SAF1_YEAST - dbPTM
SAF1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAF1_YEAST
UniProt AC P38352
Protein Name SCF-associated factor 1
Gene Name SAF1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 637
Subcellular Localization
Protein Description Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Targets AAH1 adenine deaminase for proteasome-dependent degradation upon entry into quiescence. Targets also URA7..
Protein Sequence MSEVESREKEPDAGLSPDIVQATLPFLSSDDIKNLSQTNKYYNTLLDFDHSKILWHELFHKAFGTLKTNDEPFQGRNSAEFKTCTETILREAFPTLSWQEVYQLRAYDAKFYSWGYLKHGRLGYTASSNNELVATSLNGPSPRFKYGVNTPTEVPWFNSRTTSRTSNFTPSEDPLSAIKKDGDEIIAQVSSGGFSFQILTESGNLYSSGSTFSGGLKGPGPSGSQHDYNPFREMIHNMERSYPRITSRSNGSTVNTTGTFSGRRMSGSHPSTAYEPGNATTAQHITIDSGGAPAASPGGSHSGVPRTTMPSMGPHENIYSQIEMLERSANKAVPGNNHIRRMFARNSFPLYSGRDENLGSFNDIQFVAVSSGRSHFLAMDTDNNIYSWDSTESDQGVKIEFANLPSRATNPILKIASGWNFNCCYIYKVGLVAWKERDAIQKGESFAFAKYEIVPNTNDVNGDSRIVDFACLQDNCVFFINNNGDKLWKYHNGLNQIVDLNIVGKLCKINACFASLVLFTDTHCYTLKVTNGDVDKDSLTELDINENVISVASGDYHTVALTERGHLYSWGIESQDCGCLGLGPSEKIVNELHIGNWEGQRNIRVVKPTKIELPEDYICVSVTAGGWQTGALIIKKH
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
2Phosphorylation------MSEVESREK
------CCCCCCCCC		50.8028889911
6Phosphorylation--MSEVESREKEPDA
--CCCCCCCCCCCCC		51.4127717283
16PhosphorylationKEPDAGLSPDIVQAT
CCCCCCCCHHHHHHH		21.4322369663
23PhosphorylationSPDIVQATLPFLSSD
CHHHHHHHCCCCCHH		20.2022369663
28PhosphorylationQATLPFLSSDDIKNL
HHHCCCCCHHHHCCH		31.9122369663
29PhosphorylationATLPFLSSDDIKNLS
HHCCCCCHHHHCCHH		41.2622369663
67UbiquitinationHKAFGTLKTNDEPFQ
HHHHCCCCCCCCCCC		45.1524961812
78PhosphorylationEPFQGRNSAEFKTCT
CCCCCCCCHHHHHHH		28.0221440633
165PhosphorylationNSRTTSRTSNFTPSE
CCCCCCCCCCCCCCC		27.9924930733
166PhosphorylationSRTTSRTSNFTPSED
CCCCCCCCCCCCCCC		28.9228889911
169PhosphorylationTSRTSNFTPSEDPLS
CCCCCCCCCCCCCHH		30.1019684113
171PhosphorylationRTSNFTPSEDPLSAI
CCCCCCCCCCCHHHH		52.1227214570
176PhosphorylationTPSEDPLSAIKKDGD
CCCCCCHHHHHCCCC		33.0824930733
249PhosphorylationYPRITSRSNGSTVNT
CCCEEECCCCCEEEC		45.3622369663
252PhosphorylationITSRSNGSTVNTTGT
EEECCCCCEEECCEE		33.1722369663
253PhosphorylationTSRSNGSTVNTTGTF
EECCCCCEEECCEEE		21.1222369663
256PhosphorylationSNGSTVNTTGTFSGR
CCCCEEECCEEECCC		23.4322369663
257PhosphorylationNGSTVNTTGTFSGRR
CCCEEECCEEECCCC		29.0822369663
259PhosphorylationSTVNTTGTFSGRRMS
CEEECCEEECCCCCC		16.7322369663
261PhosphorylationVNTTGTFSGRRMSGS
EECCEEECCCCCCCC		31.0922369663
266PhosphorylationTFSGRRMSGSHPSTA
EECCCCCCCCCCCCC		35.0221440633
268PhosphorylationSGRRMSGSHPSTAYE
CCCCCCCCCCCCCCC		25.5628889911
271PhosphorylationRMSGSHPSTAYEPGN
CCCCCCCCCCCCCCC		21.9019779198
272PhosphorylationMSGSHPSTAYEPGNA
CCCCCCCCCCCCCCC		37.4019779198
274PhosphorylationGSHPSTAYEPGNATT
CCCCCCCCCCCCCCC		23.8128889911
302PhosphorylationASPGGSHSGVPRTTM
CCCCCCCCCCCCCCC		43.0919779198
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 SAF1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAF1_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 SAF1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADE_YEASTAAH1physical
11805837
YBY9_YEASTYBR139Wphysical
11805837
PRTB_YEASTPRB1physical
11805837
CDC53_YEASTCDC53physical
11805837
ADE_YEASTAAH1physical
17517885
SKP1_YEASTSKP1physical
17517885
CDC53_YEASTCDC53physical
19763088
PRTB_YEASTPRB1physical
24389104
CBPY_YEASTPRC1physical
24389104
YBY9_YEASTYBR139Wphysical
24389104
ADE_YEASTAAH1physical
24389104
CDC10_YEASTCDC10genetic
27708008
RPB1_YEASTRPO21genetic
27708008
PDC2_YEASTPDC2genetic
27708008
RMRP_YEASTSNM1genetic
27708008
SMD1_YEASTSMD1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
POB3_YEASTPOB3genetic
27708008
PRTB_YEASTPRB1physical
26161950
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAF1_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-16; SER-28 AND SER-266,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-16 AND SER-29, AND MASSSPECTROMETRY.
"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-16, AND MASSSPECTROMETRY.

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