Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heterochromatin protein 1

Gene

Su(var)205

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241Histone H3K9me2
Binding sitei45 – 451Histone H3K9me2
Binding sitei48 – 481Histone H3K9me2

GO - Molecular functioni

  • chromatin binding Source: FlyBase
  • histone binding Source: FlyBase
  • methylated histone binding Source: FlyBase
  • mRNA binding Source: FlyBase
  • rDNA binding Source: FlyBase
  • RNA binding Source: FlyBase
  • satellite DNA binding Source: FlyBase

GO - Biological processi

  • chromatin silencing Source: FlyBase
  • chromatin silencing at centromere Source: FlyBase
  • chromosome organization Source: FlyBase
  • DNA hypermethylation Source: FlyBase
  • establishment of chromatin silencing Source: FlyBase
  • gene silencing Source: FlyBase
  • heterochromatin assembly Source: FlyBase
  • histone H4-K20 trimethylation Source: FlyBase
  • mitotic nuclear division Source: CACAO
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • neurogenesis Source: FlyBase
  • positive regulation of extent of heterochromatin assembly Source: FlyBase
  • positive regulation of histone H3-K9 dimethylation Source: FlyBase
  • positive regulation of methylation-dependent chromatin silencing Source: FlyBase
  • positive regulation of transcription, DNA-templated Source: FlyBase
  • regulation of apoptotic process Source: FlyBase
  • regulation of histone methylation Source: FlyBase
  • regulation of transcription, DNA-templated Source: FlyBase
  • telomere maintenance Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-DME-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP05205.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterochromatin protein 1
Short name:
HP1
Alternative name(s):
Non-histone chromosomal protein C1A9 antigen
Gene namesi
Name:Su(var)205
Synonyms:HP1
ORF Names:CG8409
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0003607. Su(var)205.

Subcellular locationi

  • Nucleusnucleoplasm 1 Publication

  • Note: Colocalizes with Arp6 on centric heterochromatin.

GO - Cellular componenti

  • chromosome Source: FlyBase
  • chromosome, centromeric region Source: FlyBase
  • chromosome, telomeric region Source: FlyBase
  • condensed chromosome Source: FlyBase
  • condensed nuclear chromosome, centromeric region Source: FlyBase
  • euchromatin Source: FlyBase
  • heterochromatin Source: FlyBase
  • nuclear heterochromatin Source: FlyBase
  • nucleoplasm Source: UniProtKB-SubCell
  • nucleus Source: FlyBase
  • pericentric heterochromatin Source: FlyBase
  • polytene chromosome Source: FlyBase
  • polytene chromosome, telomeric region Source: FlyBase
  • polytene chromosome band Source: FlyBase
  • polytene chromosome chromocenter Source: FlyBase
  • polytene chromosome puff Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101S → A: 3-fold lower H3 binding affinity. 1 Publication
Mutagenesisi26 – 261V → M: Abolishes H3 binding. Does not affect piwi binding. 2 Publications
Mutagenesisi191 – 1911I → E: Abolishes piwi binding. 1 Publication
Mutagenesisi200 – 2001W → A: Abolishes piwi binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 206206Heterochromatin protein 1PRO_0000080197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111Phosphoserine1 Publication
Modified residuei15 – 151Phosphoserine2 Publications
Modified residuei102 – 1021Phosphoserine1 Publication
Modified residuei103 – 1031Phosphoserine1 Publication
Modified residuei113 – 1131Phosphoserine1 Publication
Modified residuei127 – 1271Phosphothreonine1 Publication
Modified residuei128 – 1281Phosphothreonine2 Publications
Modified residuei134 – 1341Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP05205.

PTM databases

iPTMnetiP05205.

Expressioni

Gene expression databases

BgeeiP05205.
GenevisibleiP05205. DM.

Interactioni

Subunit structurei

Homodimer; probably associates with Su(var)3-9. Interacts with Mcm10. Interacts (via chromoshadow domain) with piwi (via N-terminal region).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Atf-2-RBQ9W0Z53EBI-155532,EBI-94769
cavQ95RV24EBI-155532,EBI-104820
His3:CG33854P022993EBI-155532,EBI-522090
Mcm10Q9VIE62EBI-155532,EBI-91264

GO - Molecular functioni

  • histone binding Source: FlyBase
  • methylated histone binding Source: FlyBase

Protein-protein interaction databases

BioGridi60248. 34 interactions.
DIPiDIP-21869N.
IntActiP05205. 29 interactions.
MINTiMINT-271388.
STRINGi7227.FBpp0079251.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 3512Combined sources
Beta strandi38 – 458Combined sources
Helixi50 – 523Combined sources
Beta strandi54 – 574Combined sources
Helixi58 – 603Combined sources
Helixi64 – 7310Combined sources
Turni142 – 1465Combined sources
Beta strandi149 – 15810Combined sources
Beta strandi161 – 1688Combined sources
Beta strandi175 – 1784Combined sources
Helixi179 – 1857Combined sources
Helixi187 – 19610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KNAX-ray2.10A17-76[»]
1KNEX-ray2.40A17-76[»]
1Q3LX-ray1.64A17-76[»]
3P7JX-ray2.30A/B131-206[»]
ProteinModelPortaliP05205.
SMRiP05205. Positions 23-74, 141-201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05205.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 8259Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini147 – 20559Chromo 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 206112Binds to Su(var)39Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 236Poly-Glu

Sequence similaritiesi

Contains 2 chromo domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1911. Eukaryota.
ENOG4111JKD. LUCA.
GeneTreeiENSGT00510000046310.
InParanoidiP05205.
KOiK11587.
OMAiHFYEERL.
OrthoDBiEOG7QRQWW.
PhylomeDBiP05205.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 2 hits.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05205-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKIDNPES SAKVSDAEEE EEEYAVEKII DRRVRKGKVE YYLKWKGYPE
60 70 80 90 100
TENTWEPENN LDCQDLIQQY EASRKDEEKS AASKKDRPSS SAKAKETQGR
110 120 130 140 150
ASSSTSTASK RKSEEPTAPS GNKSKRTTDA EQDTIPVSGS TGFDRGLEAE
160 170 180 190 200
KILGASDNNG RLTFLIQFKG VDQAEMVPSS VANEKIPRMV IHFYEERLSW

YSDNED
Length:206
Mass (Da):23,185
Last modified:November 1, 1995 - v2
Checksum:i6A5B204C487526B7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051T → A in strain: NC322, NC358 and NC359. 1 Publication
Natural varianti126 – 1261R → C in strain: NC390. 1 Publication
Natural varianti134 – 1341T → S in strain: MW25. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57574 Genomic DNA. Translation: AAA28620.1.
M14131 mRNA. Translation: AAA28402.1. Sequence problems.
FJ218607 Genomic DNA. Translation: ACI96755.1.
FJ218612 Genomic DNA. Translation: ACI96760.1.
FJ218613 Genomic DNA. Translation: ACI96761.1.
FJ218614 Genomic DNA. Translation: ACI96762.1.
FJ218615 Genomic DNA. Translation: ACI96763.1.
FJ218616 Genomic DNA. Translation: ACI96764.1.
FJ218617 Genomic DNA. Translation: ACI96765.1.
FJ218618 Genomic DNA. Translation: ACI96766.1.
FJ218619 Genomic DNA. Translation: ACI96767.1.
FJ218620 Genomic DNA. Translation: ACI96768.1.
FJ218621 Genomic DNA. Translation: ACI96769.1.
FJ218622 Genomic DNA. Translation: ACI96770.1.
FJ218623 Genomic DNA. Translation: ACI96771.1.
FJ218624 Genomic DNA. Translation: ACI96772.1.
FJ218625 Genomic DNA. Translation: ACI96773.1.
FJ218626 Genomic DNA. Translation: ACI96774.1.
FJ218627 Genomic DNA. Translation: ACI96775.1.
FJ218628 Genomic DNA. Translation: ACI96776.1.
FJ218629 Genomic DNA. Translation: ACI96777.1.
FJ218630 Genomic DNA. Translation: ACI96778.1.
FJ218631 Genomic DNA. Translation: ACI96779.1.
FJ218632 Genomic DNA. Translation: ACI96780.1.
FJ218633 Genomic DNA. Translation: ACI96781.1.
FJ218634 Genomic DNA. Translation: ACI96782.1.
FJ218635 Genomic DNA. Translation: ACI96783.1.
FJ218636 Genomic DNA. Translation: ACI96784.1.
FJ218637 Genomic DNA. Translation: ACI96785.1.
FJ218638 Genomic DNA. Translation: ACI96786.1.
FJ218639 Genomic DNA. Translation: ACI96787.1.
AE014134 Genomic DNA. Translation: AAF52618.1.
AE014134 Genomic DNA. Translation: AAN11156.1.
AY061119 mRNA. Translation: AAL28667.1.
PIRiA39268.
RefSeqiNP_476755.1. NM_057407.4.
NP_723361.1. NM_164799.2.
UniGeneiDm.3713.

Genome annotation databases

EnsemblMetazoaiFBtr0079635; FBpp0079251; FBgn0003607.
FBtr0079636; FBpp0079252; FBgn0003607.
GeneIDi34119.
KEGGidme:Dmel_CG8409.
UCSCiCG8409-RB. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57574 Genomic DNA. Translation: AAA28620.1.
M14131 mRNA. Translation: AAA28402.1. Sequence problems.
FJ218607 Genomic DNA. Translation: ACI96755.1.
FJ218612 Genomic DNA. Translation: ACI96760.1.
FJ218613 Genomic DNA. Translation: ACI96761.1.
FJ218614 Genomic DNA. Translation: ACI96762.1.
FJ218615 Genomic DNA. Translation: ACI96763.1.
FJ218616 Genomic DNA. Translation: ACI96764.1.
FJ218617 Genomic DNA. Translation: ACI96765.1.
FJ218618 Genomic DNA. Translation: ACI96766.1.
FJ218619 Genomic DNA. Translation: ACI96767.1.
FJ218620 Genomic DNA. Translation: ACI96768.1.
FJ218621 Genomic DNA. Translation: ACI96769.1.
FJ218622 Genomic DNA. Translation: ACI96770.1.
FJ218623 Genomic DNA. Translation: ACI96771.1.
FJ218624 Genomic DNA. Translation: ACI96772.1.
FJ218625 Genomic DNA. Translation: ACI96773.1.
FJ218626 Genomic DNA. Translation: ACI96774.1.
FJ218627 Genomic DNA. Translation: ACI96775.1.
FJ218628 Genomic DNA. Translation: ACI96776.1.
FJ218629 Genomic DNA. Translation: ACI96777.1.
FJ218630 Genomic DNA. Translation: ACI96778.1.
FJ218631 Genomic DNA. Translation: ACI96779.1.
FJ218632 Genomic DNA. Translation: ACI96780.1.
FJ218633 Genomic DNA. Translation: ACI96781.1.
FJ218634 Genomic DNA. Translation: ACI96782.1.
FJ218635 Genomic DNA. Translation: ACI96783.1.
FJ218636 Genomic DNA. Translation: ACI96784.1.
FJ218637 Genomic DNA. Translation: ACI96785.1.
FJ218638 Genomic DNA. Translation: ACI96786.1.
FJ218639 Genomic DNA. Translation: ACI96787.1.
AE014134 Genomic DNA. Translation: AAF52618.1.
AE014134 Genomic DNA. Translation: AAN11156.1.
AY061119 mRNA. Translation: AAL28667.1.
PIRiA39268.
RefSeqiNP_476755.1. NM_057407.4.
NP_723361.1. NM_164799.2.
UniGeneiDm.3713.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KNAX-ray2.10A17-76[»]
1KNEX-ray2.40A17-76[»]
1Q3LX-ray1.64A17-76[»]
3P7JX-ray2.30A/B131-206[»]
ProteinModelPortaliP05205.
SMRiP05205. Positions 23-74, 141-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60248. 34 interactions.
DIPiDIP-21869N.
IntActiP05205. 29 interactions.
MINTiMINT-271388.
STRINGi7227.FBpp0079251.

PTM databases

iPTMnetiP05205.

Proteomic databases

PaxDbiP05205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079635; FBpp0079251; FBgn0003607.
FBtr0079636; FBpp0079252; FBgn0003607.
GeneIDi34119.
KEGGidme:Dmel_CG8409.
UCSCiCG8409-RB. d. melanogaster.

Organism-specific databases

CTDi34119.
FlyBaseiFBgn0003607. Su(var)205.

Phylogenomic databases

eggNOGiKOG1911. Eukaryota.
ENOG4111JKD. LUCA.
GeneTreeiENSGT00510000046310.
InParanoidiP05205.
KOiK11587.
OMAiHFYEERL.
OrthoDBiEOG7QRQWW.
PhylomeDBiP05205.

Enzyme and pathway databases

ReactomeiR-DME-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP05205.

Miscellaneous databases

EvolutionaryTraceiP05205.
GenomeRNAii34119.
PROiP05205.

Gene expression databases

BgeeiP05205.
GenevisibleiP05205. DM.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 2 hits.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a nonhistone chromosomal protein associated with heterochromatin in Drosophila melanogaster and its gene."
    James T.C., Elgin S.C.R.
    Mol. Cell. Biol. 6:3862-3872(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Mutation in a heterochromatin-specific chromosomal protein is associated with suppression of position-effect variegation in Drosophila melanogaster."
    Eissenberg J.C., James T.C., Forster-Hartnett D.W., Hartnett T., Ngan V., Elgin S.C.R.
    Proc. Natl. Acad. Sci. U.S.A. 87:9923-9927(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
  3. "Molecular population genetics and evolution of Drosophila meiosis genes."
    Anderson J.A., Gilliland W.D., Langley C.H.
    Genetics 181:177-185(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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.
  4. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  7. "A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants."
    Singh P.B., Miller J.R., Pearce J., Kothary R., Burton R.D., Paro R., James T.C., Gaunt S.J.
    Nucleic Acids Res. 19:789-794(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN CHROMO.
  8. "An actin-related protein in Drosophila colocalizes with heterochromatin protein 1 in pericentric heterochromatin."
    Frankel S., Sigel E.A., Craig C., Elgin S.C., Mooseker M.S., Artavanis-Tsakonas S.
    J. Cell Sci. 110:1999-2012(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3."
    Jacobs S.A., Taverna S.D., Zhang Y., Briggs S.D., Li J., Eissenberg J.C., Allis C.D., Khorasanizadeh S.
    EMBO J. 20:5232-5241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: QUATERNARY STRUCTURE, MUTAGENESIS OF SER-10 AND VAL-26.
  10. "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing."
    Schotta G., Ebert A., Krauss V., Fischer A., Hoffmann J., Rea S., Jenuwein T., Dorn R., Reuter G.
    EMBO J. 21:1121-1131(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SU(VAR)39.
  11. "Drosophila MCM10 interacts with members of the prereplication complex and is required for proper chromosome condensation."
    Christensen T.W., Tye B.K.
    Mol. Biol. Cell 14:2206-2215(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MCM10.
  12. "Drosophila PIWI associates with chromatin and interacts directly with HP1a."
    Brower-Toland B., Findley S.D., Jiang L., Liu L., Yin H., Dus M., Zhou P., Elgin S.C., Lin H.
    Genes Dev. 21:2300-2311(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIWI, MUTAGENESIS OF VAL-26; ILE-191 AND TRP-200.
  13. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-127; THR-128 AND THR-134, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15; SER-102; SER-103; SER-113 AND THR-128, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  15. "Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail."
    Jacobs S.A., Khorasanizadeh S.
    Science 295:2080-2083(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 17-76.

Entry informationi

Entry nameiHP1_DROME
AccessioniPrimary (citable) accession number: P05205
Secondary accession number(s): A4V0F1
, B6UVR4, B6UVS1, B6UVS2, B6UVS3, B6UVT2, B6UVT6, B6UVT7, Q9VLR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 169 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.