MYL9_MOUSE - dbPTM
MYL9_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYL9_MOUSE
UniProt AC Q9CQ19
Protein Name Myosin regulatory light polypeptide 9
Gene Name Myl9
Organism Mus musculus (Mouse).
Sequence Length 172
Subcellular Localization
Protein Description Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion..
Protein Sequence MSSKRAKAKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLEGMMNEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEASGFIHEDHLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILKHGAKDKDD
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
2Acetylation------MSSKRAKAK
------CCCHHHHCC
44.56-
19PhosphorylationKKRPQRATSNVFAMF
CCCCHHHHHHHHHHC
24.0327087446
20PhosphorylationKRPQRATSNVFAMFD
CCCHHHHHHHHHHCC
29.9727087446
29PhosphorylationVFAMFDQSQIQEFKE
HHHHCCHHHHHHHHH
30.9724925903
51UbiquitinationNRDGFIDKEDLHDML
CCCCCCCHHHHHHHH
48.59-
135PhosphorylationTTMGDRFTDEEVDEM
HHHHCCCCHHHHHHH
43.3117242355
150UbiquitinationYREAPIDKKGNFNYV
HHHCCCCCCCCCCCC
64.4027667366
151UbiquitinationREAPIDKKGNFNYVE
HHCCCCCCCCCCCCH
56.17-

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
19TPhosphorylationKinaseCITP49025
Uniprot
19TPhosphorylationKinaseDAPK3O43293
PSP
19TPhosphorylationKinaseMYLKP11799
GPS
19TPhosphorylationKinaseROCK2P70336
Uniprot
19TPhosphorylationKinaseMLCK-Uniprot
20SPhosphorylationKinaseCITP49025
Uniprot
20SPhosphorylationKinaseDAPK1Q80YE7
Uniprot
20SPhosphorylationKinaseDAPK2Q8VDF3
Uniprot
20SPhosphorylationKinaseDAPK3O43293
PSP
20SPhosphorylationKinaseDAPK3O54784
Uniprot
20SPhosphorylationKinaseMYLKP11799
GPS
20SPhosphorylationKinasePAK1O88643
Uniprot
20SPhosphorylationKinaseROCK1P70335
Uniprot
20SPhosphorylationKinaseROCK2P70336
Uniprot
20SPhosphorylationKinaseCDC42BP-Uniprot
20SPhosphorylationKinaseMLCK-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYL9_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 MYL9_MOUSE !!

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

Oops, there are no PPI records of MYL9_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYL9_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-20; SER-29 ANDTHR-135, AND MASS SPECTROMETRY.
"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 THR-19 AND SER-20, AND MASSSPECTROMETRY.

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