RL21A_SCHPO - dbPTM
RL21A_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL21A_SCHPO
UniProt AC Q9UUC1
Protein Name 60S ribosomal protein L21-A
Gene Name rpl2101
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 160
Subcellular Localization
Protein Description
Protein Sequence MPHSYGIRARTRYTFQRGFREHGQIRLSTYLKTYKVGDIVDIKVNGAVQKGMPHKYYHGKTGVVYNVTQSSVGVLIYKVVGNRYMEKRVNVRIEHVKHSKCRQDFLDRVKANEAKRKEAKAQGKTVQLRRQPAPPAKAHFVSTENNEPVTLHPVAYDTTI
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
4Phosphorylation----MPHSYGIRART
----CCCCCCCHHHC
21.1329996109
33PhosphorylationRLSTYLKTYKVGDIV
EEEEEEEEEEECCEE
26.4425720772
158PhosphorylationLHPVAYDTTI-----
EEEEEEECCC-----
17.4524763107

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 RL21A_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL21A_SCHPO !!

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 RL21A_SCHPO !!

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

Oops, there are no PPI records of RL21A_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL21A_SCHPO

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Related Literatures of Post-Translational Modification

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