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Database: UniProt
Entry: CBX1_HUMAN
LinkDB: CBX1_HUMAN
Original site: 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   27-MAR-2024, entry version 190.
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.
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   INTERACTION WITH CHD3 AND CHD4, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   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   [25]
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   [26]
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). Interacts
CC       with CHD3 (PubMed:28977666). Interacts with CHD4 (PubMed:28977666).
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       ECO:0000269|PubMed:28977666}.
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:28977666, ECO:0000269|PubMed:9169582}.
CC       Note=Unassociated with chromosomes during 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; 259.
DR   DIP; DIP-28135N; -.
DR   IntAct; P83916; 136.
DR   MINT; P83916; -.
DR   STRING; 9606.ENSP00000377060; -.
DR   BindingDB; P83916; -.
DR   ChEMBL; CHEMBL1741193; -.
DR   GlyGen; P83916; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000377060; -.
DR   PeptideAtlas; P83916; -.
DR   ProteomicsDB; 57742; -.
DR   Pumba; P83916; -.
DR   TopDownProteomics; P83916; -.
DR   ABCD; P83916; 5 sequenced antibodies.
DR   Antibodypedia; 3221; 380 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   AGR; HGNC:1551; -.
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; LMAWLEF; -.
DR   OrthoDB; 75895at2759; -.
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; 229 hits in 1128 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 214 other cell types or 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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0001940; C:male pronucleus; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0003677; F:DNA binding; EXP:DisProt.
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:0060090; F:molecular adaptor activity; EXP:DisProt.
DR   GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd18650; CD_HP1beta_Cbx1; 1.
DR   CDD; cd18654; CSD_HP1beta_Cbx1; 1.
DR   DisProt; DP02856; -.
DR   Gene3D; 2.40.50.40; -; 2.
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   PANTHER; PTHR22812; CHROMOBOX PROTEIN; 1.
DR   PANTHER; PTHR22812:SF157; CHROMOBOX PROTEIN HOMOLOG 1; 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; 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
//
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