PYRF_YEAST - dbPTM
PYRF_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PYRF_YEAST
UniProt AC P03962
Protein Name Orotidine 5'-phosphate decarboxylase
Gene Name URA3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 267
Subcellular Localization
Protein Description
Protein Sequence MSKATYKERAATHPSPVAAKLFNIMHEKQTNLCASLDVRTTKELLELVEALGPKICLLKTHVDILTDFSMEGTVKPLKALSAKYNFLLFEDRKFADIGNTVKLQYSAGVYRIAEWADITNAHGVVGPGIVSGLKQAAEEVTKEPRGLLMLAELSCKGSLATGEYTKGTVDIAKSDKDFVIGFIAQRDMGGRDEGYDWLIMTPGVGLDDKGDALGQQYRTVDDVVSTGSDIIIVGRGLFAKGRDAKVEGERYRKAGWEAYLRRCGQQN
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
2Acetylation------MSKATYKER
------CCCHHHHHH
30.8822814378
5Phosphorylation---MSKATYKERAAT
---CCCHHHHHHHCC
38.5727017623
12PhosphorylationTYKERAATHPSPVAA
HHHHHHCCCCCHHHH
33.0823749301
15PhosphorylationERAATHPSPVAAKLF
HHHCCCCCHHHHHHH
25.1323749301
20UbiquitinationHPSPVAAKLFNIMHE
CCCHHHHHHHHHHHH
43.8223749301
28UbiquitinationLFNIMHEKQTNLCAS
HHHHHHHHCCCCCHH
47.9823749301
42UbiquitinationSLDVRTTKELLELVE
HCCCCCHHHHHHHHH
45.8323749301
54UbiquitinationLVEALGPKICLLKTH
HHHHHCHHEEEEEHH
44.2323749301
59UbiquitinationGPKICLLKTHVDILT
CHHEEEEEHHHHHHH
24.5223749301
75UbiquitinationFSMEGTVKPLKALSA
CCCCCCCCCHHHHHH
44.4622817900
78UbiquitinationEGTVKPLKALSAKYN
CCCCCCHHHHHHHCC
56.6723749301
83UbiquitinationPLKALSAKYNFLLFE
CHHHHHHHCCEEEEC
37.0322817900
93UbiquitinationFLLFEDRKFADIGNT
EEEECCCCCCCCCCE
58.1723749301
102UbiquitinationADIGNTVKLQYSAGV
CCCCCEEEEEEECCC
28.0323749301
142UbiquitinationQAAEEVTKEPRGLLM
HHHHHHHCCCCHHHH
71.5423749301
176UbiquitinationVDIAKSDKDFVIGFI
EEEHHCCCCEEEEEE
61.2218433149
209UbiquitinationPGVGLDDKGDALGQQ
CCCCCCCCCCCCCCC
59.3623749301
219PhosphorylationALGQQYRTVDDVVST
CCCCCEEEHHHHHHC
24.2928889911
228PhosphorylationDDVVSTGSDIIIVGR
HHHHHCCCCEEEECC
26.2328889911
240UbiquitinationVGRGLFAKGRDAKVE
ECCCHHHCCCCCEEC
47.3323749301
245UbiquitinationFAKGRDAKVEGERYR
HHCCCCCEECCHHHH
45.1422817900
253UbiquitinationVEGERYRKAGWEAYL
ECCHHHHHHCHHHHH
42.1723749301

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
-KUbiquitinationE3 ubiquitin ligaseSSM4P40318
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PYRF_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 PYRF_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RNQ1_YEASTRNQ1physical
11805837
PYRF_YEASTURA3physical
10688190
ARO9_YEASTARO9genetic
10207060
ARO80_YEASTARO80genetic
10207060
GAP1_YEASTGAP1genetic
10207060
FUR4_YEASTFUR4genetic
9829833
YJF5_YEASTYJL055Wgenetic
18186026
PYRF_YEASTURA3physical
19435314
PMP1_YEASTPMP1physical
26404137

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PYRF_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 THR-219 AND SER-228, ANDMASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-93; LYS-209 AND LYS-253,AND MASS SPECTROMETRY.

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