RCN2_YEAST - dbPTM
RCN2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RCN2_YEAST
UniProt AC Q12044
Protein Name Regulator of calcineurin 2
Gene Name RCN2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 265
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MANQKQMRTQILITDIPSGKFTSKWPTQLEKTLFKEQFPNLQSHLQYYTPLPFLNRIIIIFDNEDDTLQVFKFLQELLAKENSGPMKLFVTESLLNNQHPRSRSTDDAVSLQDNNLALLEDHRNKPLLSINTDPGVTGVDSSSLNKGGSSLSPDKSSLESPTMLKLSTDSKPFSYQEPLPKLSRSSSSTSNLSLNRSSQTSLPSQLENKDKSASGTKCLFASKPLGLTIDTSTRSNAASCTENDVNATASNPPKSPSITVNEFFH
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
14PhosphorylationMRTQILITDIPSGKF
HCEEEEEEECCCCCC		25.1630377154
20AcetylationITDIPSGKFTSKWPT
EEECCCCCCCCCCCC		50.2124489116
24AcetylationPSGKFTSKWPTQLEK
CCCCCCCCCCCHHHH		54.8824489116
31AcetylationKWPTQLEKTLFKEQF
CCCCHHHHHHHHHHC		60.1524489116
72UbiquitinationDDTLQVFKFLQELLA
CCHHHHHHHHHHHHH		46.4317644757
87UbiquitinationKENSGPMKLFVTESL
HCCCCCCEEEEEHHH		41.7417644757
102PhosphorylationLNNQHPRSRSTDDAV
HCCCCCCCCCCCCCC		34.7322369663
104PhosphorylationNQHPRSRSTDDAVSL
CCCCCCCCCCCCCHH		37.1222369663
105PhosphorylationQHPRSRSTDDAVSLQ
CCCCCCCCCCCCHHH		36.4722369663
110PhosphorylationRSTDDAVSLQDNNLA
CCCCCCCHHHCCCCE		23.2522369663
129PhosphorylationHRNKPLLSINTDPGV
HCCCCCEEEECCCCC		22.8322369663
132PhosphorylationKPLLSINTDPGVTGV
CCCEEEECCCCCCCC		41.7322369663
137PhosphorylationINTDPGVTGVDSSSL
EECCCCCCCCCHHHC		37.0929136822
141PhosphorylationPGVTGVDSSSLNKGG
CCCCCCCHHHCCCCC		21.3024909858
142PhosphorylationGVTGVDSSSLNKGGS
CCCCCCHHHCCCCCC		34.0929136822
143PhosphorylationVTGVDSSSLNKGGSS
CCCCCHHHCCCCCCC		39.6629136822
149PhosphorylationSSLNKGGSSLSPDKS
HHCCCCCCCCCCCHH		36.4522369663
150PhosphorylationSLNKGGSSLSPDKSS
HCCCCCCCCCCCHHH		35.8222369663
152PhosphorylationNKGGSSLSPDKSSLE
CCCCCCCCCCHHHCC		32.7622369663
156PhosphorylationSSLSPDKSSLESPTM
CCCCCCHHHCCCCCE		47.7622369663
157PhosphorylationSLSPDKSSLESPTML
CCCCCHHHCCCCCEE		41.7322369663
160PhosphorylationPDKSSLESPTMLKLS
CCHHHCCCCCEEEEC		30.8522369663
162PhosphorylationKSSLESPTMLKLSTD
HHHCCCCCEEEECCC		44.4022369663
168PhosphorylationPTMLKLSTDSKPFSY
CCEEEECCCCCCCCC		55.5222369663
170PhosphorylationMLKLSTDSKPFSYQE
EEEECCCCCCCCCCC		42.1719779198
171AcetylationLKLSTDSKPFSYQEP
EEECCCCCCCCCCCC		53.5524489116
174PhosphorylationSTDSKPFSYQEPLPK
CCCCCCCCCCCCCCC		34.1422369663
175PhosphorylationTDSKPFSYQEPLPKL
CCCCCCCCCCCCCCC		19.7828132839
181AcetylationSYQEPLPKLSRSSSS
CCCCCCCCCCCCCCC		67.7724489116
183PhosphorylationQEPLPKLSRSSSSTS
CCCCCCCCCCCCCCC		35.9222369663
185PhosphorylationPLPKLSRSSSSTSNL
CCCCCCCCCCCCCCC		31.0622369663
186PhosphorylationLPKLSRSSSSTSNLS
CCCCCCCCCCCCCCC		27.4822369663
187PhosphorylationPKLSRSSSSTSNLSL
CCCCCCCCCCCCCCC		38.5922369663
188PhosphorylationKLSRSSSSTSNLSLN
CCCCCCCCCCCCCCC		37.4922369663
189PhosphorylationLSRSSSSTSNLSLNR
CCCCCCCCCCCCCCC		24.4722369663
190PhosphorylationSRSSSSTSNLSLNRS
CCCCCCCCCCCCCCC		37.4122369663
193PhosphorylationSSSTSNLSLNRSSQT
CCCCCCCCCCCCCCC		28.0522369663
197PhosphorylationSNLSLNRSSQTSLPS
CCCCCCCCCCCCCCH		26.2322369663
198PhosphorylationNLSLNRSSQTSLPSQ
CCCCCCCCCCCCCHH		33.9522369663
200PhosphorylationSLNRSSQTSLPSQLE
CCCCCCCCCCCHHHC		33.8922369663
201PhosphorylationLNRSSQTSLPSQLEN
CCCCCCCCCCHHHCC		30.5522369663
204PhosphorylationSSQTSLPSQLENKDK
CCCCCCCHHHCCCCC		53.3322369663
217AcetylationDKSASGTKCLFASKP
CCCCCCCEEEEECCC		32.2525381059
239PhosphorylationSTRSNAASCTENDVN
CCCCCCCCCCCCCCC		21.1119779198
241PhosphorylationRSNAASCTENDVNAT
CCCCCCCCCCCCCCC		35.0126447709
248PhosphorylationTENDVNATASNPPKS
CCCCCCCCCCCCCCC		25.9726447709
250PhosphorylationNDVNATASNPPKSPS
CCCCCCCCCCCCCCC		45.5822369663
255PhosphorylationTASNPPKSPSITVNE
CCCCCCCCCCEEHHC		29.6522369663
257PhosphorylationSNPPKSPSITVNEFF
CCCCCCCCEEHHCCC		37.6722369663
259PhosphorylationPPKSPSITVNEFFH-
CCCCCCEEHHCCCC-		22.9322890988
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 RCN2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
152SPhosphorylation

17330950
160SPhosphorylation

17330950
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 RCN2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUP2_YEASTCUP2physical
10688190
TAF6_YEASTTAF6physical
11283351
RCN1_YEASTRCN1genetic
19273587
DCOR_YEASTSPE1genetic
27708008
UBR2_YEASTUBR2genetic
27708008
ATG8_YEASTATG8genetic
27708008
CSN9_YEASTCSN9genetic
27708008
MSH4_YEASTMSH4genetic
27708008
ATG1_YEASTATG1genetic
27708008
LPLA_YEASTAIM22genetic
27708008
SSH4_YEASTSSH4genetic
27708008
NNK1_YEASTNNK1genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
ERG3_YEASTERG3genetic
27708008
YL149_YEASTYLR149Cgenetic
27708008
LIPB_YEASTLIP2genetic
27708008
ARV1_YEASTARV1genetic
27708008
FKS1_YEASTFKS1genetic
27708008
VIP1_YEASTVIP1genetic
27708008
ATG3_YEASTATG3genetic
27708008
CHMU_YEASTARO7genetic
27708008
PP2B1_YEASTCNA1physical
24930733
PP2B2_YEASTCMP2physical
24930733
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RCN2_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-102; SER-104; THR-105;SER-110; THR-132; SER-150; SER-152; SER-156; SER-157; SER-160;THR-162; SER-183; SER-185; SER-186; SER-187; SER-188; THR-189;SER-193; SER-197; SER-198; THR-200; SER-201; SER-255 AND SER-257, 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 SER-102; SER-104; SER-110;THR-132; SER-152; SER-160; SER-183; SER-186; SER-187; THR-189;SER-198; SER-201 AND SER-257, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; THR-132; SER-152;SER-160 AND SER-183, AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-160, 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: PROTEIN SEQUENCE OF 102-123 AND 147-196, PHOSPHORYLATION [LARGE SCALEANALYSIS] AT SER-104; THR-105; SER-152; SER-157; SER-160; SER-183 ANDSER-193, AND MASS SPECTROMETRY.

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