CBX1_HUMAN
ID CBX1_HUMAN Reviewed; 185 AA.
AC P83916; P23197;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Chromobox protein homolog 1;
DE AltName: Full=HP1Hsbeta;
DE AltName: Full=Heterochromatin protein 1 homolog beta;
DE Short=HP1 beta;
DE AltName: Full=Heterochromatin protein p25;
DE AltName: Full=M31;
DE AltName: Full=Modifier 1 protein;
DE AltName: Full=p25beta;
GN Name=CBX1; Synonyms=CBX;
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], AND SUBCELLULAR LOCATION.
RC TISSUE=Liver tumor;
RX PubMed=9169582; DOI=10.1007/s004120050219;
RA Furuta K., Chan E.K.L., Kiyosawa K., Reimer G., Luderschmidt C., Tan E.M.;
RT "Heterochromatin protein HP1Hsbeta (p25beta) and its localization with
RT centromeres in mitosis.";
RL Chromosoma 106:11-19(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 8-25; 122-137; 140-150 AND 156-167, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION, AND LACK OF 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 [5]
RP INTERACTION WITH SUV39H1.
RX PubMed=10202156; DOI=10.1093/emboj/18.7.1923;
RA Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G.,
RA Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G., Jenuwein T.;
RT "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9
RT encode centromere-associated proteins which complex with the
RT heterochromatin component M31.";
RL EMBO J. 18:1923-1938(1999).
RN [6]
RP INTERACTION WITH EMSY.
RX PubMed=14651845; DOI=10.1016/s0092-8674(03)00930-9;
RA Hughes-Davies L., Huntsman D., Ruas M., Fuks F., Bye J., Chin S.-F.,
RA Milner J., Brown L.A., Hsu F., Gilks B., Nielsen T., Schulzer M., Chia S.,
RA Ragaz J., Cahn A., Linger L., Ozdag H., Cattaneo E., Jordanova E.S.,
RA Schuuring E., Yu D.S., Venkitaraman A., Ponder B., Doherty A., Aparicio S.,
RA Bentley D., Theillet C., Ponting C.P., Caldas C., Kouzarides T.;
RT "EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer.";
RL Cell 115:523-535(2003).
RN [7]
RP MUTAGENESIS OF ILE-161.
RX PubMed=15947784; DOI=10.1038/sj.embor.7400415;
RA Ekblad C.M.S., Chavali G.B., Basu B.P., Freund S.M.V., Veprintsev D.,
RA Hughes-Davies L., Kouzarides T., Doherty A.J., Itzhaki L.S.;
RT "Binding of EMSY to HP1beta: implications for recruitment of HP1beta and
RT BS69.";
RL EMBO Rep. 6:675-680(2005).
RN [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY
RP 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-91 AND SER-175, AND
RP 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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY
RP 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 [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-9, AND IDENTIFICATION BY MASS
RP 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 [22]
RP INTERACTION WITH HDGFL2.
RX PubMed=26721387; DOI=10.1093/nar/gkv1526;
RA Baude A., Aaes T.L., Zhai B., Al-Nakouzi N., Oo H.Z., Daugaard M.,
RA Rohde M., Jaeaettelae M.;
RT "Hepatoma-derived growth factor-related protein 2 promotes DNA repair by
RT homologous recombination.";
RL Nucleic Acids Res. 44:2214-2226(2016).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-33; LYS-99 AND LYS-150,
RP 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 [24]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 104-175 IN COMPLEX WITH EMSY.
RX PubMed=16615912; DOI=10.1016/j.str.2006.01.007;
RA Huang Y., Myers M.P., Xu R.-M.;
RT "Crystal structure of the HP1-EMSY complex reveals an unusual mode of HP1
RT binding.";
RL Structure 14:703-712(2006).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 108-185 IN COMPLEX WITH SGO1, AND
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).
CC -!- FUNCTION: Component of heterochromatin. Recognizes and binds histone H3
CC tails methylated at 'Lys-9', leading to epigenetic repression.
CC Interaction with lamin B receptor (LBR) can contribute to the
CC association of the heterochromatin with the inner nuclear membrane.
CC {ECO:0000250|UniProtKB:P83917}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts directly with CHAF1A,
CC EMSY, LBR, TIF1/TIF1A and TRIM28/TIF1B PXVXL motif via the chromoshadow
CC domain (PubMed:14651845, PubMed:16615912). Interacts directly with
CC histone H3 methylated at 'Lys-9' via the chromo domain (By similarity).
CC Interacts with SUV39H1 and SETDB1, KMT5B and KMT5C (PubMed:10202156,
CC PubMed:15899859). Interacts with PRDM6 (By similarity). Interacts with
CC POGZ (PubMed:20850016, PubMed:20562864). Interacts with CHAMP1
CC (PubMed:20850016). Interacts with INCENP (PubMed:21346195). Interacts
CC with SGO1; the CBX1 homodimer binds to one molecule of SGO1
CC (PubMed:21346195). Interacts with LRIF1 (via PxVxL motif)
CC (PubMed:23542155). Interacts with HDGFL2 (PubMed:26721387).
CC {ECO:0000250|UniProtKB:P83917, ECO:0000269|PubMed:10202156,
CC ECO:0000269|PubMed:14651845, ECO:0000269|PubMed:15899859,
CC ECO:0000269|PubMed:16615912, ECO:0000269|PubMed:20562864,
CC ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:21346195,
CC ECO:0000269|PubMed:23542155, ECO:0000269|PubMed:26721387}.
CC -!- INTERACTION:
CC P83916; Q9H2P0: ADNP; NbExp=4; IntAct=EBI-78129, EBI-1764854;
CC P83916; Q6IQ32: ADNP2; NbExp=4; IntAct=EBI-78129, EBI-2838654;
CC P83916; P05067: APP; NbExp=6; IntAct=EBI-78129, EBI-77613;
CC P83916; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-78129, EBI-742750;
CC P83916; P43681: CHRNA4; NbExp=3; IntAct=EBI-78129, EBI-7132379;
CC P83916; P50570-2: DNM2; NbExp=3; IntAct=EBI-78129, EBI-10968534;
CC P83916; Q7Z589: EMSY; NbExp=3; IntAct=EBI-78129, EBI-6598631;
CC P83916; P06241: FYN; NbExp=3; IntAct=EBI-78129, EBI-515315;
CC P83916; P68431: H3C12; NbExp=12; IntAct=EBI-78129, EBI-79722;
CC P83916; P42858: HTT; NbExp=15; IntAct=EBI-78129, EBI-466029;
CC P83916; Q99732: LITAF; NbExp=3; IntAct=EBI-78129, EBI-725647;
CC P83916; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-78129, EBI-739832;
CC P83916; P10588: NR2F6; NbExp=2; IntAct=EBI-78129, EBI-2681496;
CC P83916; Q5FBB7: SGO1; NbExp=2; IntAct=EBI-78129, EBI-989069;
CC P83916; Q92673: SORL1; NbExp=3; IntAct=EBI-78129, EBI-1171329;
CC P83916; P23497-2: SP100; NbExp=3; IntAct=EBI-78129, EBI-6589365;
CC P83916; O43463: SUV39H1; NbExp=4; IntAct=EBI-78129, EBI-349968;
CC P83916; P09936: UCHL1; NbExp=4; IntAct=EBI-78129, EBI-714860;
CC P83916; Q8ND82: ZNF280C; NbExp=4; IntAct=EBI-78129, EBI-8831272;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10460410,
CC ECO:0000269|PubMed:9169582}. Note=Unassociated with chromosomes during
CC mitosis.
CC -!- TISSUE SPECIFICITY: Expressed in all adult and embryonic tissues.
CC -!- PTM: Not phosphorylated.
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 -!- WEB RESOURCE: Name=Wikipedia; Note=Heterochromatin protein 1 entry;
CC URL="https://en.wikipedia.org/wiki/Heterochromatin_Protein_1";
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DR EMBL; U35451; AAB81548.1; -; mRNA.
DR EMBL; BC002609; AAH02609.1; -; mRNA.
DR EMBL; BC021302; AAH21302.1; -; mRNA.
DR CCDS; CCDS11525.1; -.
DR PIR; G02080; G02080.
DR RefSeq; NP_001120700.1; NM_001127228.1.
DR RefSeq; NP_006798.1; NM_006807.4.
DR PDB; 2FMM; X-ray; 1.80 A; A/B/C/D=104-175.
DR PDB; 3F2U; X-ray; 1.80 A; A=20-73.
DR PDB; 3Q6S; X-ray; 1.93 A; A/B/C/D=108-185.
DR PDB; 5T1G; X-ray; 1.90 A; A=108-185.
DR PDB; 6D07; X-ray; 2.10 A; A/B=20-73.
DR PDB; 6D08; X-ray; 2.10 A; A/B=20-73.
DR PDBsum; 2FMM; -.
DR PDBsum; 3F2U; -.
DR PDBsum; 3Q6S; -.
DR PDBsum; 5T1G; -.
DR PDBsum; 6D07; -.
DR PDBsum; 6D08; -.
DR AlphaFoldDB; P83916; -.
DR SMR; P83916; -.
DR BioGRID; 116151; 172.
DR DIP; DIP-28135N; -.
DR IntAct; P83916; 134.
DR MINT; P83916; -.
DR STRING; 9606.ENSP00000377060; -.
DR BindingDB; P83916; -.
DR ChEMBL; CHEMBL1741193; -.
DR iPTMnet; P83916; -.
DR MetOSite; P83916; -.
DR PhosphoSitePlus; P83916; -.
DR SwissPalm; P83916; -.
DR BioMuta; CBX1; -.
DR DMDM; 48428808; -.
DR EPD; P83916; -.
DR jPOST; P83916; -.
DR MassIVE; P83916; -.
DR PaxDb; P83916; -.
DR PeptideAtlas; P83916; -.
DR PRIDE; P83916; -.
DR ProteomicsDB; 57742; -.
DR TopDownProteomics; P83916; -.
DR ABCD; P83916; 5 sequenced antibodies.
DR Antibodypedia; 3221; 350 antibodies from 39 providers.
DR DNASU; 10951; -.
DR Ensembl; ENST00000225603.9; ENSP00000225603.4; ENSG00000108468.15.
DR Ensembl; ENST00000393408.7; ENSP00000377060.3; ENSG00000108468.15.
DR GeneID; 10951; -.
DR KEGG; hsa:10951; -.
DR MANE-Select; ENST00000225603.9; ENSP00000225603.4; NM_001127228.2; NP_001120700.1.
DR CTD; 10951; -.
DR DisGeNET; 10951; -.
DR GeneCards; CBX1; -.
DR HGNC; HGNC:1551; CBX1.
DR HPA; ENSG00000108468; Low tissue specificity.
DR MIM; 604511; gene.
DR neXtProt; NX_P83916; -.
DR OpenTargets; ENSG00000108468; -.
DR PharmGKB; PA26126; -.
DR VEuPathDB; HostDB:ENSG00000108468; -.
DR eggNOG; KOG1911; Eukaryota.
DR GeneTree; ENSGT00940000154152; -.
DR HOGENOM; CLU_045874_1_0_1; -.
DR InParanoid; P83916; -.
DR OMA; SNEENTW; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; P83916; -.
DR TreeFam; TF350503; -.
DR PathwayCommons; P83916; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR SignaLink; P83916; -.
DR SIGNOR; P83916; -.
DR BioGRID-ORCS; 10951; 225 hits in 1049 CRISPR screens.
DR ChiTaRS; CBX1; human.
DR EvolutionaryTrace; P83916; -.
DR GeneWiki; CBX1; -.
DR GenomeRNAi; 10951; -.
DR Pharos; P83916; Tbio.
DR PRO; PR:P83916; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P83916; protein.
DR Bgee; ENSG00000108468; Expressed in ganglionic eminence and 212 other tissues.
DR ExpressionAtlas; P83916; baseline and differential.
DR Genevisible; P83916; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0010369; C:chromocenter; IEA:Ensembl.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; TAS:ProtInc.
DR GO; GO:0001940; C:male pronucleus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR DisProt; DP02856; -.
DR IDEAL; IID00275; -.
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 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; Direct protein sequencing; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..185
FT /note="Chromobox protein homolog 1"
FT /id="PRO_0000080199"
FT DOMAIN 21..79
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 117..175
FT /note="Chromo 2; shadow subtype"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 63..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 16
FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B"
FT /evidence="ECO:0000250"
FT SITE 21
FT /note="Histone H3K9me2 binding"
FT /evidence="ECO:0000250"
FT SITE 23
FT /note="Histone H3A7 binding"
FT /evidence="ECO:0000250"
FT SITE 40
FT /note="Histone H3A7 binding"
FT /evidence="ECO:0000250"
FT SITE 42
FT /note="Histone H3A7 binding"
FT /evidence="ECO:0000250"
FT SITE 42
FT /note="Histone H3K9me2 binding"
FT /evidence="ECO:0000250"
FT SITE 45
FT /note="Histone H3K9me2 binding"
FT /evidence="ECO:0000250"
FT SITE 58
FT /note="Histone H3A7 binding"
FT /evidence="ECO:0000250"
FT SITE 60
FT /note="Histone H3A7 binding"
FT /evidence="ECO:0000250"
FT SITE 125
FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B"
FT /evidence="ECO:0000250"
FT SITE 126
FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B"
FT /evidence="ECO:0000250"
FT SITE 135
FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B"
FT /evidence="ECO:0000250"
FT SITE 146
FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B"
FT /evidence="ECO:0000250"
FT SITE 167
FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B"
FT /evidence="ECO:0000250"
FT SITE 168
FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B"
FT /evidence="ECO:0000250"
FT SITE 170
FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B"
FT /evidence="ECO:0000250"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 9
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 161
FT /note="I->E: Abolishes homodimer formation and binding to
FT EMSY."
FT /evidence="ECO:0000269|PubMed:15947784"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:3F2U"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:3F2U"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3F2U"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3F2U"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3F2U"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:3F2U"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:2FMM"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:2FMM"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:2FMM"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:2FMM"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:2FMM"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:2FMM"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:2FMM"
SQ SEQUENCE 185 AA; 21418 MW; BE687AF9C66E48E3 CRC64;
MGKKQNKKKV EEVLEEEEEE YVVEKVLDRR VVKGKVEYLL KWKGFSDEDN TWEPEENLDC
PDLIAEFLQS QKTAHETDKS EGGKRKADSD SEDKGEESKP KKKKEESEKP RGFARGLEPE
RIIGATDSSG ELMFLMKWKN SDEADLVPAK EANVKCPQVV ISFYEERLTW HSYPSEDDDK
KDDKN