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Database: UniProt
Entry: F1QM86_DANRE
LinkDB: F1QM86_DANRE
Original site: F1QM86_DANRE 
ID   F1QM86_DANRE            Unreviewed;       212 AA.
AC   F1QM86; A0A8M1PFU2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Chromobox homolog 1a (HP1 beta homolog Drosophila) {ECO:0000313|Ensembl:ENSDARP00000118656};
DE   SubName: Full=Chromobox protein homolog 1 {ECO:0000313|RefSeq:NP_956040.2};
GN   Name=cbx1a {ECO:0000313|Ensembl:ENSDARP00000118656,
GN   ECO:0000313|RefSeq:NP_956040.2,
GN   ECO:0000313|ZFIN:ZDB-GENE-030131-4945};
GN   Synonyms=cbx1 {ECO:0000313|RefSeq:NP_956040.2}, wu:fe14b09
GN   {ECO:0000313|RefSeq:NP_956040.2}, zgc:55739
GN   {ECO:0000313|RefSeq:NP_956040.2};
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:ENSDARP00000118656};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000118656}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118656};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:NP_956040.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_956040.2};
RX   PubMed=24240475;
RA   Huang H.T., Kathrein K.L., Barton A., Gitlin Z., Huang Y.H., Ward T.P.,
RA   Hofmann O., Dibiase A., Song A., Tyekucheva S., Hide W., Zhou Y., Zon L.I.;
RT   "A network of epigenetic regulators guides developmental haematopoiesis in
RT   vivo.";
RL   Nat. Cell Biol. 15:1516-1525(2013).
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000118656, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118656};
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   [4] {ECO:0000313|RefSeq:NP_956040.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_956040.2};
RX   PubMed=25059688;
RA   Baumgart M., Groth M., Priebe S., Savino A., Testa G., Dix A., Ripa R.,
RA   Spallotta F., Gaetano C., Ori M., Terzibasi Tozzini E., Guthke R.,
RA   Platzer M., Cellerino A.;
RT   "RNA-seq of the aging brain in the short-lived fish N. furzeri - conserved
RT   pathways and novel genes associated with neurogenesis.";
RL   Aging Cell 13:965-974(2014).
RN   [5] {ECO:0000313|RefSeq:NP_956040.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_956040.2};
RX   PubMed=24467753;
RA   Rakshambikai R., Srinivasan N., Gadkari R.A.;
RT   "Repertoire of protein kinases encoded in the genome of zebrafish shows
RT   remarkably large population of PIM kinases.";
RL   J. Bioinform. Comput. Biol. 12:1350014-1350014(2014).
RN   [6] {ECO:0000313|RefSeq:NP_956040.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_956040.2};
RX   PubMed=25485542;
RA   Solin S.L., Wang Y., Mauldin J., Schultz L.E., Lincow D.E., Brodskiy P.A.,
RA   Jones C.A., Syrkin-Nikolau J., Linn J.M., Essner J.J., Hostetter J.M.,
RA   Whitley E.M., Cameron J.D., Chou H.H., Severin A.J., Sakaguchi D.S.,
RA   McGrail M.;
RT   "Molecular and cellular characterization of a zebrafish optic pathway tumor
RT   line implicates glia-derived progenitors in tumorigenesis.";
RL   PLoS ONE 9:e114888-e114888(2014).
RN   [7] {ECO:0000313|RefSeq:NP_956040.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_956040.2};
RX   PubMed=25985063;
RA   Sheng Y., Zhao W., Song Y., Li Z., Luo M., Lei Q., Cheng H., Zhou R.;
RT   "Proteomic analysis of three gonad types of swamp eel reveals genes
RT   differentially expressed during sex reversal.";
RL   Sci. Rep. 5:10176-10176(2015).
RN   [8] {ECO:0000313|RefSeq:NP_956040.2}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_956040.2};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AL953901; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR450718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_956040.2; NM_199746.2.
DR   STRING; 7955.ENSDARP00000118656; -.
DR   PaxDb; 7955-ENSDARP00000118656; -.
DR   Ensembl; ENSDART00000143088.2; ENSDARP00000118656.1; ENSDARG00000004189.10.
DR   Ensembl; ENSDART00000191483.1; ENSDARP00000146902.1; ENSDARG00000110945.1.
DR   GeneID; 326746; -.
DR   KEGG; dre:326746; -.
DR   AGR; ZFIN:ZDB-GENE-030131-4945; -.
DR   CTD; 326746; -.
DR   ZFIN; ZDB-GENE-030131-4945; cbx1a.
DR   eggNOG; KOG1911; Eukaryota.
DR   HOGENOM; CLU_045874_1_2_1; -.
DR   OMA; YNTWEKE; -.
DR   OrthoDB; 75895at2759; -.
DR   TreeFam; TF350503; -.
DR   Proteomes; UP000000437; Alternate scaffold 3.
DR   Proteomes; UP000000437; Chromosome 3.
DR   Bgee; ENSDARG00000004189; Expressed in gastrula and 29 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0005721; C:pericentric heterochromatin; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd18654; CSD_HP1beta_Cbx1; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR017984; Chromo_dom_subgr.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR008251; Chromo_shadow_dom.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   PANTHER; PTHR22812:SF160; CHROMOBOX HOMOLOG 1A (HP1 BETA HOMOLOG DROSOPHILA)-RELATED; 1.
DR   PANTHER; PTHR22812; CHROMOBOX PROTEIN; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF01393; Chromo_shadow; 1.
DR   PRINTS; PR00504; CHROMODOMAIN.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00300; ChSh; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 2.
PE   1: Evidence at protein level;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1QM86};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT   DOMAIN          50..108
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          144..202
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   212 AA;  24252 MW;  F5BE5BB2522DDEB1 CRC64;
     MSMSQPTETV SDAPSVTEEV SPDSKLAATA GKKQTKKKVE DVVEEEEEEY VVEKVLDRRV
     VKGRVEYLLK WKGFSEEDNT WEPEDNLDCP DLIAEYMTKH KINDDKKESS AKRKESDTDG
     GGEDSRPKKR KDEQDKPRGF ARGLDPERII GATDSSGELM FLMKWKNSDE ADLVPAKEAN
     VKCPQVVISF YEERLTWHSY PSEEEEKKDD KN
//
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