USMG5_MOUSE - dbPTM
USMG5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID USMG5_MOUSE
UniProt AC Q78IK2
Protein Name Up-regulated during skeletal muscle growth protein 5
Gene Name Usmg5
Organism Mus musculus (Mouse).
Sequence Length 58
Subcellular Localization Mitochondrion membrane
Single-pass membrane protein.
Protein Description Plays a critical role in maintaining the ATP synthase population in mitochondria..
Protein Sequence MAGAESDGQFQFTGIKKYFNSYTLTGRMNCVLATYGGIALLVLYFKLRPKKTPAVKAT
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
17SuccinylationFQFTGIKKYFNSYTL
EEECCHHHHCCEEEC
53.8324315375

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 USMG5_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of USMG5_MOUSE !!

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 USMG5_MOUSE !!

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

Oops, there are no PPI records of USMG5_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of USMG5_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16 AND LYS-17, AND MASSSPECTROMETRY.

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