PSP1_YEAST - dbPTM
PSP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSP1_YEAST
UniProt AC P50896
Protein Name Protein PSP1
Gene Name PSP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 841
Subcellular Localization Cytoplasm. Mitochondrion.
Protein Description DNA polymerase alpha mutation suppressor..
Protein Sequence MDLPTVNSTTSISDNVDLKNYYEDLLFKNNSGKSLSDLPRKLNDNSNNSGSDTVDPLAGLNNLRNSIKSAGNGMENRRTFDDIDFMGRFPYLPPVPNQQQQPFSHQNGFIQEHPSSNLTSFQMSSSNSEPMSAPPISSNNNNLNSTQMGNYQAQQRSFPQFNGNSFHSNGNDLMGNRMDSDYMRLMNKTNIGFTSNSGSNFAAPSHSAGNPSSMNNQQVPSFNWQQPSHPESTIRRSSYISDTLINHQMPDARQKQTSQVQQQHAQGFNLFNSRFNYDNLNSTHLTAKGVPEFGNGVQPPYPYDNEPNNASISNSNNNNNSHNMVPMQQFRRNTQPVASFNPSLPTFQQQQQQPQQPQQPRNVNVPTSFNGERVDDVQLVQLQRSSSVPSSTNSHNLQNENSNEGNVSLDNGLVLIQGKHLTSSKTLHDLYSDCGSGYFASSAVFEFTDNIKKMLKLHDSNESYDAKNMGLIDEEGNTYQSLLNFLDILRSCNMNYVNDPESNNGIVSNNGGNKNRRKGSFTTELSCRNANNSFLPYTPLVLVALKNGKLELLSTPQATNLLLKRGDLVIIDGDRGRDLVLVVEPSVDLNLALFINFLKKKIHFDSLITSESQHYRNDEFIQMLIDSKNGQKKKLNPKLYDVVELTELIIPSKQVLRFATPWEVTTNLHNKFEDELKALHIAQSKLQALNDNSKSQNTNDSSSNNFTNAATYSKPKLNIKILNAEFQFDRKKLTFYYVCEERNDFRDLIKELFKYYKTRIWLCAIPNNLSIDSKYYDKQQKELKLYQNIVKNYNAEDLMNVNEFSQNRGNNRVNFAPPLNEIELDNFQIAVYEELVHELFH
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
5Phosphorylation---MDLPTVNSTTSI
---CCCCCCCCCCCC		39.3522369663
8PhosphorylationMDLPTVNSTTSISDN
CCCCCCCCCCCCCCC		28.8222369663
9PhosphorylationDLPTVNSTTSISDNV
CCCCCCCCCCCCCCC		21.2522369663
10PhosphorylationLPTVNSTTSISDNVD
CCCCCCCCCCCCCCC		24.7122369663
11PhosphorylationPTVNSTTSISDNVDL
CCCCCCCCCCCCCCC		21.8622369663
13PhosphorylationVNSTTSISDNVDLKN
CCCCCCCCCCCCCCH		23.9322369663
31PhosphorylationDLLFKNNSGKSLSDL
HHHCCCCCCCCHHHC		57.9221082442
34PhosphorylationFKNNSGKSLSDLPRK
CCCCCCCCHHHCCHH		36.3122369663
36PhosphorylationNNSGKSLSDLPRKLN
CCCCCCHHHCCHHHC		44.1622369663
46PhosphorylationPRKLNDNSNNSGSDT
CHHHCCCCCCCCCCC		40.0122369663
49PhosphorylationLNDNSNNSGSDTVDP
HCCCCCCCCCCCCCH		43.8822369663
51PhosphorylationDNSNNSGSDTVDPLA
CCCCCCCCCCCCHHH		29.9022369663
53PhosphorylationSNNSGSDTVDPLAGL
CCCCCCCCCCHHHHH		28.6222369663
66PhosphorylationGLNNLRNSIKSAGNG
HHHHHHHHHHHCCCC		25.5921551504
69PhosphorylationNLRNSIKSAGNGMEN
HHHHHHHHCCCCCCC		39.4724930733
79PhosphorylationNGMENRRTFDDIDFM
CCCCCCCCCCCCCCC		28.3328889911
180PhosphorylationLMGNRMDSDYMRLMN
CCCCCCCHHHHHHHH		22.6930377154
237PhosphorylationPESTIRRSSYISDTL
CCHHHCCHHHHHHHH		20.0422890988
238PhosphorylationESTIRRSSYISDTLI
CHHHCCHHHHHHHHH		25.3617330950
239PhosphorylationSTIRRSSYISDTLIN
HHHCCHHHHHHHHHH		12.9922890988
241PhosphorylationIRRSSYISDTLINHQ
HCCHHHHHHHHHHCC		19.1322890988
243PhosphorylationRSSYISDTLINHQMP
CHHHHHHHHHHCCCC		23.8122890988
334PhosphorylationMQQFRRNTQPVASFN
HHHHHHCCCCCCCCC		32.2225533186
339PhosphorylationRNTQPVASFNPSLPT
HCCCCCCCCCCCCHH		26.2819779198
367PhosphorylationPRNVNVPTSFNGERV
CCCCCCCCCCCCEEC		41.4930377154
368PhosphorylationRNVNVPTSFNGERVD
CCCCCCCCCCCEECC		15.6230377154
385PhosphorylationQLVQLQRSSSVPSST
EEEEEECCCCCCCCC		17.6319779198
386PhosphorylationLVQLQRSSSVPSSTN
EEEEECCCCCCCCCC		37.2327017623
387PhosphorylationVQLQRSSSVPSSTNS
EEEECCCCCCCCCCC		39.0219779198
390PhosphorylationQRSSSVPSSTNSHNL
ECCCCCCCCCCCCCC		47.8727017623
392PhosphorylationSSSVPSSTNSHNLQN
CCCCCCCCCCCCCCC		45.1121440633
431PhosphorylationSKTLHDLYSDCGSGY
CCCHHHHHHHCCCCC		14.4421440633
432PhosphorylationKTLHDLYSDCGSGYF
CCHHHHHHHCCCCCC		33.4521440633
441PhosphorylationCGSGYFASSAVFEFT
CCCCCCCCHHHEECC		14.6621440633
463PhosphorylationKLHDSNESYDAKNMG
HHCCCCCCCCHHHCC		32.3430377154
520PhosphorylationNKNRRKGSFTTELSC
CCCCCCCCEEEHHEE		23.5822369663
522PhosphorylationNRRKGSFTTELSCRN
CCCCCCEEEHHEEEC		22.5122890988
523PhosphorylationRRKGSFTTELSCRNA
CCCCCEEEHHEEECC		32.6822890988
526PhosphorylationGSFTTELSCRNANNS
CCEEEHHEEECCCCC		12.5622890988
533PhosphorylationSCRNANNSFLPYTPL
EEECCCCCCCCCCCE		28.1530377154
537PhosphorylationANNSFLPYTPLVLVA
CCCCCCCCCCEEEEE		24.1230377154
684PhosphorylationKALHIAQSKLQALND
HHHHHHHHHHHHHHC		26.7227017623
685AcetylationALHIAQSKLQALNDN
HHHHHHHHHHHHHCC		32.3224489116
695PhosphorylationALNDNSKSQNTNDSS
HHHCCCCCCCCCCCC		28.6028889911
701PhosphorylationKSQNTNDSSSNNFTN
CCCCCCCCCCCCCCC		37.4221551504
702PhosphorylationSQNTNDSSSNNFTNA
CCCCCCCCCCCCCCC		39.6930377154
707PhosphorylationDSSSNNFTNAATYSK
CCCCCCCCCCCCCCC		26.5221551504
750AcetylationNDFRDLIKELFKYYK
CCHHHHHHHHHHHHH		56.5124489116
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 PSP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSP1_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 PSP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF12_YEASTTAF12genetic
17314980
RSC6_YEASTRSC6genetic
17314980
SSB1_YEASTSSB1physical
19536198
BEM1_YEASTBEM1genetic
20093466
RLA1_YEASTRPP1Agenetic
20093466
PMT7_YEASTPMT7genetic
20093466
AAKG_YEASTSNF4genetic
20093466
ASK10_YEASTASK10genetic
20093466
ELP2_YEASTELP2genetic
20093466
YOR1_YEASTYOR1genetic
20093466
ACE2_YEASTACE2genetic
20093466
SUB1_YEASTSUB1genetic
20093466
MOT3_YEASTMOT3genetic
20093466
CIK1_YEASTCIK1genetic
20093466
SCS7_YEASTSCS7genetic
20093466
VPS27_YEASTVPS27genetic
20093466
GGPPS_YEASTBTS1genetic
20093466
CMR1_YEASTCMR1genetic
22842922
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSP1_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-31; SER-34; SER-36;SER-51; SER-238; SER-241 AND SER-520, 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-49 AND SER-520, 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-520, AND MASSSPECTROMETRY.

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