RAS1_YEAST - dbPTM
RAS1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAS1_YEAST
UniProt AC P01119
Protein Name Ras-like protein 1
Gene Name RAS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 309
Subcellular Localization Cell membrane
Lipid-anchor.
Protein Description The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP..
Protein Sequence MQGNKSTIREYKIVVVGGGGVGKSALTIQFIQSYFVDEYDPTIEDSYRKQVVIDDKVSILDILDTAGQEEYSAMREQYMRTGEGFLLVYSVTSRNSFDELLSYYQQIQRVKDSDYIPVVVVGNKLDLENERQVSYEDGLRLAKQLNAPFLETSAKQAINVDEAFYSLIRLVRDDGGKYNSMNRQLDNTNEIRDSELTSSATADREKKNNGSYVLDNSLTNAGTGSSSKSAVNHNGETTKRTDEKNYVNQNNNNEGNTKYSSNGNGNRSDISRGNQNNALNSRSKQSAEPQKNSSANARKESSGGCCIIC
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
5Ubiquitination---MQGNKSTIREYK
---CCCCCCCCCEEE
56.6623749301
49UbiquitinationTIEDSYRKQVVIDDK
CCCHHHCCEEEECCC
38.9323749301
143UbiquitinationEDGLRLAKQLNAPFL
HHHHHHHHHHCCCCC
60.9723749301
177UbiquitinationLVRDDGGKYNSMNRQ
HHHCCCCCCCCCCCC
46.9523749301
178PhosphorylationVRDDGGKYNSMNRQL
HHCCCCCCCCCCCCC
18.7524961812
180PhosphorylationDDGGKYNSMNRQLDN
CCCCCCCCCCCCCCC
17.8421551504
188PhosphorylationMNRQLDNTNEIRDSE
CCCCCCCCHHCCHHH
33.6219823750
194PhosphorylationNTNEIRDSELTSSAT
CCHHCCHHHCCCCCC
25.3421440633
197PhosphorylationEIRDSELTSSATADR
HCCHHHCCCCCCCCH
19.3122890988
198PhosphorylationIRDSELTSSATADRE
CCHHHCCCCCCCCHH
30.5119823750
199PhosphorylationRDSELTSSATADREK
CHHHCCCCCCCCHHH
25.1419823750
201PhosphorylationSELTSSATADREKKN
HHCCCCCCCCHHHHC
30.9219823750
207UbiquitinationATADREKKNNGSYVL
CCCCHHHHCCCCEEE
51.3923749301
211PhosphorylationREKKNNGSYVLDNSL
HHHHCCCCEEECCCC
17.7522369663
212PhosphorylationEKKNNGSYVLDNSLT
HHHCCCCEEECCCCC
13.3622369663
217PhosphorylationGSYVLDNSLTNAGTG
CCEEECCCCCCCCCC
35.9222369663
219PhosphorylationYVLDNSLTNAGTGSS
EEECCCCCCCCCCCC
23.8922369663
223PhosphorylationNSLTNAGTGSSSKSA
CCCCCCCCCCCCCCC
31.3220377248
225PhosphorylationLTNAGTGSSSKSAVN
CCCCCCCCCCCCCCC
31.1425521595
226PhosphorylationTNAGTGSSSKSAVNH
CCCCCCCCCCCCCCC
43.0322369663
227PhosphorylationNAGTGSSSKSAVNHN
CCCCCCCCCCCCCCC
32.1220377248
229PhosphorylationGTGSSSKSAVNHNGE
CCCCCCCCCCCCCCC
39.1225521595
238PhosphorylationVNHNGETTKRTDEKN
CCCCCCCCCCCCCCC
17.7721440633
239UbiquitinationNHNGETTKRTDEKNY
CCCCCCCCCCCCCCC
61.8022817900
244UbiquitinationTTKRTDEKNYVNQNN
CCCCCCCCCCCCCCC
57.2823749301
258UbiquitinationNNNEGNTKYSSNGNG
CCCCCCCEECCCCCC
47.3223749301
259PhosphorylationNNEGNTKYSSNGNGN
CCCCCCEECCCCCCC
18.4519823750
260PhosphorylationNEGNTKYSSNGNGNR
CCCCCEECCCCCCCH
20.9119823750
261PhosphorylationEGNTKYSSNGNGNRS
CCCCEECCCCCCCHH
45.7421440633
268PhosphorylationSNGNGNRSDISRGNQ
CCCCCCHHHHCCCCH
43.2119684113
271PhosphorylationNGNRSDISRGNQNNA
CCCHHHHCCCCHHHH
38.8419684113
281PhosphorylationNQNNALNSRSKQSAE
CHHHHHHHHHHHCCC
38.4927214570
283PhosphorylationNNALNSRSKQSAEPQ
HHHHHHHHHHCCCCC
34.5619823750
286PhosphorylationLNSRSKQSAEPQKNS
HHHHHHHCCCCCCCC
38.0327214570
305S-palmitoylationRKESSGGCCIIC---
CHHHCCCEEEEC---
1.39-
305S-palmitoylationRKESSGGCCIIC---
CHHHCCCEEEEC---
1.393513173
306MethylationKESSGGCCIIC----
HHHCCCEEEEC----
2.382050108
306FarnesylationKESSGGCCIIC----
HHHCCCEEEEC----
2.381763050
306FarnesylationKESSGGCCIIC----
HHHCCCEEEEC----
2.381763050

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 RAS1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAS1_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 RAS1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAS1_YEASTRAS1physical
9228053
CDC15_YEASTCDC15genetic
7502049
CDC25_YEASTCDC25genetic
8246881
CDC5_YEASTCDC5genetic
7502049
DBF2_YEASTDBF2genetic
7502049
SPO12_YEASTSPO12genetic
7502049
TEM1_YEASTTEM1genetic
7502049
RAS2_YEASTRAS2genetic
7502049
RAS2_YEASTRAS2genetic
6327067
RAS2_YEASTRAS2genetic
3145192
KAPR_YEASTBCY1genetic
2981630
REG1_YEASTREG1genetic
2823100
KAPR_YEASTBCY1genetic
2823100
KAPA_YEASTTPK1genetic
2823100
PDE2_YEASTPDE2genetic
2827010
CYAA_YEASTCYR1genetic
1991451
AKR1_YEASTAKR1physical
11283351
RAS2_YEASTRAS2genetic
3549283
RAS2_YEASTRAS2genetic
8246881
KAPA_YEASTTPK1genetic
8246881
TSA1_YEASTTSA1physical
18719252
IPYR_YEASTIPP1genetic
19269370
NPP1_YEASTNPP1genetic
19269370
REG1_YEASTREG1genetic
19269370
RAS2_YEASTRAS2genetic
19269370
RTG1_YEASTRTG1genetic
19269370
KAPA_YEASTTPK1genetic
3036373
KAPB_YEASTTPK2genetic
3036373
KAPC_YEASTTPK3genetic
3036373
KAPA_YEASTTPK1genetic
3889915
KAPR_YEASTBCY1genetic
3889915
RAS2_YEASTRAS2genetic
3889915
KAPB_YEASTTPK2genetic
15030478
RTG1_YEASTRTG1genetic
20526336
YNT4_YEASTYNL194Cgenetic
20526336
YPT31_YEASTYPT31genetic
20526336
RAS2_YEASTRAS2genetic
20526336
VPS5_YEASTVPS5genetic
20526336
VPS17_YEASTVPS17genetic
20526336
YAK1_YEASTYAK1genetic
21457714
KAPA_YEASTTPK1genetic
21457714
KAPB_YEASTTPK2genetic
21457714
KAPC_YEASTTPK3genetic
21457714
PDE2_YEASTPDE2genetic
2558053
RAS2_YEASTRAS2genetic
2558053
YAK1_YEASTYAK1genetic
2558053
KAPR_YEASTBCY1genetic
2558053
ERF3_YEASTSUP35genetic
27708008
SLD3_YEASTSLD3genetic
27708008
DCOR_YEASTSPE1genetic
27708008
RAS2_YEASTRAS2genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAS1_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-198; SER-199; THR-201AND THR-219, AND MASS SPECTROMETRY.
Prenylation
ReferencePubMed
"RAM2, an essential gene of yeast, and RAM1 encode the two polypeptidecomponents of the farnesyltransferase that prenylates a-factor and Rasproteins.";
He B., Chen P., Chen S.-Y., Vancura K.L., Michaelis S., Powers S.;
Proc. Natl. Acad. Sci. U.S.A. 88:11373-11377(1991).
Cited for: ISOPRENYLATION AT CYS-306 BY RAM1-RAM2.

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