Home

PPP2R4 (human)

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; EC 5.2.1.8; Motility/polarity/chemotaxis Cellular Component: protein phosphatase type 2A complex; cytoplasm; nucleolus; nucleus Molecular Function: peptidyl-prolyl cis-trans isomerase activity; protein homodimerization activity; protein phosphatase 2A binding; protein heterodimerization activity; ATPase activity; protein phosphatase type 2A regulator activity; ATP binding; protein tyrosine phosphatase activator activity; receptor binding Biological Process: ATP catabolic process; positive regulation of phosphoprotein phosphatase activity; negative regulation of protein amino acid dephosphorylation; protein folding; positive regulation of apoptosis; negative regulation of phosphoprotein phosphatase activity; regulation of phosphoprotein phosphatase activity; positive regulation of protein amino acid dephosphorylation Reference #:  Q15257 (UniProtKB) Alt. Names/Synonyms: MGC2184; Phosphotyrosyl phosphatase activator; PP2A; PP2A phosphatase activator; PP2A subunit B' isoform PR53; PP2A, subunit B'; PP2A, subunit B', PR53 isoform; PPP2R4; PR53; protein phosphatase 2A activator, regulatory subunit 4; 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: 40,668 Da Basal Isoelectric point: 5.63  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below PPP2R4 2G62 - A=22-358 (human) 2HV6 - A/B=1-358 (human) 2HV7 - A/B/C/D/E/F/G/H=1-358 (human) 2IXM - A=20-357 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 2G62 2HV6 2HV7 2IXM  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	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

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.			human
0	1		K27-u	TQNFIIPkKEIHTVP
0	1		K62-a	LNEGVKGkKLTFEYR
0	14		Y223-p	VFKVFNRyLEVMRKL
0	1		K277-u	PRHFVDEkAVNENHK
0	1		K331-a	QGLIRMYkAECLEkF
0	1		K337-a	YkAECLEkFPVIQHF
0	1		K345-a	FPVIQHFkFGSLLPI

	mouse
K27	TQNFIIPKKEIHTVP
K62	LNEGVKGKKLTFDYK
Y188	VFKVFDRYLEVMRKL
K242	PRHFVDEKAVSENHK
K296	QGLIRMYKAECLEKF
K302	YKAECLEKFPVIQHF
K310	FPVIQHFKFGSLLPI

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.