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Heterochromatin protein 1 (HP1) (Non-histone chromosomal protein C1A9 antigen)

 HP1_DROME               Reviewed;         206 AA.
P05205; A4V0F1; B6UVR4; B6UVS1; B6UVS2; B6UVS3; B6UVT2; B6UVT6;
B6UVT7; Q9VLR6;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
18-JUL-2018, entry version 191.
RecName: Full=Heterochromatin protein 1;
Short=HP1;
AltName: Full=Non-histone chromosomal protein C1A9 antigen;
Name=Su(var)205; Synonyms=HP1; ORFNames=CG8409;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3099166; DOI=10.1128/MCB.6.11.3862;
James T.C., Elgin S.C.R.;
"Identification of a nonhistone chromosomal protein associated with
heterochromatin in Drosophila melanogaster and its gene.";
Mol. Cell. Biol. 6:3862-3872(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
PubMed=2124708; DOI=10.1073/pnas.87.24.9923;
Eissenberg J.C., James T.C., Forster-Hartnett D.W., Hartnett T.,
Ngan V., Elgin S.C.R.;
"Mutation in a heterochromatin-specific chromosomal protein is
associated with suppression of position-effect variegation in
Drosophila melanogaster.";
Proc. Natl. Acad. Sci. U.S.A. 87:9923-9927(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-105; CYS-126 AND
SER-134.
STRAIN=MW11, MW25, MW27, MW38, MW56, MW6, MW63, MW9, NC301, NC303,
NC304, NC306, NC319, NC322, NC335, NC336, NC350, NC357, NC358, NC359,
NC361, NC362, NC375, NC390, NC397, NC399, NC732, NC740, and NC774;
PubMed=18984573; DOI=10.1534/genetics.108.093807;
Anderson J.A., Gilliland W.D., Langley C.H.;
"Molecular population genetics and evolution of Drosophila meiosis
genes.";
Genetics 181:177-185(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
DOMAIN CHROMO.
PubMed=1708124; DOI=10.1093/nar/19.4.789;
Singh P.B., Miller J.R., Pearce J., Kothary R., Burton R.D., Paro R.,
James T.C., Gaunt S.J.;
"A sequence motif found in a Drosophila heterochromatin protein is
conserved in animals and plants.";
Nucleic Acids Res. 19:789-794(1991).
[8]
SUBCELLULAR LOCATION.
PubMed=9378752;
Frankel S., Sigel E.A., Craig C., Elgin S.C., Mooseker M.S.,
Artavanis-Tsakonas S.;
"An actin-related protein in Drosophila colocalizes with
heterochromatin protein 1 in pericentric heterochromatin.";
J. Cell Sci. 110:1999-2012(1997).
[9]
FUNCTION, AND MUTAGENESIS OF VAL-26.
PubMed=11566886; DOI=10.1093/emboj/20.18.5232;
Jacobs S.A., Taverna S.D., Zhang Y., Briggs S.D., Li J.,
Eissenberg J.C., Allis C.D., Khorasanizadeh S.;
"Specificity of the HP1 chromo domain for the methylated N-terminus of
histone H3.";
EMBO J. 20:5232-5241(2001).
[10]
INTERACTION WITH SU(VAR)39.
PubMed=11867540; DOI=10.1093/emboj/21.5.1121;
Schotta G., Ebert A., Krauss V., Fischer A., Hoffmann J., Rea S.,
Jenuwein T., Dorn R., Reuter G.;
"Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation
and heterochromatic gene silencing.";
EMBO J. 21:1121-1131(2002).
[11]
INTERACTION WITH MCM10.
PubMed=12808023; DOI=10.1091/mbc.E02-11-0706;
Christensen T.W., Tye B.K.;
"Drosophila MCM10 interacts with members of the prereplication complex
and is required for proper chromosome condensation.";
Mol. Biol. Cell 14:2206-2215(2003).
[12]
INTERACTION WITH PIWI, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF VAL-26; ILE-191 AND TRP-200.
PubMed=17875665; DOI=10.1101/gad.1564307;
Brower-Toland B., Findley S.D., Jiang L., Liu L., Yin H., Dus M.,
Zhou P., Elgin S.C., Lin H.;
"Drosophila PIWI associates with chromatin and interacts directly with
HP1a.";
Genes Dev. 21:2300-2311(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-127; THR-128 AND
THR-134, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15; SER-102;
SER-103; SER-113 AND THR-128, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[15]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 17-76, AND FUNCTION.
PubMed=11859155; DOI=10.1126/science.1069473;
Jacobs S.A., Khorasanizadeh S.;
"Structure of HP1 chromodomain bound to a lysine 9-methylated histone
H3 tail.";
Science 295:2080-2083(2002).
-!- FUNCTION: Structural component of heterochromatin, involved in
gene repression and the modification of position-effect-
variegation. Recognizes and binds histone H3 tails methylated at
'Lys-9', leading to epigenetic repression.
{ECO:0000269|PubMed:11566886, ECO:0000269|PubMed:11859155}.
-!- SUBUNIT: Homodimer; probably associates with Su(var)3-9. Interacts
with Mcm10. Interacts (via chromoshadow domain) with piwi (via N-
terminal region). {ECO:0000269|PubMed:11867540,
ECO:0000269|PubMed:12808023, ECO:0000269|PubMed:17875665}.
-!- INTERACTION:
Q9W0Z5:Atf-2-RB; NbExp=3; IntAct=EBI-155532, EBI-94769;
Q95RV2:cav; NbExp=6; IntAct=EBI-155532, EBI-104820;
P02255:His1:CG33843; NbExp=2; IntAct=EBI-155532, EBI-151629;
P02299:His3:CG33854; NbExp=8; IntAct=EBI-155532, EBI-522090;
Q8IQ92:HP4; NbExp=4; IntAct=EBI-155532, EBI-89649;
Q9VIE6:Mcm10; NbExp=2; IntAct=EBI-155532, EBI-91264;
B7Z0L8:moi; NbExp=3; IntAct=EBI-155532, EBI-15755079;
P45975:Su(var)3-9; NbExp=3; IntAct=EBI-155532, EBI-110378;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:9378752}. Chromosome
{ECO:0000269|PubMed:17875665, ECO:0000269|PubMed:9378752}.
Note=Colocalizes with Arp6 on centric heterochromatin.
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EMBL; M57574; AAA28620.1; -; Genomic_DNA.
EMBL; M14131; AAA28402.1; ALT_SEQ; mRNA.
EMBL; FJ218607; ACI96755.1; -; Genomic_DNA.
EMBL; FJ218612; ACI96760.1; -; Genomic_DNA.
EMBL; FJ218613; ACI96761.1; -; Genomic_DNA.
EMBL; FJ218614; ACI96762.1; -; Genomic_DNA.
EMBL; FJ218615; ACI96763.1; -; Genomic_DNA.
EMBL; FJ218616; ACI96764.1; -; Genomic_DNA.
EMBL; FJ218617; ACI96765.1; -; Genomic_DNA.
EMBL; FJ218618; ACI96766.1; -; Genomic_DNA.
EMBL; FJ218619; ACI96767.1; -; Genomic_DNA.
EMBL; FJ218620; ACI96768.1; -; Genomic_DNA.
EMBL; FJ218621; ACI96769.1; -; Genomic_DNA.
EMBL; FJ218622; ACI96770.1; -; Genomic_DNA.
EMBL; FJ218623; ACI96771.1; -; Genomic_DNA.
EMBL; FJ218624; ACI96772.1; -; Genomic_DNA.
EMBL; FJ218625; ACI96773.1; -; Genomic_DNA.
EMBL; FJ218626; ACI96774.1; -; Genomic_DNA.
EMBL; FJ218627; ACI96775.1; -; Genomic_DNA.
EMBL; FJ218628; ACI96776.1; -; Genomic_DNA.
EMBL; FJ218629; ACI96777.1; -; Genomic_DNA.
EMBL; FJ218630; ACI96778.1; -; Genomic_DNA.
EMBL; FJ218631; ACI96779.1; -; Genomic_DNA.
EMBL; FJ218632; ACI96780.1; -; Genomic_DNA.
EMBL; FJ218633; ACI96781.1; -; Genomic_DNA.
EMBL; FJ218634; ACI96782.1; -; Genomic_DNA.
EMBL; FJ218635; ACI96783.1; -; Genomic_DNA.
EMBL; FJ218636; ACI96784.1; -; Genomic_DNA.
EMBL; FJ218637; ACI96785.1; -; Genomic_DNA.
EMBL; FJ218638; ACI96786.1; -; Genomic_DNA.
EMBL; FJ218639; ACI96787.1; -; Genomic_DNA.
EMBL; AE014134; AAF52618.1; -; Genomic_DNA.
EMBL; AE014134; AAN11156.1; -; Genomic_DNA.
EMBL; AY061119; AAL28667.1; -; mRNA.
PIR; A39268; A39268.
RefSeq; NP_476755.1; NM_057407.4.
RefSeq; NP_723361.1; NM_164799.2.
UniGene; Dm.3713; -.
PDB; 1KNA; X-ray; 2.10 A; A=17-76.
PDB; 1KNE; X-ray; 2.40 A; A=17-76.
PDB; 1Q3L; X-ray; 1.64 A; A=17-76.
PDB; 3P7J; X-ray; 2.30 A; A/B=131-206.
PDB; 5KOG; X-ray; 1.52 A; A=17-76.
PDB; 6ASZ; X-ray; 1.52 A; A=17-76.
PDB; 6AT0; X-ray; 1.28 A; A=17-76.
PDBsum; 1KNA; -.
PDBsum; 1KNE; -.
PDBsum; 1Q3L; -.
PDBsum; 3P7J; -.
PDBsum; 5KOG; -.
PDBsum; 6ASZ; -.
PDBsum; 6AT0; -.
ProteinModelPortal; P05205; -.
SMR; P05205; -.
BioGrid; 60248; 94.
DIP; DIP-21869N; -.
ELM; P05205; -.
IntAct; P05205; 43.
MINT; P05205; -.
STRING; 7227.FBpp0079251; -.
iPTMnet; P05205; -.
PaxDb; P05205; -.
PRIDE; P05205; -.
EnsemblMetazoa; FBtr0079635; FBpp0079251; FBgn0003607.
EnsemblMetazoa; FBtr0079636; FBpp0079252; FBgn0003607.
GeneID; 34119; -.
KEGG; dme:Dmel_CG8409; -.
UCSC; CG8409-RB; d. melanogaster.
CTD; 34119; -.
FlyBase; FBgn0003607; Su(var)205.
eggNOG; KOG1911; Eukaryota.
eggNOG; ENOG4111JKD; LUCA.
GeneTree; ENSGT00510000046310; -.
InParanoid; P05205; -.
KO; K11587; -.
OMA; PETENTW; -.
OrthoDB; EOG091G0RBS; -.
PhylomeDB; P05205; -.
Reactome; R-DME-73777; RNA Polymerase I Chain Elongation.
Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; P05205; -.
ChiTaRS; Su(var)205; fly.
EvolutionaryTrace; P05205; -.
GenomeRNAi; 34119; -.
PRO; PR:P05205; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0003607; -.
Genevisible; P05205; DM.
GO; GO:0005694; C:chromosome; IDA:FlyBase.
GO; GO:0000775; C:chromosome, centromeric region; TAS:FlyBase.
GO; GO:0000781; C:chromosome, telomeric region; IDA:FlyBase.
GO; GO:0000793; C:condensed chromosome; IDA:FlyBase.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IDA:FlyBase.
GO; GO:0000791; C:euchromatin; IDA:FlyBase.
GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
GO; GO:0005720; C:nuclear heterochromatin; IDA:FlyBase.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005721; C:pericentric heterochromatin; IDA:FlyBase.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0005704; C:polytene chromosome band; IDA:FlyBase.
GO; GO:0005701; C:polytene chromosome chromocenter; IDA:FlyBase.
GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
GO; GO:0035012; C:polytene chromosome, telomeric region; IDA:FlyBase.
GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
GO; GO:0042393; F:histone binding; NAS:FlyBase.
GO; GO:0030544; F:Hsp70 protein binding; IDA:CAFA.
GO; GO:0035064; F:methylated histone binding; TAS:FlyBase.
GO; GO:0003729; F:mRNA binding; NAS:FlyBase.
GO; GO:0030674; F:protein binding, bridging; IDA:CAFA.
GO; GO:0044877; F:protein-containing complex binding; IDA:CAFA.
GO; GO:0000182; F:rDNA binding; IDA:FlyBase.
GO; GO:0003723; F:RNA binding; IDA:FlyBase.
GO; GO:0070063; F:RNA polymerase binding; IDA:CAFA.
GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IDA:CAFA.
GO; GO:0003696; F:satellite DNA binding; IDA:FlyBase.
GO; GO:0006342; P:chromatin silencing; HMP:FlyBase.
GO; GO:0030702; P:chromatin silencing at centromere; HMP:FlyBase.
GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
GO; GO:0006343; P:establishment of chromatin silencing; IMP:FlyBase.
GO; GO:0016458; P:gene silencing; IDA:FlyBase.
GO; GO:0031507; P:heterochromatin assembly; IDA:FlyBase.
GO; GO:0034773; P:histone H4-K20 trimethylation; IMP:FlyBase.
GO; GO:0000278; P:mitotic cell cycle; IDA:CACAO.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:FlyBase.
GO; GO:0033697; P:positive regulation of extent of heterochromatin assembly; IMP:FlyBase.
GO; GO:1905646; P:positive regulation of FACT complex assembly; IDA:CAFA.
GO; GO:1900111; P:positive regulation of histone H3-K9 dimethylation; IDA:FlyBase.
GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; IMP:FlyBase.
GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:CAFA.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:FlyBase.
GO; GO:1905632; P:protein localization to euchromatin; IDA:CAFA.
GO; GO:0042981; P:regulation of apoptotic process; IMP:FlyBase.
GO; GO:0031060; P:regulation of histone methylation; IMP:FlyBase.
GO; GO:1905634; P:regulation of protein localization to chromatin; IMP:CAFA.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
GO; GO:0000723; P:telomere maintenance; IMP:FlyBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00024; CHROMO; 1.
InterPro; IPR016197; Chromo-like_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR017984; Chromo_dom_subgr.
InterPro; IPR023780; Chromo_domain.
InterPro; IPR008251; Chromo_shadow_dom.
InterPro; IPR023779; Chromodomain_CS.
Pfam; PF00385; Chromo; 1.
Pfam; PF01393; Chromo_shadow; 1.
PRINTS; PR00504; CHROMODOMAIN.
SMART; SM00298; CHROMO; 2.
SMART; SM00300; ChSh; 1.
SUPFAM; SSF54160; SSF54160; 2.
PROSITE; PS00598; CHROMO_1; 1.
PROSITE; PS50013; CHROMO_2; 2.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Chromosome; Complete proteome;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation.
CHAIN 1 206 Heterochromatin protein 1.
/FTId=PRO_0000080197.
DOMAIN 24 82 Chromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
DOMAIN 147 205 Chromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
REGION 95 206 Binds to Su(var)39.
COMPBIAS 18 23 Poly-Glu.
BINDING 24 24 Histone H3K9me2.
BINDING 45 45 Histone H3K9me2.
BINDING 48 48 Histone H3K9me2.
MOD_RES 11 11 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000269|PubMed:17372656,
ECO:0000269|PubMed:18327897}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 127 127 Phosphothreonine.
{ECO:0000269|PubMed:17372656}.
MOD_RES 128 128 Phosphothreonine.
{ECO:0000269|PubMed:17372656,
ECO:0000269|PubMed:18327897}.
MOD_RES 134 134 Phosphothreonine.
{ECO:0000269|PubMed:17372656}.
VARIANT 105 105 T -> A (in strain: NC322, NC358 and
NC359). {ECO:0000269|PubMed:18984573}.
VARIANT 126 126 R -> C (in strain: NC390).
{ECO:0000269|PubMed:18984573}.
VARIANT 134 134 T -> S (in strain: MW25).
{ECO:0000269|PubMed:18984573}.
MUTAGEN 26 26 V->M: Impairs chromo domain folding and
histone H3 binding. Does not affect piwi
binding. {ECO:0000269|PubMed:11566886,
ECO:0000269|PubMed:17875665}.
MUTAGEN 191 191 I->E: Abolishes piwi binding.
{ECO:0000269|PubMed:17875665}.
MUTAGEN 200 200 W->A: Abolishes piwi binding.
{ECO:0000269|PubMed:17875665}.
STRAND 23 35 {ECO:0000244|PDB:6AT0}.
STRAND 38 45 {ECO:0000244|PDB:6AT0}.
HELIX 50 52 {ECO:0000244|PDB:6AT0}.
STRAND 54 57 {ECO:0000244|PDB:6AT0}.
HELIX 58 60 {ECO:0000244|PDB:6AT0}.
HELIX 64 73 {ECO:0000244|PDB:6AT0}.
TURN 142 146 {ECO:0000244|PDB:3P7J}.
STRAND 149 158 {ECO:0000244|PDB:3P7J}.
STRAND 161 168 {ECO:0000244|PDB:3P7J}.
STRAND 175 178 {ECO:0000244|PDB:3P7J}.
HELIX 179 185 {ECO:0000244|PDB:3P7J}.
HELIX 187 196 {ECO:0000244|PDB:3P7J}.
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


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