HP1_DROME
ID HP1_DROME Reviewed; 206 AA.
AC P05205; A4V0F1; B6UVR4; B6UVS1; B6UVS2; B6UVS3; B6UVT2; B6UVT6; B6UVT7;
AC Q9VLR6;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Heterochromatin protein 1;
DE Short=HP1;
DE AltName: Full=Non-histone chromosomal protein C1A9 antigen;
GN Name=Su(var)205; Synonyms=HP1; ORFNames=CG8409;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3099166; DOI=10.1128/mcb.6.11.3862-3872.1986;
RA James T.C., Elgin S.C.R.;
RT "Identification of a nonhistone chromosomal protein associated with
RT heterochromatin in Drosophila melanogaster and its gene.";
RL Mol. Cell. Biol. 6:3862-3872(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=2124708; DOI=10.1073/pnas.87.24.9923;
RA Eissenberg J.C., James T.C., Forster-Hartnett D.W., Hartnett T., Ngan V.,
RA Elgin S.C.R.;
RT "Mutation in a heterochromatin-specific chromosomal protein is associated
RT with suppression of position-effect variegation in Drosophila
RT melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9923-9927(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-105; CYS-126 AND
RP SER-134.
RC STRAIN=MW11, MW25, MW27, MW38, MW56, MW6, MW63, MW9, NC301, NC303, NC304,
RC NC306, NC319, NC322, NC335, NC336, NC350, NC357, NC358, NC359, NC361,
RC NC362, NC375, NC390, NC397, NC399, NC732, NC740, and NC774;
RX PubMed=18984573; DOI=10.1534/genetics.108.093807;
RA Anderson J.A., Gilliland W.D., Langley C.H.;
RT "Molecular population genetics and evolution of Drosophila meiosis genes.";
RL Genetics 181:177-185(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP DOMAIN CHROMO.
RX PubMed=1708124; DOI=10.1093/nar/19.4.789;
RA Singh P.B., Miller J.R., Pearce J., Kothary R., Burton R.D., Paro R.,
RA James T.C., Gaunt S.J.;
RT "A sequence motif found in a Drosophila heterochromatin protein is
RT conserved in animals and plants.";
RL Nucleic Acids Res. 19:789-794(1991).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=9378752; DOI=10.1242/jcs.110.17.1999;
RA Frankel S., Sigel E.A., Craig C., Elgin S.C., Mooseker M.S.,
RA Artavanis-Tsakonas S.;
RT "An actin-related protein in Drosophila colocalizes with heterochromatin
RT protein 1 in pericentric heterochromatin.";
RL J. Cell Sci. 110:1999-2012(1997).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF VAL-26.
RX PubMed=11566886; DOI=10.1093/emboj/20.18.5232;
RA Jacobs S.A., Taverna S.D., Zhang Y., Briggs S.D., Li J., Eissenberg J.C.,
RA Allis C.D., Khorasanizadeh S.;
RT "Specificity of the HP1 chromo domain for the methylated N-terminus of
RT histone H3.";
RL EMBO J. 20:5232-5241(2001).
RN [10]
RP INTERACTION WITH SU(VAR)39.
RX PubMed=11867540; DOI=10.1093/emboj/21.5.1121;
RA Schotta G., Ebert A., Krauss V., Fischer A., Hoffmann J., Rea S.,
RA Jenuwein T., Dorn R., Reuter G.;
RT "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and
RT heterochromatic gene silencing.";
RL EMBO J. 21:1121-1131(2002).
RN [11]
RP INTERACTION WITH MCM10.
RX PubMed=12808023; DOI=10.1091/mbc.e02-11-0706;
RA Christensen T.W., Tye B.K.;
RT "Drosophila MCM10 interacts with members of the prereplication complex and
RT is required for proper chromosome condensation.";
RL Mol. Biol. Cell 14:2206-2215(2003).
RN [12]
RP INTERACTION WITH PIWI, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP VAL-26; ILE-191 AND TRP-200.
RX PubMed=17875665; DOI=10.1101/gad.1564307;
RA Brower-Toland B., Findley S.D., Jiang L., Liu L., Yin H., Dus M., Zhou P.,
RA Elgin S.C., Lin H.;
RT "Drosophila PIWI associates with chromatin and interacts directly with
RT HP1a.";
RL Genes Dev. 21:2300-2311(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-127; THR-128 AND
RP THR-134, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15; SER-102; SER-103;
RP SER-113 AND THR-128, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 17-76, AND FUNCTION.
RX PubMed=11859155; DOI=10.1126/science.1069473;
RA Jacobs S.A., Khorasanizadeh S.;
RT "Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3
RT tail.";
RL Science 295:2080-2083(2002).
CC -!- FUNCTION: Structural component of heterochromatin, involved in gene
CC repression and the modification of position-effect-variegation.
CC Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to
CC epigenetic repression. {ECO:0000269|PubMed:11566886,
CC ECO:0000269|PubMed:11859155}.
CC -!- SUBUNIT: Homodimer; probably associates with Su(var)3-9. Interacts with
CC Mcm10. Interacts (via chromoshadow domain) with piwi (via N-terminal
CC region). {ECO:0000269|PubMed:11867540, ECO:0000269|PubMed:12808023,
CC ECO:0000269|PubMed:17875665}.
CC -!- INTERACTION:
CC P05205; Q9W0Z5: Atf-2; NbExp=3; IntAct=EBI-155532, EBI-94769;
CC P05205; Q95RV2: cav; NbExp=5; IntAct=EBI-155532, EBI-104820;
CC P05205; P02255: His1:CG33843; NbExp=2; IntAct=EBI-155532, EBI-151629;
CC P05205; P02299: His3:CG33854; NbExp=3; IntAct=EBI-155532, EBI-522090;
CC P05205; Q8IQ92: HP4; NbExp=4; IntAct=EBI-155532, EBI-89649;
CC P05205; Q9VIE6: Mcm10; NbExp=2; IntAct=EBI-155532, EBI-91264;
CC P05205; B7Z0L8: moi; NbExp=3; IntAct=EBI-155532, EBI-15755079;
CC P05205; Q9VEF0: Odj; NbExp=3; IntAct=EBI-155532, EBI-141895;
CC P05205; P45975: Su(var)3-9; NbExp=3; IntAct=EBI-155532, EBI-110378;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:9378752}. Chromosome {ECO:0000269|PubMed:17875665,
CC ECO:0000269|PubMed:9378752}. Note=Colocalizes with Arp6 on centric
CC heterochromatin.
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DR EMBL; M57574; AAA28620.1; -; Genomic_DNA.
DR EMBL; M14131; AAA28402.1; ALT_SEQ; mRNA.
DR EMBL; FJ218607; ACI96755.1; -; Genomic_DNA.
DR EMBL; FJ218612; ACI96760.1; -; Genomic_DNA.
DR EMBL; FJ218613; ACI96761.1; -; Genomic_DNA.
DR EMBL; FJ218614; ACI96762.1; -; Genomic_DNA.
DR EMBL; FJ218615; ACI96763.1; -; Genomic_DNA.
DR EMBL; FJ218616; ACI96764.1; -; Genomic_DNA.
DR EMBL; FJ218617; ACI96765.1; -; Genomic_DNA.
DR EMBL; FJ218618; ACI96766.1; -; Genomic_DNA.
DR EMBL; FJ218619; ACI96767.1; -; Genomic_DNA.
DR EMBL; FJ218620; ACI96768.1; -; Genomic_DNA.
DR EMBL; FJ218621; ACI96769.1; -; Genomic_DNA.
DR EMBL; FJ218622; ACI96770.1; -; Genomic_DNA.
DR EMBL; FJ218623; ACI96771.1; -; Genomic_DNA.
DR EMBL; FJ218624; ACI96772.1; -; Genomic_DNA.
DR EMBL; FJ218625; ACI96773.1; -; Genomic_DNA.
DR EMBL; FJ218626; ACI96774.1; -; Genomic_DNA.
DR EMBL; FJ218627; ACI96775.1; -; Genomic_DNA.
DR EMBL; FJ218628; ACI96776.1; -; Genomic_DNA.
DR EMBL; FJ218629; ACI96777.1; -; Genomic_DNA.
DR EMBL; FJ218630; ACI96778.1; -; Genomic_DNA.
DR EMBL; FJ218631; ACI96779.1; -; Genomic_DNA.
DR EMBL; FJ218632; ACI96780.1; -; Genomic_DNA.
DR EMBL; FJ218633; ACI96781.1; -; Genomic_DNA.
DR EMBL; FJ218634; ACI96782.1; -; Genomic_DNA.
DR EMBL; FJ218635; ACI96783.1; -; Genomic_DNA.
DR EMBL; FJ218636; ACI96784.1; -; Genomic_DNA.
DR EMBL; FJ218637; ACI96785.1; -; Genomic_DNA.
DR EMBL; FJ218638; ACI96786.1; -; Genomic_DNA.
DR EMBL; FJ218639; ACI96787.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52618.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11156.1; -; Genomic_DNA.
DR EMBL; AY061119; AAL28667.1; -; mRNA.
DR PIR; A39268; A39268.
DR RefSeq; NP_476755.1; NM_057407.4.
DR RefSeq; NP_723361.1; NM_164799.2.
DR PDB; 1KNA; X-ray; 2.10 A; A=17-76.
DR PDB; 1KNE; X-ray; 2.40 A; A=17-76.
DR PDB; 1Q3L; X-ray; 1.64 A; A=17-76.
DR PDB; 3P7J; X-ray; 2.30 A; A/B=131-206.
DR PDB; 6ASZ; X-ray; 1.52 A; A=17-76.
DR PDB; 6AT0; X-ray; 1.28 A; A=17-76.
DR PDB; 6MHA; X-ray; 1.50 A; A=22-74.
DR PDBsum; 1KNA; -.
DR PDBsum; 1KNE; -.
DR PDBsum; 1Q3L; -.
DR PDBsum; 3P7J; -.
DR PDBsum; 6ASZ; -.
DR PDBsum; 6AT0; -.
DR PDBsum; 6MHA; -.
DR AlphaFoldDB; P05205; -.
DR SMR; P05205; -.
DR BioGRID; 60248; 133.
DR DIP; DIP-21869N; -.
DR ELM; P05205; -.
DR IntAct; P05205; 33.
DR MINT; P05205; -.
DR STRING; 7227.FBpp0079251; -.
DR iPTMnet; P05205; -.
DR PaxDb; P05205; -.
DR PRIDE; P05205; -.
DR EnsemblMetazoa; FBtr0079635; FBpp0079251; FBgn0003607.
DR EnsemblMetazoa; FBtr0079636; FBpp0079252; FBgn0003607.
DR GeneID; 34119; -.
DR KEGG; dme:Dmel_CG8409; -.
DR UCSC; CG8409-RB; d. melanogaster.
DR CTD; 34119; -.
DR FlyBase; FBgn0003607; Su(var)205.
DR VEuPathDB; VectorBase:FBgn0003607; -.
DR eggNOG; KOG1911; Eukaryota.
DR GeneTree; ENSGT00940000154152; -.
DR HOGENOM; CLU_045874_1_1_1; -.
DR InParanoid; P05205; -.
DR OMA; YIKWQGF; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; P05205; -.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P05205; -.
DR BioGRID-ORCS; 34119; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Su(var)205; fly.
DR EvolutionaryTrace; P05205; -.
DR GenomeRNAi; 34119; -.
DR PRO; PR:P05205; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003607; Expressed in eye disc (Drosophila) and 42 other tissues.
DR Genevisible; P05205; DM.
DR GO; GO:0010369; C:chromocenter; IDA:FlyBase.
DR GO; GO:0005694; C:chromosome; IDA:FlyBase.
DR GO; GO:0000775; C:chromosome, centromeric region; NAS:FlyBase.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:FlyBase.
DR GO; GO:0000793; C:condensed chromosome; IDA:FlyBase.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:FlyBase.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005701; C:polytene chromosome chromocenter; IDA:FlyBase.
DR GO; GO:0005703; C:polytene chromosome puff; TAS:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0042393; F:histone binding; NAS:FlyBase.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:CAFA.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; NAS:FlyBase.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:CAFA.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:CAFA.
DR GO; GO:0000182; F:rDNA binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0070063; F:RNA polymerase binding; IDA:CAFA.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IDA:CAFA.
DR GO; GO:0003696; F:satellite DNA binding; IDA:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:FlyBase.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:CACAO.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:FlyBase.
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; NAS:FlyBase.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; HMP:FlyBase.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IMP:FlyBase.
DR GO; GO:1905646; P:positive regulation of FACT complex assembly; IDA:CAFA.
DR GO; GO:1900111; P:positive regulation of histone H3-K9 dimethylation; IDA:FlyBase.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:CAFA.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:FlyBase.
DR GO; GO:1905632; P:protein localization to euchromatin; IDA:CAFA.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0031060; P:regulation of histone methylation; IMP:FlyBase.
DR GO; GO:1905634; P:regulation of protein localization to chromatin; IMP:CAFA.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:FlyBase.
DR DisProt; DP02865; -.
DR IDEAL; IID50064; -.
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; Chromatin regulator; Chromosome; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..206
FT /note="Heterochromatin protein 1"
FT /id="PRO_0000080197"
FT DOMAIN 24..82
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 147..205
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..206
FT /note="Binds to Su(var)39"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 24
FT /note="Histone H3K9me2 binding"
FT SITE 45
FT /note="Histone H3K9me2 binding"
FT SITE 48
FT /note="Histone H3K9me2 binding"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 127
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 134
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VARIANT 105
FT /note="T -> A (in strain: NC322, NC358 and NC359)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 126
FT /note="R -> C (in strain: NC390)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 134
FT /note="T -> S (in strain: MW25)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT MUTAGEN 26
FT /note="V->M: Impairs chromo domain folding and histone H3
FT binding. Does not affect piwi binding."
FT /evidence="ECO:0000269|PubMed:11566886,
FT ECO:0000269|PubMed:17875665"
FT MUTAGEN 191
FT /note="I->E: Abolishes piwi binding."
FT /evidence="ECO:0000269|PubMed:17875665"
FT MUTAGEN 200
FT /note="W->A: Abolishes piwi binding."
FT /evidence="ECO:0000269|PubMed:17875665"
FT STRAND 23..35
FT /evidence="ECO:0007829|PDB:6AT0"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:6AT0"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6AT0"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6AT0"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:6AT0"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:6AT0"
FT TURN 142..146
FT /evidence="ECO:0007829|PDB:3P7J"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:3P7J"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:3P7J"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:3P7J"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:3P7J"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:3P7J"
SQ SEQUENCE 206 AA; 23185 MW; 6A5B204C487526B7 CRC64;
MGKKIDNPES SAKVSDAEEE EEEYAVEKII DRRVRKGKVE YYLKWKGYPE TENTWEPENN
LDCQDLIQQY EASRKDEEKS AASKKDRPSS SAKAKETQGR ASSSTSTASK RKSEEPTAPS
GNKSKRTTDA EQDTIPVSGS TGFDRGLEAE KILGASDNNG RLTFLIQFKG VDQAEMVPSS
VANEKIPRMV IHFYEERLSW YSDNED
