RS16B_YEAST - dbPTM
RS16B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS16B_YEAST
UniProt AC P0CX52
Protein Name 40S ribosomal protein S16-B {ECO:0000303|PubMed:9559554}
Gene Name RPS16B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 143
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 MSAVPSVQTFGKKKSATAVAHVKAGKGLIKVNGSPITLVEPEILRFKVYEPLLLVGLDKFSNIDIRVRVTGGGHVSQVYAIRQAIAKGLVAYHQKYVDEQSKNELKKAFTSYDRTLLIADSRRPEPKKFGGKGARSRFQKSYR
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------MSAVPSVQT
------CCCCCCCCC		37.661544921
2Phosphorylation------MSAVPSVQT
------CCCCCCCCC		37.6622369663
6Phosphorylation--MSAVPSVQTFGKK
--CCCCCCCCCCCCC		21.9130377154
9PhosphorylationSAVPSVQTFGKKKSA
CCCCCCCCCCCCCCC		32.0030377154
15PhosphorylationQTFGKKKSATAVAHV
CCCCCCCCCEEEEEE		39.4722369663
17PhosphorylationFGKKKSATAVAHVKA
CCCCCCCEEEEEEEC		28.8422369663
26UbiquitinationVAHVKAGKGLIKVNG
EEEEECCCCEEEECC		56.2422817900
30UbiquitinationKAGKGLIKVNGSPIT
ECCCCEEEECCEECE		34.3923749301
34PhosphorylationGLIKVNGSPITLVEP
CEEEECCEECEEECH		14.1322369663
37PhosphorylationKVNGSPITLVEPEIL
EECCEECEEECHHHE		28.3021440633
47UbiquitinationEPEILRFKVYEPLLL
CHHHEECCCCCCEEE		37.1623749301
59UbiquitinationLLLVGLDKFSNIDIR
EEEEEECCCCCCEEE		56.5923749301
61PhosphorylationLVGLDKFSNIDIRVR
EEEECCCCCCEEEEE		38.3217287358
70PhosphorylationIDIRVRVTGGGHVSQ
CEEEEEEECCCCHHH		21.3917287358
76PhosphorylationVTGGGHVSQVYAIRQ
EECCCCHHHHHHHHH		14.3017287358
87UbiquitinationAIRQAIAKGLVAYHQ
HHHHHHHHHHHHHHH		46.8217644757
92PhosphorylationIAKGLVAYHQKYVDE
HHHHHHHHHHHHCCH		9.4121082442
95UbiquitinationGLVAYHQKYVDEQSK
HHHHHHHHHCCHHHH		33.6517644757
102UbiquitinationKYVDEQSKNELKKAF
HHCCHHHHHHHHHHH		54.8823749301
106UbiquitinationEQSKNELKKAFTSYD
HHHHHHHHHHHHHCC		35.5622817900
107UbiquitinationQSKNELKKAFTSYDR
HHHHHHHHHHHHCCC		62.4523749301
110PhosphorylationNELKKAFTSYDRTLL
HHHHHHHHHCCCEEE		31.1028889911
111PhosphorylationELKKAFTSYDRTLLI
HHHHHHHHCCCEEEE		20.6921440633
112PhosphorylationLKKAFTSYDRTLLIA
HHHHHHHCCCEEEEE		13.3419779198
115PhosphorylationAFTSYDRTLLIADSR
HHHHCCCEEEEECCC		24.0220377248
121PhosphorylationRTLLIADSRRPEPKK
CEEEEECCCCCCCCC		22.5920377248
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 RS16B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS16B_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 RS16B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RRP14_YEASTRRP14physical
17804645
RQC2_YEASTTAE2genetic
20691087
RTC6_YEASTRTC6genetic
20691087
MET28_YEASTMET28genetic
27708008
PIR5_YEASTYJL160Cgenetic
27708008
LGE1_YEASTLGE1genetic
27708008
DAP1_YEASTDAP1genetic
27708008
YAJ3_YEASTYAR023Cgenetic
27708008
FUI1_YEASTFUI1genetic
27708008
ETR1_YEASTETR1genetic
27708008
CSG2_YEASTCSG2genetic
27708008
GIP1_YEASTGIP1genetic
27708008
CCZ1_YEASTCCZ1genetic
27708008
MBA1_YEASTMBA1genetic
27708008
LSM6_YEASTLSM6genetic
27708008
CAJ1_YEASTCAJ1genetic
27708008
FTR1_YEASTFTR1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
SGF73_YEASTSGF73genetic
27708008
MON1_YEASTMON1genetic
27708008
SYF2_YEASTSYF2genetic
27708008
DOG1_YEASTDOG1genetic
27708008
STB5_YEASTSTB5genetic
27708008
SGN1_YEASTSGN1genetic
27708008
GPX3_YEASTHYR1genetic
27708008
LPLA_YEASTAIM22genetic
27708008
DENR_YEASTTMA22genetic
27708008
EF1G2_YEASTTEF4genetic
27708008
CTK1_YEASTCTK1genetic
27708008
DOA1_YEASTDOA1genetic
27708008
HBS1_YEASTHBS1genetic
27708008
SIC1_YEASTSIC1genetic
27708008
XDJ1_YEASTXDJ1genetic
27708008
DPH6_YEASTDPH6genetic
27708008
GBLP_YEASTASC1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
SPO1_YEASTSPO1genetic
27708008
FKBP_YEASTFPR1genetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
DCAM_YEASTSPE2genetic
27708008
DIA2_YEASTDIA2genetic
27708008
SUR1_YEASTSUR1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
NEW1_YEASTNEW1genetic
27708008
YP027_YEASTYPR027Cgenetic
27708008
VPS4_YEASTVPS4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS16B_YEAST

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"NH2-terminal acetylation of ribosomal proteins of Saccharomycescerevisiae.";
Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
J. Biol. Chem. 267:5442-5445(1992).
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-26, AND ACETYLATION AT SER-2 BYNATA.
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-34, 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-61; THR-70 AND SER-76,AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory