CBX8_HUMAN
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 03-AUG-2022, entry version 188.
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.
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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; 293.
DR CORUM; Q9HC52; -.
DR DIP; DIP-44566N; -.
DR IntAct; Q9HC52; 205.
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 BioMuta; CBX8; -.
DR DMDM; 78099843; -.
DR EPD; Q9HC52; -.
DR jPOST; Q9HC52; -.
DR MassIVE; Q9HC52; -.
DR MaxQB; Q9HC52; -.
DR PaxDb; Q9HC52; -.
DR PeptideAtlas; Q9HC52; -.
DR PRIDE; Q9HC52; -.
DR ProteomicsDB; 81638; -.
DR ABCD; Q9HC52; 1 sequenced antibody.
DR Antibodypedia; 19753; 698 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 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; 1628171at2759; -.
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; 12 hits in 1084 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 101 other tissues.
DR ExpressionAtlas; Q9HC52; baseline and differential.
DR Genevisible; Q9HC52; HS.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016574; P:histone ubiquitination; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
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 Pfam; PF17218; CBX7_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 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; 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
