RTS3_YEAST - dbPTM
RTS3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTS3_YEAST
UniProt AC P53289
Protein Name Protein phosphatase type 2A regulatory subunit RTS3
Gene Name RTS3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 263
Subcellular Localization Cytoplasm . Nucleus .
Protein Description May be a component of a protein phosphatase type 2A (PP2A) complex. Negatively regulates SIT4 phosphatase, a modulators of caffeine sensitivity..
Protein Sequence MIATSRAVNMNKESKHKKAVAKPCRERQTSVTRAMRPAVARDPRRLSTSSSPSSSPMSAQRRLSREEIINEMEKEQDAIVVRLLREIETLKEENSRLKNQLHHPVPARRSSPFFEGESAILDDDDCNYGYTLDTPKLKLTDGASRHTVLPLTPKDSMTHISHSARRSSRNASISNGTSISDTIFPIETKIHSAPTTNRNLPSADLPHHTLLPRSLSGISSSDLTESGALLHDRRRRSSNYSLDGSNSLKADLMAKRFQTGSLK
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
47PhosphorylationARDPRRLSTSSSPSS
HCCCCCCCCCCCCCC
25.1622369663
48PhosphorylationRDPRRLSTSSSPSSS
CCCCCCCCCCCCCCC
36.9022369663
49PhosphorylationDPRRLSTSSSPSSSP
CCCCCCCCCCCCCCC
25.9922369663
50PhosphorylationPRRLSTSSSPSSSPM
CCCCCCCCCCCCCCH
46.4822369663
51PhosphorylationRRLSTSSSPSSSPMS
CCCCCCCCCCCCCHH
28.6822369663
53PhosphorylationLSTSSSPSSSPMSAQ
CCCCCCCCCCCHHHH
45.4522369663
54PhosphorylationSTSSSPSSSPMSAQR
CCCCCCCCCCHHHHH
41.6722369663
55PhosphorylationTSSSPSSSPMSAQRR
CCCCCCCCCHHHHHH
29.0322369663
58PhosphorylationSPSSSPMSAQRRLSR
CCCCCCHHHHHHHCH
25.3222369663
74UbiquitinationEIINEMEKEQDAIVV
HHHHHHHHHHHHHHH
60.4017644757
91UbiquitinationLREIETLKEENSRLK
HHHHHHHHHHHHHHH
71.1017644757
98UbiquitinationKEENSRLKNQLHHPV
HHHHHHHHHHCCCCC
41.3517644757
110PhosphorylationHPVPARRSSPFFEGE
CCCCCCCCCCCCCCC
36.4917563356
111PhosphorylationPVPARRSSPFFEGES
CCCCCCCCCCCCCCC
24.7421440633
118PhosphorylationSPFFEGESAILDDDD
CCCCCCCCCCCCCCC
31.3128889911
152PhosphorylationRHTVLPLTPKDSMTH
CCCEEECCCCCCCHH
26.7617563356
154UbiquitinationTVLPLTPKDSMTHIS
CEEECCCCCCCHHHC
58.1417644757
156PhosphorylationLPLTPKDSMTHISHS
EECCCCCCCHHHCHH
31.5424961812
158PhosphorylationLTPKDSMTHISHSAR
CCCCCCCHHHCHHHH
21.7324961812
161PhosphorylationKDSMTHISHSARRSS
CCCCHHHCHHHHHHH
12.0924961812
163PhosphorylationSMTHISHSARRSSRN
CCHHHCHHHHHHHCC
19.3824961812
167PhosphorylationISHSARRSSRNASIS
HCHHHHHHHCCCCCC
28.2624961812
168PhosphorylationSHSARRSSRNASISN
CHHHHHHHCCCCCCC
27.9524961812
172PhosphorylationRRSSRNASISNGTSI
HHHHCCCCCCCCCCC
30.0528152593
174PhosphorylationSSRNASISNGTSISD
HHCCCCCCCCCCCCC
27.0628889911
177PhosphorylationNASISNGTSISDTIF
CCCCCCCCCCCCCEE
27.4319779198
180PhosphorylationISNGTSISDTIFPIE
CCCCCCCCCCEEEEE
28.5927017623
188PhosphorylationDTIFPIETKIHSAPT
CCEEEEEEEECCCCC
35.7027017623
189UbiquitinationTIFPIETKIHSAPTT
CEEEEEEEECCCCCC
26.1517644757
192PhosphorylationPIETKIHSAPTTNRN
EEEEEECCCCCCCCC
39.1417563356
214PhosphorylationHHTLLPRSLSGISSS
CCCCCCCCCCCCCHH
25.5822369663
216PhosphorylationTLLPRSLSGISSSDL
CCCCCCCCCCCHHHC
35.0122369663
219PhosphorylationPRSLSGISSSDLTES
CCCCCCCCHHHCCCC
27.5822369663
220PhosphorylationRSLSGISSSDLTESG
CCCCCCCHHHCCCCC
26.4222369663
221PhosphorylationSLSGISSSDLTESGA
CCCCCCHHHCCCCCC
29.8322369663
224PhosphorylationGISSSDLTESGALLH
CCCHHHCCCCCCCCC
32.8522369663
226PhosphorylationSSSDLTESGALLHDR
CHHHCCCCCCCCCCC
24.9122369663
237PhosphorylationLHDRRRRSSNYSLDG
CCCCCHHCCCCCCCC
22.5622369663
238PhosphorylationHDRRRRSSNYSLDGS
CCCCHHCCCCCCCCC
37.6722369663
240PhosphorylationRRRRSSNYSLDGSNS
CCHHCCCCCCCCCCC
16.7422369663
241PhosphorylationRRRSSNYSLDGSNSL
CHHCCCCCCCCCCCH
25.0022369663
245PhosphorylationSNYSLDGSNSLKADL
CCCCCCCCCCHHHHH
23.9428132839
247PhosphorylationYSLDGSNSLKADLMA
CCCCCCCCHHHHHHH
32.7019779198
255UbiquitinationLKADLMAKRFQTGSL
HHHHHHHHHHCCCCC
39.5217644757
261PhosphorylationAKRFQTGSLK-----
HHHHCCCCCC-----
36.0529136822
263UbiquitinationRFQTGSLK-------
HHCCCCCC-------
61.0517644757

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 RTS3_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTS3_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 RTS3_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SA185_YEASTSAP185physical
16554755
2ABA_YEASTCDC55physical
16429126
PP2A1_YEASTPPH21physical
16429126
2AAA_YEASTTPD3physical
16429126
BCH2_YEASTBCH2physical
16429126
SA185_YEASTSAP185physical
16429126
PP11_YEASTSIT4physical
16429126
DYN3_YEASTDYN3physical
18467557
RTG3_YEASTRTG3genetic
19269370
RV161_YEASTRVS161genetic
20093466
BRE1_YEASTBRE1genetic
20093466
PACC_YEASTRIM101genetic
20093466
HSE1_YEASTHSE1genetic
20093466
RS27B_YEASTRPS27Bgenetic
20093466
AIM18_YEASTAIM18genetic
20093466
FIS1_YEASTFIS1genetic
20093466
MRX5_YEASTYJL147Cgenetic
20093466
CYP7_YEASTCPR7genetic
20093466
COXM1_YEASTCMC1genetic
20093466
HAP4_YEASTHAP4genetic
20093466
BLI1_YEASTBLI1genetic
20093466
VPS24_YEASTVPS24genetic
20093466
IXR1_YEASTIXR1genetic
20093466
MRT4_YEASTMRT4genetic
20093466
DNM1_YEASTDNM1genetic
20093466
SIC1_YEASTSIC1genetic
20093466
SRN2_YEASTSRN2genetic
20093466
COX8_YEASTCOX8genetic
20093466
VPS9_YEASTVPS9genetic
20093466
MSS1_YEASTMSS1genetic
20093466
RIM13_YEASTRIM13genetic
20093466
PFKA2_YEASTPFK2genetic
20093466
MKS1_YEASTMKS1genetic
20093466
MAS5_YEASTYDJ1genetic
20093466
COX5A_YEASTCOX5Agenetic
20093466
VPS27_YEASTVPS27genetic
20093466
ATP23_YEASTATP23genetic
20093466
WHI2_YEASTWHI2genetic
20093466
2ABA_YEASTCDC55physical
20489023
SA190_YEASTSAP190physical
20489023
PP11_YEASTSIT4physical
20489023
SP110_YEASTSPC110physical
20489023
2AAA_YEASTTPD3physical
20489023
SDS24_YEASTSDS24genetic
21360731
SDS23_YEASTSDS23genetic
21360731
HSE1_YEASTHSE1genetic
21360731
PP11_YEASTSIT4genetic
21360731
RM49_YEASTMRP49genetic
27708008
CSG2_YEASTCSG2genetic
27708008
CCZ1_YEASTCCZ1genetic
27708008
CLPX_YEASTMCX1genetic
27708008
MGR1_YEASTMGR1genetic
27708008
RV161_YEASTRVS161genetic
27708008
MTU1_YEASTSLM3genetic
27708008
BRE1_YEASTBRE1genetic
27708008
ATG31_YEASTATG31genetic
27708008
DPB4_YEASTDPB4genetic
27708008
CHI2_YEASTCTS2genetic
27708008
SHE9_YEASTSHE9genetic
27708008
SNF1_YEASTSNF1genetic
27708008
TYW3_YEASTTYW3genetic
27708008
HSE1_YEASTHSE1genetic
27708008
SNF6_YEASTSNF6genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
COX23_YEASTCOX23genetic
27708008
FIS1_YEASTFIS1genetic
27708008
MRX5_YEASTYJL147Cgenetic
27708008
CYP7_YEASTCPR7genetic
27708008
ILM1_YEASTILM1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
MRT4_YEASTMRT4genetic
27708008
IXR1_YEASTIXR1genetic
27708008
HAP4_YEASTHAP4genetic
27708008
DOA1_YEASTDOA1genetic
27708008
DNM1_YEASTDNM1genetic
27708008
SRN2_YEASTSRN2genetic
27708008
ARV1_YEASTARV1genetic
27708008
ART10_YEASTART10genetic
27708008
ATP10_YEASTATP10genetic
27708008
COX8_YEASTCOX8genetic
27708008
RCF1_YEASTRCF1genetic
27708008
VPS9_YEASTVPS9genetic
27708008
MAC1_YEASTMAC1genetic
27708008
MSS1_YEASTMSS1genetic
27708008
SSO2_YEASTSSO2genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
MAS5_YEASTYDJ1genetic
27708008
VPS27_YEASTVPS27genetic
27708008
ATP23_YEASTATP23genetic
27708008
BRE5_YEASTBRE5genetic
27708008
WHI2_YEASTWHI2genetic
27708008
VPS4_YEASTVPS4genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RTS3_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-47; SER-49; SER-50;SER-51; SER-111; SER-118; THR-152; SER-172; SER-192; SER-216; SER-219;SER-238 AND SER-241, AND MASS 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 SER-110; THR-152; SER-192;SER-216; SER-219; SER-220 AND SER-238, AND MASS SPECTROMETRY.

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