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Protein Page:
PPP2R4 (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PPP2R4 PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine- protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activty of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A. Associates with PP2A heterodimeric core enzyme PP2A(D), composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A). Interacts with PPP2CB. Widely expressed. Belongs to the PTPA-type PPIase family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Protein phosphatase, regulatory subunit; Motility/polarity/chemotaxis; EC 5.2.1.8
Cellular Component: protein phosphatase type 2A complex; cytoplasm; nucleus
Molecular Function: peptidyl-prolyl cis-trans isomerase activity; protein homodimerization activity; protein phosphatase 2A binding; phosphatase activator activity; ATPase activity; nucleotide binding; protein phosphatase type 2A regulator activity; isomerase activity; ATP binding; protein tyrosine phosphatase activator activity; receptor binding
Biological Process: positive regulation of phosphoprotein phosphatase activity; ATP catabolic process; positive regulation of catalytic activity; negative regulation of protein amino acid dephosphorylation; protein peptidyl-prolyl isomerization; protein folding; positive regulation of apoptosis; mitotic spindle organization and biogenesis in nucleus; negative regulation of phosphoprotein phosphatase activity; regulation of phosphoprotein phosphatase activity; positive regulation of protein amino acid dephosphorylation
Reference #:  P58389 (UniProtKB)
Alt. Names/Synonyms: 2610042B21Rik; C77440; MGC60706; MGC7129; N28142; OTTMUSP00000018234; Phosphotyrosyl phosphatase activator; PP2A, subunit B', PR53 isoform; Ppp2r4; PR53; protein phosphatase 2A, regulatory subunit B (PR 53); PTPA; Serine/threonine-protein phosphatase 2A activator; Serine/threonine-protein phosphatase 2A regulatory subunit 4; Serine/threonine-protein phosphatase 2A regulatory subunit B'
Gene Symbols: Ppp2r4
Molecular weight: 36,710 Da
Basal Isoelectric point: 5.95  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PPP2R4

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

 
0 1 K27 TQNFIIPKKEIHTVP
0 1 K62 LNEGVKGKKLTFDYK
0 13 Y188 VFKVFDRYLEVMRKL
0 1 K242 PRHFVDEKAVSENHK
0 1 K286 SAVPSWSKVNQGLIR
0 1 K296 QGLIRMYKAECLEKF
0 1 K302 YKAECLEKFPVIQHF
0 1 K310 FPVIQHFKFGSLLPI
  human

 
K27-ub TQNFIIPkKEIHTVP
K62-ac LNEGVKGkKLTFEYR
Y223-p VFKVFNRyLEVMRKL
K277-ub PRHFVDEkAVNENHK
K321-ac SAVPSWSkVNQGLIR
K331-ac QGLIRMYkAECLEkF
K337-ac YkAECLEkFPVIQHF
K345-ac FPVIQHFkFGSLLPI
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