RL17B_YEAST - dbPTM
RL17B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL17B_YEAST
UniProt AC P46990
Protein Name 60S ribosomal protein L17-B {ECO:0000303|PubMed:9559554}
Gene Name RPL17B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 184
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 MARYGATSTNPAKSASARGSYLRVSFKNTRETAQAINGWELTKAQKYLDQVLDHQRAIPFRRFNSSIGRTAQGKEFGVTKARWPAKSVKFVQGLLQNAAANAEAKGLDATKLYVSHIQVNQAPKQRRRTYRAHGRINKYESSPSHIELVVTEKEEAVAKAAEKKVVRLTSRQRGRIAAQKRISA
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
7Phosphorylation-MARYGATSTNPAKS
-CCCCCCCCCCCCCC		31.5522369663
8PhosphorylationMARYGATSTNPAKSA
CCCCCCCCCCCCCCC		26.1722369663
9PhosphorylationARYGATSTNPAKSAS
CCCCCCCCCCCCCCC		40.6522369663
13UbiquitinationATSTNPAKSASARGS
CCCCCCCCCCCCCCC		48.0523749301
14PhosphorylationTSTNPAKSASARGSY
CCCCCCCCCCCCCCE		29.5717287358
16PhosphorylationTNPAKSASARGSYLR
CCCCCCCCCCCCEEE		26.1128889911
20PhosphorylationKSASARGSYLRVSFK
CCCCCCCCEEEEEEE		18.5522369663
21PhosphorylationSASARGSYLRVSFKN
CCCCCCCEEEEEEEC		11.0122369663
25PhosphorylationRGSYLRVSFKNTRET
CCCEEEEEEECHHHH		24.8622369663
32PhosphorylationSFKNTRETAQAINGW
EEECHHHHHHHHCHH		22.3021440633
43UbiquitinationINGWELTKAQKYLDQ
HCHHHHHHHHHHHHH		62.5423749301
46UbiquitinationWELTKAQKYLDQVLD
HHHHHHHHHHHHHHH		53.2823749301
46AcetylationWELTKAQKYLDQVLD
HHHHHHHHHHHHHHH		53.2824489116
65PhosphorylationIPFRRFNSSIGRTAQ
CCHHHCCCCCCCCCC		22.1825533186
66PhosphorylationPFRRFNSSIGRTAQG
CHHHCCCCCCCCCCC		30.1126040289
70PhosphorylationFNSSIGRTAQGKEFG
CCCCCCCCCCCCCCC		20.3717287358
74UbiquitinationIGRTAQGKEFGVTKA
CCCCCCCCCCCCCCC		37.4823749301
80UbiquitinationGKEFGVTKARWPAKS
CCCCCCCCCCCCHHH		33.2823749301
86UbiquitinationTKARWPAKSVKFVQG
CCCCCCHHHHHHHHH		52.2622817900
87PhosphorylationKARWPAKSVKFVQGL
CCCCCHHHHHHHHHH		32.4221440633
89UbiquitinationRWPAKSVKFVQGLLQ
CCCHHHHHHHHHHHH		47.0823749301
105UbiquitinationAAANAEAKGLDATKL
HHHHHHHCCCCCCEE		52.0623749301
111UbiquitinationAKGLDATKLYVSHIQ
HCCCCCCEEEEEEEE		39.2723749301
113PhosphorylationGLDATKLYVSHIQVN
CCCCCEEEEEEEECC		11.0621440633
115PhosphorylationDATKLYVSHIQVNQA
CCCEEEEEEEECCCC		11.0028152593
124UbiquitinationIQVNQAPKQRRRTYR
EECCCCHHHHHHHHH		60.4923749301
138UbiquitinationRAHGRINKYESSPSH
HHHCCCCCCCCCCCE		48.2822817900
139PhosphorylationAHGRINKYESSPSHI
HHCCCCCCCCCCCEE		19.2929734811
141PhosphorylationGRINKYESSPSHIEL
CCCCCCCCCCCEEEE		44.4522369663
142PhosphorylationRINKYESSPSHIELV
CCCCCCCCCCEEEEE		20.6222369663
144PhosphorylationNKYESSPSHIELVVT
CCCCCCCCEEEEEEE		38.7622369663
153UbiquitinationIELVVTEKEEAVAKA
EEEEEECHHHHHHHH		52.0324961812
159UbiquitinationEKEEAVAKAAEKKVV
CHHHHHHHHHHHHHH		41.3417644757
170PhosphorylationKKVVRLTSRQRGRIA
HHHHHHHHHHHCCHH		30.8917287358
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 RL17B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL17B_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 RL17B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRI2_YEASTPRI2genetic
27708008
CWC16_YEASTYJU2genetic
27708008
BET3_YEASTBET3genetic
27708008
MED14_YEASTRGR1genetic
27708008
UFD2_YEASTUFD2genetic
27708008
RV167_YEASTRVS167genetic
27708008
CDC27_YEASTCDC27genetic
27708008
ORC2_YEASTORC2genetic
27708008
EXO84_YEASTEXO84genetic
27708008
TFB1_YEASTTFB1genetic
27708008
RMRP_YEASTSNM1genetic
27708008
PP12_YEASTGLC7genetic
27708008
RPN11_YEASTRPN11genetic
27708008
STT3_YEASTSTT3genetic
27708008
PRS8_YEASTRPT6genetic
27708008
RPN1_YEASTRPN1genetic
27708008
MED6_YEASTMED6genetic
27708008
FDFT_YEASTERG9genetic
27708008
KTHY_YEASTCDC8genetic
27708008
SEC13_YEASTSEC13genetic
27708008
SEC22_YEASTSEC22genetic
27708008
ERO1_YEASTERO1genetic
27708008
SMY2_YEASTSMY2genetic
27708008
GCS1_YEASTGCS1genetic
27708008
SNQ2_YEASTSNQ2genetic
27708008
IPT1_YEASTIPT1genetic
27708008
PLP1_YEASTPLP1genetic
27708008
HEL2_YEASTHEL2genetic
27708008
PHM6_YEASTPHM6genetic
27708008
XRS2_YEASTXRS2genetic
27708008
VMA21_YEASTVMA21genetic
27708008
ILM1_YEASTILM1genetic
27708008
CHMU_YEASTARO7genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
DOM34_YEASTDOM34genetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL17B_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-65 AND TYR-113, AND MASSSPECTROMETRY.
"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-20; SER-25; SER-65 ANDSER-170, 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-65, AND MASSSPECTROMETRY.

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