RS21_CAEEL - dbPTM
RS21_CAEEL - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS21_CAEEL
UniProt AC P49197
Protein Name 40S ribosomal protein S21
Gene Name rps-21
Organism Caenorhabditis elegans.
Sequence Length 88
Subcellular Localization Cytoplasm, cytosol . Cytoplasm . Rough endoplasmic reticulum . Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity).
Protein Description
Protein Sequence MQNDAGQTVELYVPRKCSSSNRIIGPKDHASVQIDFVDVDPETGRMIPGKSTRYAICGAIRRMGESDDAILRLAQKDGLVPRDDVKSN
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
66PhosphorylationAIRRMGESDDAILRL
HHHHHCCCHHHHHHH
34.7530078680
87PhosphorylationVPRDDVKSN------
CCHHHCCCC------
47.8526392051

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 RS21_CAEEL !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS21_CAEEL !!

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 RS21_CAEEL !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSSA_CAEELrps-0physical
18692475

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS21_CAEEL

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Related Literatures of Post-Translational Modification

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