Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Serine/threonine-protein phosphatase 4 catalytic subunit  

UniProtKB / Swiss-Prot ID :  PP4C_RABIT

Gene Name (Synonyms) : 
PPP4C  

Species :  Oryctolagus cuniculus (Rabbit). 

Subcellular Localization :  Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, centrosome. 

Protein Function :  Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C- PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on Ser-140 (gamma-H2AFX) generated during DNA replication and required for DNA DSB repair. Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase (By similarity). In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin (By similarity). 

Protein Sequence MAEISDLDRQIEQLLRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGG...
Predicted Secondary Structure CCCCCHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHCCCCCEECCCCEEEEECCCCCHHHHHHHHHHHC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
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Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
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Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
307Leucine methyl ester.ADYFL
CCCCC
5.81UniProtKB
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Carboxymethylation of nuclear protein serine/threonine phosphataseX.";
Kloeker S., Bryant J.C., Strack S., Colbran R.J., Wadzinski B.E.;
Biochem. J. 327:481-486(1997).
Cited for: METHYLATION AT LEU-307.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures