JARD2_DANRE
ID JARD2_DANRE Reviewed; 1319 AA.
AC Q1LVC2;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein Jumonji;
DE AltName: Full=Jumonji/ARID domain-containing protein 2;
GN Name=jarid2b; Synonyms=jmj; ORFNames=si:dkey-211c3.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Regulator of histone methyltransferase complexes that plays
CC an essential role in embryonic development. Acts by modulating histone
CC methyltransferase activity and promoting the recruitment of histone
CC methyltransferase complexes to their target genes. Binds DNA and
CC mediates the recruitment of the PRC2 complex to target genes in
CC embryonic stem cells. Does not have histone demethylase activity but
CC regulates activity of various histone methyltransferase complexes. In
CC embryonic stem cells, it associates with the PRC2 complex and inhibits
CC trimethylation of 'Lys-27' of histone H3 (H3K27me3) by the PRC2
CC complex, thereby playing a key role in differentiation of embryonic
CC stem cells and normal development (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associates with the PRC2 complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with the PRC2 complex
CC on chromatin.
CC -!- DOMAIN: The ARID domain is required to target the PRC2 complex to its
CC target genes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JARID2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK04931.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAK05400.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX842609; CAK04931.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX890540; CAK04931.1; JOINED; Genomic_DNA.
DR EMBL; BX890540; CAK05400.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX842609; CAK05400.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001189388.1; NM_001202459.1.
DR AlphaFoldDB; Q1LVC2; -.
DR SMR; Q1LVC2; -.
DR STRING; 7955.ENSDARP00000114402; -.
DR PaxDb; Q1LVC2; -.
DR Ensembl; ENSDART00000089836; ENSDARP00000084269; ENSDARG00000062268.
DR GeneID; 558456; -.
DR KEGG; dre:558456; -.
DR CTD; 558456; -.
DR ZFIN; ZDB-GENE-060503-246; jarid2b.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000159220; -.
DR InParanoid; Q1LVC2; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; Q1LVC2; -.
DR TreeFam; TF323264; -.
DR Reactome; R-DRE-212300; PRC2 methylates histones and DNA.
DR PRO; PR:Q1LVC2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000062268; Expressed in blastula and 12 other tissues.
DR ExpressionAtlas; Q1LVC2; baseline and differential.
DR GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0031061; P:negative regulation of histone methylation; ISS:UniProtKB.
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:0048863; P:stem cell differentiation; ISS:UniProtKB.
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 3: Inferred from homology;
KW Chromatin regulator; Developmental protein; Differentiation; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1319
FT /note="Protein Jumonji"
FT /id="PRO_0000391908"
FT DOMAIN 607..648
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 671..779
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 954..1118
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 96..102
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 944..948
FT /note="GSGFP motif"
FT COMPBIAS 74..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..528
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1319 AA; 148226 MW; BDA78F7F5C6E03D6 CRC64;
MSKERPKRNI IQKKYDDNDG MPWSEERVVR KVLYLSLKEF KSAQKRQLCD GIDDEGKGPN
ASLSNGQLNG SKGGHKEDGS RSQRKDGGGE YSVDGPAKKR PRLHAQRKFA QSQPNSPSNT
PVKMADPSLP TPLTHITFLS RRKPKTEDFL TFICLRGSPA LPSNMAYFGC SQDEEDLEDE
DEIEEEKAPS VASTSCQSTP KKGKPHGKIN GLVLNGHKVH KDKELTPRSK ARESSVGRDR
SERCDESEIS HKHTAATAKS HNTNGHNYRR AAEELRKQVS KVNGLTRASS VGTHKASGKK
QKDFRLPSKT VKYTATVSKG HVTYTKAKRE LVKKAKLNHS KHGASAGLRA YSNNHHHNSH
HATSNGHGRP QLSHSGKAQS INAKTRKQVL LSNGVHKMTN GSRLNGRLNG RHSAREEEVV
DRPVRQGLRN SKRRSDAMTL LGAVTESEET KTKQQTTEVK KAKVQPSPLE TRSKKALNQF
KSPNIVTIAH SITEMAASPI QKTGPAPPPS PPAAPASPSM PQNPAIPEPA RQRPKRASAG
KLMFIRKAQQ RAQTNPTLNR TTSTTSASKS FKPAEPTHTP PPRLDRDRER ERERERSRAR
YAALGDVPIF KPSSREFQDP LVYLDSFREQ VESCGLCRVL PPTDWRPECK LNDEMRFVTQ
VQRIHKLGRR WGPNVQKLAC IKKHLKSQGI SMDQPPVIGK SFKSSAFRSA FVCIGGCEVD
LARFSELVCD LGGMQQVMDL KKWSRLADLL RIPKSAQDRL AKLQEAYLQF LLSYDLLSPE
ELQRLEQEVR AEKEALERKR GPLEGHSDNG HHSLALPRYE PKNGLNGLSH RNGFRNHHKE
PDIQRQAGRR RLFAQEKKGE KVECEETEEE MEDEGVLSDQ HKCIYKGRSV SLTTFYRIAR
NTMMMYFNKE PGAAEVEQDY WRIVEQRDCH VAVHYGKVDT NTHGSGFPVG KSEPFSKHGW
NLTVLPNNSG SILRHLGAVP GVTIPWLNIG MVFSTSCWSQ DQNRLPYIDY LHTGADCIWY
SIPAEEKTKL DKVVHTLLQA NGTPGLEMLE KNVMISPEVL CREGIKVHRT VQQSGQFVVV
FPGAFVSRVC CGYSVSETVH FATPQWMNLG YEAAKDLKCR RIAKPFSMEK LLYQIATAEA
KRENRLVLST ISSLLKDLRN IEMKQRQELY EAGLLSSARY CTHDHNQSPA DTRKKPRKWL
ALESSERRCQ MCQHLCYLSM VVQENENVVF CLECALHYVE KHKNCRGLKM MYRYDEEQIN
SLVNQVCGKA LVRSGSEVCN GSSPIKPPAK RGPRKRESMK ITLIPLPTHP SKSAAAAVS
