HP1_DROME - dbPTM
HP1_DROME - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
10PhosphorylationKKIDNPESSAKVSDA
CCCCCHHHCCCCCCH
36.5319429919
11PhosphorylationKIDNPESSAKVSDAE
CCCCHHHCCCCCCHH
30.3719429919
15PhosphorylationPESSAKVSDAEEEEE
HHHCCCCCCHHHHHH
30.3221082442
24PhosphorylationAEEEEEEYAVEKIID
HHHHHHHHHHHHHHH
21.1625749252
38AcetylationDRRVRKGKVEYYLKW
HHHHHCCCCEEEEEE
34.6221791702
89PhosphorylationASKKDRPSSSAKAKE
HHCCCCCCCHHHHHH
37.5129892262
90PhosphorylationSKKDRPSSSAKAKET
HCCCCCCCHHHHHHH
36.6829892262
102PhosphorylationKETQGRASSSTSTAS
HHHCCCCCCCCCCHH
24.3825749252
103PhosphorylationETQGRASSSTSTASK
HHCCCCCCCCCCHHH
36.3322817900
106PhosphorylationGRASSSTSTASKRKS
CCCCCCCCCHHHHCC
24.7527794539
109PhosphorylationSSSTSTASKRKSEEP
CCCCCCHHHHCCCCC
32.8427794539
113PhosphorylationSTASKRKSEEPTAPS
CCHHHHCCCCCCCCC
51.7521082442
117PhosphorylationKRKSEEPTAPSGNKS
HHCCCCCCCCCCCCC
55.2519429919
120PhosphorylationSEEPTAPSGNKSKRT
CCCCCCCCCCCCCCC
53.1619429919
124PhosphorylationTAPSGNKSKRTTDAE
CCCCCCCCCCCCCCC
31.2219429919
127PhosphorylationSGNKSKRTTDAEQDT
CCCCCCCCCCCCCCC
32.5319429919
128PhosphorylationGNKSKRTTDAEQDTI
CCCCCCCCCCCCCCC
36.9319429919
134PhosphorylationTTDAEQDTIPVSGST
CCCCCCCCCCCCCCC
27.2018984573
199PhosphorylationHFYEERLSWYSDNED
EHHHHHHHHCCCCCC
30.1420450229
202PhosphorylationEERLSWYSDNED---
HHHHHHCCCCCC---
27.9219429919

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HP1_DROME !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MMD4_DROMEmod(mdg4)genetic
8248257
SSRP1_DROMESsrpphysical
20889714
SPT16_DROMEdre4physical
20889714
SMCA4_HUMANSMARCA4physical
20011120
KDM4A_DROMEKdm4Aphysical
19061644
STAT_DROMEStat92Ephysical
18344984
SETB1_DROMEegggenetic
19487560
NIPB_DROMENipped-Bphysical
24990964
HP1_DROMESu(var)205physical
11566886
HP1_DROMESu(var)205physical
21472955
HP1_DROMESu(var)205physical
23793104
BOREA_DROMEborrphysical
24990964
PIWI_DROMEpiwiphysical
17875665
PIWI_DROMEpiwiphysical
21472955
PIWI_DROMEpiwiphysical
23793104
ORC5_DROMEOrc5physical
9363940
MCM10_DROMEMcm10physical
20498296
KDM4A_DROMEKdm4Aphysical
24990964
ORC6_DROMEOrc6physical
9363940
SETB1_DROMEeggphysical
24990964
EZ_DROMEE(z)physical
25954320
LSDA_DROMESu(var)3-3physical
24990964
PC_DROMEPcphysical
25954320
SLE_DROMEslephysical
24990964
SUV39_DROMESu(var)3-9physical
24990964
SUV39_DROMESu(var)3-9physical
11867540
SUV39_DROMESu(var)3-9physical
23559249
ORC2_DROMEOrc2physical
9363940
SCC4_DROMECG4203physical
24990964
STAT_DROMEStat92Ephysical
25177369
CAV_DROMEcavphysical
11408576
CAV_DROMEcavphysical
12376620
CAV_DROMEcavphysical
12826664
CAV_DROMEcavphysical
19181850
CAV_DROMEcavphysical
26566042
ATRX_DROMEXNPphysical
24990964
H2AV_DROMEHis2Avphysical
25591068
MES4_DROMEMes-4physical
24990964
SUUR_DROMESuURphysical
24990964
SUUR_DROMESuURphysical
18445687
SUZ12_DROMESu(z)12physical
25954320

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HP1_DROME

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

TOP