ID CBX8_HUMAN Reviewed; 389 AA. AC Q9HC52; Q96H39; Q9NR07; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 3. DT 27-MAR-2024, entry version 197. DE RecName: Full=Chromobox protein homolog 8; DE AltName: Full=Polycomb 3 homolog; DE Short=Pc3; DE Short=hPc3; DE AltName: Full=Rectachrome 1; GN Name=CBX8; Synonyms=PC3, RC1; 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 [MRNA]. RX PubMed=10825164; DOI=10.1074/jbc.m001835200; RA Bardos J.I., Saurin A.J., Tissot C., Duprez E., Freemont P.S.; RT "HPC3 is a new human polycomb orthologue that interacts and associates with RT RING1 and Bmi1 and has transcriptional repression properties."; RL J. Biol. Chem. 275:28785-28792(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-317. RC TISSUE=Colon carcinoma; RA Michael M.Z., James R.J.; RT "Isolation of Polycomb and Trithorax-related genes that are expressed in RT human colorectal mucosa."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-317. RC TISSUE=Embryo; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Muscle; 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 [5] RP INTERACTION WITH MLLT3. RX PubMed=11313972; DOI=10.1038/sj.onc.1204108; RA Garcia-Cuellar M.P., Zilles O., Schreiner S.A., Birke M., Winkler T.H., RA Slany R.K.; RT "The ENL moiety of the childhood leukemia-associated MLL-ENL oncoprotein RT recruits human Polycomb 3."; RL Oncogene 20:411-419(2001). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A PRC1-LIKE RP HPRC-H COMPLEX WITH BMI1; CBX2; CBX4; PHC1; PHC2; PHC3; RING1 AND RNF2. RX PubMed=12167701; DOI=10.1128/mcb.22.17.6070-6078.2002; RA Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P., RA Kingston R.E.; RT "The core of the polycomb repressive complex is compositionally and RT functionally conserved in flies and humans."; RL Mol. Cell. Biol. 22:6070-6078(2002). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-130; SER-256; RP SER-265 AND SER-352, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND INTERACTION WITH BMI1 AND PCGF2. 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-191 AND SER-352, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-256; SER-265; RP SER-311 AND SER-332, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-311, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 8-61 IN COMPLEX WITH HISTONE H3 RP PEPTIDE. 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 {ECO:0000269|PubMed:21282530}. CC -!- SUBUNIT: Component of a PRC1-like complex. Interacts with RING1 RNF2, CC PCGF1, PCGF2, PCGF3, BMI1, PCGF5 and PCGF6. Interacts with MLLT3 and CC histone H3. Interacts with PHC2 (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q9HC52; O94929-2: ABLIM3; NbExp=3; IntAct=EBI-712912, EBI-11961672; CC Q9HC52; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-712912, EBI-1642333; CC Q9HC52; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-712912, EBI-11524452; CC Q9HC52; Q6W2J9: BCOR; NbExp=9; IntAct=EBI-712912, EBI-950027; CC Q9HC52; P35226: BMI1; NbExp=30; IntAct=EBI-712912, EBI-2341576; CC Q9HC52; Q13137: CALCOCO2; NbExp=6; IntAct=EBI-712912, EBI-739580; CC Q9HC52; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-712912, EBI-3866279; CC Q9HC52; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-712912, EBI-11530605; CC Q9HC52; O00257: CBX4; NbExp=4; IntAct=EBI-712912, EBI-722425; CC Q9HC52; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-712912, EBI-10171416; CC Q9HC52; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-712912, EBI-2808286; CC Q9HC52; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-712912, EBI-739624; CC Q9HC52; Q92997: DVL3; NbExp=3; IntAct=EBI-712912, EBI-739789; CC Q9HC52; Q13643: FHL3; NbExp=5; IntAct=EBI-712912, EBI-741101; CC Q9HC52; A1L4K1: FSD2; NbExp=6; IntAct=EBI-712912, EBI-5661036; CC Q9HC52; P51114-2: FXR1; NbExp=3; IntAct=EBI-712912, EBI-11022345; CC Q9HC52; O75420: GIGYF1; NbExp=3; IntAct=EBI-712912, EBI-947774; CC Q9HC52; Q08379: GOLGA2; NbExp=6; IntAct=EBI-712912, EBI-618309; CC Q9HC52; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-712912, EBI-5916454; CC Q9HC52; Q96D09: GPRASP2; NbExp=6; IntAct=EBI-712912, EBI-473189; CC Q9HC52; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-712912, EBI-717919; CC Q9HC52; P16401: H1-5; NbExp=2; IntAct=EBI-712912, EBI-5327611; CC Q9HC52; Q6NT76: HMBOX1; NbExp=8; IntAct=EBI-712912, EBI-2549423; CC Q9HC52; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-712912, EBI-10961706; CC Q9HC52; O75031: HSF2BP; NbExp=3; IntAct=EBI-712912, EBI-7116203; CC Q9HC52; Q13422: IKZF1; NbExp=3; IntAct=EBI-712912, EBI-745305; CC Q9HC52; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-712912, EBI-11522367; CC Q9HC52; A0A0C4DFT8: JADE2; NbExp=3; IntAct=EBI-712912, EBI-12094820; CC Q9HC52; Q96N16: JAKMIP1; NbExp=3; IntAct=EBI-712912, EBI-2680803; CC Q9HC52; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-712912, EBI-2556193; CC Q9HC52; Q92993: KAT5; NbExp=2; IntAct=EBI-712912, EBI-399080; CC Q9HC52; Q7L273: KCTD9; NbExp=6; IntAct=EBI-712912, EBI-4397613; CC Q9HC52; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-712912, EBI-2125614; CC Q9HC52; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-712912, EBI-14069005; CC Q9HC52; Q15323: KRT31; NbExp=3; IntAct=EBI-712912, EBI-948001; CC Q9HC52; O76011: KRT34; NbExp=3; IntAct=EBI-712912, EBI-1047093; CC Q9HC52; Q6A162: KRT40; NbExp=6; IntAct=EBI-712912, EBI-10171697; CC Q9HC52; Q9Y333: LSM2; NbExp=3; IntAct=EBI-712912, EBI-347416; CC Q9HC52; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-712912, EBI-741037; CC Q9HC52; Q8IYB1: MB21D2; NbExp=3; IntAct=EBI-712912, EBI-11323212; CC Q9HC52; P23508: MCC; NbExp=3; IntAct=EBI-712912, EBI-307531; CC Q9HC52; Q99750: MDFI; NbExp=3; IntAct=EBI-712912, EBI-724076; CC Q9HC52; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-712912, EBI-10172526; CC Q9HC52; P42568: MLLT3; NbExp=2; IntAct=EBI-712912, EBI-716132; CC Q9HC52; Q9HCE1: MOV10; NbExp=5; IntAct=EBI-712912, EBI-1055820; CC Q9HC52; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-712912, EBI-742948; CC Q9HC52; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-712912, EBI-11522433; CC Q9HC52; Q15742: NAB2; NbExp=3; IntAct=EBI-712912, EBI-8641936; CC Q9HC52; Q9BSM1: PCGF1; NbExp=7; IntAct=EBI-712912, EBI-749901; CC Q9HC52; P35227: PCGF2; NbExp=11; IntAct=EBI-712912, EBI-2129767; CC Q9HC52; Q3KNV8: PCGF3; NbExp=4; IntAct=EBI-712912, EBI-2339807; CC Q9HC52; Q86SE9: PCGF5; NbExp=4; IntAct=EBI-712912, EBI-2827999; CC Q9HC52; Q9BYE7: PCGF6; NbExp=4; IntAct=EBI-712912, EBI-1048026; CC Q9HC52; Q9C0D0: PHACTR1; NbExp=3; IntAct=EBI-712912, EBI-7971325; CC Q9HC52; Q8IXK0: PHC2; NbExp=8; IntAct=EBI-712912, EBI-713786; CC Q9HC52; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-712912, EBI-14066006; CC Q9HC52; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-712912, EBI-79165; CC Q9HC52; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-712912, EBI-10232538; CC Q9HC52; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-712912, EBI-742388; CC Q9HC52; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-712912, EBI-302345; CC Q9HC52; Q9UL42: PNMA2; NbExp=6; IntAct=EBI-712912, EBI-302355; CC Q9HC52; O15160: POLR1C; NbExp=3; IntAct=EBI-712912, EBI-1055079; CC Q9HC52; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-712912, EBI-11320284; CC Q9HC52; P31321: PRKAR1B; NbExp=3; IntAct=EBI-712912, EBI-2805516; CC Q9HC52; Q86WH2: RASSF3; NbExp=3; IntAct=EBI-712912, EBI-2845202; CC Q9HC52; Q06587: RING1; NbExp=18; IntAct=EBI-712912, EBI-752313; CC Q9HC52; Q99496: RNF2; NbExp=11; IntAct=EBI-712912, EBI-722416; CC Q9HC52; Q96KN7: RPGRIP1; NbExp=3; IntAct=EBI-712912, EBI-1050213; CC Q9HC52; Q86VW0: SESTD1; NbExp=3; IntAct=EBI-712912, EBI-6117072; CC Q9HC52; P35711: SOX5; NbExp=3; IntAct=EBI-712912, EBI-3505701; CC Q9HC52; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-712912, EBI-529518; CC Q9HC52; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-712912, EBI-11139477; CC Q9HC52; Q12800: TFCP2; NbExp=6; IntAct=EBI-712912, EBI-717422; CC Q9HC52; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-712912, EBI-1105213; CC Q9HC52; Q12933: TRAF2; NbExp=6; IntAct=EBI-712912, EBI-355744; CC Q9HC52; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-712912, EBI-492476; CC Q9HC52; P36406: TRIM23; NbExp=3; IntAct=EBI-712912, EBI-740098; CC Q9HC52; P14373: TRIM27; NbExp=3; IntAct=EBI-712912, EBI-719493; CC Q9HC52; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-712912, EBI-2130429; CC Q9HC52; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-712912, EBI-739485; CC Q9HC52; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-712912, EBI-744794; CC Q9HC52; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-712912, EBI-9090990; CC Q9HC52; Q495M9: USH1G; NbExp=3; IntAct=EBI-712912, EBI-8601749; CC Q9HC52; P51784: USP11; NbExp=5; IntAct=EBI-712912, EBI-306876; CC Q9HC52; Q93009: USP7; NbExp=7; IntAct=EBI-712912, EBI-302474; CC Q9HC52; P08670: VIM; NbExp=3; IntAct=EBI-712912, EBI-353844; CC Q9HC52; O43829: ZBTB14; NbExp=6; IntAct=EBI-712912, EBI-10176632; CC Q9HC52; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-712912, EBI-742740; CC Q9HC52; Q96C00: ZBTB9; NbExp=3; IntAct=EBI-712912, EBI-395708; CC Q9HC52; O15231: ZNF185; NbExp=3; IntAct=EBI-712912, EBI-6874731; CC Q9HC52; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-712912, EBI-527853; CC -!- SUBCELLULAR LOCATION: Nucleus {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. The hPRC-H complex purification reported by PubMed:12167701 CC probably presents a mixture of different complexes. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF174482; AAG09180.1; -; mRNA. DR EMBL; AF266479; AAF76328.2; -; mRNA. DR EMBL; AK074560; BAC11061.1; -; mRNA. DR EMBL; BC008937; AAH08937.1; -; mRNA. DR EMBL; BC009376; AAH09376.1; -; mRNA. DR EMBL; BC019289; AAH19289.1; -; mRNA. DR CCDS; CCDS11765.1; -. DR RefSeq; NP_065700.1; NM_020649.2. DR PDB; 2N4Q; NMR; -; A=327-349. DR PDB; 3I91; X-ray; 1.55 A; A/B=8-61. DR PDB; 5EQ0; X-ray; 1.18 A; A=7-61. DR PDBsum; 2N4Q; -. DR PDBsum; 3I91; -. DR PDBsum; 5EQ0; -. DR AlphaFoldDB; Q9HC52; -. DR SMR; Q9HC52; -. DR BioGRID; 121487; 307. DR ComplexPortal; CPX-2621; Polycomb repressive complex 1, RING1-PCGF2-CBX8-PHC1 variant. DR ComplexPortal; CPX-2622; Polycomb repressive complex 1, RING1-PCGF2-CBX8-PHC2 variant. DR ComplexPortal; CPX-2623; Polycomb repressive complex 1, RING1-PCGF2-CBX8-PHC3 variant. DR ComplexPortal; CPX-7516; Polycomb repressive complex 1, RING1-PCGF4-CBX8-PHC1 variant. DR ComplexPortal; CPX-7517; Polycomb repressive complex 1, RING1-PCGF4-CBX8-PHC2 variant. DR ComplexPortal; CPX-7518; Polycomb repressive complex 1, RING1-PCGF4-CBX8-PHC3 variant. DR ComplexPortal; CPX-7533; Polycomb repressive complex 1, RING2-PCGF2-CBX8-PHC1 variant. DR ComplexPortal; CPX-7534; Polycomb repressive complex 1, RING2-PCGF2-CBX8-PHC2 variant. DR ComplexPortal; CPX-7535; Polycomb repressive complex 1, RING2-PCGF2-CBX8-PHC3 variant. DR ComplexPortal; CPX-7554; Polycomb repressive complex 1, RING2-PCGF4-CBX8-PHC1 variant. DR ComplexPortal; CPX-7555; Polycomb repressive complex 1, RING2-PCGF4-CBX8-PHC2 variant. DR ComplexPortal; CPX-7556; Polycomb repressive complex 1, RING2-PCGF4-CBX8-PHC3 variant. DR CORUM; Q9HC52; -. DR DIP; DIP-44566N; -. DR IntAct; Q9HC52; 207. DR MINT; Q9HC52; -. DR STRING; 9606.ENSP00000269385; -. DR BindingDB; Q9HC52; -. DR ChEMBL; CHEMBL3232684; -. DR GlyGen; Q9HC52; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9HC52; -. DR MetOSite; Q9HC52; -. DR PhosphoSitePlus; Q9HC52; -. DR SwissPalm; Q9HC52; -. DR BioMuta; CBX8; -. DR DMDM; 78099843; -. DR EPD; Q9HC52; -. DR jPOST; Q9HC52; -. DR MassIVE; Q9HC52; -. DR MaxQB; Q9HC52; -. DR PaxDb; 9606-ENSP00000269385; -. DR PeptideAtlas; Q9HC52; -. DR ProteomicsDB; 81638; -. DR Pumba; Q9HC52; -. DR ABCD; Q9HC52; 1 sequenced antibody. DR Antibodypedia; 19753; 799 antibodies from 38 providers. DR DNASU; 57332; -. DR Ensembl; ENST00000269385.9; ENSP00000269385.4; ENSG00000141570.11. DR GeneID; 57332; -. DR KEGG; hsa:57332; -. DR MANE-Select; ENST00000269385.9; ENSP00000269385.4; NM_020649.3; NP_065700.1. DR UCSC; uc002jxd.3; human. DR AGR; HGNC:15962; -. DR CTD; 57332; -. DR DisGeNET; 57332; -. DR GeneCards; CBX8; -. DR HGNC; HGNC:15962; CBX8. DR HPA; ENSG00000141570; Low tissue specificity. DR MIM; 617354; gene. DR neXtProt; NX_Q9HC52; -. DR OpenTargets; ENSG00000141570; -. DR PharmGKB; PA26133; -. DR VEuPathDB; HostDB:ENSG00000141570; -. DR eggNOG; KOG2748; Eukaryota. DR GeneTree; ENSGT00940000158476; -. DR HOGENOM; CLU_042051_0_1_1; -. DR InParanoid; Q9HC52; -. DR OMA; HPENHGH; -. DR OrthoDB; 75895at2759; -. DR PhylomeDB; Q9HC52; -. DR TreeFam; TF106456; -. DR PathwayCommons; Q9HC52; -. DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors. DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins. DR Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins. DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription. DR SignaLink; Q9HC52; -. DR BioGRID-ORCS; 57332; 15 hits in 1164 CRISPR screens. DR EvolutionaryTrace; Q9HC52; -. DR GeneWiki; CBX8; -. DR GenomeRNAi; 57332; -. DR Pharos; Q9HC52; Tchem. DR PRO; PR:Q9HC52; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9HC52; Protein. DR Bgee; ENSG00000141570; Expressed in right uterine tube and 102 other cell types or tissues. DR ExpressionAtlas; Q9HC52; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl. 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; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl. DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:Ensembl. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. 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 GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl. DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl. DR CDD; cd18627; CD_polycomb_like; 1. DR Gene3D; 2.40.50.40; -; 1. DR IDEAL; IID00682; -. DR InterPro; IPR033773; CBX7_C. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR000953; Chromo/chromo_shadow_dom. DR InterPro; IPR023780; Chromo_domain. DR InterPro; IPR023779; Chromodomain_CS. DR PANTHER; PTHR46389:SF1; CHROMOBOX PROTEIN HOMOLOG 8; 1. DR PANTHER; PTHR46389; POLYCOMB GROUP PROTEIN PC; 1. DR Pfam; PF17218; CBX7_C; 1. DR Pfam; PF00385; Chromo; 1. DR SMART; SM00298; CHROMO; 1. DR SUPFAM; SSF54160; Chromo domain-like; 1. DR PROSITE; PS00598; CHROMO_1; 1. DR PROSITE; PS50013; CHROMO_2; 1. DR Genevisible; Q9HC52; HS. PE 1: Evidence at protein level; KW 3D-structure; Chromatin regulator; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; Transcription; Transcription regulation. FT CHAIN 1..389 FT /note="Chromobox protein homolog 8" FT /id="PRO_0000080215" FT DOMAIN 11..69 FT /note="Chromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053" FT REGION 124..241 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 298..327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 129..143 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 144..211 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 110 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 130 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 191 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 256 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 265 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 311 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 332 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 352 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT VARIANT 317 FT /note="G -> V (in dbSNP:rs4889891)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2" FT /id="VAR_014954" FT STRAND 9..11 FT /evidence="ECO:0007829|PDB:5EQ0" FT STRAND 13..22 FT /evidence="ECO:0007829|PDB:5EQ0" FT STRAND 25..32 FT /evidence="ECO:0007829|PDB:5EQ0" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:5EQ0" FT STRAND 41..44 FT /evidence="ECO:0007829|PDB:5EQ0" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:5EQ0" FT HELIX 51..59 FT /evidence="ECO:0007829|PDB:5EQ0" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:2N4Q" FT HELIX 339..342 FT /evidence="ECO:0007829|PDB:2N4Q" SQ SEQUENCE 389 AA; 43396 MW; 651263C85B0ECD93 CRC64; MELSAVGERV FAAEALLKRR IRKGRMEYLV KWKGWSQKYS TWEPEENILD ARLLAAFEER EREMELYGPK KRGPKPKTFL LKAQAKAKAK TYEFRSDSAR GIRIPYPGRS PQDLASTSRA REGLRNMGLS PPASSTSTSS TCRAEAPRDR DRDRDRDRER DRERERERER ERERERERER GTSRVDDKPS SPGDSSKKRG PKPRKELPDP SQRPLGEPSA GLGEYLKGRK LDDTPSGAGK FPAGHSVIQL ARRQDSDLVQ CGVTSPSSAE ATGKLAVDTF PARVIKHRAA FLEAKGQGAL DPNGTRVRHG SGPPSSGGGL YRDMGAQGGR PSLIARIPVA RILGDPEEES WSPSLTNLEK VVVTDVTSNF LTVTIKESNT DQGFFKEKR //