PPR1_YEAST - dbPTM
PPR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPR1_YEAST
UniProt AC P07272
Protein Name Pyrimidine pathway regulatory protein 1
Gene Name PPR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 904
Subcellular Localization Nucleus.
Protein Description Positive regulator of URA1 and URA3 expression..
Protein Sequence MKQKKFNSKKSNRTDLSKRGDSPNIGISKSRTACKRCRLKKIKCDQEFPSCKRCAKLEVPCVSLDPATGKDVPRSYVFFLEDRLAVMMRVLKEYGVDPTKIRGNIPATSDDEPFDLKKYSSVSSLGEEGILPHNGLLADYLVQKGNSMASSAITSKSMASPQTINVQRKEFLVNSKKQDGSALLPETGSPMTSDARAEELRRCNKEISALGTMRESSFNSFLGDSSGISFAKLVFTATNFRQDSGDDVLDEDIKQREQKYNGYAEAENNPHFDPLELPPRHAAEVMISRFFVDTNSQLPLLHRELFLKKYFEPIYGPWNPNIALASDQTGINSAFEIPITSAFSAHTEPKRENVTEKIDVCSSVDVPWYDTWETSQKVNMRPIVELPTKFHIPYFFLNIIFAIGHATQVLKSDITTVATYKRRATKYIASLFSSSDRLEALAGTLLMVIYSIMRPNVPGVWYTMGSVLRLTVDLGLHSEKINKNYDAFTREIRRRLFWCVYSLDRQICSYFGRPFGIPEESITTRYPSLLDDSFITLTNREIDDYSDLPSPNPSSKVIALAMYKIRRIQASIVRILYAPGAELPRRFMDLESWRIETYNELERWFQVDVPKNFEMMNCKFNSIWFDLNYHYSKSILYGLSPKFPTLNDTAFKIVLDSTKGTIDVFYNLCVNKKIGYTWVAVHNMFMTGMTYLYVNFYSKNNINDCQEKVSEYTEKVLIVLKNLIGFCESAKTCYTSYKILSSVVIKLKFMQINDAKGIFSDSNPLTSQANRMSSYDKKTNVLGFDDGTFDNKVFNRTNFEEKAPFDIPLDEFFTELEKHSNVSQFNTLDVSEGNQVINESASTNTSSALNCQSYTNNQDIMDILFQVTSGSVWDEFFVRSGNGNEGESSYDISKGKNSESGGIF
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
22PhosphorylationDLSKRGDSPNIGISK
CHHHCCCCCCCCCCC		23.7520377248
151PhosphorylationKGNSMASSAITSKSM
CCCCCCCHHHCCCCC		17.7219779198
155PhosphorylationMASSAITSKSMASPQ
CCCHHHCCCCCCCCC		19.3419779198
157PhosphorylationSSAITSKSMASPQTI
CHHHCCCCCCCCCEE		21.2421551504
160PhosphorylationITSKSMASPQTINVQ
HCCCCCCCCCEEEEE		14.6521440633
189PhosphorylationALLPETGSPMTSDAR
CCCCCCCCCCCCHHH		20.9323749301
193PhosphorylationETGSPMTSDARAEEL
CCCCCCCCHHHHHHH		24.0327017623
216PhosphorylationALGTMRESSFNSFLG
HHHHCCHHHHHHHHC		29.8427017623
217PhosphorylationLGTMRESSFNSFLGD
HHHCCHHHHHHHHCC		24.5628889911
244PhosphorylationATNFRQDSGDDVLDE
CCCCCCCCCCCCCCH		35.4628889911
677PhosphorylationVNKKIGYTWVAVHNM
CCCCCCCEEEEEEHH		14.3027017623
687PhosphorylationAVHNMFMTGMTYLYV
EEEHHHHCCCCEEEE		16.7330377154
690PhosphorylationNMFMTGMTYLYVNFY
HHHHCCCCEEEEEEE		16.2427017623
691PhosphorylationMFMTGMTYLYVNFYS
HHHCCCCEEEEEEEC		6.2730377154
693PhosphorylationMTGMTYLYVNFYSKN
HCCCCEEEEEEECCC		5.2827017623
732PhosphorylationGFCESAKTCYTSYKI
HHHHCCCHHHHHHHH		15.5127017623
734PhosphorylationCESAKTCYTSYKILS
HHCCCHHHHHHHHHH		12.1728889911
735PhosphorylationESAKTCYTSYKILSS
HCCCHHHHHHHHHHH		27.9427017623
736PhosphorylationSAKTCYTSYKILSSV
CCCHHHHHHHHHHHH		9.6527017623
737PhosphorylationAKTCYTSYKILSSVV
CCHHHHHHHHHHHHH		8.3427017623
741PhosphorylationYTSYKILSSVVIKLK
HHHHHHHHHHHHHEE		25.2626447709
742PhosphorylationTSYKILSSVVIKLKF
HHHHHHHHHHHHEEE		19.5627017623
760PhosphorylationNDAKGIFSDSNPLTS
CCCCCCCCCCCCCCC		37.9021551504
762PhosphorylationAKGIFSDSNPLTSQA
CCCCCCCCCCCCCHH		38.8721551504
779PhosphorylationMSSYDKKTNVLGFDD
CCCCCCCCCCCCCCC		35.9821551504
788PhosphorylationVLGFDDGTFDNKVFN
CCCCCCCCCCCCCCC		34.5121551504
880PhosphorylationWDEFFVRSGNGNEGE
EEEEEEECCCCCCCC		31.1628889911
893PhosphorylationGESSYDISKGKNSES
CCCCCCCCCCCCCCC		32.2428889911
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 PPR1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPR1_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 PPR1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPR1_YEASTPPR1physical
7958913
SEF1_YEASTSEF1genetic
20959818
SAS3_YEASTSAS3genetic
20959818
AATC_YEASTAAT2genetic
20959818
CTK1_YEASTCTK1genetic
21127252
KCS1_YEASTKCS1genetic
21127252
MET18_YEASTMET18genetic
21127252
IME1_YEASTIME1genetic
21127252
RTG3_YEASTRTG3genetic
21127252
PP2C1_YEASTPTC1genetic
21127252
ELM1_YEASTELM1genetic
21127252
PACC_YEASTRIM101genetic
21127252
RXT2_YEASTRXT2genetic
21127252
SNF11_YEASTSNF11genetic
27708008
XRN1_YEASTXRN1genetic
27708008
OSH3_YEASTOSH3genetic
27708008
STB5_YEASTSTB5genetic
27708008
VPS53_YEASTVPS53genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
HMX1_YEASTHMX1genetic
27708008
MMS22_YEASTMMS22genetic
27708008
ENB1_YEASTENB1genetic
27708008
WHI5_YEASTWHI5genetic
27708008
ODC2_YEASTODC2genetic
27708008
YAR1_YEASTYAR1genetic
27708008
ASNS1_YEASTASN1genetic
27708008
RU2A_YEASTLEA1genetic
29674565
MDM10_YEASTMDM10genetic
29674565
KIN28_YEASTKIN28genetic
29674565
LSM6_YEASTLSM6genetic
29674565
PT122_YEASTPET122genetic
29674565
SKI8_YEASTSKI8genetic
29674565
BRR6_YEASTBRR6genetic
29674565
STB5_YEASTSTB5genetic
29674565
EXO70_YEASTEXO70genetic
29674565
DYHC_YEASTDYN1genetic
29674565
RL37A_YEASTRPL37Agenetic
29674565
SKI2_YEASTSKI2genetic
29674565
CAP_YEASTSRV2genetic
29674565
HSP7F_YEASTSSE1genetic
29674565
TBF1_YEASTTBF1genetic
29674565
SKI3_YEASTSKI3genetic
29674565
PFD4_YEASTGIM3genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPR1_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-160 AND SER-217, ANDMASS SPECTROMETRY.

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