ACA2_YEAST - dbPTM
ACA2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACA2_YEAST
UniProt AC P40535
Protein Name ATF/CREB activator 2
Gene Name CST6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 587
Subcellular Localization Nucleus.
Protein Description Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources..
Protein Sequence MFTGQEYHSVDSNSNKQKDNNKRGIDDTSKILNNKIPHSVSDTSAAATTTSTMNNSALSRSLDPTDINYSTNMAGVVDQIHDYTTSNRNSLTPQYSIAAGNVNSHDRVVKPSANSNYQQAAYLRQQQQQDQRQQSPSMKTEEESQLYGDILMNSGVVQDMHQNLATHTNLSQLSSTRKSAPNDSTTAPTNASNIANTASVNKQMYFMNMNMNNNPHALNDPSILETLSPFFQPFGVDVAHLPMTNPPIFQSSLPGCDEPIRRRRISISNGQISQLGEDIETLENLHNTQPPPMPNFHNYNGLSQTRNVSNKPVFNQAVPVSSIPQYNAKKVINPTKDSALGDQSVIYSKSQQRNFVNAPSKNTPAESISDLEGMTTFAPTTGGENRGKSALRESHSNPSFTPKSQGSHLNLAANTQGNPIPGTTAWKRARLLERNRIAASKCRQRKKVAQLQLQKEFNEIKDENRILLKKLNYYEKLISKFKKFSKIHLREHEKLNKDSDNNVNGTNSSNKNESMTVDSLKIIEELLMIDSDVTEVDKDTGKIIAIKHEPYSQRFGSDTDDDDIDLKPVEGGKDPDNQSLPNSEKIK
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
3Phosphorylation-----MFTGQEYHSV
-----CCCCCCCCCC		36.3430377154
9PhosphorylationFTGQEYHSVDSNSNK
CCCCCCCCCCCCCCC		27.0730377154
12PhosphorylationQEYHSVDSNSNKQKD
CCCCCCCCCCCCCCC		39.7530377154
14PhosphorylationYHSVDSNSNKQKDNN
CCCCCCCCCCCCCCC		49.7230377154
30AcetylationRGIDDTSKILNNKIP
CCCCHHHHHHHCCCC		53.9925381059
39PhosphorylationLNNKIPHSVSDTSAA
HHCCCCCCCCCCCCC		20.2622369663
41PhosphorylationNKIPHSVSDTSAAAT
CCCCCCCCCCCCCCC		37.8822369663
43PhosphorylationIPHSVSDTSAAATTT
CCCCCCCCCCCCCCC		16.8622369663
44PhosphorylationPHSVSDTSAAATTTS
CCCCCCCCCCCCCCC		22.3922369663
48PhosphorylationSDTSAAATTTSTMNN
CCCCCCCCCCCCCCC		26.3622369663
49PhosphorylationDTSAAATTTSTMNNS
CCCCCCCCCCCCCCC		17.6422369663
50PhosphorylationTSAAATTTSTMNNSA
CCCCCCCCCCCCCCH		20.1822369663
59PhosphorylationTMNNSALSRSLDPTD
CCCCCHHHCCCCCCC		21.3819779198
84PhosphorylationVDQIHDYTTSNRNSL
HHHHHHCCCCCCCCC		29.7927017623
86PhosphorylationQIHDYTTSNRNSLTP
HHHHCCCCCCCCCCC		26.4530377154
90PhosphorylationYTTSNRNSLTPQYSI
CCCCCCCCCCCCEEE		30.3122369663
92PhosphorylationTSNRNSLTPQYSIAA
CCCCCCCCCCEEEEC		14.2522369663
95PhosphorylationRNSLTPQYSIAAGNV
CCCCCCCEEEECCCC		11.8422369663
110AcetylationNSHDRVVKPSANSNY
CCCCCCCCCCCCCHH		30.3324489116
110UbiquitinationNSHDRVVKPSANSNY
CCCCCCCCCCCCCHH		30.3317644757
117PhosphorylationKPSANSNYQQAAYLR
CCCCCCHHHHHHHHH		11.2124961812
122PhosphorylationSNYQQAAYLRQQQQQ
CHHHHHHHHHHHHHH		12.8724961812
135PhosphorylationQQDQRQQSPSMKTEE
HHHHHHHCCCCCHHH		15.5928889911
137PhosphorylationDQRQQSPSMKTEEES
HHHHHCCCCCHHHHH		37.8524961812
171PhosphorylationLATHTNLSQLSSTRK
HHHHCCHHHHHHCCC		31.0128889911
178UbiquitinationSQLSSTRKSAPNDST
HHHHHCCCCCCCCCC		51.5723749301
179PhosphorylationQLSSTRKSAPNDSTT
HHHHCCCCCCCCCCC		45.7429136822
184PhosphorylationRKSAPNDSTTAPTNA
CCCCCCCCCCCCCCH		34.0119779198
185PhosphorylationKSAPNDSTTAPTNAS
CCCCCCCCCCCCCHH		29.8229136822
186PhosphorylationSAPNDSTTAPTNASN
CCCCCCCCCCCCHHH		34.2929136822
189PhosphorylationNDSTTAPTNASNIAN
CCCCCCCCCHHHHCH		40.7429136822
192PhosphorylationTTAPTNASNIANTAS
CCCCCCHHHHCHHHH		30.7329136822
197PhosphorylationNASNIANTASVNKQM
CHHHHCHHHHHCCEE		15.9930377154
199PhosphorylationSNIANTASVNKQMYF
HHHCHHHHHCCEEEE		24.9629136822
266PhosphorylationPIRRRRISISNGQIS
CHHCCCEEECCCCHH		20.3923607784
268PhosphorylationRRRRISISNGQISQL
HCCCEEECCCCHHHC		28.2823607784
273PhosphorylationSISNGQISQLGEDIE
EECCCCHHHCCCCHH		16.0923607784
281PhosphorylationQLGEDIETLENLHNT
HCCCCHHHHHHHHCC		39.4423607784
309PhosphorylationLSQTRNVSNKPVFNQ
CCCCCCCCCCCCCCC		42.5622369663
321PhosphorylationFNQAVPVSSIPQYNA
CCCCCCHHHCCCCCC		19.2430377154
322PhosphorylationNQAVPVSSIPQYNAK
CCCCCHHHCCCCCCC		38.2230377154
336AcetylationKKVINPTKDSALGDQ
CCCCCCCCCCCCCCC		51.4424489116
344PhosphorylationDSALGDQSVIYSKSQ
CCCCCCCCEEEEHHH		18.4121551504
349AcetylationDQSVIYSKSQQRNFV
CCCEEEEHHHCCCCC		35.0024489116
349UbiquitinationDQSVIYSKSQQRNFV
CCCEEEEHHHCCCCC		35.0023749301
360PhosphorylationRNFVNAPSKNTPAES
CCCCCCCCCCCCCHH		35.8121440633
363PhosphorylationVNAPSKNTPAESISD
CCCCCCCCCCHHHHH		27.8422369663
367PhosphorylationSKNTPAESISDLEGM
CCCCCCHHHHHHCCC		29.5122369663
369PhosphorylationNTPAESISDLEGMTT
CCCCHHHHHHCCCCE		45.4822369663
376PhosphorylationSDLEGMTTFAPTTGG
HHHCCCCEECCCCCC		14.6519779198
394PhosphorylationGKSALRESHSNPSFT
HHHHHHHHCCCCCCC		26.2820377248
396PhosphorylationSALRESHSNPSFTPK
HHHHHHCCCCCCCCC		60.7722369663
399PhosphorylationRESHSNPSFTPKSQG
HHHCCCCCCCCCCCC		46.1022369663
401PhosphorylationSHSNPSFTPKSQGSH
HCCCCCCCCCCCCCC		33.8622369663
403UbiquitinationSNPSFTPKSQGSHLN
CCCCCCCCCCCCCEE		52.9717644757
404PhosphorylationNPSFTPKSQGSHLNL
CCCCCCCCCCCCEEE		40.7622369663
407PhosphorylationFTPKSQGSHLNLAAN
CCCCCCCCCEEEEEC		19.7122369663
415PhosphorylationHLNLAANTQGNPIPG
CEEEEECCCCCCCCC		32.8822369663
423PhosphorylationQGNPIPGTTAWKRAR
CCCCCCCCHHHHHHH		14.1622369663
424PhosphorylationGNPIPGTTAWKRARL
CCCCCCCHHHHHHHH		36.1122369663
427UbiquitinationIPGTTAWKRARLLER
CCCCHHHHHHHHHHH		33.4417644757
427AcetylationIPGTTAWKRARLLER
CCCCHHHHHHHHHHH		33.4425381059
497AcetylationREHEKLNKDSDNNVN
HHHHHHCCCCCCCCC		69.8825381059
499PhosphorylationHEKLNKDSDNNVNGT
HHHHCCCCCCCCCCC		43.7930377154
514PhosphorylationNSSNKNESMTVDSLK
CCCCCCCCCCHHHHH		29.1930377154
516PhosphorylationSNKNESMTVDSLKII
CCCCCCCCHHHHHHH		30.3630377154
547AcetylationTGKIIAIKHEPYSQR
CCCEEEEECCCCHHH		32.6625381059
551PhosphorylationIAIKHEPYSQRFGSD
EEEECCCCHHHCCCC		17.9119823750
552PhosphorylationAIKHEPYSQRFGSDT
EEECCCCHHHCCCCC		26.1220377248
557PhosphorylationPYSQRFGSDTDDDDI
CCHHHCCCCCCCCCC		34.3322369663
559PhosphorylationSQRFGSDTDDDDIDL
HHHCCCCCCCCCCCC		42.9222369663
579PhosphorylationGKDPDNQSLPNSEKI
CCCCCCCCCCCCCCC		52.6422369663
583PhosphorylationDNQSLPNSEKIK---
CCCCCCCCCCCC---		38.0222369663
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 ACA2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACA2_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 ACA2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACA1_YEASTACA1genetic
10825197
HMO1_YEASTHMO1physical
16554755
MAM33_YEASTMAM33physical
16554755
IDI1_YEASTIDI1physical
18467557
HOS2_YEASTHOS2genetic
20959818
MRM2_YEASTMRM2genetic
27708008
RAD1_YEASTRAD1genetic
27708008
ECM15_YEASTECM15genetic
27708008
ELO2_YEASTELO2genetic
27708008
PAT1_YEASTPAT1genetic
27708008
PDP2_YEASTPTC6genetic
27708008
GCN1_YEASTGCN1genetic
27708008
EI2BA_YEASTGCN3genetic
27708008
RS10A_YEASTRPS10Agenetic
27708008
ISW2_YEASTISW2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACA2_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-90; SER-171; SER-266;SER-396; SER-404; SER-407; SER-557 AND THR-559, 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-394; SER-396; SER-557AND THR-559, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396; SER-399; SER-557AND THR-559, 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-557 AND THR-559, ANDMASS SPECTROMETRY.

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