Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Actin, alpha skeletal muscle  

UniProtKB / Swiss-Prot ID :  ACTS_MOUSE

Gene Name (Synonyms) : 
Acta1, Acta  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm, cytoskeleton. 

Protein Function :  Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. 

Protein Sequence MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLK...
Predicted Secondary Structure CCCCCCCCEEEEECCCCEEEEECCCCCCCCEEECCEEECCCCCCCCCCCCCCCEEEEHHHHCCCCCEEEE...
Protein Variant -
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
54PhosphoserineGQKDSYVGD
CCCCEEEEH
28.84Phosphositeplus
Link
55PhosphotyrosineQKDSYVGDE
CCCEEEEHH
20.70Phosphositeplus
Link
55PhosphotyrosineQKDSYVGDE
CCCEEEEHH
20.70SysPTM
Link
55Phosphotyrosine.QKDSYVGDE
CCCEEEEHH
20.70UniProtKB
Link
62PhosphoserineDEAQSKRGI
HHHHCCCCC
31.22Phosphositeplus
Link
63N6-acetyllysineEAQSKRGIL
HHHCCCCCE
42.43Phosphositeplus
Link
68PhosphothreonineRGILTLKYP
CCCEEEECC
21.20Phosphositeplus
Link
71PhosphotyrosineLTLKYPIEH
EEEECCCCC
16.74SysPTM
Link
91PhosphothreonineIWHHTFYNE
HHHHHHHHH
18.22Phosphositeplus
Link
93PhosphotyrosineHHTFYNELR
HHHHHHHHC
14.64Phosphositeplus
Link
93PhosphotyrosineHHTFYNELR
HHHHHHHHC
14.64SysPTM
Link
93Phosphotyrosine.HHTFYNELR
HHHHHHHHC
14.64UniProtKB
Link
188PhosphothreonineGRDLTDYLM
HHHHHHHHH
27.21Phosphositeplus
Link
201PhosphoserineERGYSFVTT
HCCCCCCCC
18.96Phosphositeplus
Link
205PhosphothreonineSFVTTAERE
CCCCCCCHH
22.63Phosphositeplus
Link
220PhosphotyrosineEKLCYVALD
HHHEECCCC
10.13Phosphositeplus
Link
220PhosphotyrosineEKLCYVALD
HHHEECCCC
10.13SysPTM
Link
241PhosphoserineSLEKSYELP
CCEEEEECC
17.92Phosphositeplus
Link
242PhosphotyrosineLEKSYELPD
CEEEEECCC
32.33Phosphositeplus
Link
242PhosphotyrosineLEKSYELPD
CEEEEECCC
32.33SysPTM
Link
242Phosphotyrosine.LEKSYELPD
CEEEEECCC
32.33UniProtKB
Link
325PhosphoserineALAPSTMKI
HHCCCCCEE
35.21Phosphositeplus
Link
330N6-acetyllysineTMKIKIIAP
CCEEEEECC
23.65Phosphositeplus
Link
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Drug Reference
- top -
Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-93, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55; TYR-93 AND TYR-242,AND MASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures