ECM30_YEAST - dbPTM
ECM30_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECM30_YEAST
UniProt AC Q06673
Protein Name Protein ECM30
Gene Name ECM30
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1274
Subcellular Localization Cytoplasm .
Protein Description Seems to be involved in cell wall organization and biogenesis..
Protein Sequence MGNTDSKSSSILLNHCIALVRPEDADASSPSRTSSPSPSLSVDADPLSLNLSIFKLDSGPDVEALFSDKPNVPLDTVFNDFYLDFISVDVQDFSINSSFKKILHIISSLNPPNFNNLIVFLSLYIILSANSLPASRTGLHSSRLINAIKTLSILIPIYFDRVKSSTQDHYDVFWATQHEIEGLPLQNIPLGERLLLAILKLAFQDNFTTAVTAHPSELWEIGILTNSNKYRSLLNMHHQWHLFANRLLLLRLLAALFSSDLYTSGGKQDINMFLVYWCTQMPKDKSIQFTSSLLNCTMRFILNNNKDFQSLKANFFSSDATASNWQTLYFQFVQSCLHVLNLSMSYKAQDNVITIFLTQLQREYDLKLILSSFIKIFKYPIDLAIEQESNIFNFTNNKHIDASRRRAVSTSSHDNSSSSHASLPSSSSAAYHTKPQTKPQLPEIHPLLIPMTILMTNLIDCNKCFQNYFADKFASRFIIFSIYYLKYYDYSSLSSSSSTTRSNSSTTSNGTSNDTSNERSIVELNENSVSQILLPLLNHLLLILTSKKLVLFKMLQTFNLNYYTNNLPNFYKLSNINGDINNLTFRDFTVIQLSNLILDNIKFNLQPNPIFYELIYNLLPINDEILTSSHKNDDSHDDLILLSAKKKSASPSAATSSHTSSSKLSYNAAMSLLYVLSKSSNKVYLTTYATPVFKTKDIPYMISPGFKMDLLALLLRSITIFFTLYFDDAENLLFAMVRHQSITHQINDSINSISKALDMNPNLNSHIMTLKQMGFNRKVQWKDFYQFEEITDLPQVNLYSSANQQHQNQQQGQNDNRGQNQNEDPGQENESPTPYLLFNPASLENETPGTVKHFSSTNHDKNYQVIAFIDFKSDSNLNLQHQLEYWPHRPQWPTPLTFTHKCKNPKYENFNEVWSGTVYLQILLRVIKQILSKVPEIPRIKSVQYFETLSKLSALRSDILTTIHPRLPLDVRRLTTFQPLSMHTNDKLLMWFHIATWANIFTQTSFKYEETFSHELRQFESLLDISIDECEGNTISKPTTDRLGYIRRSRGQSSVSLERTISAGSGVSTPTMALNRTKSNGSGNLMNYFFQNTAQNHFQHLRSSSSSSSITLEKTTSNSSSIRTRPNSHHVAPETNNNNSTNGNSNNSSNGGFSFFKWKWGGNNSNGGSDDTKASQRDPNVSTSIITDNLNSYMFEEEISPGVVNNIIENNIWVGTDIRLFKIANFRKESFSFLEMTSSFFKKFKFINSDNDNYNNNEFDDNTQLRYTSRGLYR
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
416PhosphorylationSTSSHDNSSSSHASL
ECCCCCCCCCCCCCC		37.3430377154
417PhosphorylationTSSHDNSSSSHASLP
CCCCCCCCCCCCCCC		41.9630377154
418PhosphorylationSSHDNSSSSHASLPS
CCCCCCCCCCCCCCC		26.4330377154
492PhosphorylationLKYYDYSSLSSSSST
HHHCCCCCCCCCCCC		26.4928889911
499PhosphorylationSLSSSSSTTRSNSST
CCCCCCCCCCCCCCC		28.3328889911
504PhosphorylationSSTTRSNSSTTSNGT
CCCCCCCCCCCCCCC		30.2428889911
507PhosphorylationTRSNSSTTSNGTSND
CCCCCCCCCCCCCCC		23.3428889911
508PhosphorylationRSNSSTTSNGTSNDT
CCCCCCCCCCCCCCC		33.0923749301
515PhosphorylationSNGTSNDTSNERSIV
CCCCCCCCCCCCEEE		37.3927017623
562PhosphorylationLQTFNLNYYTNNLPN
HHHCCCCHHCCCCCC		18.1627017623
563PhosphorylationQTFNLNYYTNNLPNF
HHCCCCHHCCCCCCE		11.2627017623
564PhosphorylationTFNLNYYTNNLPNFY
HCCCCHHCCCCCCEE		13.7927017623
571PhosphorylationTNNLPNFYKLSNING
CCCCCCEEECCCCCC		20.0527017623
635PhosphorylationSSHKNDDSHDDLILL
CCCCCCCCCCCEEEE		31.5122369663
650PhosphorylationSAKKKSASPSAATSS
EECCCCCCCCCCCCC		26.8623749301
652PhosphorylationKKKSASPSAATSSHT
CCCCCCCCCCCCCCC		28.2128889911
666PhosphorylationTSSSKLSYNAAMSLL
CCCCHHCHHHHHHHH		21.1827017623
671PhosphorylationLSYNAAMSLLYVLSK
HCHHHHHHHHHHHHC		15.5327017623
771AcetylationNSHIMTLKQMGFNRK
HHHHHHHHHCCCCCC		29.1325381059
1049PhosphorylationRLGYIRRSRGQSSVS
CHHHHCCCCCCCCEE		30.8022369663
1053PhosphorylationIRRSRGQSSVSLERT
HCCCCCCCCEEEEEE		35.2222369663
1054PhosphorylationRRSRGQSSVSLERTI
CCCCCCCCEEEEEEE		14.0822369663
1056PhosphorylationSRGQSSVSLERTISA
CCCCCCEEEEEEEEC		26.8522369663
1060PhosphorylationSSVSLERTISAGSGV
CCEEEEEEEECCCCC		15.2022369663
1062PhosphorylationVSLERTISAGSGVST
EEEEEEEECCCCCCC		26.4322369663
1065PhosphorylationERTISAGSGVSTPTM
EEEEECCCCCCCCEE		35.4222369663
1068PhosphorylationISAGSGVSTPTMALN
EECCCCCCCCEEEEC		31.9922369663
1069PhosphorylationSAGSGVSTPTMALNR
ECCCCCCCCEEEECC		22.0022369663
1071PhosphorylationGSGVSTPTMALNRTK
CCCCCCCEEEECCCC		18.3722369663
1077PhosphorylationPTMALNRTKSNGSGN
CEEEECCCCCCCCCC		37.4428889911
1079PhosphorylationMALNRTKSNGSGNLM
EEECCCCCCCCCCHH		45.9022369663
1082PhosphorylationNRTKSNGSGNLMNYF
CCCCCCCCCCHHHHH		28.8522369663
1088PhosphorylationGSGNLMNYFFQNTAQ
CCCCHHHHHHHHHHH		7.5722369663
1093PhosphorylationMNYFFQNTAQNHFQH
HHHHHHHHHHHHHHH		20.8822369663
1103PhosphorylationNHFQHLRSSSSSSSI
HHHHHHHCCCCCCCE		40.7222369663
1104PhosphorylationHFQHLRSSSSSSSIT
HHHHHHCCCCCCCEE		28.0122369663
1105PhosphorylationFQHLRSSSSSSSITL
HHHHHCCCCCCCEEE		35.1722369663
1106PhosphorylationQHLRSSSSSSSITLE
HHHHCCCCCCCEEEE		35.8722369663
1107PhosphorylationHLRSSSSSSSITLEK
HHHCCCCCCCEEEEE		30.0122369663
1108PhosphorylationLRSSSSSSSITLEKT
HHCCCCCCCEEEEEE		27.9222369663
1109PhosphorylationRSSSSSSSITLEKTT
HCCCCCCCEEEEEEC		22.8822369663
1111PhosphorylationSSSSSSITLEKTTSN
CCCCCCEEEEEECCC		30.7122369663
1115PhosphorylationSSITLEKTTSNSSSI
CCEEEEEECCCCCCC		26.5321551504
1117PhosphorylationITLEKTTSNSSSIRT
EEEEEECCCCCCCCC		39.6928889911
1119PhosphorylationLEKTTSNSSSIRTRP
EEEECCCCCCCCCCC		25.8221551504
1120PhosphorylationEKTTSNSSSIRTRPN
EEECCCCCCCCCCCC		33.7530377154
1128PhosphorylationSIRTRPNSHHVAPET
CCCCCCCCCCCCCCC		20.0421551504
1230PhosphorylationIANFRKESFSFLEMT
ECCCCHHHCCHHHHC		29.2621551504
1237PhosphorylationSFSFLEMTSSFFKKF
HCCHHHHCHHHHHHC		16.3121551504
1238PhosphorylationFSFLEMTSSFFKKFK
CCHHHHCHHHHHHCC		24.6821551504
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 ECM30_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECM30_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 ECM30_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBB_YEASTTUB2physical
16429126
UBP15_YEASTUBP15physical
16429126
PYR1_YEASTURA2physical
16429126
GET1_YEASTGET1genetic
19325107
GET2_YEASTGET2genetic
19325107
GET3_YEASTGET3genetic
19325107
GLO3_YEASTGLO3genetic
19325107
PLMT_YEASTOPI3genetic
19325107
PER1_YEASTPER1genetic
19325107
SKY1_YEASTSKY1genetic
19325107
ATC6_YEASTSPF1genetic
19325107
SRB8_YEASTSRB8genetic
19325107
VPS9_YEASTVPS9genetic
19325107
ARL1_YEASTARL1genetic
19325107
RSP5_YEASTRSP5genetic
27708008
BOS1_YEASTBOS1genetic
27708008
ARO1_YEASTARO1genetic
27708008
SNF1_YEASTSNF1genetic
27708008
AK_YEASTHOM3genetic
27708008
AROC_YEASTARO2genetic
27708008
SERB_YEASTSER2genetic
27708008
ENV10_YEASTENV10genetic
27708008
ALAM_YEASTALT1genetic
27708008
MKS1_YEASTMKS1genetic
27708008
RTG1_YEASTRTG1genetic
27708008
SERC_YEASTSER1genetic
27708008
CHMU_YEASTARO7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ECM30_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-635; SER-1056; THR-1060;SER-1062; SER-1065; SER-1105 AND SER-1106, 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-1053; SER-1054 ANDSER-1056, 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-1065, AND MASSSPECTROMETRY.

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