HSP27_DROME - dbPTM
HSP27_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP27_DROME
UniProt AC P02518
Protein Name Heat shock protein 27
Gene Name Hsp27
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 213
Subcellular Localization
Protein Description
Protein Sequence MSIIPLLHLARELDHDYRTDWGHLLEDDFGFGVHAHDLFHPRRLLLPNTLGLGRRRYSPYERSHGHHNQMSRRASGGPNALLPAVGKDGFQVCMDVSQFKPNELTVKVVDNTVVVEGKHEEREDGHGMIQRHFVRKYTLPKGFDPNEVVSTVSSDGVLTLKAPPPPSKEQAKSERIVQIQQTGPAHLSVKAPAPEAGDGKAENGSGEKMETSK
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
2Phosphorylation------MSIIPLLHL
------CCHHHHHHH
29.2623607784
49PhosphorylationRRLLLPNTLGLGRRR
HHHHCCCCCCCCCCC
21.9121082442
58PhosphorylationGLGRRRYSPYERSHG
CCCCCCCCCCCCCCC
21.1322817900
75PhosphorylationNQMSRRASGGPNALL
HHHHHHHCCCCCCCC
42.3321082442
205PhosphorylationDGKAENGSGEKMETS
CCCCCCCCCCCCCCC
56.1922817900

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 HSP27_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP27_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 HSP27_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED19_DROMEMED19physical
14605208
LIS1_DROMELis-1physical
14605208
TAD2B_DROMEAda2bphysical
14605208
REF2P_DROMEref(2)Pphysical
22036573
HSP68_DROMEHsp68physical
22036573
HSP72_DROMEHsp70Baphysical
22036573
QTRT2_DROMECG3434physical
22036573
TGT_DROMETgtphysical
22036573
RS27A_DROMERpS27Aphysical
24292889

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP27_DROME

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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-58, AND MASSSPECTROMETRY.
"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-75, AND MASSSPECTROMETRY.

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