CBX3_HUMAN
ID CBX3_HUMAN Reviewed; 183 AA.
AC Q13185; Q96CD7; Q99409; Q9BVS3; Q9P0Z6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Chromobox protein homolog 3;
DE AltName: Full=HECH;
DE AltName: Full=Heterochromatin protein 1 homolog gamma;
DE Short=HP1 gamma;
DE AltName: Full=Modifier 2 protein;
GN Name=CBX3;
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] OF 11-183.
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 [2]
RP SEQUENCE REVISION.
RA Ye Q., Worman H.J.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-183, AND PHOSPHORYLATION BY PIM1.
RX PubMed=10664448; DOI=10.1016/s0014-5793(00)01105-4;
RA Koike N., Maita H., Taira T., Ariga H., Iguchi-Ariga S.M.M.;
RT "Identification of heterochromatin protein 1 (HP1) as a phosphorylation
RT target by Pim-1 kinase and the effect of phosphorylation on the
RT transcriptional repression function of HP1.";
RL FEBS Lett. 467:17-21(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen J.H., Luo W.Q., Hu S.N., Zhou H.J., Huang X.W., Zhou Y., Yuan J.G.,
RA Qiang B.Q.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and 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 [6]
RP PROTEIN SEQUENCE OF 160-171, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP INTERACTION WITH CBX5.
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 INTERACTION WITH INCENP.
RX PubMed=9864353; DOI=10.1083/jcb.143.7.1763;
RA Ainsztein A.M., Kandels-Lewis S.E., Mackay A.M., Earnshaw W.C.;
RT "INCENP centromere and spindle targeting: identification of essential
RT conserved motifs and involvement of heterochromatin protein HP1.";
RL J. Cell Biol. 143:1763-1774(1998).
RN [9]
RP INTERACTION WITH SP100.
RX PubMed=9636146; DOI=10.1073/pnas.95.13.7316;
RA Seeler J.-S., Marchio A., Sitterlin D., Transy C., Dejean A.;
RT "Interaction of SP100 with HP1 proteins: a link between the promyelocytic
RT leukemia-associated nuclear bodies and the chromatin compartment.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7316-7321(1998).
RN [10]
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 [11]
RP INTERACTION WITH TRIM28.
RX PubMed=10330177; DOI=10.1128/mcb.19.6.4366;
RA Ryan R.F., Schultz D.C., Ayyanathan K., Singh P.B., Friedman J.R.,
RA Fredericks W.J., Rauscher F.J. III;
RT "KAP-1 corepressor protein interacts and colocalizes with heterochromatic
RT and euchromatic HP1 proteins: a potential role for Kruppel-associated box-
RT zinc finger proteins in heterochromatin-mediated gene silencing.";
RL Mol. Cell. Biol. 19:4366-4378(1999).
RN [12]
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 [13]
RP IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; BAT8; EUHMTASE1;
RP RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
RX PubMed=12004135; DOI=10.1126/science.1069861;
RA Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
RT "A complex with chromatin modifiers that occupies E2F- and Myc-responsive
RT genes in G0 cells.";
RL Science 296:1132-1136(2002).
RN [14]
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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-176, AND
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-44 AND LYS-50, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
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 [22]
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 [23]
RP RETRACTION NOTICE OF PUBMED:19880879 NOTICE FOR 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 [24]
RP INTERACTION WITH POGZ.
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-95, 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 [26]
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 [27]
RP INTERACTION WITH INCENP.
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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-95; SER-97 AND
RP SER-99, 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 [29]
RP INTERACTION WITH TTLL12.
RX PubMed=23251473; DOI=10.1371/journal.pone.0051258;
RA Brants J., Semenchenko K., Wasylyk C., Robert A., Carles A., Zambrano A.,
RA Pradeau-Aubreton K., Birck C., Schalken J.A., Poch O., de Mey J.,
RA Wasylyk B.;
RT "Tubulin tyrosine ligase like 12, a TTLL family member with SET- and TTL-
RT like domains and roles in histone and tubulin modifications and mitosis.";
RL PLoS ONE 7:E51258-E51258(2012).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP 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 [31]
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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-95; SER-97 AND
RP SER-99, 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 [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-10; LYS-21 AND LYS-103,
RP AND 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 [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-21 AND LYS-103, 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 [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-103, 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 [36]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [37]
RP FUNCTION, AND INTERACTION WITH NIPBL.
RX PubMed=28167679; DOI=10.1242/jcs.197236;
RA Bot C., Pfeiffer A., Giordano F., Manjeera D.E., Dantuma N.P., Stroem L.;
RT "Independent mechanisms recruit the cohesin loader protein NIPBL to sites
RT of DNA damage.";
RL J. Cell Sci. 130:1134-1146(2017).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-10; LYS-21; LYS-103 AND
RP LYS-154, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [39]
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 [40]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 29-86 IN COMPLEX WITH PEPTIDE.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the complex of chromobox homolog 3 (CBX3) [Homo
RT sapiens] and peptide.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Seems to be involved in transcriptional silencing in
CC heterochromatin-like complexes. Recognizes and binds histone H3 tails
CC methylated at 'Lys-9', leading to epigenetic repression. May contribute
CC to the association of the heterochromatin with the inner nuclear
CC membrane through its interaction with lamin B receptor (LBR). Involved
CC in the formation of functional kinetochore through interaction with
CC MIS12 complex proteins. Contributes to the conversion of local
CC chromatin to a heterochromatin-like repressive state through H3 'Lys-9'
CC trimethylation, mediates the recruitment of the methyltransferases
CC SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the
CC circadian target genes such as PER2 itself or PER1. Mediates the
CC recruitment of NIPBL to sites of DNA damage at double-strand breaks
CC (DSBs) (PubMed:28167679). {ECO:0000250|UniProtKB:P23198,
CC ECO:0000269|PubMed:28167679}.
CC -!- SUBUNIT: Binds directly to CHAF1A. Interacts with histone H3 methylated
CC at 'Lys-9' (PubMed:11242053). Part of the E2F6.com-1 complex in G0
CC phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1,
CC RNF2, MBLR, L3MBTL2 and YAF2. Interacts with INCENP, TRIM28/TIF1B,
CC KMT5B, KMT5C and SP100 (PubMed:10330177, PubMed:12004135,
CC PubMed:9636146). Interacts with TIF1A (By similarity). Interacts with
CC MIS12 and DSN1 (PubMed:15502821). Can interact directly with CBX5 via
CC the chromoshadow domain (PubMed:9169472). Interacts with POGZ
CC (PubMed:20850016, PubMed:20562864). Interacts with CHAMP1
CC (PubMed:20850016). The large PER complex involved in the histone
CC methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or
CC SUV39H2; CBX3 mediates the formation of the complex. Interacts with
CC INCENP (PubMed:9864353, PubMed:21346195). Interacts with NIPBL (via
CC PxVxL motif) (PubMed:28167679). Interacts with LRIF1 (via PxVxL motif)
CC (PubMed:23542155). Interacts with TTLL12 (PubMed:23251473). Interacts
CC with ZNF263; recruited to the SIX3 promoter along with other proteins
CC involved in chromatin modification and transcriptional corepression
CC where it contributes to transcriptional repression (PubMed:32051553).
CC {ECO:0000250|UniProtKB:P23198, ECO:0000269|PubMed:10330177,
CC ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:12004135,
CC ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:20562864,
CC ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:21346195,
CC ECO:0000269|PubMed:23251473, ECO:0000269|PubMed:23542155,
CC ECO:0000269|PubMed:28167679, ECO:0000269|PubMed:32051553,
CC ECO:0000269|PubMed:9169472, ECO:0000269|PubMed:9636146,
CC ECO:0000269|PubMed:9864353}.
CC -!- INTERACTION:
CC Q13185; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-78176, EBI-10173507;
CC Q13185; Q9H2P0: ADNP; NbExp=4; IntAct=EBI-78176, EBI-1764854;
CC Q13185; Q6IQ32: ADNP2; NbExp=5; IntAct=EBI-78176, EBI-2838654;
CC Q13185; Q13185: CBX3; NbExp=3; IntAct=EBI-78176, EBI-78176;
CC Q13185; Q99988: GDF15; NbExp=3; IntAct=EBI-78176, EBI-2116863;
CC Q13185; P68431: H3C12; NbExp=6; IntAct=EBI-78176, EBI-79722;
CC Q13185; Q86Y97: KMT5C; NbExp=3; IntAct=EBI-78176, EBI-7960569;
CC Q13185; P28838: LAP3; NbExp=6; IntAct=EBI-78176, EBI-2339312;
CC Q13185; Q14739: LBR; NbExp=4; IntAct=EBI-78176, EBI-1055147;
CC Q13185; Q5T3J3: LRIF1; NbExp=8; IntAct=EBI-78176, EBI-473196;
CC Q13185; Q8IWI9: MGA; NbExp=3; IntAct=EBI-78176, EBI-2815196;
CC Q13185; P52815: MRPL12; NbExp=3; IntAct=EBI-78176, EBI-358272;
CC Q13185; Q9BWN1: PRR14; NbExp=6; IntAct=EBI-78176, EBI-748167;
CC Q13185; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-78176, EBI-948156;
CC Q13185; P23497-2: SP100; NbExp=3; IntAct=EBI-78176, EBI-6589365;
CC Q13185; O75716: STK16; NbExp=3; IntAct=EBI-78176, EBI-749295;
CC Q13185; O43463: SUV39H1; NbExp=8; IntAct=EBI-78176, EBI-349968;
CC Q13185; Q13263: TRIM28; NbExp=4; IntAct=EBI-78176, EBI-78139;
CC Q13185; Q8ND82: ZNF280C; NbExp=4; IntAct=EBI-78176, EBI-8831272;
CC Q13185; Q6N043-2: ZNF280D; NbExp=3; IntAct=EBI-78176, EBI-12027202;
CC Q13185; Q5ZUS4: legAS4; Xeno; NbExp=2; IntAct=EBI-78176, EBI-8871796;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Note=Associates with
CC euchromatin and is largely excluded from constitutive heterochromatin.
CC May be associated with microtubules and mitotic poles during mitosis
CC (Potential). {ECO:0000305}.
CC -!- PTM: Phosphorylated by PIM1. Phosphorylated during interphase and
CC possibly hyper-phosphorylated during mitosis.
CC {ECO:0000269|PubMed:10460410, ECO:0000269|PubMed:10664448}.
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}.
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DR EMBL; U26312; AAB48101.1; -; mRNA.
DR EMBL; AB030905; BAA83340.1; -; mRNA.
DR EMBL; AF136630; AAF62370.1; -; mRNA.
DR EMBL; BC000954; AAH00954.1; -; mRNA.
DR EMBL; BC014380; AAH14380.1; -; mRNA.
DR CCDS; CCDS5398.1; -.
DR RefSeq; NP_009207.2; NM_007276.4.
DR RefSeq; NP_057671.2; NM_016587.3.
DR RefSeq; XP_005249668.1; XM_005249611.3.
DR PDB; 2L11; NMR; -; A=29-81.
DR PDB; 3DM1; X-ray; 2.40 A; A/C/E/G=29-86.
DR PDB; 3KUP; X-ray; 1.77 A; A/B/C/D=110-173.
DR PDB; 3TZD; X-ray; 1.81 A; A=29-81.
DR PDB; 5T1I; X-ray; 1.60 A; A/B=110-176.
DR PDB; 6HW2; X-ray; 1.94 A; B/C=109-183.
DR PDBsum; 2L11; -.
DR PDBsum; 3DM1; -.
DR PDBsum; 3KUP; -.
DR PDBsum; 3TZD; -.
DR PDBsum; 5T1I; -.
DR PDBsum; 6HW2; -.
DR AlphaFoldDB; Q13185; -.
DR BMRB; Q13185; -.
DR SMR; Q13185; -.
DR BioGRID; 116463; 527.
DR ComplexPortal; CPX-469; L3MBTL1 complex.
DR CORUM; Q13185; -.
DR DIP; DIP-5985N; -.
DR IntAct; Q13185; 138.
DR MINT; Q13185; -.
DR STRING; 9606.ENSP00000336687; -.
DR BindingDB; Q13185; -.
DR ChEMBL; CHEMBL3826866; -.
DR GlyGen; Q13185; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13185; -.
DR PhosphoSitePlus; Q13185; -.
DR SwissPalm; Q13185; -.
DR BioMuta; CBX3; -.
DR DMDM; 116241284; -.
DR SWISS-2DPAGE; Q13185; -.
DR CPTAC; CPTAC-1600; -.
DR EPD; Q13185; -.
DR jPOST; Q13185; -.
DR MassIVE; Q13185; -.
DR MaxQB; Q13185; -.
DR PaxDb; Q13185; -.
DR PeptideAtlas; Q13185; -.
DR PRIDE; Q13185; -.
DR ProteomicsDB; 59210; -.
DR TopDownProteomics; Q13185; -.
DR ABCD; Q13185; 4 sequenced antibodies.
DR Antibodypedia; 1440; 645 antibodies from 42 providers.
DR DNASU; 11335; -.
DR Ensembl; ENST00000337620.8; ENSP00000336687.4; ENSG00000122565.19.
DR Ensembl; ENST00000396386.7; ENSP00000379670.2; ENSG00000122565.19.
DR GeneID; 11335; -.
DR KEGG; hsa:11335; -.
DR MANE-Select; ENST00000396386.7; ENSP00000379670.2; NM_016587.4; NP_057671.2.
DR UCSC; uc003sxt.4; human.
DR CTD; 11335; -.
DR DisGeNET; 11335; -.
DR GeneCards; CBX3; -.
DR HGNC; HGNC:1553; CBX3.
DR HPA; ENSG00000122565; Low tissue specificity.
DR MIM; 604477; gene.
DR neXtProt; NX_Q13185; -.
DR OpenTargets; ENSG00000122565; -.
DR PharmGKB; PA26128; -.
DR VEuPathDB; HostDB:ENSG00000122565; -.
DR eggNOG; KOG1911; Eukaryota.
DR GeneTree; ENSGT00940000153305; -.
DR HOGENOM; CLU_045874_1_2_1; -.
DR InParanoid; Q13185; -.
DR OMA; MSQKRSK; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; Q13185; -.
DR TreeFam; TF350503; -.
DR PathwayCommons; Q13185; -.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; Q13185; -.
DR SIGNOR; Q13185; -.
DR BioGRID-ORCS; 11335; 61 hits in 1024 CRISPR screens.
DR ChiTaRS; CBX3; human.
DR EvolutionaryTrace; Q13185; -.
DR GeneWiki; CBX3; -.
DR GenomeRNAi; 11335; -.
DR Pharos; Q13185; Tbio.
DR PRO; PR:Q13185; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q13185; protein.
DR Bgee; ENSG00000122565; Expressed in endothelial cell and 209 other tissues.
DR ExpressionAtlas; Q13185; baseline and differential.
DR Genevisible; Q13185; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0061793; C:chromatin lock complex; IPI:ComplexPortal.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:CACAO.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; NAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:ARUK-UCL.
DR GO; GO:0090734; C:site of DNA damage; IMP:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:1990226; F:histone methyltransferase binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:ARUK-UCL.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; NAS:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR IDEAL; IID00245; -.
DR InterPro; IPR038033; CBX3.
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 PANTHER; PTHR22812:SF149; PTHR22812:SF149; 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; SSF54160; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Biological rhythms; Chromatin regulator;
KW Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23198"
FT CHAIN 2..183
FT /note="Chromobox protein homolog 3"
FT /id="PRO_0000080203"
FT DOMAIN 30..88
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 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P23198"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P23198"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 50
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 95
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 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 21
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 103
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 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 111
FT /note="A -> G (in Ref. 5; AAH14380)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="A -> V (in Ref. 4; AAF62370)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="T -> I (in Ref. 1; AAB48101 and 3; BAA83340)"
FT /evidence="ECO:0000305"
FT STRAND 29..41
FT /evidence="ECO:0007829|PDB:3TZD"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:3TZD"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3TZD"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3TZD"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3TZD"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:3TZD"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:5T1I"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:5T1I"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:5T1I"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:5T1I"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:5T1I"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:5T1I"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5T1I"
SQ SEQUENCE 183 AA; 20811 MW; 5928C63E0C93A76A CRC64;
MASNKTTLQK MGKKQNGKSK KVEEAEPEEF VVEKVLDRRV VNGKVEYFLK WKGFTDADNT
WEPEENLDCP ELIEAFLNSQ KAGKEKDGTK RKSLSDSESD DSKSKKKRDA ADKPRGFARG
LDPERIIGAT DSSGELMFLM KWKDSDEADL VLAKEANMKC PQIVIAFYEE RLTWHSCPED
EAQ
