SAP1_YEAST - dbPTM
SAP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAP1_YEAST
UniProt AC P39955
Protein Name Protein SAP1
Gene Name SAP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 897
Subcellular Localization
Protein Description
Protein Sequence MDSQRSHHILTRLTKIRRRPQQPLTDFTELYSRIANETIYYLNLEEKKRYKEALQGWKALTTDVLFKQTLIEHNYPNTQSYTKDEVSLQNGIRELYHKSVMHLKRVKKLVREEPAPRNDMPSSKTYTNHSSSFTRSTEPPPVFQMVPGRMMKTLRNRNACGYKTAYSNPSLSSYGNSTSIKRGEDAENIRVNFVPSKPLSNNASRQHKNPIEHNDPPLKKETELYSDKYISEPILIDLTNDEDDHDVGILKGHNVFDEEESDGFEFDVSDYYDNFSEVDVEEEEEEKEERRRIKTLEAIQQQMSDLSVTSSTSSNKSVSSSENVPGSCIQSLPTTAPALPSLPPPPLLNVDRASSTGALKPHSLETSTTMDSSKIRNPQISKLMKNNHVPYLKGTKSTPTLITKSTPTFITRSKSNTKPIIKSNASSPTSSLTVPNSVIQKPKTAAMAAKRVLNSKKVASNPALNTTKKSHPILKSKTAKVPNSSSKKTSSHPSRPVSNSKPYSHGASQNKKPSKNQTTSMSKTNRKIPAQKKIGSPKIEDVGTEDATEHATSLNEQREEPEIDKKVLREILEDEIIDSLQGVDRQAAKQIFAEIVVHGDEVHWDDIAGLESAKYSLKEAVVYPFLRPDLFRGLREPVRGMLLFGPPGTGKTMLARAVATESHSTFFSISASSLTSKYLGESEKLVRALFAIAKKLSPSIIFVDEIDSIMGSRNNENENESSRRIKNEFLVQWSSLSSAAAGSNKSNTNNSDTNGDEDDTRVLVLAATNLPWSIDEAARRRFVRRQYIPLPEDQTRHVQFKKLLSHQKHTLTESDFDELVKITEGYSGSDITSLAKDAAMGPLRDLGDKLLETEREMIRPIGLVDFKNSLVYIKPSVSQDGLVKYEKWASQFGSSGS
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-----MDSQRSHHIL
-----CCHHHHHHHH		26.6230377154
11PhosphorylationQRSHHILTRLTKIRR
HHHHHHHHHHHHHHC		24.0330377154
127PhosphorylationMPSSKTYTNHSSSFT
CCCCCCCCCCCCCCC		31.5230377154
130PhosphorylationSKTYTNHSSSFTRST
CCCCCCCCCCCCCCC		29.7321440633
131PhosphorylationKTYTNHSSSFTRSTE
CCCCCCCCCCCCCCC		23.1729136822
132PhosphorylationTYTNHSSSFTRSTEP
CCCCCCCCCCCCCCC		33.3825752575
134PhosphorylationTNHSSSFTRSTEPPP
CCCCCCCCCCCCCCC		26.1721440633
164PhosphorylationRNACGYKTAYSNPSL
CCCCCCCCCCCCCCH		23.5029136822
166PhosphorylationACGYKTAYSNPSLSS
CCCCCCCCCCCCHHH		17.7629136822
167PhosphorylationCGYKTAYSNPSLSSY
CCCCCCCCCCCHHHC		39.5429136822
170PhosphorylationKTAYSNPSLSSYGNS
CCCCCCCCHHHCCCC		45.1729136822
177PhosphorylationSLSSYGNSTSIKRGE
CHHHCCCCCCCCCCC		21.1128889911
179PhosphorylationSSYGNSTSIKRGEDA
HHCCCCCCCCCCCCC		26.4021551504
200PhosphorylationFVPSKPLSNNASRQH
ECCCCCCCCCCCHHC		36.2428889911
239PhosphorylationEPILIDLTNDEDDHD
CCEEEECCCCCCCCC		36.5521440633
354PhosphorylationLLNVDRASSTGALKP
CCCCCCCCCCCCCCC		29.3529136822
355PhosphorylationLNVDRASSTGALKPH
CCCCCCCCCCCCCCC		29.8529136822
356PhosphorylationNVDRASSTGALKPHS
CCCCCCCCCCCCCCC		24.7929136822
363PhosphorylationTGALKPHSLETSTTM
CCCCCCCCCCCCCCC		36.1123749301
395PhosphorylationHVPYLKGTKSTPTLI
CCCCCCCCCCCCEEE		21.8929136822
397PhosphorylationPYLKGTKSTPTLITK
CCCCCCCCCCEEEEC		39.1820377248
398PhosphorylationYLKGTKSTPTLITKS
CCCCCCCCCEEEECC		23.1122369663
400PhosphorylationKGTKSTPTLITKSTP
CCCCCCCEEEECCCC		30.7721440633
405PhosphorylationTPTLITKSTPTFITR
CCEEEECCCCCEEEC		30.8529136822
406PhosphorylationPTLITKSTPTFITRS
CEEEECCCCCEEECC		28.0927214570
413PhosphorylationTPTFITRSKSNTKPI
CCCEEECCCCCCCCC		31.6125704821
415PhosphorylationTFITRSKSNTKPIIK
CEEECCCCCCCCCEE		51.4819823750
417PhosphorylationITRSKSNTKPIIKSN
EECCCCCCCCCEECC		45.3419823750
423PhosphorylationNTKPIIKSNASSPTS
CCCCCEECCCCCCCC		27.5020377248
426PhosphorylationPIIKSNASSPTSSLT
CCEECCCCCCCCCCC		40.8922369663
427PhosphorylationIIKSNASSPTSSLTV
CEECCCCCCCCCCCC		29.7722369663
429PhosphorylationKSNASSPTSSLTVPN
ECCCCCCCCCCCCCC		32.6620377248
430PhosphorylationSNASSPTSSLTVPNS
CCCCCCCCCCCCCCC		27.0820377248
431PhosphorylationNASSPTSSLTVPNSV
CCCCCCCCCCCCCCC		30.4522369663
433PhosphorylationSSPTSSLTVPNSVIQ
CCCCCCCCCCCCCCC		35.5522369663
437PhosphorylationSSLTVPNSVIQKPKT
CCCCCCCCCCCCHHH		17.9619779198
460PhosphorylationLNSKKVASNPALNTT
HCCCCCCCCCCCCCC		46.4622369663
536PhosphorylationPAQKKIGSPKIEDVG
CHHHCCCCCCCCCCC		26.8821440633
544PhosphorylationPKIEDVGTEDATEHA
CCCCCCCCCHHHHHH		30.4629688323
548PhosphorylationDVGTEDATEHATSLN
CCCCCHHHHHHHHHH		40.4020377248
552PhosphorylationEDATEHATSLNEQRE
CHHHHHHHHHHHHCC		35.3427017623
553PhosphorylationDATEHATSLNEQREE
HHHHHHHHHHHHCCC		29.9517330950
684AcetylationKYLGESEKLVRALFA
HHHCCHHHHHHHHHH		62.6524489116
734PhosphorylationNEFLVQWSSLSSAAA
HHHHHHHHHHHCHHC		12.3321551504
735PhosphorylationEFLVQWSSLSSAAAG
HHHHHHHHHHCHHCC		29.3421551504
738PhosphorylationVQWSSLSSAAAGSNK
HHHHHHHCHHCCCCC		27.5021551504
836UbiquitinationSDITSLAKDAAMGPL
CHHHHHHHHHHHHHH		53.8723749301
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 SAP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAP1_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 SAP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APC11_YEASTAPC11physical
16554755
UBC3_YEASTCDC34genetic
27708008
SWC4_YEASTSWC4genetic
27708008
CLP1_YEASTCLP1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
UAP1_YEASTQRI1genetic
27708008
SPC97_YEASTSPC97genetic
27708008
SEC22_YEASTSEC22genetic
27708008
NUF2_YEASTNUF2genetic
27708008
TYSY_YEASTCDC21genetic
27708008
TBF1_YEASTTBF1genetic
27708008
DIM1_YEASTDIM1genetic
27708008
DIB1_YEASTDIB1genetic
27708008
RV161_YEASTRVS161genetic
27708008
RV167_YEASTRVS167genetic
27708008
CP56_YEASTDIT2genetic
27708008
MED20_YEASTSRB2genetic
27708008
ATG23_YEASTATG23genetic
27708008
MKS1_YEASTMKS1genetic
27708008
PHO80_YEASTPHO80genetic
27708008
RTG1_YEASTRTG1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAP1_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-131; SER-167; SER-423AND SER-553, AND MASS SPECTROMETRY.

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