ID CBX7_HUMAN Reviewed; 251 AA.
AC O95931; Q86T17;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 187.
DE RecName: Full=Chromobox protein homolog 7;
GN Name=CBX7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PNS;
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).
RN [3]
RP SUBCELLULAR LOCATION, INTERACTION WITH RING1, AND MUTAGENESIS OF LYS-31 AND
RP TRP-32.
RX PubMed=14647293; DOI=10.1038/ncb1077;
RA Gil J., Bernard D., Martinez D., Beach D.;
RT "Polycomb CBX7 has a unifying role in cellular lifespan.";
RL Nat. Cell Biol. 6:67-72(2004).
RN [4]
RP INTERACTION WITH RNF2.
RX PubMed=19791798; DOI=10.1021/bi901131u;
RA Bezsonova I., Walker J.R., Bacik J.P., Duan S., Dhe-Paganon S.,
RA Arrowsmith C.H.;
RT "Ring1B contains a ubiquitin-like docking module for interaction with Cbx
RT proteins.";
RL Biochemistry 48:10542-10548(2009).
RN [5]
RP FUNCTION, IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND INTERACTION WITH BMI1.
RX PubMed=19636380; DOI=10.1371/journal.pone.0006380;
RA Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J.,
RA Rodriguez-Niedenfuhr M., Gil J., Peters G.;
RT "Several distinct polycomb complexes regulate and co-localize on the INK4a
RT tumor suppressor locus.";
RL PLoS ONE 4:E6380-E6380(2009).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21060834; DOI=10.1371/journal.pone.0013732;
RA Li Q., Wang X., Lu Z., Zhang B., Guan Z., Liu Z., Zhong Q., Gu L., Zhou J.,
RA Zhu B., Ji J., Deng D.;
RT "Polycomb CBX7 directly controls trimethylation of histone H3 at lysine 9
RT at the p16 locus.";
RL PLoS ONE 5:E13732-E13732(2010).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND INTERACTION WITH RING1; RNF2;
RP PCGF1; PCGF2; PCGF3; BMI1; PCGF5 AND PCGF6.
RX PubMed=21282530; DOI=10.1074/mcp.m110.002642;
RA Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
RT "Interaction proteomics analysis of polycomb proteins defines distinct PRC1
RT Complexes in mammalian cells.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [8]
RP STRUCTURE BY NMR OF 7-62.
RG Structural genomics consortium (SGC);
RT "Solution NMR structure of the chromobox protein homolog 7.";
RL Submitted (MAR-2008) to the PDB data bank.
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 219-248 IN COMPLEX WITH RNF2,
RP INTERACTION WITH RNF2, AND MUTAGENESIS OF PHE-234 AND PHE-244.
RX PubMed=20696397; DOI=10.1016/j.str.2010.04.013;
RA Wang R., Taylor A.B., Leal B.Z., Chadwell L.V., Ilangovan U.,
RA Robinson A.K., Schirf V., Hart P.J., Lafer E.M., Demeler B., Hinck A.P.,
RA McEwen D.G., Kim C.A.;
RT "Polycomb group targeting through different binding partners of RING1B C-
RT terminal domain.";
RL Structure 18:966-975(2010).
RN [10]
RP STRUCTURE BY NMR OF 8-62, FUNCTION, AND INTERACTION WITH TRIMETHYLATED
RP LYSINE RESIDUES.
RX PubMed=21047797; DOI=10.1074/jbc.m110.191411;
RA Kaustov L., Ouyang H., Amaya M., Lemak A., Nady N., Duan S., Wasney G.A.,
RA Li Z., Vedadi M., Schapira M., Min J., Arrowsmith C.H.;
RT "Recognition and specificity determinants of the human cbx chromodomains.";
RL J. Biol. Chem. 286:521-529(2011).
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 trimethylated lysine residues in histones, and possibly also other
CC proteins. Regulator of cellular lifespan by maintaining the repression
CC of CDKN2A, but not by inducing telomerase activity.
CC {ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21047797,
CC ECO:0000269|PubMed:21060834, ECO:0000269|PubMed:21282530}.
CC -!- SUBUNIT: Component of a PRC1-like complex. Interacts with RING1 and
CC RNF2/RING1B, but not with BMI1, EED or EZH2. Interacts with PCGF1,
CC PCGF2, PCGF3, PCGF5 and PCGF6. {ECO:0000269|PubMed:14647293,
CC ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:19791798,
CC ECO:0000269|PubMed:20696397, ECO:0000269|PubMed:21047797,
CC ECO:0000269|PubMed:21282530}.
CC -!- INTERACTION:
CC O95931; P35226: BMI1; NbExp=12; IntAct=EBI-3923843, EBI-2341576;
CC O95931; Q9HCE1: MOV10; NbExp=5; IntAct=EBI-3923843, EBI-1055820;
CC O95931; Q9BSM1: PCGF1; NbExp=2; IntAct=EBI-3923843, EBI-749901;
CC O95931; P35227: PCGF2; NbExp=6; IntAct=EBI-3923843, EBI-2129767;
CC O95931; Q3KNV8: PCGF3; NbExp=2; IntAct=EBI-3923843, EBI-2339807;
CC O95931; Q9BYE7: PCGF6; NbExp=4; IntAct=EBI-3923843, EBI-1048026;
CC O95931; Q06587: RING1; NbExp=5; IntAct=EBI-3923843, EBI-752313;
CC O95931; Q99496: RNF2; NbExp=15; IntAct=EBI-3923843, EBI-722416;
CC O95931; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-3923843, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14647293,
CC ECO:0000269|PubMed:21060834, ECO:0000269|PubMed:21282530}.
CC -!- MISCELLANEOUS: The human orthologuous proteins of Drosophila Polycomb
CC group protein Pc, CBX2, CBX4, CBX6, CBX7 and CBX8, show distinct
CC nuclear localizations, contribute differently to transcriptional
CC repression, and appear to be part of distinct PRC1-like protein
CC complexes.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/43845/CBX7";
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DR EMBL; AL031846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051773; AAH51773.1; -; mRNA.
DR CCDS; CCDS13986.1; -.
DR RefSeq; NP_783640.1; NM_175709.4.
DR PDB; 2K1B; NMR; -; A=7-62.
DR PDB; 2L12; NMR; -; A=7-62.
DR PDB; 2L1B; NMR; -; A=8-62.
DR PDB; 3GS2; X-ray; 1.70 A; B/D=219-248.
DR PDB; 4MN3; X-ray; 1.54 A; A=7-62.
DR PDB; 5EPJ; X-ray; 1.60 A; A=7-62.
DR PDB; 6V2R; X-ray; 1.60 A; A=7-62.
DR PDBsum; 2K1B; -.
DR PDBsum; 2L12; -.
DR PDBsum; 2L1B; -.
DR PDBsum; 3GS2; -.
DR PDBsum; 4MN3; -.
DR PDBsum; 5EPJ; -.
DR PDBsum; 6V2R; -.
DR AlphaFoldDB; O95931; -.
DR BMRB; O95931; -.
DR SMR; O95931; -.
DR BioGRID; 117044; 45.
DR ComplexPortal; CPX-2600; Polycomb repressive complex 1, RING1-PCGF2-CBX7-PHC1 variant.
DR ComplexPortal; CPX-2601; Polycomb repressive complex 1, RING1-PCGF2-CBX7-PHC2 variant.
DR ComplexPortal; CPX-2619; Polycomb repressive complex 1, RING1-PCGF2-CBX7-PHC3 variant.
DR ComplexPortal; CPX-7513; Polycomb repressive complex 1, RING1-PCGF4-CBX7-PHC1 variant.
DR ComplexPortal; CPX-7514; Polycomb repressive complex 1, RING1-PCGF4-CBX7-PHC2 variant.
DR ComplexPortal; CPX-7515; Polycomb repressive complex 1, RING1-PCGF4-CBX7-PHC3 variant.
DR ComplexPortal; CPX-7530; Polycomb repressive complex 1, RING2-PCGF2-CBX7-PHC1 variant.
DR ComplexPortal; CPX-7531; Polycomb repressive complex 1, RING2-PCGF2-CBX7-PHC2 variant.
DR ComplexPortal; CPX-7532; Polycomb repressive complex 1, RING2-PCGF2-CBX7-PHC3 variant.
DR ComplexPortal; CPX-7551; Polycomb repressive complex 1, RING2-PCGF4-CBX7-PHC1 variant.
DR ComplexPortal; CPX-7552; Polycomb repressive complex 1, RING2-PCGF4-CBX7-PHC2 variant.
DR ComplexPortal; CPX-7553; Polycomb repressive complex 1, RING2-PCGF4-CBX7-PHC3 variant.
DR DIP; DIP-44565N; -.
DR IntAct; O95931; 35.
DR MINT; O95931; -.
DR STRING; 9606.ENSP00000216133; -.
DR BindingDB; O95931; -.
DR ChEMBL; CHEMBL1764946; -.
DR iPTMnet; O95931; -.
DR PhosphoSitePlus; O95931; -.
DR BioMuta; CBX7; -.
DR jPOST; O95931; -.
DR MassIVE; O95931; -.
DR MaxQB; O95931; -.
DR PaxDb; 9606-ENSP00000216133; -.
DR PeptideAtlas; O95931; -.
DR ProteomicsDB; 51131; -.
DR Antibodypedia; 26564; 173 antibodies from 29 providers.
DR DNASU; 23492; -.
DR Ensembl; ENST00000216133.10; ENSP00000216133.5; ENSG00000100307.13.
DR GeneID; 23492; -.
DR KEGG; hsa:23492; -.
DR MANE-Select; ENST00000216133.10; ENSP00000216133.5; NM_175709.5; NP_783640.1.
DR UCSC; uc003axb.4; human.
DR AGR; HGNC:1557; -.
DR CTD; 23492; -.
DR DisGeNET; 23492; -.
DR GeneCards; CBX7; -.
DR HGNC; HGNC:1557; CBX7.
DR HPA; ENSG00000100307; Low tissue specificity.
DR MIM; 608457; gene.
DR neXtProt; NX_O95931; -.
DR OpenTargets; ENSG00000100307; -.
DR PharmGKB; PA26132; -.
DR VEuPathDB; HostDB:ENSG00000100307; -.
DR eggNOG; KOG2748; Eukaryota.
DR GeneTree; ENSGT00940000158365; -.
DR HOGENOM; CLU_042051_1_0_1; -.
DR InParanoid; O95931; -.
DR OMA; KPHKAHK; -.
DR OrthoDB; 75895at2759; -.
DR PhylomeDB; O95931; -.
DR TreeFam; TF106456; -.
DR PathwayCommons; O95931; -.
DR SignaLink; O95931; -.
DR SIGNOR; O95931; -.
DR BioGRID-ORCS; 23492; 9 hits in 1163 CRISPR screens.
DR EvolutionaryTrace; O95931; -.
DR GenomeRNAi; 23492; -.
DR Pharos; O95931; Tchem.
DR PRO; PR:O95931; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O95931; Protein.
DR Bgee; ENSG00000100307; Expressed in cerebellar vermis and 210 other cell types or tissues.
DR ExpressionAtlas; O95931; baseline and differential.
DR Genevisible; O95931; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR CDD; cd18646; CD_Cbx7; 1.
DR Gene3D; 2.40.50.40; -; 1.
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; CHROMOBOX PROTEIN HOMOLOG 7; 1.
DR PANTHER; PTHR47277:SF1; CHROMOBOX PROTEIN HOMOLOG 7; 1.
DR Pfam; PF17218; CBX7_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR PRINTS; PR00504; CHROMODOMAIN.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..251
FT /note="Chromobox protein homolog 7"
FT /id="PRO_0000080212"
FT DOMAIN 11..69
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 190..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..236
FT /note="Required for cellular lifespan extension"
FT MUTAGEN 31
FT /note="K->A: Loss of cellular lifespan extension."
FT /evidence="ECO:0000269|PubMed:14647293"
FT MUTAGEN 32
FT /note="W->A: Loss of cellular lifespan extension."
FT /evidence="ECO:0000269|PubMed:14647293"
FT MUTAGEN 234
FT /note="F->D: Loss of interaction with RNF2."
FT /evidence="ECO:0000269|PubMed:20696397"
FT MUTAGEN 244
FT /note="F->D: Reduced interaction with RNF2."
FT /evidence="ECO:0000269|PubMed:20696397"
FT CONFLICT 77
FT /note="K -> R (in Ref. 2; AAH51773)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="A -> P (in Ref. 2; AAH51773)"
FT /evidence="ECO:0000305"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:4MN3"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:4MN3"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4MN3"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:4MN3"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4MN3"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:4MN3"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:3GS2"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:3GS2"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:3GS2"
SQ SEQUENCE 251 AA; 28341 MW; A90019C1D08812B8 CRC64;
MELSAIGEQV FAVESIRKKR VRKGKVEYLV KWKGWPPKYS TWEPEEHILD PRLVMAYEEK
EERDRASGYR KRGPKPKRLL LQRLYSMDLR SSHKAKGKEK LCFSLTCPLG SGSPEGVVKA
GAPELVDKGP LVPTLPFPLR KPRKAHKYLR LSRKKFPPRG PNLESHSHRR ELFLQEPPAP
DVLQAAGEWE PAAQPPEEEA DADLAEGPPP WTPALPSSEV TVTDITANSI TVTFREAQAA
EGFFRDRSGK F
//
