RS17A_YEAST - dbPTM
RS17A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS17A_YEAST
UniProt AC P02407
Protein Name 40S ribosomal protein S17-A {ECO:0000303|PubMed:9559554}
Gene Name RPS17A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 136
Subcellular Localization Cytoplasm .
Protein Description Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel..
Protein Sequence MGRVRTKTVKRASKALIERYYPKLTLDFQTNKRLCDEIATIQSKRLRNKIAGYTTHLMKRIQKGPVRGISFKLQEEERERKDQYVPEVSALDLSRSNGVLNVDNQTSDLVKSLGLKLPLSVINVSAQRDRRYRKRV
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
10UbiquitinationRVRTKTVKRASKALI
CCCHHHHHHHHHHHH		47.6922817900
14AcetylationKTVKRASKALIERYY
HHHHHHHHHHHHHHC		46.3424489116
14UbiquitinationKTVKRASKALIERYY
HHHHHHHHHHHHHHC		46.3423749301
142-HydroxyisobutyrylationKTVKRASKALIERYY
HHHHHHHHHHHHHHC		46.34-
23UbiquitinationLIERYYPKLTLDFQT
HHHHHCCCCEEEHHH		37.6723749301
23AcetylationLIERYYPKLTLDFQT
HHHHHCCCCEEEHHH		37.6724489116
232-HydroxyisobutyrylationLIERYYPKLTLDFQT
HHHHHCCCCEEEHHH		37.67-
32AcetylationTLDFQTNKRLCDEIA
EEEHHHCHHHHHHHH		50.5724489116
32UbiquitinationTLDFQTNKRLCDEIA
EEEHHHCHHHHHHHH		50.5723749301
40PhosphorylationRLCDEIATIQSKRLR
HHHHHHHHHHHHHHH		25.8021440633
43PhosphorylationDEIATIQSKRLRNKI
HHHHHHHHHHHHHHH		18.8520377248
44AcetylationEIATIQSKRLRNKIA
HHHHHHHHHHHHHHC		38.7924489116
44UbiquitinationEIATIQSKRLRNKIA
HHHHHHHHHHHHHHC		38.7923749301
49SuccinylationQSKRLRNKIAGYTTH
HHHHHHHHHCCHHHH		27.7423954790
49UbiquitinationQSKRLRNKIAGYTTH
HHHHHHHHHCCHHHH		27.7423749301
49AcetylationQSKRLRNKIAGYTTH
HHHHHHHHHCCHHHH		27.7424489116
53PhosphorylationLRNKIAGYTTHLMKR
HHHHHCCHHHHHHHH		10.2321440633
54PhosphorylationRNKIAGYTTHLMKRI
HHHHCCHHHHHHHHH		13.5621440633
55PhosphorylationNKIAGYTTHLMKRIQ
HHHCCHHHHHHHHHH		12.4321440633
59UbiquitinationGYTTHLMKRIQKGPV
CHHHHHHHHHHCCCC		53.3523749301
59AcetylationGYTTHLMKRIQKGPV
CHHHHHHHHHHCCCC		53.3524489116
59MethylationGYTTHLMKRIQKGPV
CHHHHHHHHHHCCCC		53.3520137074
59SuccinylationGYTTHLMKRIQKGPV
CHHHHHHHHHHCCCC		53.3523954790
63AcetylationHLMKRIQKGPVRGIS
HHHHHHHCCCCCCEE		63.9125381059
63UbiquitinationHLMKRIQKGPVRGIS
HHHHHHHCCCCCCEE		63.9123749301
632-HydroxyisobutyrylationHLMKRIQKGPVRGIS
HHHHHHHCCCCCCEE		63.91-
70PhosphorylationKGPVRGISFKLQEEE
CCCCCCEEEECCHHH		21.1017287358
72SuccinylationPVRGISFKLQEEERE
CCCCEEEECCHHHHH		42.3323954790
72AcetylationPVRGISFKLQEEERE
CCCCEEEECCHHHHH		42.3324489116
72UbiquitinationPVRGISFKLQEEERE
CCCCEEEECCHHHHH		42.3324961812
722-HydroxyisobutyrylationPVRGISFKLQEEERE
CCCCEEEECCHHHHH		42.33-
81UbiquitinationQEEERERKDQYVPEV
CHHHHHHHHHCCCCC		44.4223749301
81AcetylationQEEERERKDQYVPEV
CHHHHHHHHHCCCCC		44.4224489116
812-HydroxyisobutyrylationQEEERERKDQYVPEV
CHHHHHHHHHCCCCC		44.42-
84PhosphorylationERERKDQYVPEVSAL
HHHHHHHCCCCCHHH		28.2722369663
89PhosphorylationDQYVPEVSALDLSRS
HHCCCCCHHHHHHHC		22.8122369663
94PhosphorylationEVSALDLSRSNGVLN
CCHHHHHHHCCCCCC		33.0722369663
96PhosphorylationSALDLSRSNGVLNVD
HHHHHHHCCCCCCCC		34.2622369663
106PhosphorylationVLNVDNQTSDLVKSL
CCCCCCCCHHHHHHH		30.3828132839
107PhosphorylationLNVDNQTSDLVKSLG
CCCCCCCHHHHHHHC		21.1325521595
111SuccinylationNQTSDLVKSLGLKLP
CCCHHHHHHHCCCCC		47.4623954790
111UbiquitinationNQTSDLVKSLGLKLP
CCCHHHHHHHCCCCC		47.4623749301
111AcetylationNQTSDLVKSLGLKLP
CCCHHHHHHHCCCCC		47.4624489116
112PhosphorylationQTSDLVKSLGLKLPL
CCHHHHHHHCCCCCH		21.8621440633
116SuccinylationLVKSLGLKLPLSVIN
HHHHHCCCCCHHHHH		46.3823954790
116UbiquitinationLVKSLGLKLPLSVIN
HHHHHCCCCCHHHHH		46.3823749301
116AcetylationLVKSLGLKLPLSVIN
HHHHHCCCCCHHHHH		46.3824489116
120PhosphorylationLGLKLPLSVINVSAQ
HCCCCCHHHHHHCHH		21.0022369663
125PhosphorylationPLSVINVSAQRDRRY
CHHHHHHCHHHCHHH		17.7522369663
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 RS17A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS17A_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 RS17A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS17B_YEASTRPS17Bgenetic
6092944
ALG14_YEASTALG14genetic
16155567
APC11_YEASTAPC11genetic
16155567
BRR2_YEASTBRR2genetic
16155567
CLF1_YEASTCLF1genetic
16155567
PCNA_YEASTPOL30genetic
16155567
P5CR_YEASTPRO3genetic
16155567
PRP11_YEASTPRP11genetic
16155567
PRP38_YEASTPRP38genetic
16155567
PRP5_YEASTPRP5genetic
16155567
RIM2_YEASTRIM2genetic
16155567
RTS2_YEASTRTS2genetic
16155567
SNU56_YEASTSNU56genetic
16155567
SPC98_YEASTSPC98genetic
16155567
UGPA1_YEASTUGP1genetic
16155567
RL4P_YEASTYML6genetic
16155567
CWC22_YEASTCWC22genetic
16155567
DOP1_YEASTDOP1genetic
16155567
PRP42_YEASTPRP42genetic
16155567
TAF7_YEASTTAF7genetic
16155567
RS17B_YEASTRPS17Bgenetic
22377630
BUD31_YEASTBUD31genetic
27708008
AAR2_YEASTAAR2genetic
27708008
FBRL_YEASTNOP1genetic
27708008
PRP11_YEASTPRP11genetic
27708008
SNU23_YEASTSNU23genetic
27708008
UBC3_YEASTCDC34genetic
27708008
ERF3_YEASTSUP35genetic
27708008
SNU56_YEASTSNU56genetic
27708008
ACT_YEASTACT1genetic
27708008
PRP43_YEASTPRP43genetic
27708008
RRP41_YEASTSKI6genetic
27708008
XPO1_YEASTCRM1genetic
27708008
ATC7_YEASTNEO1genetic
27708008
MTR4_YEASTMTR4genetic
27708008
PRP21_YEASTPRP21genetic
27708008
SN114_YEASTSNU114genetic
27708008
BBP_YEASTMSL5genetic
27708008
RU1C_YEASTYHC1genetic
27708008
PRP2_YEASTPRP2genetic
27708008
IPL1_YEASTIPL1genetic
27708008
IF6_YEASTTIF6genetic
27708008
TF2B_YEASTSUA7genetic
27708008
YCY0_YEASTYCR090Cgenetic
27708008
RS17B_YEASTRPS17Bgenetic
27708008
SPO74_YEASTSPO74genetic
27708008
KEX1_YEASTKEX1genetic
27708008
ECM27_YEASTECM27genetic
27708008
SIC1_YEASTSIC1genetic
27708008
CPYI_YEASTTFS1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
SPS4_YEASTSPS4genetic
27708008
SUR1_YEASTSUR1genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS17A_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, AND MASSSPECTROMETRY.

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