D1 expression by
RT methylation of histone H3-K9.";
RL J. Biol. Chem. 284:733-739(2009).
RN [17]
RP FUNCTION, DNA-BINDING, AND DOMAIN ARID.
RX PubMed=20075857; DOI=10.1038/nature08788;
RA Pasini D., Cloos P.A., Walfridsson J., Olsson L., Bukowski J.P.,
RA Johansen J.V., Bak M., Tommerup N., Rappsilber J., Helin K.;
RT "JARID2 regulates binding of the Polycomb repressive complex 2 to target
RT genes in ES cells.";
RL Nature 464:306-310(2010).
RN [18]
RP INTERACTION WITH ESRRB.
RX PubMed=26523946; DOI=10.1002/stem.2243;
RA Iseki H., Nakachi Y., Hishida T., Yamashita-Sugahara Y., Hirasaki M.,
RA Ueda A., Tanimoto Y., Iijima S., Sugiyama F., Yagami K., Takahashi S.,
RA Okuda A., Okazaki Y.;
RT "Combined Overexpression of JARID2, PRDM14, ESRRB, and SALL4A Dramatically
RT Improves Efficiency and Kinetics of Reprogramming to Induced Pluripotent
RT Stem Cells.";
RL Stem Cells 34:322-333(2016).
RN [19]
RP STRUCTURE BY NMR OF 615-730.
RX PubMed=19455710; DOI=10.1002/prot.22449;
RA Kusunoki H., Takeuchi T., Kohno T.;
RT "Solution structure of the AT-rich interaction domain of Jumonji/JARID2.";
RL Proteins 76:1023-1028(2009).
CC -!- FUNCTION: Regulator of histone methyltransferase complexes that plays
CC an essential role in embryonic development, including heart and liver
CC development, neural tube fusion process and hematopoiesis
CC (PubMed:10807864, PubMed:12852854, PubMed:12890668, PubMed:15542826,
CC PubMed:15870077, PubMed:19010785, PubMed:20064375, PubMed:20064376,
CC PubMed:20075857). Acts as an accessory subunit for the core PRC2
CC (Polycomb repressive complex 2) complex, which mediates histone H3K27
CC (H3K27me3) trimethylation on chromatin (PubMed:20064376,
CC PubMed:20064375). Binds DNA and mediates the recruitment of the PRC2
CC complex to target genes in embryonic stem cells, thereby playing a key
CC role in stem cell differentiation and normal embryonic development
CC (PubMed:20064375, PubMed:20075857). In cardiac cells, it is required to
CC repress expression of cyclin-D1 (CCND1) by activating methylation of
CC 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone
CC methyltransferases (PubMed:12852854, PubMed:12890668, PubMed:19010785).
CC Also acts as a transcriptional repressor of ANF via its interaction
CC with GATA4 and NKX2-5 (PubMed:15542826). Participates in the negative
CC regulation of cell proliferation signaling (PubMed:10913339). Does not
CC have histone demethylase activity (PubMed:20064376).
CC {ECO:0000269|PubMed:10807864, ECO:0000269|PubMed:10913339,
CC ECO:0000269|PubMed:12852854, ECO:0000269|PubMed:12890668,
CC ECO:0000269|PubMed:15542826, ECO:0000269|PubMed:15870077,
CC ECO:0000269|PubMed:19010785, ECO:0000269|PubMed:20064375,
CC ECO:0000269|PubMed:20064376, ECO:0000269|PubMed:20075857}.
CC -!- SUBUNIT: Associates with the PRC2 complex, which consists of the core
CC components EED, EZH1 or EZH2, SUZ12, and RBBP4, and various
CC combinations of accessory subunits including AEBP2, JARID2, PHF19, MTF2
CC and EPOP (PubMed:20064376, PubMed:20064375). Found in a monomeric
CC PRC2.2 (class 2) complex consisting of at least SUZ12, RBBP4, AEBP2 and
CC JARID2 (By similarity). Facilitates nucleosome binding of the PRC2
CC complex (By similarity). Interacts with SUZ12 (via C2H2-type zinc
CC finger domain); the interaction is direct; competes with EPOP for SUZ12
CC binding (By similarity). Interacts with histone methyltransferases
CC EHMT1/GLP1 and EHMT2/G9a (By similarity). Interacts with GATA4 (via the
CC N-terminal region) (PubMed:15542826). Interacts with NKX2-5 (via the C-
CC terminal region) (PubMed:15542826). Interacts with RB1
CC (PubMed:15870077). Interacts with ZNF496 (PubMed:17521633). Interacts
CC with ESRRB (PubMed:26523946). {ECO:0000250|UniProtKB:Q92833,
CC ECO:0000269|PubMed:15542826, ECO:0000269|PubMed:15870077,
CC ECO:0000269|PubMed:17521633, ECO:0000269|PubMed:20064375,
CC ECO:0000269|PubMed:20064376, ECO:0000269|PubMed:26523946}.
CC -!- INTERACTION:
CC Q62315; Q921E6: Eed; NbExp=11; IntAct=EBI-493592, EBI-904301;
CC Q62315; P70351: Ezh1; NbExp=4; IntAct=EBI-493592, EBI-2531737;
CC Q62315; Q61188: Ezh2; NbExp=15; IntAct=EBI-493592, EBI-904311;
CC Q62315; Q08369: Gata4; NbExp=3; IntAct=EBI-493592, EBI-297008;
CC Q62315; P42582: Nkx2-5; NbExp=3; IntAct=EBI-493592, EBI-297021;
CC Q62315; Q80U70: Suz12; NbExp=13; IntAct=EBI-493592, EBI-2526494;
CC Q62315; Q5SXI5: Znf496; NbExp=6; IntAct=EBI-493592, EBI-7417351;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:10807864,
CC ECO:0000269|PubMed:10913339, ECO:0000269|PubMed:20064375,
CC ECO:0000269|PubMed:20064376}. Note=Colocalizes with the PRC2 complex on
CC chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62315-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62315-2; Sequence=VSP_038758;
CC -!- TISSUE SPECIFICITY: Widely expressed in embryos. In adults, expressed
CC at high levels in heart, skeletal muscle, brain and thymus.
CC {ECO:0000269|PubMed:10807864}.
CC -!- DOMAIN: The ARID domain is required to target the PRC2 complex to its
CC target genes.
CC -!- DOMAIN: The GSGFP motif is required for the interaction with SUZ12.
CC -!- DISRUPTION PHENOTYPE: Embryos die before 15.5 dpc and show severe
CC cardiac morphological defects and altered heart-specific gene
CC expression. Some, but not all, of the homozygotes develop an abnormal
CC groove in a region just anterior to the midbrain-hindbrain boundary on
CC the neural plate at 8-8.5 dpc and show a defect in neural tube closure
CC in the midbrain region. Variable phenotypes are observed depending on
CC the genetic backgrounds: mutant mice with a C57BL/6J X 129S1/Sv genetic
CC background die upon birth and show cardiac defects such as ventricular
CC septal defects, double-outlet right ventricle, and thin ventricular
CC wall at later embryonic stages. In addition to the thin ventricular
CC wall, mutant embryos with a pure BALB/c background show deficient cell
CC growth in the liver, thymus, and spleen. In contrast, mutant mice with
CC a C3H/He genetic background die at 11.5 dpc, which exhibit hyperplasia
CC and increased cyclin-D1 (CCND1) expression in the trabecular layer of
CC the ventricle at 10.5 dpc. {ECO:0000269|PubMed:10446263,
CC ECO:0000269|PubMed:10807864, ECO:0000269|PubMed:7758946,
CC ECO:0000269|PubMed:9376320}.
CC -!- MISCELLANEOUS: 'Jumonji' means 'cruciform' in Japanese.
CC -!- SIMILARITY: Belongs to the JARID2 family. {ECO:0000305}.
CC -!- CAUTION: Despite the presence of a JmjC domain, lacks the conserved
CC residues that bind the iron cofactor, explaining the absence of histone
CC methyltransferase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE27780.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EDL41007.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D31967; BAA06736.1; -; mRNA.
DR EMBL; AK045214; BAC32264.1; -; mRNA.
DR EMBL; AK147226; BAE27780.1; ALT_FRAME; mRNA.
DR EMBL; AK164134; BAE37641.1; -; mRNA.
DR EMBL; CH466546; EDL41007.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC003374; AAH03374.1; -; mRNA.
DR EMBL; BC052444; AAH52444.1; -; mRNA.
DR EMBL; BC060695; AAH60695.1; -; mRNA.
DR CCDS; CCDS36646.1; -. [Q62315-1]
DR PIR; T30254; T30254.
DR RefSeq; NP_001191972.1; NM_001205043.1. [Q62315-1]
DR RefSeq; NP_001191973.1; NM_001205044.1. [Q62315-1]
DR RefSeq; NP_068678.1; NM_021878.3. [Q62315-1]
DR RefSeq; XP_006516918.1; XM_006516855.3.
DR RefSeq; XP_006516919.1; XM_006516856.3.
DR RefSeq; XP_006516921.1; XM_006516858.3. [Q62315-2]
DR RefSeq; XP_006516922.1; XM_006516859.2.
DR RefSeq; XP_006516923.1; XM_006516860.2.
DR RefSeq; XP_017170888.1; XM_017315399.1.
DR PDB; 2RQ5; NMR; -; A=615-730.
DR PDBsum; 2RQ5; -.
DR AlphaFoldDB; Q62315; -.
DR BMRB; Q62315; -.
DR SMR; Q62315; -.
DR BioGRID; 200866; 23.
DR DIP; DIP-34312N; -.
DR IntAct; Q62315; 21.
DR MINT; Q62315; -.
DR STRING; 10090.ENSMUSP00000134205; -.
DR iPTMnet; Q62315; -.
DR PhosphoSitePlus; Q62315; -.
DR EPD; Q62315; -.
DR MaxQB; Q62315; -.
DR PaxDb; Q62315; -.
DR PeptideAtlas; Q62315; -.
DR PRIDE; Q62315; -.
DR ProteomicsDB; 269360; -. [Q62315-1]
DR ProteomicsDB; 269361; -. [Q62315-2]
DR Antibodypedia; 25028; 240 antibodies from 27 providers.
DR DNASU; 16468; -.
DR Ensembl; ENSMUST00000044608; ENSMUSP00000037774; ENSMUSG00000038518. [Q62315-1]
DR Ensembl; ENSMUST00000173246; ENSMUSP00000134205; ENSMUSG00000038518. [Q62315-1]
DR Ensembl; ENSMUST00000173704; ENSMUSP00000134675; ENSMUSG00000038518. [Q62315-1]
DR GeneID; 16468; -.
DR KEGG; mmu:16468; -.
DR UCSC; uc007qgr.2; mouse. [Q62315-1]
DR UCSC; uc007qgv.1; mouse. [Q62315-2]
DR CTD; 3720; -.
DR MGI; MGI:104813; Jarid2.
DR VEuPathDB; HostDB:ENSMUSG00000038518; -.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000159220; -.
DR HOGENOM; CLU_007086_0_0_1; -.
DR InParanoid; Q62315; -.
DR OMA; VFNGSNR; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; Q62315; -.
DR TreeFam; TF323264; -.
DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR BioGRID-ORCS; 16468; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Jarid2; mouse.
DR EvolutionaryTrace; Q62315; -.
DR PRO; PR:Q62315; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q62315; protein.
DR Bgee; ENSMUSG00000038518; Expressed in rostral migratory stream and 295 other tissues.
DR ExpressionAtlas; Q62315; baseline and differential.
DR Genevisible; Q62315; MM.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:MGI.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IMP:MGI.
DR GO; GO:0061649; F:ubiquitin modification-dependent histone binding; IMP:MGI.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISO:MGI.
DR GO; GO:0031061; P:negative regulation of histone methylation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IDA:UniProtKB.
DR GO; GO:1902682; P:protein localization to pericentric heterochromatin; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0048536; P:spleen development; IMP:MGI.
DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR004198; Znf_C5HC2.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Developmental protein; Differentiation; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1234
FT /note="Protein Jumonji"
FT /id="PRO_0000200592"
FT DOMAIN 555..596
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 619..711
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 882..1046
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..170
FT /note="Sufficient for interaction with the PRC2 complex"
FT /evidence="ECO:0000250|UniProtKB:Q92833"
FT REGION 169..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 104..110
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:12890668"
FT MOTIF 872..876
FT /note="GSGFP motif"
FT COMPBIAS 84..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92833"
FT MOD_RES 378
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92833"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92833"
FT VAR_SEQ 1..60
FT /note="MSKERPKRNIIQKKYDDSDGIPWSEERVVRKVLYLSLKEFKNAQKRQHGEGL
FT AGSLKAVN -> MAAPRVCQVQFLVAYLEEPGIE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038758"
FT MUTAGEN 106..107
FT /note="RK->AA: Leads to cytoplasmic relocalization."
FT /evidence="ECO:0000269|PubMed:12890668"
FT CONFLICT 873
FT /note="S -> G (in Ref. 2; BAE37641)"
FT /evidence="ECO:0000305"
FT CONFLICT 1096
FT /note="L -> Q (in Ref. 4; AAH03374)"
FT /evidence="ECO:0000305"
FT HELIX 621..635
FT /evidence="ECO:0007829|PDB:2RQ5"
FT HELIX 653..662
FT /evidence="ECO:0007829|PDB:2RQ5"
FT HELIX 666..671
FT /evidence="ECO:0007829|PDB:2RQ5"
FT HELIX 675..681
FT /evidence="ECO:0007829|PDB:2RQ5"
FT HELIX 691..700
FT /evidence="ECO:0007829|PDB:2RQ5"
FT HELIX 703..708
FT /evidence="ECO:0007829|PDB:2RQ5"
FT HELIX 711..726
FT /evidence="ECO:0007829|PDB:2RQ5"
SQ SEQUENCE 1234 AA; 137445 MW; B56E172C5E5745B5 CRC64;
MSKERPKRNI IQKKYDDSDG IPWSEERVVR KVLYLSLKEF KNAQKRQHGE GLAGSLKAVN
GLLGNAQAKA LGPASEQSEN EKDDASQVSS TSNDVSSSDF EEGPSRKRPR LQAQRKFAQS
QPNSPSTTPV KIVEPLLPPP ATQISDLSKR KPKTEDFLTF LCLRGSPALP NSMVYFGSSQ
DEEDVEEEDD ETEDVKATTN NASSSCQSTP RKGKTHKHVH NGHVFNGSSR SAREKEPAHK
HRSKEATPGK EKHSEPRADS RREQASGAQP TAASAAASSA KGLAANHQPP PSHRSAQDLR
KQVSKVNGVT RMSSLGAGTN SAKKIREVRP SPSKTVKYTA TVTKGTVTYT KAKRELVKET
KPNHHKPSSA VNHTISGKTE SSNAKTRKQV LSLGGASKST GPAASGLKAS SRLNPKSCTK
EVGGRQLREG LRNSKRRLEE AQQVDKPQSP PKKMKGVAGN AEAPGKKASA ASGEKSLLNG
HVKKEVPERS LERNRPKRAA AGKNMLGKQA HGKTEGTPCE NRSTSQPESS HKPHDPQGKP
EKGSGKSGWA AMDEIPVLRP SAKEFHDPLI YIESVRAQVE KYGMCRVIPP PDWRPECKLN
DEMRFVTQIQ HIHKLGRRWG PNVQRLACIK KHLRSQGITM DELPLIGGCE LDLACFFRLI
NEMGGMQQVT DLKKWNKLAD MLRIPKTAQD RLAKLQEAYC QYLLSYDSLS PEEHRRLEKE
VLMEKEILEK RKGPLEGHTE SDHHKFHSLP RFEPKNGLVH GVTPRNGFRS KLKEVGRAPL
KTGRRRLFAQ EKEVVKEEEE DKGVLNDFHK CIYKGRSVSL TTFYRTARNI MNMCFSKEPA
PAEIEQEYWR LVEEKDCHVA VHCGKVDTNT HGSGFPVGKS EPFSRHGWNL TVLPNNTGSI
LRHLGAVPGV TIPWLNIGMV FSTSCWSRDQ NHLPYIDYLH TGADCIWYCI PAEEENKLED
VVHTLLQGNG TPGLQMLESN VMISPEVLCK KGIKVHRTVQ QSGQFVVCFP GSFVSKVCCG
YNVSETVHFA TTQWTSMGFE TAKEMKRRHI AKPFSMEKLL YQIAQAEAKK ENGPTLSTIS
ALLDELRDTE LRQRRLLFEA GLHSSARYGS HDGNSTVADG KKKPRKWLQL ETSERRCQIC
QHLCYLSMVV QENENVVFCL ECALRHVEKQ KSCRGLKLMY RYDEEQIISL VNQICGKVSG
KHGGIENCLN KPTPKRGPRK RATVDVPPSR LPSS
