CBX7_RAT
ID CBX7_RAT Reviewed; 158 AA.
AC P60889;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Chromobox protein homolog 7;
GN Name=Cbx7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like
CC complex, a complex class required to maintain the transcriptionally
CC repressive state of many genes, including Hox genes, throughout
CC development. PcG PRC1 complex acts via chromatin remodeling and
CC modification of histones; it mediates monoubiquitination of histone H2A
CC 'Lys-119', rendering chromatin heritably changed in its expressibility.
CC Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3). Binds to
CC histone H3 trimethylated 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3).
CC May possibly also bind trimethylated lysine residues in other proteins
CC (in vitro). Binds non-coding, single-stranded and double-stranded RNA.
CC Plays a role in the timely repression of differentiation-specific genes
CC in pluripotent embryonic stem cells to maintain the undifferentiated
CC state. Regulator of cellular lifespan by maintaining the repression of
CC CDKN2A, but not by inducing telomerase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q8VDS3}.
CC -!- SUBUNIT: Component of a PRC1-like complex. Distinct PRC1-like core
CC complexes are composed of a RING1 subunit (RING1B or RING1A), one of
CC the six PCGF proteins (PCGF1-6), one PHC protein (PHC1-3) and one of
CC the CBX proteins (CBX2, CBX4, CBX6, CBX7 or CBX8). The composition of
CC the PRC1 complex may differ between the PRC1 complex in pluripotent
CC embryonic stem cells containing RNF2, CBX7 and PCGF2, and the PRC1
CC complex in differentiating cells containing RNF2, CBX2, CBX4 and BMI1.
CC Interacts with RING1. Interacts with RNF2/RING1B. Interacts with PCGF1,
CC PCGF2, PCGF3, PCGF5 and PCGF6. Interacts (via chromodomain) with
CC histone H3K9Me3 and H3K27me3. Interacts with H3K9Me2 and H4K20Me1.
CC Interacts (via chromodomain) with single-stranded and double-stranded
CC RNA; RNA binding seems to be required for the localization to chromatin
CC (By similarity). {ECO:0000250|UniProtKB:Q8VDS3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8VDS3}.
CC Chromosome {ECO:0000250|UniProtKB:Q8VDS3}. Note=Requires trimethylation
CC at 'Lys-27' (H3K27me3) for the localization to chromatin. Localizes to
CC facultative heterochromatin and to the inactivated X chromosome in
CC females. {ECO:0000250|UniProtKB:Q8VDS3}.
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DR EMBL; BC062392; AAH62392.1; -; mRNA.
DR RefSeq; NP_954548.1; NM_199117.2.
DR RefSeq; XP_006242087.1; XM_006242025.3.
DR AlphaFoldDB; P60889; -.
DR BMRB; P60889; -.
DR SMR; P60889; -.
DR IntAct; P60889; 2.
DR MINT; P60889; -.
DR STRING; 10116.ENSRNOP00000022631; -.
DR PaxDb; P60889; -.
DR GeneID; 362962; -.
DR KEGG; rno:362962; -.
DR UCSC; RGD:735027; rat.
DR CTD; 23492; -.
DR RGD; 735027; Cbx7.
DR VEuPathDB; HostDB:ENSRNOG00000016875; -.
DR eggNOG; KOG2748; Eukaryota.
DR InParanoid; P60889; -.
DR OMA; VMAYEEX; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; P60889; -.
DR TreeFam; TF106456; -.
DR PRO; PR:P60889; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000016875; Expressed in cerebellum and 20 other tissues.
DR Genevisible; P60889; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0035064; F:methylated histone binding; ISO:RGD.
DR GO; GO:0003727; F:single-stranded RNA binding; ISO:RGD.
DR GO; GO:0032183; F:SUMO binding; IBA:GO_Central.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0003006; P:developmental process involved in reproduction; IEP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:RGD.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0048733; P:sebaceous gland development; ISO:RGD.
DR InterPro; IPR043000; CBX7.
DR InterPro; IPR033773; CBX7_C.
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; IPR023779; Chromodomain_CS.
DR PANTHER; PTHR47277; PTHR47277; 2.
DR Pfam; PF17218; CBX7_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR PRINTS; PR00504; CHROMODOMAIN.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Chromosome; Nucleus; Reference proteome; Repressor;
KW RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..158
FT /note="Chromobox protein homolog 7"
FT /id="PRO_0000080214"
FT DOMAIN 11..69
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 60..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 158 AA; 17966 MW; D2D11F0406DEDC5D CRC64;
MELSAIGEQV FAVESIRKKR VRKGKVEYLV KWKGWPPKYS TWEPEEHILD PRLVMAYEEK
EEKDRASGYR KRGPKPKRLL LQESAAPDVL QATGDWEPVE QPPEEEAEAD LTNGPPPWTP
MLPSSEVTVT DITANSVTVT FREAQAAEGF FRDRSGKL
