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Database: UniProt
Entry: G1K2I1_DANRE
LinkDB: G1K2I1_DANRE
Original site: G1K2I1_DANRE 
ID   G1K2I1_DANRE            Unreviewed;      1522 AA.
AC   G1K2I1; A0A8M2BEG9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 3.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE            EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN   Name=cb264 {ECO:0000313|RefSeq:XP_005167081.1};
GN   Synonyms=jarid1bb {ECO:0000313|RefSeq:XP_005167081.1}, plu1
GN   {ECO:0000313|RefSeq:XP_005167081.1}, wu:fc44h11
GN   {ECO:0000313|RefSeq:XP_005167081.1}, zgc:85741
GN   {ECO:0000313|RefSeq:XP_005167081.1};
GN   OrderedLocusNames=kdm5bb {ECO:0000313|Ensembl:ENSDARP00000023794,
GN   ECO:0000313|RefSeq:XP_005167081.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-030424-1};
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 {ECO:0000313|Ensembl:ENSDARP00000023794};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000023794}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000023794};
RG   Ensembl;
RL   Submitted (AUG-2011) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000023794, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000023794};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   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).
RN   [3] {ECO:0000313|RefSeq:XP_005167081.1}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_005167081.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC         [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC         H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC         Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC         Evidence={ECO:0000256|ARBA:ARBA00000604};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC       {ECO:0000256|ARBA:ARBA00006801}.
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DR   EMBL; BX664742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FO704829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005167081.1; XM_005167024.4.
DR   Ensembl; ENSDART00000005583; ENSDARP00000023794; ENSDARG00000003098.
DR   Ensembl; ENSDART00000005583.9; ENSDARP00000023794.9; ENSDARG00000003098.10.
DR   GeneID; 415256; -.
DR   CTD; 415256; -.
DR   ZFIN; ZDB-GENE-030424-1; kdm5bb.
DR   OMA; PRCDIGM; -.
DR   OrthoDB; 48111at2759; -.
DR   TreeFam; TF106476; -.
DR   Proteomes; UP000000437; Chromosome 8.
DR   Bgee; ENSDARG00000003098; Expressed in tail bud paraxial mesoderm and 58 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16874; ARID_KDM5B; 1.
DR   CDD; cd15603; PHD1_KDM5B; 1.
DR   CDD; cd15607; PHD2_KDM5B; 1.
DR   CDD; cd15687; PHD3_KDM5B; 1.
DR   Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR001606; ARID_dom.
DR   InterPro; IPR036431; ARID_dom_sf.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR003349; JmjN.
DR   InterPro; IPR048615; KDM5_C-hel.
DR   InterPro; IPR047981; KDM5B_ARID.
DR   InterPro; IPR047978; KDM5B_PHD1.
DR   InterPro; IPR047979; KDM5B_PHD3.
DR   InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR004198; Znf_C5HC2.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   PANTHER; PTHR10694:SF3; LYSINE-SPECIFIC DEMETHYLASE 5B; 1.
DR   Pfam; PF01388; ARID; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF02375; JmjN; 1.
DR   Pfam; PF21323; KDM5_C-hel; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF08429; PLU-1; 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   SMART; SM00249; PHD; 3.
DR   SUPFAM; SSF46774; ARID-like; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR   PROSITE; PS51011; ARID; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51183; JMJN; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 3.
PE   1: Evidence at protein level;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:G1K2I1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          15..56
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          80..170
FT                   /note="ARID"
FT                   /evidence="ECO:0000259|PROSITE:PS51011"
FT   DOMAIN          314..364
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          458..624
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          1187..1235
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1463..1516
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          221..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1381..1400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1422..1461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          964..991
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        287..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1422..1447
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1522 AA;  173142 MW;  F61669B7DCE46377 CRC64;
     MTQQGPAEFT PPPECPVFEP SWEEFKDPFA FINKIRPIAE KTGICKVRPP PDWQPPFACD
     VDRLHFTPRI QRLNELEAQT RVKLNFLDQI AKFWDLQGCT LKIPHVERKI LDLYQLNKLV
     ADEGGFDLVC RERRWTKIAM TMGFAPGKAV GSHLRAHYER ILYPYNLFQS GTNLLAPEFA
     VKLTGFGEPP VLEECLQKPG DEVNDIDKEY KPHDLLQRQN VPLQPSNTSA PARRAKRMKT
     ESGCIKSEEG EGVENKPNLR RRMGSFVVKT EQKKEIPIQV KEEPVEIKEL NPEPEKSKPK
     KKNIPPPPVS MVDLYVCLVC GKGNDEDRLL LCDGCDDSYH TFCLIPPLTD VPKGDWRCPK
     CLTQECCKPQ EAFGFEQAHR DYTLKAFGEM ADSFKSDYFN MPVHMVPTEL VEKEFWRLVG
     TIQEDVTVEY GADIASKEFG SGFPIKGGRF KIAPHDEKYL QCGWNLNNMA MMTPSVLTHV
     TADICGMTLP WLYVGMCFSS FCWHIEDHWS YSINYLHWGE PKTWYGAPGF AAEQLEAVMK
     KLAPELFDSQ PDLLHQLVTI MNPNTLMAHG VPIYRTNQCA GEFVITFPRS YHSGFNQGFN
     FAEAVNFCTV DWMPLGRQCV DHYRQLHRYC VFSHDEMVCN MAMKADCLDV VLASAVQKDM
     QLMIKEEREL REKVRKMGVA QCELFQYDLL ADDERQCVKC RTTCYLSALT CPCRPGVQVC
     LYHTHDLCSC PISNYTLNYR FTLDDLYPMM NAVRQRAEYY DDWASRVTEV MEAKLDKKRN
     VTVFRTLLEE SNEQSFPEND LLRQLRLVTQ DAEKCSSVAQ QLLNGKRQTR YRTGKAKSPN
     QLTVEEMRSF VRQLYNLPCS LTQAPLLKEL LNSIEDFQQH SEKLLSDEVS ADAVSEIESL
     LEEGSQFDVF LPELPLLRER LEQARWLTGV HQAEDPVANP CGLSLESMRR LIDRGVGLTP
     HPSIERMMAR LQELLTVSEE LEENAQALLK ARPPESLETL CSMLTQVEGV PAYLPNCLLL
     QDTVNRAKEW LQEAESLQVG GQVPVFSSLS DMVLRAHSIP VRLEPLDQLE VQVSEVQSWK
     ETAAKTFLIK SSPFTLLEVL CPRWEMGSSL KKKKMRKMKG DCVSSGKKKF VKLDSMSDVE
     RALSDSKDSA SAMFTLAEVR LKELESLCSL RASNESKLLP TADCASLKVC VCQKPAMGAM
     LQCELCRDAF HSVCVRGPSD PLDPEAWLCP LCLRSTKPPL DKIRSLLSSL QRIRVRLPEG
     DALRYMIERS VSWQRRVREV IDSYGLSSTS QDGRGASPSQ NLYRSTGHSR KLQLCGSPSR
     CQDWAVSGQE QTVFYTEQRC IPLQGLSPEL EELMVEGLVL QVSLPETQQL YRLLLSGPPT
     TNTSHAEHKS YLTPPQTETD AITSAEKKAK RRMNRDEVDI RERGTKLKSK KQRMMGVEKR
     RERKAASVSA SDMSQSEDSE EDMTLCPAES CLQPEGEEVD WVQCDCCNRW FHMICVGVSA
     ELAAEEDYMC VSCSTSHMDR RK
//
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