MLRS_MOUSE - dbPTM
MLRS_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MLRS_MOUSE
UniProt AC P97457
Protein Name Myosin regulatory light chain 2, skeletal muscle isoform
Gene Name Mylpf
Organism Mus musculus (Mouse).
Sequence Length 169
Subcellular Localization
Protein Description
Protein Sequence MAPKKAKRRAGAEGSSNVFSMFDQTQIQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGRLNVKNEELDAMMKEASGPINFTVFLTMFGEKLKGADPEDVITGAFKVLDPEGKGTIKKQFLEELLTTQCDRFSQEEIKNMWAAFPPDVGGNVDYKNICYVITHGDAKDQE
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
2Methylation------MAPKKAKRR
------CCCHHHHHH
25.31-
15PhosphorylationRRAGAEGSSNVFSMF
HHHCCCCCCCHHHCC
15.3925521595
16PhosphorylationRAGAEGSSNVFSMFD
HHCCCCCCCHHHCCC
48.1225521595
20PhosphorylationEGSSNVFSMFDQTQI
CCCCCHHHCCCHHHH
17.7925521595
25PhosphorylationVFSMFDQTQIQEFKE
HHHCCCHHHHHHHHH
29.5023737553
31AcetylationQTQIQEFKEAFTVID
HHHHHHHHHHHHHHC
47.5919863181
31UbiquitinationQTQIQEFKEAFTVID
HHHHHHHHHHHHHHC
47.59-
35PhosphorylationQEFKEAFTVIDQNRD
HHHHHHHHHHCCCCC
24.4928464351
47AcetylationNRDGIIDKEDLRDTF
CCCCCCCHHHHHHHH
42.6021728379
47UbiquitinationNRDGIIDKEDLRDTF
CCCCCCCHHHHHHHH
42.6022790023
53PhosphorylationDKEDLRDTFAAMGRL
CHHHHHHHHHHHCCC
14.5624899341
63UbiquitinationAMGRLNVKNEELDAM
HHCCCCCCHHHHHHH
58.5322790023
63AcetylationAMGRLNVKNEELDAM
HHCCCCCCHHHHHHH
58.5321728379
75PhosphorylationDAMMKEASGPINFTV
HHHHHHCCCCEEEEE
46.3122210690
81PhosphorylationASGPINFTVFLTMFG
CCCCEEEEEEEHHHH
13.0822210690
85PhosphorylationINFTVFLTMFGEKLK
EEEEEEEHHHHHHHC
10.0522210690
92UbiquitinationTMFGEKLKGADPEDV
HHHHHHHCCCCHHHH
64.2222790023
92AcetylationTMFGEKLKGADPEDV
HHHHHHHCCCCHHHH
64.2221728379
101PhosphorylationADPEDVITGAFKVLD
CCHHHHHCCEEEEEC
23.4728464351
105UbiquitinationDVITGAFKVLDPEGK
HHHCCEEEEECCCCC
41.1622790023
105AcetylationDVITGAFKVLDPEGK
HHHCCEEEEECCCCC
41.1621728379
112AcetylationKVLDPEGKGTIKKQF
EEECCCCCCCHHHHH
51.7421728379
112UbiquitinationKVLDPEGKGTIKKQF
EEECCCCCCCHHHHH
51.7422790023
116UbiquitinationPEGKGTIKKQFLEEL
CCCCCCHHHHHHHHH
40.1222790023
117UbiquitinationEGKGTIKKQFLEELL
CCCCCHHHHHHHHHH
42.2922790023
126PhosphorylationFLEELLTTQCDRFSQ
HHHHHHHHCCHHCCH
27.4628542873
132PhosphorylationTTQCDRFSQEEIKNM
HHCCHHCCHHHHHHH
37.2622210690
137UbiquitinationRFSQEEIKNMWAAFP
HCCHHHHHHHHHHCC
43.99-
154AcetylationVGGNVDYKNICYVIT
CCCCCCCCCEEEEEE
35.0619863197
158PhosphorylationVDYKNICYVITHGDA
CCCCCEEEEEECCCC
7.3528542873
161PhosphorylationKNICYVITHGDAKDQ
CCEEEEEECCCCCCC
15.1222210690
166AcetylationVITHGDAKDQE----
EEECCCCCCCC----
65.7621728379
166UbiquitinationVITHGDAKDQE----
EEECCCCCCCC----
65.7622790023

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
-KUbiquitinationE3 ubiquitin ligaseTrim63Q38HM4
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MLRS_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 MLRS_MOUSE !!

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

Oops, there are no PPI records of MLRS_MOUSE !!

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

loading...

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 SER-16, AND MASSSPECTROMETRY.

TOP