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 24-JAN-2024, entry version 184. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000134205; -. DR PeptideAtlas; Q62315; -. DR ProteomicsDB; 269360; -. [Q62315-1] DR ProteomicsDB; 269361; -. [Q62315-2] DR Antibodypedia; 25028; 265 antibodies from 27 providers. DR DNASU; 16468; -. DR Ensembl; ENSMUST00000044608.14; ENSMUSP00000037774.8; ENSMUSG00000038518.16. [Q62315-1] DR Ensembl; ENSMUST00000173246.8; ENSMUSP00000134205.2; ENSMUSG00000038518.16. [Q62315-1] DR Ensembl; ENSMUST00000173704.8; ENSMUSP00000134675.2; ENSMUSG00000038518.16. [Q62315-1] DR GeneID; 16468; -. DR KEGG; mmu:16468; -. DR UCSC; uc007qgr.2; mouse. [Q62315-1] DR UCSC; uc007qgv.1; mouse. [Q62315-2] DR AGR; MGI:104813; -. 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; TGADCIX; -. DR OrthoDB; 48111at2759; -. DR PhylomeDB; Q62315; -. DR TreeFam; TF323264; -. DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA. DR BioGRID-ORCS; 16468; 4 hits in 84 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 299 other cell types or tissues. DR ExpressionAtlas; Q62315; baseline and differential. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB. 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:0140718; P:facultative heterochromatin formation; IDA:GO_Central. 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:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:1902682; P:protein localization to pericentric heterochromatin; IMP:MGI. DR GO; GO:0060816; P:random inactivation of X chromosome; IMP:MGI. DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. 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 CDD; cd16870; ARID_JARD2; 1. DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1. DR Gene3D; 2.60.120.650; Cupin; 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 PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1. DR PANTHER; PTHR10694:SF113; PROTEIN JUMONJI; 1. DR Pfam; PF01388; ARID; 1. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR Pfam; PF02928; zf-C5HC2; 1. DR SMART; SM01014; ARID; 1. DR SMART; SM00501; BRIGHT; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00545; JmjN; 1. DR SUPFAM; SSF46774; ARID-like; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51011; ARID; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51183; JMJN; 1. DR Genevisible; Q62315; MM. 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 //