RLIP_DROME - dbPTM
RLIP_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RLIP_DROME
UniProt AC Q9VDG2
Protein Name RalA-binding protein 1
Gene Name Rlip {ECO:0000312|EMBL:AAF55832.1}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 625
Subcellular Localization
Protein Description Participates in receptor endocytosis during interphase, is also involved in mitotic processes when endocytosis is switched off..
Protein Sequence MDFDSPEEKEFPGLYASEAADAKSRKSKEESDFSEDHDHSKKDLLIGRRKDKKEKGKDRGYAALEGESSPEEELDTKSPSKSKKSKTFKFTSSKSKEKREKSRDKSEKDSKHAEEEPSVSHKVKEKERDKEKDRDEPKKKDKEEKRKEKDKKADKKDKKDKKSKQLSQQQDDVSAAEEVLALGYPVFGVSVSLATERSRCHDGVDIPLVVRDCIDFLQDHLKCEQIYKIEPIKTRLMHFKRLYNNREHDSAVDELNLPTACSLLKLFLRELPEPLLTTDLVARFEEVASHPKVTTQQAELQQLLEQLPKCNRTLLAWVLLHFDAVIQQERHNKLNAQSLAMLLSPTLQMSHRLMVALLCHCNNLFADVQLIKYVPPLTSTSPKLPDTPEDIQTELRKQDSLLSQIHSEMNAGFITKKREEQLWEVQRIITQLKRKLRTFEKKQEKTAEEVDNSSSAPPAVASEDTTDSKPAGTPAVSTNNSISQEEPKTDTLTPKDAPNDFTIDPSTGFILLPKSNPHRENLLRLQIEYDELMEWQNELKARIVAERNEVYRLKQLYEQQSINSQMASLASGSQAPPESDYERIIEHYTRENALLEHKKNMLGMELKEERRACIALQVELRLQQF
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
5Phosphorylation---MDFDSPEEKEFP
---CCCCCHHHHCCC
33.9227794539
27PhosphorylationADAKSRKSKEESDFS
HHHHHHCCHHHCCCC
44.1619429919
31PhosphorylationSRKSKEESDFSEDHD
HHCCHHHCCCCCCCC
45.0819429919
34PhosphorylationSKEESDFSEDHDHSK
CHHHCCCCCCCCCCH
47.2919429919
40PhosphorylationFSEDHDHSKKDLLIG
CCCCCCCCHHHHHHC
47.6719429919
61PhosphorylationEKGKDRGYAALEGES
HHCCCCCCHHHCCCC
6.9219429919
68PhosphorylationYAALEGESSPEEELD
CHHHCCCCCCHHHCC
63.1519429919
69PhosphorylationAALEGESSPEEELDT
HHHCCCCCCHHHCCC
31.8421082442
76PhosphorylationSPEEELDTKSPSKSK
CCHHHCCCCCCCCCC
46.1519429919
78PhosphorylationEEELDTKSPSKSKKS
HHHCCCCCCCCCCCC
36.1819429919
80PhosphorylationELDTKSPSKSKKSKT
HCCCCCCCCCCCCCC
57.5619429919
430PhosphorylationWEVQRIITQLKRKLR
HHHHHHHHHHHHHHH
26.0222817900

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 RLIP_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RLIP_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 RLIP_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RALA_DROMERalaphysical
14605208
RL4_DROMERpL4physical
15710747
SIMA_DROMEsimaphysical
15710747
CCNB_DROMECycBphysical
12775724

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RLIP_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-68 AND SER-69, AND MASSSPECTROMETRY.

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