RL92_ARATH - dbPTM
RL92_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL92_ARATH
UniProt AC Q9SZX9
Protein Name 60S ribosomal protein L9-2
Gene Name RPL9D
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 194
Subcellular Localization
Protein Description
Protein Sequence MKTILSSETMDIPDGVAIKVNAKVIEVEGPRGKLTRDFKHLNLDFQLIKDQVTGKRQLKIDSWFGSRKTSASIRTALSHVDNLIAGVTQGFLYRMRFVYAHFPINASIDGNNKSIEIRNFLGEKKVRKVEMLDGVKIVRSEKVKDEIILEGNDIELVSRSCALINQKCHVKKKDIRKFLDGIYVSEKGKIAVEE
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
6Phosphorylation--MKTILSSETMDIP
--CCEECCCCCCCCC
23.4423111157
75PhosphorylationKTSASIRTALSHVDN
CCCHHHHHHHHHHHH
30.2222092075
158PhosphorylationGNDIELVSRSCALIN
CCCCHHHHHHHHHHC
30.9723820729

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 RL92_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL92_ARATH !!

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 RL92_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RL92_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL92_ARATH

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Related Literatures of Post-Translational Modification

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