RLA0_DROME - dbPTM
RLA0_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RLA0_DROME
UniProt AC P19889
Protein Name 60S acidic ribosomal protein P0
Gene Name RpLP0
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 317
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Ribosomal protein P0 is the functional equivalent of E.coli protein L10..
Protein Sequence MVRENKAAWKAQYFIKVVELFDEFPKCFIVGADNVGSKQMQNIRTSLRGLAVVLMGKNTMMRKAIRGHLENNPQLEKLLPHIKGNVGFVFTKGDLAEVRDKLLESKVRAPARPGAIAPLHVIIPAQNTGLGPEKTSFFQALSIPTKISKGTIEIINDVPILKPGDKVGASEATLLNMLNISPFSYGLIVNQVYDSGSIFSPEILDIKPEDLRAKFQQGVANLAAVCLSVGYPTIASAPHSIANGFKNLLAIAATTEVEFKEATTIKEYIKDPSKFAAAASASAAPAAGGATEKKEEAKKPESESEEEDDDMGFGLFD
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
270AcetylationTTIKEYIKDPSKFAA
CCHHHHCCCHHHHHH
63.7921791702
280PhosphorylationSKFAAAASASAAPAA
HHHHHHHHHHHCCCC
20.3127794539
302PhosphorylationEEAKKPESESEEEDD
HHHCCCCCCCCCCCC
55.7521082442
304PhosphorylationAKKPESESEEEDDDM
HCCCCCCCCCCCCCC
60.6321082442

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
304SPhosphorylationKinaseCK1-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RLA0_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 RLA0_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCAH_DROMENcaphysical
14605208
MESD_DROMEbocaphysical
22036573
GLT_DROMEGltphysical
22036573
CLH_DROMEChcphysical
22036573
YC17_DROMECG16817physical
22036573
TERA_DROMETER94physical
22036573
NACA_DROMENacalphaphysical
22036573
IDH3A_DROMEl(1)G0156physical
22036573
TCPG_DROMECctgammaphysical
22036573
RS10B_DROMERpS10bphysical
22036573
PCID2_DROMEPCID2physical
18086857

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RLA0_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-302 AND SER-304, ANDMASS SPECTROMETRY.

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