ID CBX5_HUMAN Reviewed; 191 AA. AC P45973; B2R8T9; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 04-NOV-2026, entry version 233. DE RecName: Full=Chromobox protein homolog 5; DE AltName: Full=Antigen p25; DE AltName: Full=Heterochromatin protein 1 homolog alpha; DE Short=HP1 alpha; GN Name=CBX5; Synonyms=HP1A; 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=8505380; DOI=10.1242/jcs.104.2.573; RA Saunders W.S., Chue C., Goebl M., Craig C., Clark R.F., Powers J.A., RA Eissenberg J.C., Elgin S.C.R., Rothfield N.F., Earnshaw W.C.; RT "Molecular cloning of a human homologue of Drosophila heterochromatin RT protein HP1 using anti-centromere autoantibodies with anti-chromo RT specificity."; RL J. Cell Sci. 104:573-582(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 2-191. RX PubMed=8663349; DOI=10.1074/jbc.271.25.14653; RA Ye Q., Worman H.J.; RT "Interaction between an integral protein of the nuclear envelope inner RT membrane and human chromodomain proteins homologous to Drosophila HP1."; RL J. Biol. Chem. 271:14653-14656(1996). RN [6] RP PROTEIN SEQUENCE OF 33-40; 56-68; 126-154 AND 160-184, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [7] RP INTERACTION WITH LBR AND CBX3. RX PubMed=9169472; DOI=10.1074/jbc.272.23.14983; RA Ye Q., Callebaut I., Pezhman A., Courvalin J.-C., Worman H.J.; RT "Domain-specific interactions of human HP1-type chromodomain proteins and RT inner nuclear membrane protein LBR."; RL J. Biol. Chem. 272:14983-14989(1997). RN [8] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=10460410; DOI=10.1007/s004120050372; RA Minc E., Allory Y., Worman H.J., Courvalin J.-C., Buendia B.; RT "Localization and phosphorylation of HP1 proteins during the cell cycle in RT mammalian cells."; RL Chromosoma 108:220-234(1999). RN [9] RP INTERACTION WITH TRIM24. RX PubMed=11313457; DOI=10.1128/mcb.21.10.3314-3324.2001; RA Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T., Chambon P., RA Dejean A.; RT "Common properties of nuclear protein SP100 and TIF1alpha chromatin factor: RT role of SUMO modification."; RL Mol. Cell. Biol. 21:3314-3324(2001). RN [10] RP INTERACTION WITH HISTONE H3 LYS-9. RX PubMed=11242053; DOI=10.1038/35065132; RA Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.; RT "Methylation of histone H3 lysine 9 creates a binding site for HP1 RT proteins."; RL Nature 410:116-120(2001). RN [11] RP INTERACTION WITH MIS12 AND DSN1. RX PubMed=15502821; DOI=10.1038/ncb1187; RA Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.; RT "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and RT outer kinetochore protein Zwint-1."; RL Nat. Cell Biol. 6:1135-1141(2004). RN [12] RP INTERACTION WITH ATRX; CHAF1A; LBR; NIPBL; SP100; STAM2 AND TRIM28. RX PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016; RA Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III; RT "The mammalian heterochromatin protein 1 binds diverse nuclear proteins RT through a common motif that targets the chromoshadow domain."; RL Biochem. Biophys. Res. Commun. 331:929-937(2005). RN [13] RP INTERACTION WITH JC VIRUS AGNOPROTEIN (MICROBIAL INFECTION). RX PubMed=15864296; DOI=10.1038/sj.embor.7400406; RA Okada Y., Suzuki T., Sunden Y., Orba Y., Kose S., Imamoto N., Takahashi H., RA Tanaka S., Hall W.W., Nagashima K., Sawa H.; RT "Dissociation of heterochromatin protein 1 from lamin B receptor induced by RT human polyomavirus agnoprotein: role in nuclear egress of viral RT particles."; RL EMBO Rep. 6:452-457(2005). RN [14] RP FUNCTION. RX PubMed=16127177; DOI=10.1074/jbc.c500229200; RA Daujat S., Zeissler U., Waldmann T., Happel N., Schneider R.; RT "HP1 binds specifically to Lys26-methylated histone H1.4, whereas RT simultaneous Ser27 phosphorylation blocks HP1 binding."; RL J. Biol. Chem. 280:38090-38095(2005). RN [15] RP INTERACTION WITH SETDB1. RX PubMed=15899859; DOI=10.1128/mcb.25.11.4552-4564.2005; RA Verschure P.J., van der Kraan I., de Leeuw W., van der Vlag J., RA Carpenter A.E., Belmont A.S., van Driel R.; RT "In vivo HP1 targeting causes large-scale chromatin condensation and RT enhanced histone lysine methylation."; RL Mol. Cell. Biol. 25:4552-4564(2005). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY RP 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13; SER-14 RP AND SER-92, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [19] RP INTERACTION WITH HNRNPU, AND SUBCELLULAR LOCATION. RX PubMed=19617346; DOI=10.1074/jbc.m109.037929; RA Ameyar-Zazoua M., Souidi M., Fritsch L., Robin P., Thomas A., Hamiche A., RA Percipalle P., Ait-Si-Ali S., Harel-Bellan A.; RT "Physical and functional interaction between heterochromatin protein 1alpha RT and the RNA-binding protein heterogeneous nuclear ribonucleoprotein U."; RL J. Biol. Chem. 284:27974-27979(2009). RN [20] RP INTERACTION WITH RRP1B. RX PubMed=19710015; DOI=10.1074/jbc.m109.023457; RA Crawford N.P., Yang H., Mattaini K.R., Hunter K.W.; RT "The metastasis efficiency modifier ribosomal RNA processing 1 homolog B RT (RRP1B) is a chromatin-associated factor."; RL J. Biol. Chem. 284:28660-28673(2009). RN [21] RP FUNCTION, AND HISTONE-BINDING. RX PubMed=19783980; DOI=10.1038/nature08448; RA Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T., RA Green A.R., Kouzarides T.; RT "JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin."; RL Nature 461:819-822(2009). RN [22] RP INTERACTION WITH BAHD1. RX PubMed=19666599; DOI=10.1073/pnas.0901259106; RA Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M., RA Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C., Feunteun J., RA Cossart P.; RT "Human BAHD1 promotes heterochromatic gene silencing."; RL Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-14; SER-92 AND RP SER-97, AND IDENTIFICATION BY 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 [24] RP INTERACTION WITH CHAMP1 AND POGZ. RX PubMed=20850016; DOI=10.1016/j.cell.2010.08.020; RA Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., RA Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.; RT "Quantitative interaction proteomics and genome-wide profiling of RT epigenetic histone marks and their readers."; RL Cell 142:967-980(2010). RN [25] RP RETRACTED PAPER. RX PubMed=19880879; DOI=10.1074/jbc.m109.065862; RA Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.; RT "ASXL1 represses retinoic acid receptor-mediated transcription through RT associating with HP1 and LSD1."; RL J. Biol. Chem. 285:18-29(2010). RN [26] RP RETRACTION NOTICE OF PUBMED:19880879. RX PubMed=25750265; DOI=10.1074/jbc.a109.065862; RA Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.; RT "Retraction: 'ASXL1 represses retinoic acid receptor-mediated transcription RT through associating with HP1 and LSD1'."; RL J. Biol. Chem. 290:6008-6008(2015). RN [27] RP FUNCTION, INTERACTION WITH NSL1 AND AURKB, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF ILE-165; THR-173 AND TRP-174. RX PubMed=20231385; DOI=10.1083/jcb.200908096; RA Kiyomitsu T., Iwasaki O., Obuse C., Yanagida M.; RT "Inner centromere formation requires hMis14, a trident kinetochore protein RT that specifically recruits HP1 to human chromosomes."; RL J. Cell Biol. 188:791-807(2010). RN [28] RP SUBUNIT, AND INTERACTION WITH NSL1. RX PubMed=20819937; DOI=10.1083/jcb.201002070; RA Petrovic A., Pasqualato S., Dube P., Krenn V., Santaguida S., Cittaro D., RA Monzani S., Massimiliano L., Keller J., Tarricone A., Maiolica A., RA Stark H., Musacchio A.; RT "The MIS12 complex is a protein interaction hub for outer kinetochore RT assembly."; RL J. Cell Biol. 190:835-852(2010). RN [29] RP INTERACTION WITH POGZ; TRIM28; CHAF1A; NIPBL AND INCENP, AND MUTAGENESIS OF RP ILE-165 AND TRP-174. RX PubMed=20562864; DOI=10.1038/ncb2075; RA Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., RA Kimura H., Obuse C.; RT "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms RT through Aurora B activation."; RL Nat. Cell Biol. 12:719-727(2010). RN [30] RP UBIQUITINATION. RX PubMed=20498703; DOI=10.1371/journal.pone.0010620; RA Chaturvedi P., Parnaik V.K.; RT "Lamin A rod domain mutants target heterochromatin protein 1alpha and beta RT for proteasomal degradation by activation of F-box protein, FBXW10."; RL PLoS ONE 5:E10620-E10620(2010). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13; SER-14; RP SER-92 AND SER-97, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [32] 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 [33] RP INTERACTION WITH INCENP, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-174. RX PubMed=21346195; DOI=10.1091/mbc.e11-01-0009; RA Kang J., Chaudhary J., Dong H., Kim S., Brautigam C.A., Yu H.; RT "Mitotic centromeric targeting of HP1 and its binding to Sgo1 are RT dispensable for sister-chromatid cohesion in human cells."; RL Mol. Biol. Cell 22:1181-1190(2011). RN [34] RP INTERACTION WITH MIS12. RX PubMed=21199919; DOI=10.1128/mcb.00815-10; RA Kiyomitsu T., Murakami H., Yanagida M.; RT "Protein interaction domain mapping of human kinetochore protein Blinkin RT reveals a consensus motif for binding of spindle assembly checkpoint RT proteins Bub1 and BubR1."; RL Mol. Cell. Biol. 31:998-1011(2011). RN [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14; SER-95 AND RP SER-97, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [36] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [37] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-92 AND SER-95, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [38] RP INTERACTION WITH LRIF1. RX PubMed=23542155; DOI=10.1038/nsmb.2532; RA Nozawa R.S., Nagao K., Igami K.T., Shibata S., Shirai N., Nozaki N., RA Sado T., Kimura H., Obuse C.; RT "Human inactive X chromosome is compacted through a PRC2-independent RT SMCHD1-HBiX1 pathway."; RL Nat. Struct. Mol. Biol. 20:566-573(2013). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13 AND RP SER-14, AND 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 [40] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-102, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [41] RP INTERACTION WITH PRR14. RX PubMed=25906157; DOI=10.1038/cddis.2015.103; RA Yang M., Yuan Z.M.; RT "A novel role of PRR14 in the regulation of skeletal myogenesis."; RL Cell Death Dis. 6:E1734-E1734(2015). RN [42] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-102, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [43] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-102, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [44] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-91; LYS-102; LYS-106; RP LYS-154 AND LYS-184, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [45] RP INTERACTION WITH CHD3 AND CHD4, AND SUBCELLULAR LOCATION. RX PubMed=28977666; DOI=10.1093/nar/gkx711; RA Hoffmeister H., Fuchs A., Erdel F., Pinz S., Groebner-Ferreira R., RA Bruckmann A., Deutzmann R., Schwartz U., Maldonado R., Huber C., RA Dendorfer A.S., Rippe K., Laengst G.; RT "CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping RT functionality."; RL Nucleic Acids Res. 45:10534-10554(2017). RN [46] RP INTERACTION WITH ZNF263. RX PubMed=32051553; DOI=10.1038/s41388-020-1206-7; RA Yu Z., Feng J., Wang W., Deng Z., Zhang Y., Xiao L., Wang Z., Liu C., RA Liu Q., Chen S., Wu M.; RT "The EGFR-ZNF263 signaling axis silences SIX3 in glioblastoma RT epigenetically."; RL Oncogene 39:3163-3178(2020). RN [47] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH TRIMETHYLATED HISTONE H3 PEPTIDE, RP SUBUNIT, AND X-RAY CRYSTALLOGRAPHY. 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). RN [48] RP INTERACTION WITH HP1BP3, AND MUTAGENESIS OF TRP-174. RX PubMed=20042602; DOI=10.1074/jbc.m109.092833; RA Hayashihara K., Uchiyama S., Shimamoto S., Kobayashi S., Tomschik M., RA Wakamatsu H., No D., Sugahara H., Hori N., Noda M., Ohkubo T., RA Zlatanova J., Matsunaga S., Fukui K.; RT "The middle region of an HP1-binding protein, HP1-BP74, associates with RT linker DNA at the entry/exit site of nucleosomal DNA."; RL J. Biol. Chem. 285:6498-6507(2010). RN [49] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ASB7. RX PubMed=40440427; DOI=10.1126/science.adq7408; RA Zhou L., Chen Z., Zou Y., Zhang X., Wang Z., Zhu H., Lin J., Huang Z., RA Zheng L., Chen J., Xie M., Zhang M., Zhang R., Zhu M., Wang Z., Zhou H., RA Gao S., Yin Y., Wu Y., Kang T.; RT "ASB7 is a negative regulator of H3K9me3 homeostasis."; RL Science 389:309-316(2025). CC -!- FUNCTION: Component of heterochromatin that recognizes and binds CC histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic CC repression (PubMed:40440427). In contrast, it is excluded from CC chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph) CC (PubMed:19783980). Also recognizes and binds histone H1.4 methylated at CC 'Lys-26' (H1.4K26me) (PubMed:16127177). Excluded from chromatin when CC histone H1.4 is Simultaneously methylated at Lys-26 (H1.4K26me) and CC phosphorylated at Ser-27 (H1.4S27Ph) (PubMed:16127177). May contribute CC to the association of heterochromatin with the inner nuclear membrane CC by interactions with the lamin-B receptor (LBR) (PubMed:19783980). CC Involved in the formation of kinetochore through interaction with the CC MIS12 complex subunit NSL1 (PubMed:19783980, PubMed:20231385). Required CC for the formation of the inner centromere (PubMed:20231385). CC {ECO:0000269|PubMed:16127177, ECO:0000269|PubMed:19783980, CC ECO:0000269|PubMed:20231385, ECO:0000269|PubMed:40440427}. CC -!- SUBUNIT: Homodimer (PubMed:20819937). Interacts with histone H3 CC methylated at 'Lys-9' (PubMed:11242053, PubMed:21047797). Interacts CC (via Chromo 2; shadow subtype domain) with the MIS12 complex subunit CC NSL1; the interaction is direct, involves dimeric CBX5, and occurs CC during interphase (PubMed:15502821, PubMed:20231385, PubMed:20819937). CC Interacts with POGZ; POGZ and PXVXL motif-containing proteins such as CC INCENP and TRIM28 compete for interaction with CBX5 (PubMed:20562864, CC PubMed:20850016, PubMed:21346195). Interacts with LRIF1 (via PxVxL CC motif) (PubMed:23542155). Interacts with INCENP (PubMed:20562864). CC Interacts with TRIM24 (PubMed:11313457). Interacts (via the CC chromoshadow domain) with ATRX; the interaction is direct CC (PubMed:15882967). Interacts (via the chromoshadow domain) with CHAF1A; CC the interaction is direct (PubMed:15882967). Interacts (via the CC chromoshadow domain) with LBR; the interaction is direct CC (PubMed:15882967, PubMed:9169472). Interacts (via the chromoshadow CC domain) with NIPBL; the interaction is direct (PubMed:15882967). CC Interacts (via the chromoshadow domain) with SP100; the interaction is CC direct (PubMed:15882967). Interacts (via the chromoshadow domain) with CC STAM2; the interaction is direct (PubMed:15882967). Interacts (via the CC chromoshadow domain) with TRIM28; the interaction is direct CC (PubMed:15882967). Interacts (via the chromoshadow domain) with CBX3; CC the interaction is direct (PubMed:9169472). Interacts with PRR14 (via CC N-terminus) (PubMed:25906157). Interacts with RRP1B (PubMed:19710015). CC Interacts with HNRNPU (via C-terminus); this interaction is, at least CC in part, RNA-dependent (PubMed:19617346). Interacts with ZNF263; CC recruited to the SIX3 promoter along with other proteins involved in CC chromatin modification and transcriptional corepression where it CC contributes to transcriptional repression (PubMed:32051553). Interacts CC with AURKB during mitosis (PubMed:20231385). Interacts with CHAMP1 CC (PubMed:20850016). Interacts with BAHD1 (PubMed:19666599). Interacts CC with HP1BP3 (PubMed:20042602). Interacts with CHD3 (PubMed:28977666). CC Interacts with CHD4 (PubMed:28977666). Interacts with SMYD5 (By CC similarity). Interacts with KMT5B (By similarity). Interacts with KMT5C CC (By similarity). Interacts with ASB7 (via PxVxL motif 1); leading to CC ASB7 recruitment to heterochromatin (PubMed:40440427). CC {ECO:0000250|UniProtKB:Q61686, ECO:0000269|PubMed:11242053, CC ECO:0000269|PubMed:11313457, ECO:0000269|PubMed:15502821, CC ECO:0000269|PubMed:15882967, ECO:0000269|PubMed:15899859, CC ECO:0000269|PubMed:19617346, ECO:0000269|PubMed:19666599, CC ECO:0000269|PubMed:19710015, ECO:0000269|PubMed:20042602, CC ECO:0000269|PubMed:20231385, ECO:0000269|PubMed:20562864, CC ECO:0000269|PubMed:20819937, ECO:0000269|PubMed:20850016, CC ECO:0000269|PubMed:21047797, ECO:0000269|PubMed:21199919, CC ECO:0000269|PubMed:21346195, ECO:0000269|PubMed:23542155, CC ECO:0000269|PubMed:25906157, ECO:0000269|PubMed:28977666, CC ECO:0000269|PubMed:32051553, ECO:0000269|PubMed:40440427, CC ECO:0000269|PubMed:9169472}. CC -!- SUBUNIT: (Microbial infection) Interacts with JC virus agnoprotein; CC this interaction induces the dissociation of CBX5 from LBR, resulting CC in destabilization of the nuclear envelope. CC {ECO:0000269|PubMed:15864296}. CC -!- INTERACTION: CC P45973; Q9H2P0: ADNP; NbExp=3; IntAct=EBI-78219, EBI-1764854; CC P45973; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-78219, EBI-2875816; CC P45973; O75143-2: ATG13; NbExp=3; IntAct=EBI-78219, EBI-20151086; CC P45973; P46100: ATRX; NbExp=2; IntAct=EBI-78219, EBI-396461; CC P45973; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-78219, EBI-742750; CC P45973; P45973: CBX5; NbExp=2; IntAct=EBI-78219, EBI-78219; CC P45973; Q13111: CHAF1A; NbExp=8; IntAct=EBI-78219, EBI-1020839; CC P45973; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-78219, EBI-9087876; CC P45973; Q9UMR2: DDX19B; NbExp=3; IntAct=EBI-78219, EBI-719232; CC P45973; P09471: GNAO1; NbExp=3; IntAct=EBI-78219, EBI-715087; CC P45973; P84243: H3-3B; NbExp=3; IntAct=EBI-78219, EBI-120658; CC P45973; Q16695: H3-4; NbExp=2; IntAct=EBI-78219, EBI-358900; CC P45973; P68431: H3C12; NbExp=11; IntAct=EBI-78219, EBI-79722; CC P45973; P62805: H4C9; NbExp=3; IntAct=EBI-78219, EBI-302023; CC P45973; Q9NQS7: INCENP; NbExp=11; IntAct=EBI-78219, EBI-307907; CC P45973; P28838: LAP3; NbExp=3; IntAct=EBI-78219, EBI-2339312; CC P45973; Q14739: LBR; NbExp=4; IntAct=EBI-78219, EBI-1055147; CC P45973; Q8N448: LNX2; NbExp=3; IntAct=EBI-78219, EBI-2340947; CC P45973; Q5T3J3: LRIF1; NbExp=11; IntAct=EBI-78219, EBI-473196; CC P45973; Q9UIS9: MBD1; NbExp=6; IntAct=EBI-78219, EBI-867196; CC P45973; Q14728: MFSD10; NbExp=3; IntAct=EBI-78219, EBI-11337904; CC P45973; P01106: MYC; NbExp=3; IntAct=EBI-78219, EBI-447544; CC P45973; Q9BZ95: NSD3; NbExp=2; IntAct=EBI-78219, EBI-3390132; CC P45973; Q9BZ95-3: NSD3; NbExp=3; IntAct=EBI-78219, EBI-22002759; CC P45973; Q96IY1: NSL1; NbExp=6; IntAct=EBI-78219, EBI-2554690; CC P45973; Q9NUD9: PIGV; NbExp=3; IntAct=EBI-78219, EBI-25836582; CC P45973; Q7Z3K3: POGZ; NbExp=8; IntAct=EBI-78219, EBI-1389308; CC P45973; Q07869: PPARA; NbExp=3; IntAct=EBI-78219, EBI-78615; CC P45973; Q9BWN1: PRR14; NbExp=12; IntAct=EBI-78219, EBI-748167; CC P45973; Q9BQF6: SENP7; NbExp=4; IntAct=EBI-78219, EBI-766251; CC P45973; Q5FBB7: SGO1; NbExp=4; IntAct=EBI-78219, EBI-989069; CC P45973; Q8NCS7: SLC44A5; NbExp=3; IntAct=EBI-78219, EBI-21504521; CC P45973; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-78219, EBI-12938570; CC P45973; P23497-2: SP100; NbExp=7; IntAct=EBI-78219, EBI-6589365; CC P45973; O43463: SUV39H1; NbExp=18; IntAct=EBI-78219, EBI-349968; CC P45973; O15273: TCAP; NbExp=6; IntAct=EBI-78219, EBI-954089; CC P45973; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-78219, EBI-765817; CC P45973; Q13263: TRIM28; NbExp=15; IntAct=EBI-78219, EBI-78139; CC P45973; Q14191: WRN; NbExp=3; IntAct=EBI-78219, EBI-368417; CC P45973; P25490: YY1; NbExp=3; IntAct=EBI-78219, EBI-765538; CC P45973; Q8ND82: ZNF280C; NbExp=3; IntAct=EBI-78219, EBI-8831272; CC P45973; Q6N043-2: ZNF280D; NbExp=3; IntAct=EBI-78219, EBI-12027202; CC P45973; Q5ZUS4: legAS4; Xeno; NbExp=6; IntAct=EBI-78219, EBI-8871796; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10460410, CC ECO:0000269|PubMed:19617346, ECO:0000269|PubMed:28977666}. Chromosome CC {ECO:0000269|PubMed:10460410, ECO:0000269|PubMed:40440427}. Chromosome, CC centromere {ECO:0000269|PubMed:10460410, ECO:0000269|PubMed:20231385, CC ECO:0000269|PubMed:21346195}. Note=Colocalizes with HNRNPU in the CC nucleus (PubMed:19617346). Component of centromeric and pericentromeric CC heterochromatin. Associates with chromosomes during mitosis CC (PubMed:40440427). Associates specifically with chromatin during CC metaphase and anaphase (PubMed:19617346). Localizes to sites of DNA CC damage (PubMed:28977666). {ECO:0000269|PubMed:19617346, CC ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:40440427}. CC -!- PTM: Phosphorylation of HP1 and LBR may be responsible for some of the CC alterations in chromatin organization and nuclear structure which occur CC at various times during the cell cycle (By similarity). Phosphorylated CC during interphase and possibly hyper-phosphorylated during mitosis. CC {ECO:0000250, ECO:0000269|PubMed:10460410}. CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:20498703}. CC -!- CAUTION: Was previously reported to interact with ASXL1. However, this CC publication has been retracted. {ECO:0000305|PubMed:19880879, CC ECO:0000305|PubMed:25750265}. 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; S62077; AAB26994.1; -; mRNA. DR EMBL; L07515; AAA72327.1; -; mRNA. DR EMBL; AK313506; BAG36286.1; -; mRNA. DR EMBL; CH471054; EAW96759.1; -; Genomic_DNA. DR EMBL; BC006821; AAH06821.1; -; mRNA. DR EMBL; U26311; AAC50553.1; -; mRNA. DR CCDS; CCDS8875.1; -. DR PIR; G01808; G01808. DR RefSeq; NP_001120793.1; NM_001127321.1. DR RefSeq; NP_001120794.1; NM_001127322.1. DR RefSeq; NP_036249.1; NM_012117.3. DR PDB; 3FDT; X-ray; 2.00 A; A=18-75. DR PDB; 3I3C; X-ray; 2.48 A; A/B/C/D=110-173. DR PDB; 8UXQ; EM; 6.30 A; A/C=2-191. DR PDB; 9CDW; X-ray; 2.40 A; A/B/C/D=111-174. DR PDB; 9CEA; X-ray; 2.15 A; A/B/C/D=113-175. DR PDB; 9CMT; X-ray; 3.17 A; A/B/D/E=112-176. DR AlphaFoldDB; P45973; -. DR BMRB; P45973; -. DR EMDB; EMD-42774; -. DR MDRepo; P45973; -. DR SMR; P45973; -. DR BioGRID; 117030; 367. DR CORUM; P45973; -. DR DIP; DIP-5986N; -. DR FunCoup; P45973; 2560. DR IntAct; P45973; 270. DR NDEx; IQUERY-CP-CBX5; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000209875; -. DR BindingDB; P45973; -. DR ChEMBL; CHEMBL3826867; -. DR DrugBank; DB09130; Copper. DR MoonDB; P45973; Predicted. DR GlyCosmos; P45973; 1 site, 1 glycan. DR GlyGen; P45973; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P45973; -. DR PhosphoSitePlus; P45973; -. DR SwissPalm; P45973; -. DR BioMuta; CBX5; -. DR DMDM; 1170338; -. DR jPOST; P45973; -. DR MassIVE; P45973; -. DR PaxDb; 9606-ENSP00000209875; -. DR PeptideAtlas; P45973; -. DR ProteomicsDB; 55691; -. DR Pumba; P45973; -. DR TopDownProteomics; P45973; -. DR ABCD; P45973; 2 sequenced antibodies. DR Antibodypedia; 4311; 1069 antibodies from 48 providers. DR DNASU; 23468; -. DR Ensembl; ENST00000209875.9; ENSP00000209875.4; ENSG00000094916.17. DR Ensembl; ENST00000439541.6; ENSP00000401009.2; ENSG00000094916.17. DR Ensembl; ENST00000550411.5; ENSP00000449207.1; ENSG00000094916.17. DR Ensembl; ENST00000882085.1; ENSP00000552144.1; ENSG00000094916.17. DR Ensembl; ENST00000882087.1; ENSP00000552146.1; ENSG00000094916.17. DR Ensembl; ENST00000882088.1; ENSP00000552147.1; ENSG00000094916.17. DR Ensembl; ENST00000882089.1; ENSP00000552148.1; ENSG00000094916.17. DR Ensembl; ENST00000882090.1; ENSP00000552149.1; ENSG00000094916.17. DR Ensembl; ENST00000882092.1; ENSP00000552151.1; ENSG00000094916.17. DR Ensembl; ENST00000882093.1; ENSP00000552152.1; ENSG00000094916.17. DR Ensembl; ENST00000882094.1; ENSP00000552153.1; ENSG00000094916.17. DR Ensembl; ENST00000882095.1; ENSP00000552154.1; ENSG00000094916.17. DR Ensembl; ENST00000930389.1; ENSP00000600448.1; ENSG00000094916.17. DR Ensembl; ENST00000930391.1; ENSP00000600450.1; ENSG00000094916.17. DR Ensembl; ENST00000930392.1; ENSP00000600451.1; ENSG00000094916.17. DR Ensembl; ENST00000930393.1; ENSP00000600452.1; ENSG00000094916.17. DR Ensembl; ENST00000930394.1; ENSP00000600453.1; ENSG00000094916.17. DR Ensembl; ENST00000930395.1; ENSP00000600454.1; ENSG00000094916.17. DR Ensembl; ENST00000930396.1; ENSP00000600455.1; ENSG00000094916.17. DR Ensembl; ENST00000930397.1; ENSP00000600456.1; ENSG00000094916.17. DR GeneID; 23468; -. DR KEGG; hsa:23468; -. DR MANE-Select; ENST00000209875.9; ENSP00000209875.4; NM_012117.3; NP_036249.1. DR AGR; HGNC:1555; -. DR ClinPGx; PA26130; -. DR CTD; 23468; -. DR DisGeNET; 23468; -. DR GeneCards; CBX5; -. DR HGNC; HGNC:1555; CBX5. DR HPA; ENSG00000094916; Tissue enhanced (choroid). DR MIM; 604478; gene. DR OpenTargets; ENSG00000094916; -. DR VEuPathDB; HostDB:ENSG00000094916; -. DR eggNOG; KOG1911; Eukaryota. DR GeneTree; ENSGT00940000158801; -. DR HOGENOM; CLU_045874_1_0_1; -. DR InParanoid; P45973; -. DR OMA; ATRCAMG; -. DR OrthoDB; 433924at2759; -. DR PAN-GO; P45973; 3 GO annotations based on evolutionary models. DR PhylomeDB; P45973; -. DR PathwayCommons; P45973; -. DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR Reactome; R-HSA-9843940; Regulation of endogenous retroelements by KRAB-ZFP proteins. DR SignaLink; P45973; -. DR SIGNOR; P45973; -. DR Agora; ENSG00000094916; -. DR BioGRID-ORCS; 23468; 11 hits in 1158 CRISPR screens. DR CD-CODE; 208F8600; Synthetic Condensate 000366. DR CD-CODE; 3F4CB227; Synthetic Condensate 000322. DR CD-CODE; 8BB8BA7F; Synthetic Condensate 000324. DR CD-CODE; 8DF372A2; Synthetic Condensate 000069. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; 98A5DA6D; Synthetic Condensate 000066. DR CD-CODE; 9F05356D; Synthetic Condensate 000062. DR CD-CODE; AA62C26E; ORC1 bodies. DR CD-CODE; AF287C13; Synthetic Condensate 000326. DR CD-CODE; B57B8AD8; Heterochromatin. DR CD-CODE; C65B6D56; Synthetic Condensate 000076. DR CD-CODE; F5834E66; Synthetic Condensate 000310. DR ChiTaRS; CBX5; human. DR EvolutionaryTrace; P45973; -. DR GeneWiki; CBX5_(gene); -. DR GenomeRNAi; 23468; -. DR Pharos; P45973; Tbio. DR PRO; PR:P45973; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P45973; protein. DR Bgee; ENSG00000094916; Expressed in tendon of biceps brachii and 202 other cell types or tissues. DR ExpressionAtlas; P45973; baseline and differential. DR GO; GO:0005694; C:chromosome; EXP:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL. DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB. DR GO; GO:0000118; C:histone deacetylase complex; ISS:BHF-UCL. DR GO; GO:0035097; C:histone methyltransferase complex; ISS:BHF-UCL. DR GO; GO:0005635; C:nuclear envelope; TAS:ProtInc. DR GO; GO:0005730; C:nucleolus; IDA:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005721; C:pericentric heterochromatin; ISS:BHF-UCL. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0090734; C:site of DNA damage; IMP:UniProtKB. DR GO; GO:0017053; C:transcription repressor complex; ISS:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:BHF-UCL. DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl. DR GO; GO:0160267; F:histone H1K26me1 reader activity; IDA:UniProtKB. DR GO; GO:0160268; F:histone H1K26me2 reader activity; IDA:UniProtKB. DR GO; GO:0062072; F:histone H3K9me2/3 reader activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:BHF-UCL. DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:UniProtKB. DR GO; GO:0030261; P:chromosome condensation; IDA:UniProt. DR GO; GO:0006974; P:DNA damage response; IMP:UniProtKB. DR GO; GO:0031507; P:heterochromatin formation; IDA:UniProt. DR GO; GO:0070828; P:heterochromatin organization; IDA:UniProt. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0097355; P:protein localization to heterochromatin; IDA:UniProtKB. DR CDD; cd18651; CD_HP1alpha_Cbx5; 1. DR CDD; cd18655; CSD_HP1alpha_Cbx5; 1. DR DisProt; DP04242; -. DR FunFam; 2.40.50.40:FF:000007; Chromobox protein homolog 1; 1. DR FunFam; 2.40.50.40:FF:000009; chromobox protein homolog 1; 1. DR Gene3D; 2.40.50.40; -; 2. DR IDEAL; IID00659; -. 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 InterPro; IPR051219; Heterochromatin_chromo-domain. DR PANTHER; PTHR22812; CHROMOBOX PROTEIN; 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; Chromo domain-like; 2. DR PROSITE; PS00598; CHROMO_1; 1. DR PROSITE; PS50013; CHROMO_2; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Centromere; Chromosome; KW Direct protein sequencing; Host-virus interaction; Isopeptide bond; KW Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; KW Repeat; Ubl conjugation. FT CHAIN 1..191 FT /note="Chromobox protein homolog 5" FT /id="PRO_0000080208" FT DOMAIN 20..78 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 70..117 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 73..89 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 12 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 40 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q13185" FT MOD_RES 92 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 95 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 97 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT CROSSLNK 32 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 91 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 102 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 106 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 154 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 184 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT MUTAGEN 165 FT /note="I->E: No effect on interaction with POGZ. Abolishes FT interaction with TRIM28, CHAF1A and NIPBL. Abolishes FT interaction with NSL1." FT /evidence="ECO:0000269|PubMed:20231385, FT ECO:0000269|PubMed:20562864" FT MUTAGEN 173 FT /note="T->D,K: Abolishes interaction with NSL1." FT /evidence="ECO:0000269|PubMed:20231385" FT MUTAGEN 174 FT /note="W->A: Abolishes interaction with TRIM28, CHAF1A, FT NIPBL and HP1BP3, fails to localize to centromeres in FT mitosis. Abolishes interaction with NSL1." FT /evidence="ECO:0000269|PubMed:20042602, FT ECO:0000269|PubMed:20231385, ECO:0000269|PubMed:20562864, FT ECO:0000269|PubMed:21346195" FT STRAND 19..31 FT /evidence="ECO:0007829|PDB:3FDT" FT STRAND 34..41 FT /evidence="ECO:0007829|PDB:3FDT" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:3FDT" FT STRAND 50..53 FT /evidence="ECO:0007829|PDB:3FDT" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:3FDT" FT HELIX 60..67 FT /evidence="ECO:0007829|PDB:3FDT" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:9CEA" FT STRAND 123..130 FT /evidence="ECO:0007829|PDB:9CEA" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:9CMT" FT STRAND 137..142 FT /evidence="ECO:0007829|PDB:9CEA" FT STRAND 149..152 FT /evidence="ECO:0007829|PDB:9CEA" FT HELIX 153..159 FT /evidence="ECO:0007829|PDB:9CEA" FT HELIX 161..171 FT /evidence="ECO:0007829|PDB:9CEA" FT STRAND 172..175 FT /evidence="ECO:0007829|PDB:9CMT" SQ SEQUENCE 191 AA; 22225 MW; 16FFC476367093B1 CRC64; MGKKTKRTAD SSSSEDEEEY VVEKVLDRRV VKGQVEYLLK WKGFSEEHNT WEPEKNLDCP ELISEFMKKY KKMKEGENNK PREKSESNKR KSNFSNSADD IKSKKKREQS NDIARGFERG LEPEKIIGAT DSCGDLMFLM KWKDTDEADL VLAKEANVKC PQIVIAFYEE RLTWHAYPED AENKEKETAK S //