CBX3_MOUSE
ID CBX3_MOUSE Reviewed; 183 AA.
AC P23198; Q921C4;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 25-MAY-2022, entry version 187.
DE RecName: Full=Chromobox protein homolog 3;
DE AltName: Full=Heterochromatin protein 1 homolog gamma;
DE Short=HP1 gamma;
DE AltName: Full=M32;
DE AltName: Full=Modifier 2 protein;
GN Name=Cbx3;
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 [GENOMIC DNA].
RA Jones D.O., Mattei M.-G., Horsley D., Cowell I.G., Singh P.B.;
RT "The gene and pseudogenes of Cbx3.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-183.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=1708124; DOI=10.1093/nar/19.4.789;
RA Singh P.B., Miller J.R., Pearce J., Kothary R., Burton R.D., Paro R.,
RA James T.C., Gaunt S.J.;
RT "A sequence motif found in a Drosophila heterochromatin protein is
RT conserved in animals and plants.";
RL Nucleic Acids Res. 19:789-794(1991).
RN [3]
RP PROTEIN SEQUENCE OF 160-171.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=8751383; DOI=10.1159/000134363;
RA Horsley D., Hutchings A., Butcher G.W., Singh P.B.;
RT "M32, a murine homologue of Drosophila heterochromatin protein 1 (HP1),
RT localises to euchromatin within interphase nuclei and is largely excluded
RT from constitutive heterochromatin.";
RL Cytogenet. Cell Genet. 73:308-311(1996).
RN [5]
RP INTERACTION WITH TIF1A.
RX PubMed=8978696;
RA le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F.,
RA Losson R., Chambon P.;
RT "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT control of transcription by nuclear receptors.";
RL EMBO J. 15:6701-6715(1996).
RN [6]
RP INTERACTION WITH KMT5B AND KMT5C.
RX PubMed=15145825; DOI=10.1101/gad.300704;
RA Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G.,
RA Reinberg D., Jenuwein T.;
RT "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at
RT constitutive heterochromatin.";
RL Genes Dev. 18:1251-1262(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-95 AND SER-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-5 AND LYS-44, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP FUNCTION IN CIRCADIAN RHYTHMS, AND IDENTIFICATION IN A LARGE PER COMPLEX.
RX PubMed=24413057; DOI=10.1038/nsmb.2746;
RA Duong H.A., Weitz C.J.;
RT "Temporal orchestration of repressive chromatin modifiers by circadian
RT clock Period complexes.";
RL Nat. Struct. Mol. Biol. 21:126-132(2014).
CC -!- FUNCTION: Component of heterochromatin. Recognizes and binds histone H3
CC tails methylated at 'Lys-9', leading to epigenetic repression. Probably
CC involved in the repression of many genes located in euchromatin, such
CC as E2F1, MYC and CDC25A. Involved in the formation of functional
CC kinetochore through interaction with MIS12 complex proteins.
CC Contributes to the conversion of local chromatin to a heterochromatin-
CC like repressive state through H3 'Lys-9' trimethylation, mediates the
CC recruitment of the methyltransferases SUV39H1 and/or SUV39H2 by the PER
CC complex to the E-box elements of the circadian target genes such as
CC PER2 itself or PER1 (PubMed:24413057). Mediates the recruitment of
CC NIPBL to sites of DNA damage at double-strand breaks (DSBs) (By
CC similarity). {ECO:0000250|UniProtKB:Q13185,
CC ECO:0000269|PubMed:24413057}.
CC -!- SUBUNIT: Binds directly to CHAF1A. Interacts with histone H3 methylated
CC at 'Lys-9' (By similarity). Part of the E2F6.com-1 complex in G0 phase
CC composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2,
CC MBLR, L3MBTL2 and YAF2 (By similarity). Interacts with INCENP,
CC TRIM28/TIF1B and SP100 (By similarity). Interacts with TIF1/TIF1A
CC (PubMed:8978696). Interacts with MIS12 and DSN1 (By similarity). Can
CC interact directly with CBX5 via the chromoshadow domain (By
CC similarity). Interacts with KMT5B and KMT5C (PubMed:15145825).
CC Interacts with POGZ (By similarity). Interacts with CHAMP1 (By
CC similarity). The large PER complex involved in the histone methylation
CC is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2;
CC CBX3 mediates the formation of the complex (PubMed:24413057). Interacts
CC with INCENP (By similarity). Interacts with NIPBL (via PxVxL motif) (By
CC similarity). Interacts with LRIF1 (via PxVxL motif) (By similarity).
CC Interacts with TTLL12 (By similarity). Interacts with ZNF263; recruited
CC to the SIX3 promoter along with other proteins involved in chromatin
CC modification and transcriptional corepression where it contributes to
CC transcriptional repression (By similarity).
CC {ECO:0000250|UniProtKB:Q13185, ECO:0000269|PubMed:15145825,
CC ECO:0000269|PubMed:24413057, ECO:0000269|PubMed:8978696}.
CC -!- INTERACTION:
CC P23198; Q13263: TRIM28; Xeno; NbExp=2; IntAct=EBI-78162, EBI-78139;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8751383}. Note=May be
CC associated with microtubules and mitotic poles during mitosis
CC (Potential). Associates with euchromatin and is largely excluded from
CC constitutive heterochromatin. {ECO:0000305}.
CC -!- PTM: Phosphorylated by PIM1. Phosphorylated during interphase and
CC possibly hyper-phosphorylated during mitosis.
CC {ECO:0000250|UniProtKB:Q13185}.
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DR EMBL; X56683; CAA40012.1; -; mRNA.
DR EMBL; AJ278617; CAC42944.1; -; Genomic_DNA.
DR EMBL; AJ278618; CAC42944.1; JOINED; Genomic_DNA.
DR EMBL; AJ278619; CAC42944.1; JOINED; Genomic_DNA.
DR PIR; S26846; S26846.
DR AlphaFoldDB; P23198; -.
DR BMRB; P23198; -.
DR SMR; P23198; -.
DR ComplexPortal; CPX-470; L3MBTL1 complex.
DR DIP; DIP-28136N; -.
DR IntAct; P23198; 16.
DR MINT; P23198; -.
DR STRING; 10090.ENSMUSP00000031862; -.
DR iPTMnet; P23198; -.
DR PhosphoSitePlus; P23198; -.
DR SwissPalm; P23198; -.
DR REPRODUCTION-2DPAGE; IPI00129468; -.
DR EPD; P23198; -.
DR jPOST; P23198; -.
DR MaxQB; P23198; -.
DR PaxDb; P23198; -.
DR PeptideAtlas; P23198; -.
DR PRIDE; P23198; -.
DR ProteomicsDB; 265569; -.
DR MGI; MGI:108515; Cbx3.
DR eggNOG; KOG1911; Eukaryota.
DR InParanoid; P23198; -.
DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR ChiTaRS; Cbx3; mouse.
DR PRO; PR:P23198; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P23198; protein.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0061793; C:chromatin lock complex; ISO:MGI.
DR GO; GO:0010369; C:chromocenter; IDA:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; ISO:MGI.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0035985; C:senescence-associated heterochromatin focus; ISO:MGI.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:1990226; F:histone methyltransferase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR038033; CBX3.
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:SF149; PTHR22812:SF149; 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; SSF54160; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Biological rhythms; Chromatin regulator;
KW Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..183
FT /note="Chromobox protein homolog 3"
FT /id="PRO_0000080204"
FT DOMAIN 30..88
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 121..179
FT /note="Chromo 2; shadow subtype"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 50
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT CROSSLNK 103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
SQ SEQUENCE 183 AA; 20855 MW; 2FF3AD53B883E27E CRC64;
MASNKTTLQK MGKKQNGKSK KVEEAEPEEF VVEKVLDRRV VNGKVEYFLK WKGFTDADNT
WEPEENLDCP ELIEDFLNSQ KAGKEKDGTK RKSLSDSESD DSKSKKKRDA ADKPRGFARG
LDPERIIGAT DSSGELMFLM KWKDSDEADL VLAKEANMKC PQIVIAFYEE RLTWHSCPED
EAQ
