GPRK2_DROME - dbPTM
GPRK2_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPRK2_DROME
UniProt AC P32866
Protein Name G protein-coupled receptor kinase 2
Gene Name Gprk2
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 714
Subcellular Localization Membrane . Associated with nurse cell and oocyte plasma membranes during much of oogenesis.
Protein Description Specifically phosphorylates the activated forms of G protein-coupled receptors (By similarity). Required during oogenesis and embryogenesis; component of a signaling pathway that functions during egg chamber maturation..
Protein Sequence MELENIVANTVYLKAREGGSDSNKGKSKKWRKILQFPHISQCINLKDKLDISYGYVIDQQPIGRELFRLFCENKRPVYFRYITFLDEVVKYEIEYISNRIFIGHDIGRRFLDVEAQLELRNGSGGDALDAETQEELLLNSSNANPTETAETEHCNNTTANNCNNINNSNNSQHSSDINHKKLDTRNHNGDDATGNGSSHQDDGDESVKCQEGHDDAEKGGGGEGGGGGKCVPVGGYPDELVLDVLNDDLIAQVRNKLNSGGKDIFAQCVNAVKAFLAGEPFREFESSMYFHRYLQWKWLEAQPITYKTFRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLTIMNGGDLKFHIYNMGGEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVRGRVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQLLAKSIKQRLGCRNGRMGGQDVMAHPFFHSTQLNWRRLEAGMLEPPFVPDPHAVYAKDVLDIEQFSTVKGVNIDESDTNFYTKFNTGSVSISWQNEMMETECFRELNVFGPEECPTPDLQINAAPEPDKAGCFPFRRKKKQPARTQPIPIPEHLLTTSHSVSSTTVES
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
193PhosphorylationNHNGDDATGNGSSHQ
CCCCCCCCCCCCCCC
37.8719429919
197PhosphorylationDDATGNGSSHQDDGD
CCCCCCCCCCCCCCC
28.7519429919
198PhosphorylationDATGNGSSHQDDGDE
CCCCCCCCCCCCCCC
26.9419429919
612PhosphorylationVLDIEQFSTVKGVNI
CCCHHHCEECCCCCC
31.8019429919
613PhosphorylationLDIEQFSTVKGVNID
CCHHHCEECCCCCCC
27.7628490779
702PhosphorylationPIPEHLLTTSHSVSS
CCCHHHHCCCCCCCC
32.3919429919
703PhosphorylationIPEHLLTTSHSVSST
CCHHHHCCCCCCCCC
25.1419429919
704PhosphorylationPEHLLTTSHSVSSTT
CHHHHCCCCCCCCCC
14.4519429919
706PhosphorylationHLLTTSHSVSSTTVE
HHHCCCCCCCCCCCC
24.3819429919
708PhosphorylationLTTSHSVSSTTVES-
HCCCCCCCCCCCCC-
25.6119429919
709PhosphorylationTTSHSVSSTTVES--
CCCCCCCCCCCCC--
26.4119429919
710PhosphorylationTSHSVSSTTVES---
CCCCCCCCCCCC---
27.6219429919
711PhosphorylationSHSVSSTTVES----
CCCCCCCCCCC----
24.9919429919
714PhosphorylationVSSTTVES-------
CCCCCCCC-------
40.9819429919

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 GPRK2_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPRK2_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 GPRK2_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDE4B_DROMEdncgenetic
11319866
PDE4E_DROMEdncgenetic
11319866
PDE4C_DROMEdncgenetic
11319866
PDE4A_DROMEdncgenetic
11319866
FOG_DROMEfoggenetic
24026125
SMO_DROMEsmogenetic
17483466
KAPC_DROMEPka-C1genetic
22096079
CACT_DROMEcactphysical
20421637
GPRK2_DROMEGprk2physical
20844016

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPRK2_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-612 AND THR-613, ANDMASS SPECTROMETRY.

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