ECM25_YEAST - dbPTM
ECM25_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECM25_YEAST
UniProt AC P32525
Protein Name Protein ECM25
Gene Name ECM25
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 599
Subcellular Localization Cytoplasm .
Protein Description May be involved in cell wall organization and biogenesis..
Protein Sequence MIDINVNNIFFRSYSVDPNSGHAIYVFDSTYLPASDEIGDKQVYDLLINALMDRLVMKLPQAPYSLVIFSSGFSQRKISWVYGIKMFAKLPKETKFYLQKIFIVHESFFVRSVYQVISNAMNFNFLDSKDSQHDFPSLVHVLDLTSLSELIDITRLRISLNVYLYDYQIREHINVPEEYYNRLTPLAIRQYRQLVFDKIFKKLQNDALLCELIFQKPGNYKKVNIFLDIIKRNNYIDLSQWDIYSLASVWLNYFIKNKAKPLIPIELIPLPIVDDLKFTSETFRKIIKFNQYQDLFMVIIPFFNRIIAHGESTKHDSRTLSKALTPALCKEKLSMMTNDRLAIGSRYIKNLLDFFPEIAKEISSPPSSVSSSSTIPVLPKPRKSSPTRYSELGCLTLPRSRSPSPQRSVTSPTYTPVALQNTPVLKPKSSSRNVSSPSFNAKPPLPIKAVTRPQLSLTSNSNTDLALASSSTDTLSSPTKTPSADSLPLSNSSTDLTISDNIKEMVKDEPAKDKNSVETDIFVQQFESLTLVQNAKIKKFDKELQEKKKKNETTSKTADKFSQKGYSDIKASNKVSRLAALYEERLQGLQVMNEMKQRW
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
363PhosphorylationPEIAKEISSPPSSVS
HHHHHHCCCCCCCCC		37.5722369663
364PhosphorylationEIAKEISSPPSSVSS
HHHHHCCCCCCCCCC		46.6322369663
367PhosphorylationKEISSPPSSVSSSST
HHCCCCCCCCCCCCC		46.9123749301
368PhosphorylationEISSPPSSVSSSSTI
HCCCCCCCCCCCCCC		31.6222369663
370PhosphorylationSSPPSSVSSSSTIPV
CCCCCCCCCCCCCCC		26.8422369663
371PhosphorylationSPPSSVSSSSTIPVL
CCCCCCCCCCCCCCC		26.5922369663
372PhosphorylationPPSSVSSSSTIPVLP
CCCCCCCCCCCCCCC		24.8022369663
373PhosphorylationPSSVSSSSTIPVLPK
CCCCCCCCCCCCCCC		32.1022369663
374PhosphorylationSSVSSSSTIPVLPKP
CCCCCCCCCCCCCCC		31.1122369663
384PhosphorylationVLPKPRKSSPTRYSE
CCCCCCCCCCCCHHH		42.7119823750
385PhosphorylationLPKPRKSSPTRYSEL
CCCCCCCCCCCHHHC		33.0721440633
387PhosphorylationKPRKSSPTRYSELGC
CCCCCCCCCHHHCCC		44.1621440633
389PhosphorylationRKSSPTRYSELGCLT
CCCCCCCHHHCCCEE		14.6919823750
390PhosphorylationKSSPTRYSELGCLTL
CCCCCCHHHCCCEEC		24.0519823750
396PhosphorylationYSELGCLTLPRSRSP
HHHCCCEECCCCCCC		38.5019823750
400PhosphorylationGCLTLPRSRSPSPQR
CCEECCCCCCCCCCC		34.8619684113
402PhosphorylationLTLPRSRSPSPQRSV
EECCCCCCCCCCCCC		30.8616445868
404PhosphorylationLPRSRSPSPQRSVTS
CCCCCCCCCCCCCCC		34.6119684113
408PhosphorylationRSPSPQRSVTSPTYT
CCCCCCCCCCCCCCC		25.2122369663
410PhosphorylationPSPQRSVTSPTYTPV
CCCCCCCCCCCCCCC		30.1822369663
411PhosphorylationSPQRSVTSPTYTPVA
CCCCCCCCCCCCCCC		17.0622369663
413PhosphorylationQRSVTSPTYTPVALQ
CCCCCCCCCCCCCCC		39.5322369663
414PhosphorylationRSVTSPTYTPVALQN
CCCCCCCCCCCCCCC		16.6622369663
415PhosphorylationSVTSPTYTPVALQNT
CCCCCCCCCCCCCCC		17.4823749301
422PhosphorylationTPVALQNTPVLKPKS
CCCCCCCCCCCCCCC		11.2122369663
429PhosphorylationTPVLKPKSSSRNVSS
CCCCCCCCCCCCCCC		41.9124961812
430PhosphorylationPVLKPKSSSRNVSSP
CCCCCCCCCCCCCCC		39.1724961812
431PhosphorylationVLKPKSSSRNVSSPS
CCCCCCCCCCCCCCC		34.6624961812
435PhosphorylationKSSSRNVSSPSFNAK
CCCCCCCCCCCCCCC		39.8322369663
436PhosphorylationSSSRNVSSPSFNAKP
CCCCCCCCCCCCCCC		21.9322369663
438PhosphorylationSRNVSSPSFNAKPPL
CCCCCCCCCCCCCCC		32.8322369663
451PhosphorylationPLPIKAVTRPQLSLT
CCCCCEECCCEEEEE		41.3022369663
456PhosphorylationAVTRPQLSLTSNSNT
EECCCEEEEECCCCC		25.1022369663
458PhosphorylationTRPQLSLTSNSNTDL
CCCEEEEECCCCCCE		23.6122369663
459PhosphorylationRPQLSLTSNSNTDLA
CCEEEEECCCCCCEE		43.4822369663
461PhosphorylationQLSLTSNSNTDLALA
EEEEECCCCCCEEEE		40.6520377248
463PhosphorylationSLTSNSNTDLALASS
EEECCCCCCEEEECC		32.0122369663
469PhosphorylationNTDLALASSSTDTLS
CCCEEEECCCCCCCC		26.1822369663
470PhosphorylationTDLALASSSTDTLSS
CCEEEECCCCCCCCC		31.4822369663
471PhosphorylationDLALASSSTDTLSSP
CEEEECCCCCCCCCC		28.0122369663
472PhosphorylationLALASSSTDTLSSPT
EEEECCCCCCCCCCC		34.6422369663
474PhosphorylationLASSSTDTLSSPTKT
EECCCCCCCCCCCCC		28.7322369663
476PhosphorylationSSSTDTLSSPTKTPS
CCCCCCCCCCCCCCC		36.0422369663
477PhosphorylationSSTDTLSSPTKTPSA
CCCCCCCCCCCCCCC		39.4420377248
479PhosphorylationTDTLSSPTKTPSADS
CCCCCCCCCCCCCCC		49.8822369663
481PhosphorylationTLSSPTKTPSADSLP
CCCCCCCCCCCCCCC		25.5922369663
483PhosphorylationSSPTKTPSADSLPLS
CCCCCCCCCCCCCCC		50.3622369663
486PhosphorylationTKTPSADSLPLSNSS
CCCCCCCCCCCCCCC		31.4419823750
490PhosphorylationSADSLPLSNSSTDLT
CCCCCCCCCCCCCEE		32.5025521595
492PhosphorylationDSLPLSNSSTDLTIS
CCCCCCCCCCCEEEC		31.1025521595
493PhosphorylationSLPLSNSSTDLTISD
CCCCCCCCCCEEECH		30.1425521595
494PhosphorylationLPLSNSSTDLTISDN
CCCCCCCCCEEECHH		34.5422369663
497PhosphorylationSNSSTDLTISDNIKE
CCCCCCEEECHHHHH		22.6522369663
499PhosphorylationSSTDLTISDNIKEMV
CCCCEEECHHHHHHH		21.2628889911
570UbiquitinationQKGYSDIKASNKVSR
HHCCHHHHHCHHHHH		51.2423749301
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 ECM25_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECM25_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 ECM25_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BPH1_YEASTBPH1genetic
23891562
SPO22_YEASTSPO22genetic
23891562
ATC3_YEASTDRS2genetic
27708008
GPR1_YEASTGPR1genetic
27708008
GNTK_YEASTYDR248Cgenetic
27708008
UBP3_YEASTUBP3genetic
27708008
ICE2_YEASTICE2genetic
27708008
ALN_YEASTDAL1genetic
27708008
YJH0_YEASTYJL070Cgenetic
27708008
YJ24_YEASTKCH1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
MRT4_YEASTMRT4genetic
27708008
ELM1_YEASTELM1genetic
27708008
PTR2_YEASTPTR2genetic
27708008
ECM22_YEASTECM22genetic
27708008
YPT6_YEASTYPT6genetic
27708008
TSR2_YEASTTSR2genetic
27708008
MSC1_YEASTMSC1genetic
27708008
RAD14_YEASTRAD14genetic
27708008
SIW14_YEASTSIW14genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
TOM7_YEASTTOM7genetic
27708008
RNH2A_YEASTRNH201genetic
27708008
MKS1_YEASTMKS1genetic
27708008
RAS2_YEASTRAS2genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
AIM44_YEASTAIM44genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ECM25_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-408; SER-411; THR-413;SER-436; THR-458; SER-461; SER-471; SER-492; SER-493 AND THR-494, 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-408 AND SER-411, 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-411, AND MASSSPECTROMETRY.
"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-402, AND MASSSPECTROMETRY.

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