MTSSL_MOUSE - dbPTM
MTSSL_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTSSL_MOUSE
UniProt AC Q6P9S0
Protein Name MTSS1-like protein
Gene Name Mtss1l
Organism Mus musculus (Mouse).
Sequence Length 715
Subcellular Localization Cytoplasm . Cell projection, ruffle . Colocalizes with RAC1 within membrane ruffles.
Protein Description Involved in plasma membrane dynamics. Potentiated PDGF-mediated formation of membrane ruffles and lamellipodia in fibroblasts, acting via RAC1 activation. May function in actin bundling..
Protein Sequence METAEKECGALGGLFQAIVNDMKSSYPIWEDFNSKAAKLHSQLRTTVLAAVAFLDAFQKVADMATNTRGATRDIGSALTRMCMRHRSIETKLRQFTNALLESLINPLQERIEDWKKSANQLDKDHAKEYKRARHEIKKKSSDTLKLQKKARKGKGDLQPQLDSALQDVNDMYLLLEETEKQAVRRALIEERGRFCTFITFLQPVVNGELTMLGEITHLQGIIDDLVVLTADPHKLPPASEQVIKDLKGSDYSWSYQTPPSSPSSSNSRKSSMCSLAQPATTRLSSVSSHDSGFVSQDPTYSKPPSPMPSDITSQKSSSSASSEASETCQSVSECSSPTSDWTKAGPHEQPSATTLQRRKDRVEHLRDTEPGPTGGGTVGSSGEEVPRTRMSPATIAAKHGEEVSPAASDLAMVLTRGLSLEHQKSSRDSLQYSSGYSTQTTTPSCSEDTIPSQGSDYDCYSVNGDADSEGPPEFDKSSTIPRNSNIAQNYRRLIQTKRPASTAGLPTAGLPTAMGLPSGAPPGVATIRRTPSTKPTVRRALSSAGPIPIRPPIVPVKTPTVPDSPGYVGPTRAGSEECVFYTDEVASPLAPDLAKASPKRLSLPNTAWGSQSPEVASYGGGAAVGLATEDEEQQLAANRHSLVEKLGELVAGAHALGEGQFPFPTALSATPSEETPTPPPAATSDPPAEDMLVAIRRGVRLRRTVTNDRSAPRIL
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
115AcetylationQERIEDWKKSANQLD
HHHHHHHHHHHHHCC
49.5323806337
116AcetylationERIEDWKKSANQLDK
HHHHHHHHHHHHCCH
51.0123806337

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 MTSSL_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTSSL_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 MTSSL_MOUSE !!

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

Oops, there are no PPI records of MTSSL_MOUSE !!

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257 AND SER-261, ANDMASS SPECTROMETRY.

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