RS103_ARATH - dbPTM
RS103_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS103_ARATH
UniProt AC Q9LTF2
Protein Name 40S ribosomal protein S10-3
Gene Name RPS10C
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 179
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MIISEANRKEICKYLFKEGVCFAKKDFNLAKHPLIDVPNLQVIKLMQSFKSKEYVRETFAWMHYYWFLTNEGIEFLRTYLNLPSDVVPATLKKSAKPGGRPFGGPPGDRSRGPRHEGGDRPRFGDRDGYRAGPRAGGEFGGEKGGAPADYQPSFQGSGRGFGRGAGGYSAAAPSGSGLP
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
1Sulfoxidation-------MIISEANR
-------CCCCHHHH
5.7625693801
110PhosphorylationGGPPGDRSRGPRHEG
CCCCCCCCCCCCCCC
46.4525561503
157PhosphorylationYQPSFQGSGRGFGRG
CCCCCCCCCCCCCCC
17.9730407730

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 RS103_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS103_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 RS103_ARATH !!

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

Oops, there are no PPI records of RS103_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS103_ARATH

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Related Literatures of Post-Translational Modification

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