PP4R2_YEAST - dbPTM
PP4R2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP4R2_YEAST
UniProt AC P38193
Protein Name Serine/threonine-protein phosphatase 4 regulatory subunit 2
Gene Name PSY4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 441
Subcellular Localization Nucleus .
Protein Description Regulatory subunit of the histone H2A phosphatase complex, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint..
Protein Sequence MSSTMLDDVDNNMMGIKSISLYELLSDVVKQGDKTRLVTAGPEQVLPDLIRHITETIPFDLFINLKNEMNDARNLVTRLNWLGKFLNDNFLQNHTFPFTILRICELCYDPFKYYKINELEKFVNALEKCCMVTSSWQVFDKTHGEKQEDDKEKDINFIKNQEDVSLMKIPWMTENNTRELAPFIREIDSIMSVNLGYDDEDEEEGFFDGDEDREMGNKSKRNVLLKDENFMVEEYYEDDCGINDDNSDNKGQNCQSDVTKNNSDDEDDDDNDDDYREDGADEDDEDDDHMGSTDDDEDDDEDRQAGESTKVQNFDKKNETPRKRKPTDLDNFEYDESPSFTNMDLTTPKKYKHTATGRFSIIESPSSSLLNAMDGSNEISSSQEEEKEDAHENHEGRSEGLLPGDELVSPSMSSSQEDKMVAIAGITYRENISSPLGKKSR
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
2Phosphorylation------MSSTMLDDV
------CCCCCCCCC		34.2230377154
189PhosphorylationPFIREIDSIMSVNLG
HHHHHHHHHEEEECC		26.3328889911
192PhosphorylationREIDSIMSVNLGYDD
HHHHHHEEEECCCCC		13.2428889911
256PhosphorylationNKGQNCQSDVTKNNS
CCCCCCCCCCCCCCC		35.9328889911
259PhosphorylationQNCQSDVTKNNSDDE
CCCCCCCCCCCCCCC		32.8028889911
263PhosphorylationSDVTKNNSDDEDDDD
CCCCCCCCCCCCCCC		56.6928889911
292PhosphorylationEDDDHMGSTDDDEDD
CCCCCCCCCCCCCCC		22.5328889911
293PhosphorylationDDDHMGSTDDDEDDD
CCCCCCCCCCCCCCH		37.4028889911
320PhosphorylationNFDKKNETPRKRKPT
CCCCCCCCCCCCCCC		37.4728889911
327PhosphorylationTPRKRKPTDLDNFEY
CCCCCCCCCCCCCCC		52.8319823750
334PhosphorylationTDLDNFEYDESPSFT
CCCCCCCCCCCCCCC		22.3728889911
337PhosphorylationDNFEYDESPSFTNMD
CCCCCCCCCCCCCCC		23.9724961812
339PhosphorylationFEYDESPSFTNMDLT
CCCCCCCCCCCCCCC		54.7228889911
341PhosphorylationYDESPSFTNMDLTTP
CCCCCCCCCCCCCCC		33.6924961812
346PhosphorylationSFTNMDLTTPKKYKH
CCCCCCCCCCCCEEC		36.4725521595
347PhosphorylationFTNMDLTTPKKYKHT
CCCCCCCCCCCEECC		40.1717563356
364PhosphorylationGRFSIIESPSSSLLN
CCEEEEECCCHHHHH		21.4820377248
367PhosphorylationSIIESPSSSLLNAMD
EEEECCCHHHHHHCC		28.5219779198
368PhosphorylationIIESPSSSLLNAMDG
EEECCCHHHHHHCCC		41.0119779198
376PhosphorylationLLNAMDGSNEISSSQ
HHHHCCCCCCCCCCH		27.3330377154
380PhosphorylationMDGSNEISSSQEEEK
CCCCCCCCCCHHHHH		20.1219779198
381PhosphorylationDGSNEISSSQEEEKE
CCCCCCCCCHHHHHH		41.5219779198
382PhosphorylationGSNEISSSQEEEKED
CCCCCCCCHHHHHHH		34.5219779198
409PhosphorylationLPGDELVSPSMSSSQ
CCCCCCCCCCCCCCH		24.7125752575
411PhosphorylationGDELVSPSMSSSQED
CCCCCCCCCCCCHHH		24.6430377154
413PhosphorylationELVSPSMSSSQEDKM
CCCCCCCCCCHHHHE		31.0425704821
414PhosphorylationLVSPSMSSSQEDKMV
CCCCCCCCCHHHHEE		27.6528889911
415PhosphorylationVSPSMSSSQEDKMVA
CCCCCCCCHHHHEEE		30.2225752575
427PhosphorylationMVAIAGITYRENISS
EEEEEEEEEEHHCCC		18.6624961812
428PhosphorylationVAIAGITYRENISSP
EEEEEEEEEHHCCCC		17.6321440633
433PhosphorylationITYRENISSPLGKKS
EEEEHHCCCCCCCCC		37.1722369663
434PhosphorylationTYRENISSPLGKKSR
EEEHHCCCCCCCCCC		21.9822369663
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_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PP4R2_YEAST !!
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_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP4C_YEASTPPH3physical
11805826
SPT5_YEASTSPT5physical
11805826
TRM3_YEASTTRM3physical
11805826
PP4R3_YEASTPSY2physical
11805826
PP4R3_YEASTPSY2physical
16085932
PP4C_YEASTPPH3physical
16085932
SPT4_YEASTSPT4physical
16085932
SPT5_YEASTSPT5physical
16085932
PP4C_YEASTPPH3physical
16554755
SSD1_YEASTSSD1physical
16554755
SPT5_YEASTSPT5physical
16554755
PP4R3_YEASTPSY2physical
16554755
PP4C_YEASTPPH3physical
16429126
PP4R3_YEASTPSY2physical
16429126
SPT5_YEASTSPT5physical
16429126
TRM3_YEASTTRM3physical
16429126
SSD1_YEASTSSD1physical
16299494
SPT5_YEASTSPT5physical
16299494
PP4R3_YEASTPSY2physical
16299494
PP4C_YEASTPPH3physical
16299494
H2B1_YEASTHTB1physical
16299494
H2B2_YEASTHTB2physical
16299494
SPT4_YEASTSPT4physical
16299494
RFA2_YEASTRFA2genetic
19269370
HSP31_YEASTHSP31physical
19536198
H2A1_YEASTHTA1physical
18647348
H2A2_YEASTHTA2physical
18647348
PP4R3_YEASTPSY2physical
20826334
FUS3_YEASTFUS3genetic
21127252
APC11_YEASTAPC11genetic
27708008
PRP9_YEASTPRP9genetic
27708008
DPOD_YEASTPOL3genetic
27708008
UBC3_YEASTCDC34genetic
27708008
TAF12_YEASTTAF12genetic
27708008
TFB1_YEASTTFB1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
STT3_YEASTSTT3genetic
27708008
CDC20_YEASTCDC20genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
ARP3_YEASTARP3genetic
27708008
CDC11_YEASTCDC11genetic
27708008
NTR2_YEASTNTR2genetic
27708008
TAD3_YEASTTAD3genetic
27708008
VTI1_YEASTVTI1genetic
27708008
RFC4_YEASTRFC4genetic
27708008
CH10_YEASTHSP10genetic
27708008
APC5_YEASTAPC5genetic
27708008
NAB3_YEASTNAB3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PP4R2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414 AND SER-415, ANDMASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-347 AND SER-434, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND MASSSPECTROMETRY.

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