JARD2_HUMAN
ID JARD2_HUMAN Reviewed; 1246 AA.
AC Q92833; A8K9Z6; B7Z5S5; B7Z8L0; Q5U5L5; Q86X63;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Protein Jumonji;
DE AltName: Full=Jumonji/ARID domain-containing protein 2;
GN Name=JARID2; Synonyms=JMJ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8894700; DOI=10.1093/hmg/5.10.1637;
RA Berge-Lefranc J.-L., Jay P., Massacrier A., Cau P., Mattei M.-G., Bauer S.,
RA Marsollier C., Berta P., Fontes M.;
RT "Characterization of the human jumonji gene.";
RL Hum. Mol. Genet. 5:1637-1641(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Thymus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland, and Testis;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-378, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND ASSOCIATION WITH THE PRC2 COMPLEX.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-455, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10] {ECO:0007744|PDB:5WAI}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 147-165 IN COMPLEX WITH AEBP2;
RP RBBP4 AND SUZ12, FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX, INTERACTION
RP WITH SUZ12, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 149-LYS-LYS-150 AND
RP 151-LYS--LYS-153.
RX PubMed=29499137; DOI=10.1016/j.molcel.2018.01.039;
RA Chen S., Jiao L., Shubbar M., Yang X., Liu X.;
RT "Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for
RT Chromatin Binding.";
RL Mol. Cell 69:840-852.e5(2018).
RN [11] {ECO:0007744|PDB:6NQ3}
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 147-165 IN COMPLEX WITH RBBP4;
RP SUZ12 AND PHF19, FUNCTION, AND ASSOCIATION WITH THE PRC2 COMPLEX.
RX PubMed=31959557; DOI=10.1016/j.molcel.2019.12.019;
RA Chen S., Jiao L., Liu X., Yang X., Liu X.;
RT "A Dimeric Structural Scaffold for PRC2-PCL Targeting to CpG Island
RT Chromatin.";
RL Mol. Cell 77:1265-1278.e7(2020).
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: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:20075857,
CC PubMed:29499137, PubMed:31959557). Binds DNA and mediates the
CC recruitment of the PRC2 complex to target genes in embryonic stem
CC cells, thereby playing a key role in stem cell differentiation and
CC normal embryonic development (PubMed:20075857). In cardiac cells, it is
CC required to repress expression of cyclin-D1 (CCND1) by activating
CC methylation of 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and
CC G9a/EHMT2 histone methyltransferases (By similarity). Also acts as a
CC transcriptional repressor of ANF via its interaction with GATA4 and
CC NKX2-5 (By similarity). Participates in the negative regulation of cell
CC proliferation signaling (By similarity). Does not have histone
CC demethylase activity (By similarity). {ECO:0000250|UniProtKB:Q62315,
CC ECO:0000269|PubMed:20075857, ECO:0000269|PubMed:29499137,
CC ECO:0000269|PubMed:31959557}.
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:29499137, PubMed:31959557). Found in a monomeric
CC PRC2.2 (class 2) complex consisting of at least SUZ12, RBBP4, AEBP2 and
CC JARID2 (PubMed:29499137). Facilitates nucleosome binding of the PRC2
CC complex (PubMed:29499137). Interacts with SUZ12 (via C2H2-type zinc
CC finger domain); the interaction is direct; competes with EPOP for SUZ12
CC binding (PubMed:29499137). Interacts with histone methyltransferases
CC EHMT1/GLP1 and EHMT2/G9a (By similarity). Interacts with GATA4 (via the
CC N-terminal region) (By similarity). Interacts with NKX2-5 (via the C-
CC terminal region) (By similarity). Interacts with RB1 (By similarity).
CC Interacts with ZNF496 (By similarity). Interacts with ESRRB (By
CC similarity). {ECO:0000250|UniProtKB:Q62315,
CC ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:31959557}.
CC -!- INTERACTION:
CC Q92833-1; O75530: EED; NbExp=4; IntAct=EBI-15825247, EBI-923794;
CC Q92833-1; Q15910: EZH2; NbExp=7; IntAct=EBI-15825247, EBI-530054;
CC Q92833-1; Q15022: SUZ12; NbExp=7; IntAct=EBI-15825247, EBI-1264675;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:20075857,
CC ECO:0000269|PubMed:29499137}. Note=Colocalizes with the PRC2 complex on
CC chromatin. {ECO:0000269|PubMed:29499137}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92833-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92833-2; Sequence=VSP_038756, VSP_038757;
CC Name=3;
CC IsoId=Q92833-3; Sequence=VSP_045041;
CC -!- TISSUE SPECIFICITY: During embryogenesis, predominantly expressed in
CC neurons and particularly in dorsal root ganglion cells.
CC -!- DOMAIN: The ARID domain is required to target the PRC2 complex to its
CC target genes. {ECO:0000250}.
CC -!- DOMAIN: The GSGFP motif is required for the interaction with SUZ12.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50822.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U57592; AAC50822.1; ALT_FRAME; mRNA.
DR EMBL; AK292861; BAF85550.1; -; mRNA.
DR EMBL; AK299349; BAH13011.1; -; mRNA.
DR EMBL; AK303610; BAH13996.1; -; mRNA.
DR EMBL; AL021938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55357.1; -; Genomic_DNA.
DR EMBL; BC046184; AAH46184.1; -; mRNA.
DR EMBL; BC046246; AAH46246.1; -; mRNA.
DR CCDS; CCDS4533.1; -. [Q92833-1]
DR CCDS; CCDS58996.1; -. [Q92833-3]
DR RefSeq; NP_001253969.1; NM_001267040.1. [Q92833-3]
DR RefSeq; NP_004964.2; NM_004973.3. [Q92833-1]
DR RefSeq; XP_005249146.1; XM_005249089.3.
DR RefSeq; XP_016866323.1; XM_017010834.1. [Q92833-3]
DR RefSeq; XP_016866324.1; XM_017010835.1. [Q92833-3]
DR PDB; 5HYN; X-ray; 2.95 A; E/J/P/U=110-121.
DR PDB; 5LS6; X-ray; 3.47 A; Q/R/S/T=110-120.
DR PDB; 5WAI; X-ray; 2.90 A; D/H=147-165.
DR PDB; 6C23; EM; 3.90 A; B/E=106-450.
DR PDB; 6C24; EM; 3.50 A; B/E=106-450.
DR PDB; 6NQ3; X-ray; 2.89 A; D/H=147-165.
DR PDB; 6WKR; EM; 3.50 A; B/E=1-450.
DR PDB; 7KSO; EM; 3.90 A; F=1-1246.
DR PDBsum; 5HYN; -.
DR PDBsum; 5LS6; -.
DR PDBsum; 5WAI; -.
DR PDBsum; 6C23; -.
DR PDBsum; 6C24; -.
DR PDBsum; 6NQ3; -.
DR PDBsum; 6WKR; -.
DR PDBsum; 7KSO; -.
DR AlphaFoldDB; Q92833; -.
DR BMRB; Q92833; -.
DR SMR; Q92833; -.
DR BioGRID; 109923; 37.
DR DIP; DIP-45494N; -.
DR IntAct; Q92833; 26.
DR MINT; Q92833; -.
DR STRING; 9606.ENSP00000341280; -.
DR iPTMnet; Q92833; -.
DR PhosphoSitePlus; Q92833; -.
DR BioMuta; JARID2; -.
DR DMDM; 61252601; -.
DR EPD; Q92833; -.
DR jPOST; Q92833; -.
DR MassIVE; Q92833; -.
DR MaxQB; Q92833; -.
DR PaxDb; Q92833; -.
DR PeptideAtlas; Q92833; -.
DR PRIDE; Q92833; -.
DR ProteomicsDB; 6958; -.
DR ProteomicsDB; 75511; -. [Q92833-1]
DR ProteomicsDB; 75512; -. [Q92833-2]
DR Antibodypedia; 25028; 240 antibodies from 27 providers.
DR DNASU; 3720; -.
DR Ensembl; ENST00000341776.7; ENSP00000341280.2; ENSG00000008083.14. [Q92833-1]
DR Ensembl; ENST00000397311.4; ENSP00000380478.3; ENSG00000008083.14. [Q92833-3]
DR GeneID; 3720; -.
DR KEGG; hsa:3720; -.
DR MANE-Select; ENST00000341776.7; ENSP00000341280.2; NM_004973.4; NP_004964.2.
DR UCSC; uc003nbj.5; human. [Q92833-1]
DR CTD; 3720; -.
DR DisGeNET; 3720; -.
DR GeneCards; JARID2; -.
DR HGNC; HGNC:6196; JARID2.
DR HPA; ENSG00000008083; Tissue enhanced (bone).
DR MIM; 601594; gene.
DR neXtProt; NX_Q92833; -.
DR OpenTargets; ENSG00000008083; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA29995; -.
DR VEuPathDB; HostDB:ENSG00000008083; -.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000159220; -.
DR HOGENOM; CLU_007086_0_0_1; -.
DR InParanoid; Q92833; -.
DR OMA; VFNGSNR; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; Q92833; -.
DR TreeFam; TF323264; -.
DR PathwayCommons; Q92833; -.
DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR SignaLink; Q92833; -.
DR SIGNOR; Q92833; -.
DR BioGRID-ORCS; 3720; 18 hits in 1115 CRISPR screens.
DR ChiTaRS; JARID2; human.
DR GeneWiki; JARID2; -.
DR GenomeRNAi; 3720; -.
DR Pharos; Q92833; Tbio.
DR PRO; PR:Q92833; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q92833; protein.
DR Bgee; ENSG00000008083; Expressed in secondary oocyte and 211 other tissues.
DR Genevisible; Q92833; HS.
DR GO; GO:0035098; C:ESC/E(Z) complex; IEA:Ensembl.
DR GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:0061649; F:ubiquitin modification-dependent histone binding; IEA:Ensembl.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IEA:Ensembl.
DR GO; GO:0031061; P:negative regulation of histone methylation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; ISS:UniProtKB.
DR GO; GO:1902682; P:protein localization to pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
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..1246
FT /note="Protein Jumonji"
FT /id="PRO_0000200591"
FT DOMAIN 557..598
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 621..713
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 884..1048
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 59..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:0000269|PubMed:29499137"
FT REGION 169..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 104..110
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 874..878
FT /note="GSGFP motif"
FT COMPBIAS 60..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 378
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..172
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045041"
FT VAR_SEQ 1..60
FT /note="MSKERPKRNIIQKKYDDSDGIPWSEERVVRKVLYLSLKEFKNSQKRQHAEGI
FT AGSLKTVN -> MAAPRVCQVQFLVAYLEEPGIE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038756"
FT VAR_SEQ 949..1246
FT /note="WYCIPAEEENKLEDVVHTLLQANGTPGLQMLESNVMISPEVLCKEGIKVHRT
FT VQQSGQFVVCFPGSFVSKVCCGYSVSETVHFATTQWTSMGFETAKEMKRRHIAKPFSME
FT KLLYQIAQAEAKKENGPTLSTISALLDELRDTELRQRRQLFEAGLHSSARYGSHDGSST
FT VADGKKKPRKWLQLETSERRCQICQHLCYLSMVVQENENVVFCLECALRHVEKQKSCRG
FT LKLMYRYDEEQIISLVNQICGKVSGKNGSIENCLSKPTPKRGPRKRATVDVPPSRLSAS
FT SSSKSASSSS -> CLSVEPVFPHLSVAVGSIVDLGISFLPCGDTRVMYPVESVAWRGV
FT LGPRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038757"
FT MUTAGEN 149..150
FT /note="KR->DE,AA: Abolishes nucleosome binding activity of
FT a minimal SUZ12-RBBP4-AEBP2-JARID2 PRC2 complex."
FT /evidence="ECO:0000269|PubMed:29499137"
FT MUTAGEN 151..153
FT /note="KPK->EPE,APA: Abolishes nucleosome binding activity
FT of a minimal SUZ12-RBBP4-AEBP2-JARID2 PRC2 complex."
FT /evidence="ECO:0000269|PubMed:29499137"
FT CONFLICT 250
FT /note="K -> E (in Ref. 2; BAH13011)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="C -> S (in Ref. 2; BAH13011)"
FT /evidence="ECO:0000305"
FT CONFLICT 673
FT /note="D -> E (in Ref. 1; AAC50822)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="A -> S (in Ref. 1; AAC50822)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="R -> K (in Ref. 1; AAC50822)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="D -> E (in Ref. 1; AAC50822)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="L -> I (in Ref. 1; AAC50822)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="F -> L (in Ref. 1; AAC50822)"
FT /evidence="ECO:0000305"
FT CONFLICT 1212
FT /note="S -> H (in Ref. 1; AAC50822)"
FT /evidence="ECO:0000305"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:6WKR"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:6WKR"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:6WKR"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6WKR"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:6C24"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:6C24"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:6NQ3"
SQ SEQUENCE 1246 AA; 138734 MW; E4929984259110DB CRC64;
MSKERPKRNI IQKKYDDSDG IPWSEERVVR KVLYLSLKEF KNSQKRQHAE GIAGSLKTVN
GLLGNDQSKG LGPASEQSEN EKDDASQVSS TSNDVSSSDF EEGPSRKRPR LQAQRKFAQS
QPNSPSTTPV KIVEPLLPPP ATQISDLSKR KPKTEDFLTF LCLRGSPALP NSMVYFGSSQ
DEEEVEEEDD ETEDVKTATN NASSSCQSTP RKGKTHKHVH NGHVFNGSSR STREKEPVQK
HKSKEATPAK EKHSDHRADS RREQASANHP AAAPSTGSSA KGLAATHHHP PLHRSAQDLR
KQVSKVNGVT RMSSLGAGVT SAKKMREVRP SPSKTVKYTA TVTKGAVTYT KAKRELVKDT
KPNHHKPSSA VNHTISGKTE SSNAKTRKQV LSLGGASKST GPAVNGLKVS GRLNPKSCTK
EVGGRQLREG LQLREGLRNS KRRLEEAHQA EKPQSPPKKM KGAAGPAEGP GKKAPAERGL
LNGHVKKEVP ERSLERNRPK RATAGKSTPG RQAHGKADSA SCENRSTSQP ESVHKPQDSG
KAEKGGGKAG WAAMDEIPVL RPSAKEFHDP LIYIESVRAQ VEKFGMCRVI PPPDWRPECK
LNDEMRFVTQ IQHIHKLGRR WGPNVQRLAC IKKHLKSQGI TMDELPLIGG CELDLACFFR
LINEMGGMQQ VTDLKKWNKL ADMLRIPRTA QDRLAKLQEA YCQYLLSYDS LSPEEHRRLE
KEVLMEKEIL EKRKGPLEGH TENDHHKFHP LPRFEPKNGL IHGVAPRNGF RSKLKEVGQA
QLKTGRRRLF AQEKEVVKEE EEDKGVLNDF HKCIYKGRSV SLTTFYRTAR NIMSMCFSKE
PAPAEIEQEY WRLVEEKDCH VAVHCGKVDT NTHGSGFPVG KSEPFSRHGW NLTVLPNNTG
SILRHLGAVP GVTIPWLNIG MVFSTSCWSR DQNHLPYIDY LHTGADCIWY CIPAEEENKL
EDVVHTLLQA NGTPGLQMLE SNVMISPEVL CKEGIKVHRT VQQSGQFVVC FPGSFVSKVC
CGYSVSETVH FATTQWTSMG FETAKEMKRR HIAKPFSMEK LLYQIAQAEA KKENGPTLST
ISALLDELRD TELRQRRQLF EAGLHSSARY GSHDGSSTVA DGKKKPRKWL QLETSERRCQ
ICQHLCYLSM VVQENENVVF CLECALRHVE KQKSCRGLKL MYRYDEEQII SLVNQICGKV
SGKNGSIENC LSKPTPKRGP RKRATVDVPP SRLSASSSSK SASSSS
