RG68F_DROME - dbPTM
RG68F_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RG68F_DROME
UniProt AC Q9VTU3
Protein Name Rho GTPase-activating protein 68F
Gene Name RhoGAP68F
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 476
Subcellular Localization
Protein Description Functions as a GTPase-activating protein (GAP) for RhoA/Rho1 during gastrulation by converting it to an inactive GDP-bound state..
Protein Sequence MDAHSRFAPRLPGPAINPIVDNSDEPQPSLSDLHDFEPKLEFDDTELLAPSPLEKDVMVGDFVLAEDPELEPEEDVNPLEDDFEDQLREQSENFQTPRNKCDFLGTDKQGRHIFGIYASRFPEKSQLEGFVREIIKEIEPFVENDYILVYFHQGLKEDNKPSAQFLWNSYKELDRNFRKNLKTLYVVHPTWFIRVIWNFFSPFISDKFRKKLVYISSLDELRQALGLNKLKLPDNICDLDDKLNPSRKPSTPPPSSNINASRQQQHKMATTHQFGVPLKFIVMNSPCLNSIPPIVRKCVDSLSITGVIDTEGIFRRSGNHSEIMALKERVNRGEDVDLKSVNVHVIAGLLKSFLRDLAEPLLTFELYEDVTGFLDWPKEERSRNVTQLIREKLPEENYELFKYIVEFLVRVMDCEDLNKMTSSNLAIVFGPNFLWSRSTSTSLEEIAPINAFVDFVLQNHKDIYLIDVNQRTVSVD
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
29PhosphorylationNSDEPQPSLSDLHDF
CCCCCCCCHHHHHCC
34.9517372656
31PhosphorylationDEPQPSLSDLHDFEP
CCCCCCHHHHHCCCC
42.3322817900
51PhosphorylationDTELLAPSPLEKDVM
CCCCCCCCCCCCCCE
36.1919429919
250PhosphorylationLNPSRKPSTPPPSSN
CCCCCCCCCCCCCCC
57.4919429919
251PhosphorylationNPSRKPSTPPPSSNI
CCCCCCCCCCCCCCC
48.6319429919
255PhosphorylationKPSTPPPSSNINASR
CCCCCCCCCCCCHHH
41.6219429919
256PhosphorylationPSTPPPSSNINASRQ
CCCCCCCCCCCHHHH
47.7219429919
261PhosphorylationPSSNINASRQQQHKM
CCCCCCHHHHHHHHH
26.5719429919

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 RG68F_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RG68F_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 RG68F_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GUS_DROMEgusphysical
15575970
PP4C_DROMEPp4-19Cphysical
15575970
FRY_DROMEfryphysical
15575970
CP6A9_DROMECyp6a9physical
15575970
CEG1A_DROMECenG1Aphysical
15575970

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RG68F_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-29 AND SER-31, AND MASSSPECTROMETRY.
"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 THR-251, AND MASSSPECTROMETRY.

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