RL16B_YEAST - dbPTM
RL16B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL16B_YEAST
UniProt AC P26785
Protein Name 60S ribosomal protein L16-B {ECO:0000303|PubMed:9559554}
Gene Name RPL16B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 198
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 MSQPVVVIDAKDHLLGRLASTIAKQVLNGQKIVVVRAEALNISGEFFRNKLKYHDFLRKATAFNKTRGPFHFRAPSRILYKAIRGMVSHKTARGKAALERLKIFEGIPPPYDKKKRVVVPQALRVLRLKPGRKYTTLGKLSTSVGWKYEDVVAKLEDKRKVRSAEYYAKKRAFTKKVSSASAAASESDVAKQLASFGY
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------MSQPVVVID
------CCCCEEEEE		43.1010601260
2Phosphorylation------MSQPVVVID
------CCCCEEEEE		43.1022369663
11SuccinylationPVVVIDAKDHLLGRL
CEEEEECCHHHHHHH		41.7723954790
11UbiquitinationPVVVIDAKDHLLGRL
CEEEEECCHHHHHHH		41.7724961812
11AcetylationPVVVIDAKDHLLGRL
CEEEEECCHHHHHHH		41.7724489116
20PhosphorylationHLLGRLASTIAKQVL
HHHHHHHHHHHHHHH		25.5727214570
21PhosphorylationLLGRLASTIAKQVLN
HHHHHHHHHHHHHHC		21.2430377154
24SuccinylationRLASTIAKQVLNGQK
HHHHHHHHHHHCCCE		36.7723954790
24AcetylationRLASTIAKQVLNGQK
HHHHHHHHHHHCCCE		36.7724489116
24UbiquitinationRLASTIAKQVLNGQK
HHHHHHHHHHHCCCE		36.7723749301
31UbiquitinationKQVLNGQKIVVVRAE
HHHHCCCEEEEEEEE		38.5823749301
31AcetylationKQVLNGQKIVVVRAE
HHHHCCCEEEEEEEE		38.5824489116
43PhosphorylationRAEALNISGEFFRNK
EEEEECCCHHHHHHH		31.0617287358
50UbiquitinationSGEFFRNKLKYHDFL
CHHHHHHHHHHHHHH		41.9422817900
52UbiquitinationEFFRNKLKYHDFLRK
HHHHHHHHHHHHHHH		41.9923749301
65UbiquitinationRKATAFNKTRGPFHF
HHHHHCCCCCCCCCC		32.9023749301
81AcetylationAPSRILYKAIRGMVS
CCHHHHHHHHHHHHC		33.6124489116
90UbiquitinationIRGMVSHKTARGKAA
HHHHHCCCCHHCHHH		36.0523749301
102AcetylationKAALERLKIFEGIPP
HHHHHHHHHCCCCCC		52.1224489116
102UbiquitinationKAALERLKIFEGIPP
HHHHHHHHHCCCCCC		52.1217644757
113UbiquitinationGIPPPYDKKKRVVVP
CCCCCCCCCCCEECC		55.1122817900
114UbiquitinationIPPPYDKKKRVVVPQ
CCCCCCCCCCEECCH		42.8022817900
115UbiquitinationPPPYDKKKRVVVPQA
CCCCCCCCCEECCHH		57.0522817900
129UbiquitinationALRVLRLKPGRKYTT
HHHHHCCCCCCCEEE		38.7022817900
133UbiquitinationLRLKPGRKYTTLGKL
HCCCCCCCEEECCCC		53.5223749301
135PhosphorylationLKPGRKYTTLGKLST
CCCCCCEEECCCCCC		20.6927214570
136PhosphorylationKPGRKYTTLGKLSTS
CCCCCEEECCCCCCC		30.3530377154
139UbiquitinationRKYTTLGKLSTSVGW
CCEEECCCCCCCCCC		42.2323749301
143PhosphorylationTLGKLSTSVGWKYED
ECCCCCCCCCCCHHH		18.4321440633
154AcetylationKYEDVVAKLEDKRKV
CHHHHHHHHHHHHHH		40.5824489116
154UbiquitinationKYEDVVAKLEDKRKV
CHHHHHHHHHHHHHH		40.5823749301
154SuccinylationKYEDVVAKLEDKRKV
CHHHHHHHHHHHHHH		40.5823954790
158AcetylationVVAKLEDKRKVRSAE
HHHHHHHHHHHHHHH		44.7524489116
158UbiquitinationVVAKLEDKRKVRSAE
HHHHHHHHHHHHHHH		44.7522817900
160UbiquitinationAKLEDKRKVRSAEYY
HHHHHHHHHHHHHHH		47.9822817900
163PhosphorylationEDKRKVRSAEYYAKK
HHHHHHHHHHHHHHH		28.5628889911
169UbiquitinationRSAEYYAKKRAFTKK
HHHHHHHHHHHHHHH		27.0323749301
170UbiquitinationSAEYYAKKRAFTKKV
HHHHHHHHHHHHHHH		40.5622817900
175UbiquitinationAKKRAFTKKVSSASA
HHHHHHHHHHHHHHH		44.7322817900
176UbiquitinationKKRAFTKKVSSASAA
HHHHHHHHHHHHHHH		44.2723749301
178PhosphorylationRAFTKKVSSASAAAS
HHHHHHHHHHHHHHC		29.1222369663
179PhosphorylationAFTKKVSSASAAASE
HHHHHHHHHHHHHCH		29.2722369663
181PhosphorylationTKKVSSASAAASESD
HHHHHHHHHHHCHHH		22.0122369663
185PhosphorylationSSASAAASESDVAKQ
HHHHHHHCHHHHHHH		32.6722369663
187PhosphorylationASAAASESDVAKQLA
HHHHHCHHHHHHHHH		34.5822369663
191UbiquitinationASESDVAKQLASFGY
HCHHHHHHHHHHCCC		45.7723749301
191AcetylationASESDVAKQLASFGY
HCHHHHHHHHHHCCC		45.7724489116
195PhosphorylationDVAKQLASFGY----
HHHHHHHHCCC----		28.0025521595
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 RL16B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL16B_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 RL16B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL16A_YEASTRPL16Agenetic
3282992
RS3_YEASTRPS3physical
19398006
RL35A_YEASTRPL35Aphysical
19398006
RL35B_YEASTRPL35Aphysical
19398006
SRS2_YEASTSRS2genetic
21459050
RL13A_YEASTRPL13Agenetic
27708008
MRM2_YEASTMRM2genetic
27708008
RL40A_YEASTRPL40Bgenetic
27708008
RL40B_YEASTRPL40Bgenetic
27708008
EDE1_YEASTEDE1genetic
27708008
BUD31_YEASTBUD31genetic
27708008
PAT1_YEASTPAT1genetic
27708008
ADH7_YEASTADH7genetic
27708008
SLX5_YEASTSLX5genetic
27708008
RPN4_YEASTRPN4genetic
27708008
VAM6_YEASTVAM6genetic
27708008
SAN1_YEASTSAN1genetic
27708008
NUM1_YEASTNUM1genetic
27708008
DIN7_YEASTDIN7genetic
27708008
LSM6_YEASTLSM6genetic
27708008
PAC11_YEASTPAC11genetic
27708008
RAD4_YEASTRAD4genetic
27708008
SGF73_YEASTSGF73genetic
27708008
VAM7_YEASTVAM7genetic
27708008
SMI1_YEASTSMI1genetic
27708008
HTD2_YEASTHTD2genetic
27708008
ARP1_YEASTARP1genetic
27708008
WSS1_YEASTWSS1genetic
27708008
RL16A_YEASTRPL16Agenetic
27708008
LSM1_YEASTLSM1genetic
27708008
YJU6_YEASTYJL206Cgenetic
27708008
DOHH_YEASTLIA1genetic
27708008
MOG1_YEASTMOG1genetic
27708008
FRMSR_YEASTYKL069Wgenetic
27708008
DYHC_YEASTDYN1genetic
27708008
LDB18_YEASTLDB18genetic
27708008
SIC1_YEASTSIC1genetic
27708008
ALAM_YEASTALT1genetic
27708008
HMX1_YEASTHMX1genetic
27708008
FKS1_YEASTFKS1genetic
27708008
DYN3_YEASTDYN3genetic
27708008
LIS1_YEASTPAC1genetic
27708008
PMA2_YEASTPMA2genetic
27708008
ARL3_YEASTARL3genetic
27708008
NIP80_YEASTNIP100genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
BRR1_YEASTBRR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL16B_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"The action of N-terminal acetyltransferases on yeast ribosomalproteins.";
Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
J. Biol. Chem. 274:37035-37040(1999).
Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND PARTIAL ACETYLATION AT SER-2 BYNATA.
"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: PROTEIN SEQUENCE OF 2-26, AND ACETYLATION AT SER-2 BY NATA.
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-181; SER-185 ANDSER-187, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, 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-43; SER-179 AND SER-181,AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, ANDMASS 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-195, AND MASSSPECTROMETRY.

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