P4R3A_HUMAN - dbPTM
P4R3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P4R3A_HUMAN
UniProt AC Q6IN85
Protein Name Serine/threonine-protein phosphatase 4 regulatory subunit 3A {ECO:0000312|HGNC:HGNC:20219}
Gene Name PPP4R3A {ECO:0000312|HGNC:HGNC:20219}
Organism Homo sapiens (Human).
Sequence Length 833
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Nucleus . In interphase localized in the cytoplasm and in the nucleus (with higher levels). During metaphase located in pericentriolar regions.
Protein Description Regulatory subunit of serine/threonine-protein phosphatase 4. May regulate the activity of PPP4C at centrosomal microtubule organizing centers. 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..
Protein Sequence MTDTRRRVKVYTLNEDRQWDDRGTGHVSSGYVERLKGMSLLVRAESDGSLLLESKINPNTAYQKQQDTLIVWSEAENYDLALSFQEKAGCDEIWEKICQVQGKDPSVDITQDLVDESEEERFDDMSSPGLELPSCELSRLEEIAELVASSLPSPLRREKLALALENEGYIKKLLELFHVCEDLENIEGLHHLYEIIKGIFLLNRTALFEVMFSEECIMDVIGCLEYDPALSQPRKHREFLTKTAKFKEVIPISDPELKQKIHQTYRVQYIQDMVLPTPSVFEENMLSTLHSFIFFNKVEIVGMLQEDEKFLTDLFAQLTDEATDEEKRQELVNFLKEFCAFSQTLQPQNRDAFFKTLSNMGILPALEVILGMDDTQVRSAATDIFSYLVEYNPSMVREFVMQEAQQNDDVSKKLTEQKITSKDILLINLIIEHMICDTDPELGGAVQLMGLLRTLVDPENMLATANKTEKTEFLGFFYKHCMHVLTAPLLANTTEDKPSKDDFQTAQLLALVLELLTFCVEHHTYHIKNYIINKDILRRVLVLMASKHAFLALCALRFKRKIIGLKDEFYNRYIMKSFLFEPVVKAFLNNGSRYNLMNSAIIEMFEFIRVEDIKSLTAHVIENYWKALEDVDYVQTFKGLKLRFEQQRERQDNPKLDSMRSILRNHRYRRDARTLEDEEEMWFNTDEDDMEDGEAVVSPSDKTKNDDDIMDPISKFMERKKLKESEEKEVLLKTNLSGRQSPSFKLSLSSGTKTNLTSQSSTTNLPGSPGSPGSPGSPGSPGSVPKNTSQTAAITTKGGLVGLVDYPDDDEDDDEDEDKEDTLPLSKKAKFDS
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
11PhosphorylationTRRRVKVYTLNEDRQ
CCCCEEEEEECCCCC		10.3728985074
12PhosphorylationRRRVKVYTLNEDRQW
CCCEEEEEECCCCCC		26.5428985074
17MethylationVYTLNEDRQWDDRGT
EEEECCCCCCCCCCC		33.05-
46PhosphorylationSLLVRAESDGSLLLE
EEEEEEECCCCEEEE		46.4130108239
49PhosphorylationVRAESDGSLLLESKI
EEEECCCCEEEEEEC		22.3430108239
54PhosphorylationDGSLLLESKINPNTA
CCCEEEEEECCCCCC		38.5130108239
106PhosphorylationQVQGKDPSVDITQDL
HHCCCCCCCCCHHHH		42.4229978859
110PhosphorylationKDPSVDITQDLVDES
CCCCCCCHHHHCCCC		16.1523663014
117 (in isoform 2)Phosphorylation-45.9327251275
117PhosphorylationTQDLVDESEEERFDD
HHHHCCCCHHHCCCC		45.9319664994
117 (in isoform 5)Phosphorylation-45.93-
126PhosphorylationEERFDDMSSPGLELP
HHCCCCCCCCCCCCC		40.1430266825
127PhosphorylationERFDDMSSPGLELPS
HCCCCCCCCCCCCCC		19.1519664994
127 (in isoform 5)Phosphorylation-19.15-
127 (in isoform 2)Phosphorylation-19.15-
134PhosphorylationSPGLELPSCELSRLE
CCCCCCCCCHHHHHH		32.6123663014
138PhosphorylationELPSCELSRLEEIAE
CCCCCHHHHHHHHHH		16.7223663014
149PhosphorylationEIAELVASSLPSPLR
HHHHHHHHCCCCHHH		25.5726434776
150PhosphorylationIAELVASSLPSPLRR
HHHHHHHCCCCHHHH		34.2626434776
153PhosphorylationLVASSLPSPLRREKL
HHHHCCCCHHHHHHH		41.6928450419
153 (in isoform 2)Phosphorylation-41.6927251275
169PhosphorylationLALENEGYIKKLLEL
HHHHCCHHHHHHHHH		11.9119658100
231PhosphorylationLEYDPALSQPRKHRE
HHCCHHHCCCHHHHH		40.0024719451
312PhosphorylationQEDEKFLTDLFAQLT
CCCHHHHHHHHHHHC		33.5128509920
319PhosphorylationTDLFAQLTDEATDEE
HHHHHHHCCCCCCHH		21.5129449344
323PhosphorylationAQLTDEATDEEKRQE
HHHCCCCCCHHHHHH		41.7328509920
327 (in isoform 4)Ubiquitination-58.2821890473
337 (in isoform 4)Ubiquitination-48.3721890473
346 (in isoform 4)Ubiquitination-40.7021890473
356PhosphorylationNRDAFFKTLSNMGIL
CHHHHHHHHHHCCHH		30.20-
411PhosphorylationAQQNDDVSKKLTEQK
HHHCCHHHHHHHHCC		30.9429978859
416AcetylationDVSKKLTEQKITSKD
HHHHHHHHCCCCHHH		61.3819608861
416MethylationDVSKKLTEQKITSKD
HHHHHHHHCCCCHHH		61.3819608861
486PhosphorylationKHCMHVLTAPLLANT
HHHHHHHHHHHHCCC		25.7423322592
494PhosphorylationAPLLANTTEDKPSKD
HHHHCCCCCCCCCCC		41.8323322592
553 (in isoform 2)Ubiquitination-1.5921890473
563 (in isoform 2)Ubiquitination-6.2421890473
566UbiquitinationKRKIIGLKDEFYNRY
HHHHHCCCHHHHHHH		50.42-
566 (in isoform 1)Ubiquitination-50.4221890473
572 (in isoform 2)Ubiquitination-15.8121890473
573PhosphorylationKDEFYNRYIMKSFLF
CHHHHHHHHHHHHCC		11.17-
576 (in isoform 1)Ubiquitination-28.6221890473
576UbiquitinationFYNRYIMKSFLFEPV
HHHHHHHHHHCCHHH		28.6221890473
585UbiquitinationFLFEPVVKAFLNNGS
HCCHHHHHHHHHCCC		33.392189047
585 (in isoform 1)Ubiquitination-33.3921890473
633PhosphorylationKALEDVDYVQTFKGL
HHHCCCCHHHHCCCH		8.36-
642 (in isoform 2)Acetylation-10.23-
645 (in isoform 2)Phosphorylation-39.0924719451
655AcetylationRERQDNPKLDSMRSI
HHHCCCCCHHHHHHH		71.7919608861
655MethylationRERQDNPKLDSMRSI
HHHCCCCCHHHHHHH		71.7923644510
658PhosphorylationQDNPKLDSMRSILRN
CCCCCHHHHHHHHHH		26.9126434776
661PhosphorylationPKLDSMRSILRNHRY
CCHHHHHHHHHHCCC		19.8226434776
674PhosphorylationRYRRDARTLEDEEEM
CCCCCCCCCCCHHHH		35.9028348404
685 (in isoform 2)Phosphorylation-31.1527251275
685PhosphorylationEEEMWFNTDEDDMED
HHHHCCCCCHHHCCC		31.1526074081
698PhosphorylationEDGEAVVSPSDKTKN
CCCCEECCCCCCCCC		16.4628102081
700PhosphorylationGEAVVSPSDKTKNDD
CCEECCCCCCCCCCC		44.2126074081
703PhosphorylationVVSPSDKTKNDDDIM
ECCCCCCCCCCCCCC		39.8226074081
710SulfoxidationTKNDDDIMDPISKFM
CCCCCCCCHHHHHHH		6.8821406390
714PhosphorylationDDIMDPISKFMERKK
CCCCHHHHHHHHHHH		25.8126074081
715AcetylationDIMDPISKFMERKKL
CCCHHHHHHHHHHHC		49.8325953088
721 (in isoform 2)Phosphorylation-71.6424719451
728 (in isoform 2)Phosphorylation-49.4224719451
733MethylationEEKEVLLKTNLSGRQ
HHHHHHHHHCCCCCC		31.07115980891
734PhosphorylationEKEVLLKTNLSGRQS
HHHHHHHHCCCCCCC		41.1623927012
737PhosphorylationVLLKTNLSGRQSPSF
HHHHHCCCCCCCCCE		33.7223401153
741PhosphorylationTNLSGRQSPSFKLSL
HCCCCCCCCCEEEEC		22.5820201521
743PhosphorylationLSGRQSPSFKLSLSS
CCCCCCCCEEEECCC		40.0223927012
747PhosphorylationQSPSFKLSLSSGTKT
CCCCEEEECCCCCCC		27.1326434776
749PhosphorylationPSFKLSLSSGTKTNL
CCEEEECCCCCCCCC		24.2825159151
750PhosphorylationSFKLSLSSGTKTNLT
CEEEECCCCCCCCCC		56.6326434776
752PhosphorylationKLSLSSGTKTNLTSQ
EEECCCCCCCCCCCC		36.3223312004
754PhosphorylationSLSSGTKTNLTSQSS
ECCCCCCCCCCCCCC		34.9922115753
755 (in isoform 2)Phosphorylation-42.76-
757PhosphorylationSGTKTNLTSQSSTTN
CCCCCCCCCCCCCCC		27.1322115753
758PhosphorylationGTKTNLTSQSSTTNL
CCCCCCCCCCCCCCC		31.0922115753
758 (in isoform 2)Phosphorylation-31.0924719451
760PhosphorylationKTNLTSQSSTTNLPG
CCCCCCCCCCCCCCC		29.4422115753
761PhosphorylationTNLTSQSSTTNLPGS
CCCCCCCCCCCCCCC		31.4522115753
761 (in isoform 2)Phosphorylation-31.4524719451
762PhosphorylationNLTSQSSTTNLPGSP
CCCCCCCCCCCCCCC		25.5822115753
763PhosphorylationLTSQSSTTNLPGSPG
CCCCCCCCCCCCCCC		36.3822115753
764 (in isoform 2)Phosphorylation-44.3124719451
767 (in isoform 2)Phosphorylation-50.0324719451
768PhosphorylationSTTNLPGSPGSPGSP
CCCCCCCCCCCCCCC		24.9330278072
770 (in isoform 2)Phosphorylation-48.44-
771PhosphorylationNLPGSPGSPGSPGSP
CCCCCCCCCCCCCCC		29.4925159151
774PhosphorylationGSPGSPGSPGSPGSP
CCCCCCCCCCCCCCC		29.4925159151
777PhosphorylationGSPGSPGSPGSPGSV
CCCCCCCCCCCCCCC		29.4925159151
780PhosphorylationGSPGSPGSPGSVPKN
CCCCCCCCCCCCCCC		29.4925159151
783PhosphorylationGSPGSPGSVPKNTSQ
CCCCCCCCCCCCCCC		38.3330278072
789PhosphorylationGSVPKNTSQTAAITT
CCCCCCCCCCEEEEE		34.6225159151
806PhosphorylationGLVGLVDYPDDDEDD
CEEEEECCCCCCCCC		10.9029978859
822PhosphorylationEDEDKEDTLPLSKKA
CCCCCCCCCCHHHHC		31.2221815630
826PhosphorylationKEDTLPLSKKAKFDS
CCCCCCHHHHCCCCC		30.1229978859
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 P4R3A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P4R3A_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 P4R3A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP4C_HUMANPPP4Cphysical
16085932
PP4R2_HUMANPPP4R2physical
16085932
PP4C_HUMANPPP4Cphysical
21423269
HDAC1_HUMANHDAC1physical
21423269
RPB1_HUMANPOLR2Aphysical
22939629
AMPD2_HUMANAMPD2physical
22863883
BRCC3_HUMANBRCC3physical
22863883
ICAL_HUMANCASTphysical
22863883
DDB2_HUMANDDB2physical
22863883
HNRPR_HUMANHNRNPRphysical
22863883
MTA2_HUMANMTA2physical
22863883
PP4R2_HUMANPPP4R2physical
22863883
PSA2_HUMANPSMA2physical
22863883
PSB1_HUMANPSMB1physical
22863883
TELO2_HUMANTELO2physical
22863883
THIC_HUMANACAT2physical
26344197
CCAR2_HUMANCCAR2physical
26344197
EHMT1_HUMANEHMT1physical
26344197
EHMT2_HUMANEHMT2physical
26344197
RPB1_HUMANPOLR2Aphysical
26344197
SNX12_HUMANSNX12physical
26344197
SNX3_HUMANSNX3physical
26344197
BUB1B_HUMANBUB1Bphysical
26496610
CLK1_HUMANCLK1physical
26496610
MED1_HUMANMED1physical
26496610
PP4C_HUMANPPP4Cphysical
26496610
PTPRA_HUMANPTPRAphysical
26496610
PRP16_HUMANDHX38physical
26496610
COBL1_HUMANCOBLL1physical
26496610
NADAP_HUMANSLC4A1APphysical
26496610
FBX28_HUMANFBXO28physical
26496610
SIR1_HUMANSIRT1physical
26496610
COG4_HUMANCOG4physical
26496610
NECT3_HUMANPVRL3physical
26496610
ITSN2_HUMANITSN2physical
26496610
NSF1C_HUMANNSFL1Cphysical
26496610
SYF1_HUMANXAB2physical
26496610
SFR15_HUMANSCAF4physical
26496610
CATIN_HUMANCACTINphysical
26496610
DOCK5_HUMANDOCK5physical
26496610
LRCH3_HUMANLRCH3physical
26496610
SKAP_HUMANKNSTRNphysical
26496610
PP4R2_HUMANPPP4R2physical
26496610
P4R3B_HUMANSMEK2physical
28514442
PP4C_HUMANPPP4Cphysical
28514442
PTPA_HUMANPPP2R4physical
28514442
PPME1_HUMANPPME1physical
28514442
ATRIP_HUMANATRIPphysical
25533186
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 P4R3A_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-655, 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-771; SER-774 ANDSER-777, AND MASS 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-117; SER-771; SER-774AND SER-783, AND MASS 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-741, AND MASSSPECTROMETRY.

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