UniProt ID | HP1_DROME | |
---|---|---|
UniProt AC | P05205 | |
Protein Name | Heterochromatin protein 1 | |
Gene Name | Su(var)205 | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 206 | |
Subcellular Localization | Nucleus, nucleoplasm . Chromosome . Colocalizes with Arp6 on centric heterochromatin. | |
Protein Description | 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.. | |
Protein Sequence | MGKKIDNPESSAKVSDAEEEEEEYAVEKIIDRRVRKGKVEYYLKWKGYPETENTWEPENNLDCQDLIQQYEASRKDEEKSAASKKDRPSSSAKAKETQGRASSSTSTASKRKSEEPTAPSGNKSKRTTDAEQDTIPVSGSTGFDRGLEAEKILGASDNNGRLTFLIQFKGVDQAEMVPSSVANEKIPRMVIHFYEERLSWYSDNED | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
10 | Phosphorylation | KKIDNPESSAKVSDA CCCCCHHHCCCCCCH | 36.53 | 19429919 | |
11 | Phosphorylation | KIDNPESSAKVSDAE CCCCHHHCCCCCCHH | 30.37 | 19429919 | |
15 | Phosphorylation | PESSAKVSDAEEEEE HHHCCCCCCHHHHHH | 30.32 | 21082442 | |
24 | Phosphorylation | AEEEEEEYAVEKIID HHHHHHHHHHHHHHH | 21.16 | 25749252 | |
38 | Acetylation | DRRVRKGKVEYYLKW HHHHHCCCCEEEEEE | 34.62 | 21791702 | |
89 | Phosphorylation | ASKKDRPSSSAKAKE HHCCCCCCCHHHHHH | 37.51 | 29892262 | |
90 | Phosphorylation | SKKDRPSSSAKAKET HCCCCCCCHHHHHHH | 36.68 | 29892262 | |
102 | Phosphorylation | KETQGRASSSTSTAS HHHCCCCCCCCCCHH | 24.38 | 25749252 | |
103 | Phosphorylation | ETQGRASSSTSTASK HHCCCCCCCCCCHHH | 36.33 | 22817900 | |
106 | Phosphorylation | GRASSSTSTASKRKS CCCCCCCCCHHHHCC | 24.75 | 27794539 | |
109 | Phosphorylation | SSSTSTASKRKSEEP CCCCCCHHHHCCCCC | 32.84 | 27794539 | |
113 | Phosphorylation | STASKRKSEEPTAPS CCHHHHCCCCCCCCC | 51.75 | 21082442 | |
117 | Phosphorylation | KRKSEEPTAPSGNKS HHCCCCCCCCCCCCC | 55.25 | 19429919 | |
120 | Phosphorylation | SEEPTAPSGNKSKRT CCCCCCCCCCCCCCC | 53.16 | 19429919 | |
124 | Phosphorylation | TAPSGNKSKRTTDAE CCCCCCCCCCCCCCC | 31.22 | 19429919 | |
127 | Phosphorylation | SGNKSKRTTDAEQDT CCCCCCCCCCCCCCC | 32.53 | 19429919 | |
128 | Phosphorylation | GNKSKRTTDAEQDTI CCCCCCCCCCCCCCC | 36.93 | 19429919 | |
134 | Phosphorylation | TTDAEQDTIPVSGST CCCCCCCCCCCCCCC | 27.20 | 18984573 | |
199 | Phosphorylation | HFYEERLSWYSDNED EHHHHHHHHCCCCCC | 30.14 | 20450229 | |
202 | Phosphorylation | EERLSWYSDNED--- HHHHHHCCCCCC--- | 27.92 | 19429919 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of HP1_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HP1_DROME !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of HP1_DROME !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15; SER-102;SER-103; SER-113 AND THR-128, AND MASS SPECTROMETRY. | |
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-127; THR-128 ANDTHR-134, AND MASS SPECTROMETRY. |