PP4R2_HUMAN - dbPTM
PP4R2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP4R2_HUMAN
UniProt AC Q9NY27
Protein Name Serine/threonine-protein phosphatase 4 regulatory subunit 2
Gene Name PPP4R2
Organism Homo sapiens (Human).
Sequence Length 417
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Ionizing radiation induces relocalization to nuclear foci and colocalization with RPA2.
Protein Description Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair..
Protein Sequence MDVERLQEALKDFEKRGKKEVCPVLDQFLCHVAKTGETMIQWSQFKGYFIFKLEKVMDDFRTSAPEPRGPPNPNVEYIPFDEMKERILKIVTGFNGIPFTIQRLCELLTDPRRNYTGTDKFLRGVEKNVMVVSCVYPSSEKNNSNSLNRMNGVMFPGNSPSYTERSNINGPGTPRPLNRPKVSLSAPMTTNGLPESTDSKEANLQQNEEKNHSDSSTSESEVSSVSPLKNKHPDEDAVEAEGHEVKRLRFDKEGEVRETASQTTSSEISSVMVGETEASSSSQDKDKDSRCTRQHCTEEDEEEDEEEEEESFMTSREMIPERKNQEKESDDALTVNEETSEENNQMEESDVSQAEKDLLHSEGSENEGPVSSSSSDCRETEELVGSNSSKTGEILSESSMENDDEATEVTDEPMEQD
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
11UbiquitinationERLQEALKDFEKRGK
HHHHHHHHHHHHCCC		68.38-
15UbiquitinationEALKDFEKRGKKEVC
HHHHHHHHCCCCCCC		67.46-
19UbiquitinationDFEKRGKKEVCPVLD
HHHHCCCCCCCHHHH		59.20-
52UbiquitinationFKGYFIFKLEKVMDD
CCEEEEEEEHHHHHH		51.42-
55 (in isoform 1)Ubiquitination-53.9821890473
55UbiquitinationYFIFKLEKVMDDFRT
EEEEEEHHHHHHHHH		53.9821890473
84UbiquitinationYIPFDEMKERILKIV
CCCHHHHHHHHHHHH		41.62-
120UbiquitinationRNYTGTDKFLRGVEK
CCCCCCHHHHHCCCC		46.25-
127UbiquitinationKFLRGVEKNVMVVSC
HHHHCCCCCEEEEEE		53.05-
136PhosphorylationVMVVSCVYPSSEKNN
EEEEEEECCCCCCCC		11.1723403867
138PhosphorylationVVSCVYPSSEKNNSN
EEEEECCCCCCCCCC		33.1823403867
139PhosphorylationVSCVYPSSEKNNSNS
EEEECCCCCCCCCCC		48.3525627689
141UbiquitinationCVYPSSEKNNSNSLN
EECCCCCCCCCCCCC		64.47-
144PhosphorylationPSSEKNNSNSLNRMN
CCCCCCCCCCCCCCC		36.8726074081
146PhosphorylationSEKNNSNSLNRMNGV
CCCCCCCCCCCCCCC		27.1726074081
159PhosphorylationGVMFPGNSPSYTERS
CCCCCCCCCCCCCCC		22.5729255136
161PhosphorylationMFPGNSPSYTERSNI
CCCCCCCCCCCCCCC		44.5029255136
162PhosphorylationFPGNSPSYTERSNIN
CCCCCCCCCCCCCCC		18.9223927012
163PhosphorylationPGNSPSYTERSNING
CCCCCCCCCCCCCCC		29.2929255136
166PhosphorylationSPSYTERSNINGPGT
CCCCCCCCCCCCCCC		35.5126074081
173PhosphorylationSNINGPGTPRPLNRP
CCCCCCCCCCCCCCC		21.1825159151
183PhosphorylationPLNRPKVSLSAPMTT
CCCCCCEEECCCCCC		23.8022199227
185PhosphorylationNRPKVSLSAPMTTNG
CCCCEEECCCCCCCC		23.8722199227
188SulfoxidationKVSLSAPMTTNGLPE
CEEECCCCCCCCCCC		7.8421406390
189PhosphorylationVSLSAPMTTNGLPES
EEECCCCCCCCCCCC		18.9520068231
190PhosphorylationSLSAPMTTNGLPEST
EECCCCCCCCCCCCC		22.4927251275
196PhosphorylationTTNGLPESTDSKEAN
CCCCCCCCCCCHHHH		35.2620068231
197PhosphorylationTNGLPESTDSKEANL
CCCCCCCCCCHHHHH		42.5020068231
199PhosphorylationGLPESTDSKEANLQQ
CCCCCCCCHHHHHHH		32.2720068231
213PhosphorylationQNEEKNHSDSSTSES
HHHHHCCCCCCCCHH		48.8923927012
215PhosphorylationEEKNHSDSSTSESEV
HHHCCCCCCCCHHHH		38.2323927012
216PhosphorylationEKNHSDSSTSESEVS
HHCCCCCCCCHHHHH		40.7323927012
217PhosphorylationKNHSDSSTSESEVSS
HCCCCCCCCHHHHHC		40.2323927012
218PhosphorylationNHSDSSTSESEVSSV
CCCCCCCCHHHHHCC		40.8623927012
220PhosphorylationSDSSTSESEVSSVSP
CCCCCCHHHHHCCCC		42.9623927012
223PhosphorylationSTSESEVSSVSPLKN
CCCHHHHHCCCCCCC		22.4423401153
224PhosphorylationTSESEVSSVSPLKNK
CCHHHHHCCCCCCCC		31.6129255136
226PhosphorylationESEVSSVSPLKNKHP
HHHHHCCCCCCCCCC		26.8529255136
229UbiquitinationVSSVSPLKNKHPDED
HHCCCCCCCCCCCCC		68.30-
231UbiquitinationSVSPLKNKHPDEDAV
CCCCCCCCCCCCCHH		55.73-
246UbiquitinationEAEGHEVKRLRFDKE
HHCCCEEEEEEECCC		42.61-
246AcetylationEAEGHEVKRLRFDKE
HHCCCEEEEEEECCC		42.6125953088
252AcetylationVKRLRFDKEGEVRET
EEEEEECCCCCEEEC		65.9819608861
259PhosphorylationKEGEVRETASQTTSS
CCCCEEECCCCCCCH		22.5030576142
261PhosphorylationGEVRETASQTTSSEI
CCEEECCCCCCCHHH		35.1620068231
263PhosphorylationVRETASQTTSSEISS
EEECCCCCCCHHHHE		26.5930576142
264PhosphorylationRETASQTTSSEISSV
EECCCCCCCHHHHEE		23.7120068231
265PhosphorylationETASQTTSSEISSVM
ECCCCCCCHHHHEEE		29.3930576142
266PhosphorylationTASQTTSSEISSVMV
CCCCCCCHHHHEEEE		36.5420068231
269PhosphorylationQTTSSEISSVMVGET
CCCCHHHHEEEECCC		16.9023312004
270PhosphorylationTTSSEISSVMVGETE
CCCHHHHEEEECCCC		21.6423312004
276PhosphorylationSSVMVGETEASSSSQ
HEEEECCCCCCCCCC		30.8120068231
279PhosphorylationMVGETEASSSSQDKD
EECCCCCCCCCCCCC		25.2320068231
280PhosphorylationVGETEASSSSQDKDK
ECCCCCCCCCCCCCC		40.8520068231
281PhosphorylationGETEASSSSQDKDKD
CCCCCCCCCCCCCCC		29.5320068231
282PhosphorylationETEASSSSQDKDKDS
CCCCCCCCCCCCCCC		44.3320068231
297PhosphorylationRCTRQHCTEEDEEED
CCCHHHCCCCCHHHC		40.0424043423
311PhosphorylationDEEEEEESFMTSREM
CHHHHHHHHHHHHHH		24.4824043423
314PhosphorylationEEEESFMTSREMIPE
HHHHHHHHHHHHCCC		23.7124043423
315PhosphorylationEEESFMTSREMIPER
HHHHHHHHHHHCCCH		17.9224043423
352PhosphorylationQMEESDVSQAEKDLL
HCCHHHHHHHHHHHH		28.7621082442
361PhosphorylationAEKDLLHSEGSENEG
HHHHHHHCCCCCCCC		43.5530266825
364PhosphorylationDLLHSEGSENEGPVS
HHHHCCCCCCCCCCC		32.9530266825
371PhosphorylationSENEGPVSSSSSDCR
CCCCCCCCCCCCHHH		27.8628450419
372PhosphorylationENEGPVSSSSSDCRE
CCCCCCCCCCCHHHH		34.1823927012
373PhosphorylationNEGPVSSSSSDCRET
CCCCCCCCCCHHHHH		26.7623927012
374PhosphorylationEGPVSSSSSDCRETE
CCCCCCCCCHHHHHH		31.9523927012
375PhosphorylationGPVSSSSSDCRETEE
CCCCCCCCHHHHHHH		42.5525849741
380PhosphorylationSSSDCRETEELVGSN
CCCHHHHHHHHHCCC		18.5324247654
386PhosphorylationETEELVGSNSSKTGE
HHHHHHCCCCCCCCC		26.5121815630
388PhosphorylationEELVGSNSSKTGEIL
HHHHCCCCCCCCCCC		34.6025159151
389PhosphorylationELVGSNSSKTGEILS
HHHCCCCCCCCCCCC		38.1921815630
398PhosphorylationTGEILSESSMENDDE
CCCCCCHHHCCCCCC		31.4425954137
399PhosphorylationGEILSESSMENDDEA
CCCCCHHHCCCCCCC		26.5128348404
407PhosphorylationMENDDEATEVTDEPM
CCCCCCCCCCCCCCC		29.0128348404
410PhosphorylationDDEATEVTDEPMEQD
CCCCCCCCCCCCCCC		28.5428348404
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

Oops, there are no upstream regulatory protein records of PP4R2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PP4R2_HUMAN !!
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 PP4R2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX20_HUMANDDX20physical
12668731
GEMI4_HUMANGEMIN4physical
12668731
PP4C_HUMANPPP4Cphysical
12668731
PP4C_HUMANPPP4Cphysical
10769191
PP4C_HUMANPPP4Cphysical
18715871
PP4C_HUMANPPP4Cphysical
16085932
P4R3A_HUMANSMEK1physical
16085932
P4R3B_HUMANSMEK2physical
16085932
TIPRL_HUMANTIPRLphysical
16085932
TRA2B_HUMANTRA2Bphysical
22939629
TPM1_HUMANTPM1physical
22939629
TCPG_HUMANCCT3physical
22863883
PAAF1_HUMANPAAF1physical
22863883
VASP_HUMANVASPphysical
22863883
CUTA_HUMANCUTAphysical
26344197
DNJA1_HUMANDNAJA1physical
26344197
PP4C_HUMANPPP4Cphysical
26344197
P4R3A_HUMANSMEK1physical
26344197
P4R3B_HUMANSMEK2physical
26344197
PP4C_HUMANPPP4Cphysical
26496610
NADAP_HUMANSLC4A1APphysical
26496610
P4R3A_HUMANSMEK1physical
26496610
P4R3B_HUMANSMEK2physical
26496610
TPC13_HUMANTRAPPC13physical
26496610
EMSA1_HUMANELMSAN1physical
26496610
F133B_HUMANFAM133Bphysical
26496610
NPHP4_HUMANNPHP4physical
26496610
CT451_HUMANCT45A1physical
26496610
P4R3A_HUMANSMEK1physical
28514442
P4R3B_HUMANSMEK2physical
28514442
PP4C_HUMANPPP4Cphysical
28514442
PRP16_HUMANDHX38physical
28514442
CCDC6_HUMANCCDC6physical
28514442
TIPRL_HUMANTIPRLphysical
28514442
UBP15_HUMANUSP15physical
27173435
MCM2_HUMANMCM2physical
27173435
MCM4_HUMANMCM4physical
27173435
MCM6_HUMANMCM6physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PP4R2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-252, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY.

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