1433E_DROME - dbPTM
1433E_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 1433E_DROME
UniProt AC P92177
Protein Name 14-3-3 protein epsilon
Gene Name 14-3-3epsilon
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 262
Subcellular Localization
Protein Description Positively regulates Ras-mediated pathways. Acts downstream or parallel to Raf, but upstream of nuclear factors in Ras signaling. Three mutants have been isolated, that suppress the rough eye phenotype caused by mutated Ras1 (sev-Ras1 v12). Inhibits yki activity by restricting its nuclear localization..
Protein Sequence MTERENNVYKAKLAEQAERYDEMVEAMKKVASMDVELTVEERNLLSVAYKNVIGARRASWRIITSIEQKEENKGAEEKLEMIKTYRGQVEKELRDICSDILNVLEKHLIPCATSGESKVFYYKMKGDYHRYLAEFATGSDRKDAAENSLIAYKAASDIAMNDLPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQAEEVDPNAGDGEPKEQIQDVEDQDVS
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
46PhosphorylationVEERNLLSVAYKNVI
HHHHHHHHHHHHHHH
14.1022668510
49PhosphorylationRNLLSVAYKNVIGAR
HHHHHHHHHHHHHHH
10.8419429919
69AcetylationIITSIEQKEENKGAE
EEEEHHHHHHCCCHH
54.9621791702
78AcetylationENKGAEEKLEMIKTY
HCCCHHHHHHHHHHH
41.0521791702
83AcetylationEEKLEMIKTYRGQVE
HHHHHHHHHHHHHHH
37.8921791702
91AcetylationTYRGQVEKELRDICS
HHHHHHHHHHHHHHH
64.2921791702
139PhosphorylationLAEFATGSDRKDAAE
HHHHHCCCCHHHHHH
29.8622817900
208PhosphorylationDAIAELDTLSEESYK
HHHHHHHCCCHHHCC
44.8229892262
210PhosphorylationIAELDTLSEESYKDS
HHHHHCCCHHHCCCH
41.2219429919
213PhosphorylationLDTLSEESYKDSTLI
HHCCCHHHCCCHHHH
33.1719429919
262PhosphorylationDVEDQDVS-------
CCCCCCCC-------
42.6719429919

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 1433E_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 1433E_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 1433E_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SH3BG_DROMESh3betaphysical
22036573
TNG2_DROMETango2physical
22036573
RS27A_DROMERpS27Aphysical
24292889
ITA1_DROMEmewgenetic
22500634
ITA2_DROMEifgenetic
22500634
1433Z_DROME14-3-3zetagenetic
12431373
1433Z_DROME14-3-3zetagenetic
17660572
RAS2_DROMERas64Bgenetic
22500634
FOXO_DROMEfoxogenetic
18665908
RHEB_DROMERhebphysical
27151460
YAP1_DROMEykiphysical
26887950
NDE1_DROMEnudEphysical
23987511
TCTP_DROMETctpphysical
27151460

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 1433E_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-262, AND MASSSPECTROMETRY.

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