RS17B_YEAST - dbPTM
RS17B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS17B_YEAST
UniProt AC P14127
Protein Name 40S ribosomal protein S17-B {ECO:0000303|PubMed:9559554}
Gene Name RPS17B {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 MGRVRTKTVKRASKALIERYYPKLTLDFQTNKRLCDEIATIQSKRLRNKIAGYTTHLMKRIQKGPVRGISFKLQEEERERKDQYVPEVSALDLSRSNGVLNVDNQTSDLVKSLGLKLPLSVINVSAQRDRRYRKRN
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
14UbiquitinationKTVKRASKALIERYY
HHHHHHHHHHHHHHC		46.3423749301
23UbiquitinationLIERYYPKLTLDFQT
HHHHHCCCCEEEHHH		37.6723749301
32UbiquitinationTLDFQTNKRLCDEIA
EEEHHHCHHHHHHHH		50.5723749301
40PhosphorylationRLCDEIATIQSKRLR
HHHHHHHHHHHHHHH		25.8021440633
43PhosphorylationDEIATIQSKRLRNKI
HHHHHHHHHHHHHHH		18.8520377248
44UbiquitinationEIATIQSKRLRNKIA
HHHHHHHHHHHHHHC		38.7923749301
49UbiquitinationQSKRLRNKIAGYTTH
HHHHHHHHHCCHHHH		27.7423749301
53PhosphorylationLRNKIAGYTTHLMKR
HHHHHCCHHHHHHHH		10.2321440633
54PhosphorylationRNKIAGYTTHLMKRI
HHHHCCHHHHHHHHH		13.5621440633
55PhosphorylationNKIAGYTTHLMKRIQ
HHHCCHHHHHHHHHH		12.4321440633
59UbiquitinationGYTTHLMKRIQKGPV
CHHHHHHHHHHCCCC		53.3523749301
63UbiquitinationHLMKRIQKGPVRGIS
HHHHHHHCCCCCCEE		63.9123749301
70PhosphorylationKGPVRGISFKLQEEE
CCCCCCEEEECCHHH		21.1017287358
72UbiquitinationPVRGISFKLQEEERE
CCCCEEEECCHHHHH		42.3324961812
81UbiquitinationQEEERERKDQYVPEV
CHHHHHHHHHCCCCC		44.4223749301
84PhosphorylationERERKDQYVPEVSAL
HHHHHHHCCCCCHHH		28.2722369663
89PhosphorylationDQYVPEVSALDLSRS
HHCCCCCHHHHHHHC		22.8122369663
94PhosphorylationEVSALDLSRSNGVLN
CCHHHHHHHCCCCCC		33.0724909858
96PhosphorylationSALDLSRSNGVLNVD
HHHHHHHCCCCCCCC		34.2622369663
106PhosphorylationVLNVDNQTSDLVKSL
CCCCCCCCHHHHHHH		30.3828132839
107PhosphorylationLNVDNQTSDLVKSLG
CCCCCCCHHHHHHHC		21.1325521595
111UbiquitinationNQTSDLVKSLGLKLP
CCCHHHHHHHCCCCC		47.4623749301
112PhosphorylationQTSDLVKSLGLKLPL
CCHHHHHHHCCCCCH		21.8621440633
116UbiquitinationLVKSLGLKLPLSVIN
HHHHHCCCCCHHHHH		46.3823749301
120PhosphorylationLGLKLPLSVINVSAQ
HCCCCCHHHHHHHHH		21.0022369663
125PhosphorylationPLSVINVSAQRDRRY
CHHHHHHHHHHHHHH		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 RS17B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS17B_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 RS17B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BOS1_YEASTBOS1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
RL31B_YEASTRPL31Bgenetic
27708008
DGK1_YEASTDGK1genetic
27708008
SYIC_YEASTILS1genetic
27708008
APC11_YEASTAPC11genetic
27708008
GLE1_YEASTGLE1genetic
27708008
UBC3_YEASTCDC34genetic
27708008
CDC1_YEASTCDC1genetic
27708008
CDC4_YEASTCDC4genetic
27708008
COAD_YEASTCAB4genetic
27708008
SEC22_YEASTSEC22genetic
27708008
CLP1_YEASTCLP1genetic
27708008
SYH_YEASTHTS1genetic
27708008
RPN7_YEASTRPN7genetic
27708008
SWD1_YEASTSWD1genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
ECM21_YEASTECM21genetic
27708008
RV161_YEASTRVS161genetic
27708008
RIM1_YEASTRIM1genetic
27708008
NHP10_YEASTNHP10genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
UBP1_YEASTUBP1genetic
27708008
TPS2_YEASTTPS2genetic
27708008
PMP3_YEASTPMP3genetic
27708008
RAD4_YEASTRAD4genetic
27708008
DLDH_YEASTLPD1genetic
27708008
MRM2_YEASTMRM2genetic
27708008
XRN1_YEASTXRN1genetic
27708008
GTS1_YEASTGTS1genetic
27708008
RIM4_YEASTRIM4genetic
27708008
URM1_YEASTURM1genetic
27708008
DAL81_YEASTDAL81genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
SAC1_YEASTSAC1genetic
27708008
LDB18_YEASTLDB18genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
POC1_YEASTPBA1genetic
27708008
COA4_YEASTCOA4genetic
27708008
DIA1_YEASTDIA1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
IRA2_YEASTIRA2genetic
27708008
WHI5_YEASTWHI5genetic
27708008
SUR1_YEASTSUR1genetic
27708008
QCR2_YEASTQCR2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS17B_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-43; SER-96; SER-120 ANDSER-125, AND MASS SPECTROMETRY.
"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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