RM54_HUMAN - dbPTM
RM54_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RM54_HUMAN
UniProt AC Q6P161
Protein Name 39S ribosomal protein L54, mitochondrial
Gene Name MRPL54
Organism Homo sapiens (Human).
Sequence Length 138
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MATKRLFGATRTWAGWGAWELLNPATSGRLLARDYAKKPVMKGAKSGKGAVTSEALKDPDVCTDPVQLTTYAMGVNIYKEGQDVPLKPDAEYPEWLFEMNLGPPKTLEELDPESREYWRRLRKQNIWRHNRLSKNKRL
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
3Phosphorylation-----MATKRLFGAT
-----CCCCCCCCCC
18.5224719451
62GlutathionylationALKDPDVCTDPVQLT
HHCCCCCCCCCHHHE
4.6922555962
106PhosphorylationMNLGPPKTLEELDPE
CCCCCCCCHHHHCHH
45.2127966365
115MethylationEELDPESREYWRRLR
HHHCHHHHHHHHHHH
39.09115483797

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 RM54_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RM54_HUMAN !!

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 RM54_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT07_HUMANMRPS7physical
22939629

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RM54_HUMAN

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Related Literatures of Post-Translational Modification

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