CBX3_PONAB
ID CBX3_PONAB Reviewed; 183 AA.
AC Q5R6X7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Chromobox protein homolog 3;
DE AltName: Full=Heterochromatin protein 1 homolog gamma;
DE Short=HP1 gamma;
GN Name=CBX3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Seems to be involved in transcriptional silencing in
CC heterochromatin-like complexes. Recognizes and binds histone H3 tails
CC methylated at 'Lys-9', leading to epigenetic repression. May contribute
CC to the association of the heterochromatin with the inner nuclear
CC membrane through its interaction with lamin B receptor (LBR). Involved
CC in the formation of functional kinetochore through interaction with
CC MIS12 complex proteins. Contributes to the conversion of local
CC chromatin to a heterochromatin-like repressive state through H3 'Lys-9'
CC trimethylation, mediates the recruitment of the methyltransferases
CC SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the
CC circadian target genes such as PER2 itself or PER1. Mediates the
CC recruitment of NIPBL to sites of DNA damage at double-strand breaks
CC (DSBs). {ECO:0000250|UniProtKB:P23198, ECO:0000250|UniProtKB:Q13185}.
CC -!- SUBUNIT: Binds directly to CHAF1A. Interacts with histone H3 methylated
CC at 'Lys-9'. Part of the E2F6.com-1 complex in G0 phase composed of
CC E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR,
CC L3MBTL2 and YAF2. Interacts with INCENP, TRIM28/TIF1B and SP100 (By
CC similarity). Interacts with TIF1/TIF1A (By similarity). Interacts with
CC MIS12 and DSN1. Can interact directly with CBX5 via the chromoshadow
CC domain (By similarity). Interacts with KMT5B and KMT5C (By similarity).
CC Interacts with POGZ. Interacts with CHAMP1. The large PER complex
CC involved in the histone methylation is composed of at least PER2, CBX3,
CC TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the
CC complex (By similarity). Interacts with INCENP. Interacts with NIPBL
CC (via PxVxL motif). Interacts with LRIF1 (via PxVxL motif) (By
CC similarity). Interacts with TTLL12 (By similarity). Interacts with
CC ZNF263; recruited to the SIX3 promoter along with other proteins
CC involved in chromatin modification and transcriptional corepression
CC where it contributes to transcriptional repression (By similarity).
CC {ECO:0000250|UniProtKB:P23198, ECO:0000250|UniProtKB:Q13185}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Note=May be associated
CC with microtubules and mitotic poles during mitosis (Potential).
CC Associates with euchromatin and is largely excluded from constitutive
CC heterochromatin (By similarity). {ECO:0000250, 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; CR860350; CAH92483.1; -; mRNA.
DR RefSeq; NP_001126464.1; NM_001132992.1.
DR RefSeq; XP_009241191.1; XM_009242916.1.
DR RefSeq; XP_009241192.1; XM_009242917.1.
DR RefSeq; XP_009241193.1; XM_009242918.1.
DR AlphaFoldDB; Q5R6X7; -.
DR BMRB; Q5R6X7; -.
DR SMR; Q5R6X7; -.
DR STRING; 9601.ENSPPYP00000019856; -.
DR Ensembl; ENSPPYT00000020641; ENSPPYP00000019856; ENSPPYG00000017714.
DR GeneID; 100173451; -.
DR KEGG; pon:100173451; -.
DR CTD; 11335; -.
DR eggNOG; KOG1911; Eukaryota.
DR GeneTree; ENSGT00940000153305; -.
DR HOGENOM; CLU_045874_1_2_1; -.
DR InParanoid; Q5R6X7; -.
DR OMA; RLTWHTN; -.
DR OrthoDB; 1628171at2759; -.
DR TreeFam; TF350503; -.
DR Proteomes; UP000001595; Chromosome 7.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; ISS:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Biological rhythms; Chromatin regulator; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23198"
FT CHAIN 2..183
FT /note="Chromobox protein homolog 3"
FT /id="PRO_0000080205"
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 79..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..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:0000250|UniProtKB:P23198"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P23198"
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:0000250|UniProtKB:Q13185"
FT MOD_RES 50
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
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:0000250|UniProtKB:Q13185"
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; 20811 MW; 5928C63E0C93A76A CRC64;
MASNKTTLQK MGKKQNGKSK KVEEAEPEEF VVEKVLDRRV VNGKVEYFLK WKGFTDADNT
WEPEENLDCP ELIEAFLNSQ KAGKEKDGTK RKSLSDSESD DSKSKKKRDA ADKPRGFARG
LDPERIIGAT DSSGELMFLM KWKDSDEADL VLAKEANMKC PQIVIAFYEE RLTWHSCPED
EAQ
