RS24B_YEAST - dbPTM
RS24B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS24B_YEAST
UniProt AC P0CX32
Protein Name 40S ribosomal protein S24-B {ECO:0000303|PubMed:9559554}
Gene Name RPS24B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 135
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 MSDAVTIRTRKVISNPLLARKQFVVDVLHPNRANVSKDELREKLAEVYKAEKDAVSVFGFRTQFGGGKSVGFGLVYNSVAEAKKFEPTYRLVRYGLAEKVEKASRQQRKQKKNRDKKIFGTGKRLAKKVARRNAD
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
2Phosphorylation------MSDAVTIRT
------CCCCEEECC		33.9924961812
2Acetylation------MSDAVTIRT
------CCCCEEECC		33.9922814378
6Phosphorylation--MSDAVTIRTRKVI
--CCCCEEECCCHHH		13.3828889911
9PhosphorylationSDAVTIRTRKVISNP
CCCEEECCCHHHCCH		30.8724961812
11UbiquitinationAVTIRTRKVISNPLL
CEEECCCHHHCCHHH		43.2223749301
14PhosphorylationIRTRKVISNPLLARK
ECCCHHHCCHHHHCC		35.0722369663
21UbiquitinationSNPLLARKQFVVDVL
CCHHHHCCCEEEEEC		42.3423749301
36PhosphorylationHPNRANVSKDELREK
CCCCCCCCHHHHHHH		33.9122369663
37UbiquitinationPNRANVSKDELREKL
CCCCCCCHHHHHHHH		51.4422817900
43UbiquitinationSKDELREKLAEVYKA
CHHHHHHHHHHHHHH		46.7123749301
49UbiquitinationEKLAEVYKAEKDAVS
HHHHHHHHHHHHCEE		56.0723749301
52UbiquitinationAEVYKAEKDAVSVFG
HHHHHHHHHCEEEEE		56.7123749301
56PhosphorylationKAEKDAVSVFGFRTQ
HHHHHCEEEEEEEEE		17.2828152593
62PhosphorylationVSVFGFRTQFGGGKS
EEEEEEEEEECCCCE		26.4528889911
68UbiquitinationRTQFGGGKSVGFGLV
EEEECCCCEEEEEEE		45.2923749301
69PhosphorylationTQFGGGKSVGFGLVY
EEECCCCEEEEEEEE		30.6521440633
83UbiquitinationYNSVAEAKKFEPTYR
ECCHHHHHCCCCHHH		49.8823749301
84UbiquitinationNSVAEAKKFEPTYRL
CCHHHHHCCCCHHHH		63.1123749301
94PhosphorylationPTYRLVRYGLAEKVE
CHHHHHHHHHHHHHH		14.7121082442
99UbiquitinationVRYGLAEKVEKASRQ
HHHHHHHHHHHHHHH		50.5223749301
102UbiquitinationGLAEKVEKASRQQRK
HHHHHHHHHHHHHHH		55.4322817900
111UbiquitinationSRQQRKQKKNRDKKI
HHHHHHHHHHHHHHH		55.8622817900
112UbiquitinationRQQRKQKKNRDKKIF
HHHHHHHHHHHHHHH		55.5122817900
116UbiquitinationKQKKNRDKKIFGTGK
HHHHHHHHHHHHHHH		44.5222817900
117UbiquitinationQKKNRDKKIFGTGKR
HHHHHHHHHHHHHHH		47.7823749301
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 RS24B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS24B_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 RS24B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YB111_YEASTYBL111Cphysical
16554755
TCM62_YEASTTCM62physical
16554755
YSW1_YEASTYSW1physical
16554755
EBP2_YEASTEBP2physical
16554755
UTH1_YEASTUTH1physical
16554755
IMB1_YEASTKAP95physical
16554755
PDR10_YEASTPDR10physical
16554755
LSP1_YEASTLSP1physical
18719252
RIM15_YEASTRIM15genetic
20093466
XRN1_YEASTXRN1genetic
20093466
ARP1_YEASTARP1genetic
20093466
YJH0_YEASTYJL070Cgenetic
20093466
SIC1_YEASTSIC1genetic
20093466
VRP1_YEASTVRP1genetic
20093466
ERG2_YEASTERG2genetic
20093466
NST1_YEASTNST1genetic
20093466
YNB1_YEASTYNL011Cgenetic
20093466
DOM34_YEASTDOM34genetic
20093466
ERP4_YEASTERP4genetic
20093466
GLO4_YEASTGLO4genetic
20093466
VPS5_YEASTVPS5genetic
20093466
PUR6_YEASTADE2genetic
20093466
LPE10_YEASTMFM1genetic
20093466
AP1G1_YEASTAPL4genetic
20093466
SPEE_YEASTSPE3genetic
20093466
CTF4_YEASTCTF4genetic
20093466
PDXH_YEASTYPR172Wgenetic
20093466
OPT2_YEASTOPT2genetic
20093466
RIM15_YEASTRIM15genetic
22282571
SWC4_YEASTSWC4genetic
27708008
MCM1_YEASTMCM1genetic
27708008
GLO4_YEASTGLO4genetic
27708008
RPN6_YEASTRPN6genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC20_YEASTCDC20genetic
27708008
CDC11_YEASTCDC11genetic
27708008
RU1C_YEASTYHC1genetic
27708008
SGT1_YEASTSGT1genetic
27708008
PSA7_YEASTPRE10genetic
27708008
RIM15_YEASTRIM15genetic
27708008
ARP1_YEASTARP1genetic
27708008
YJH0_YEASTYJL070Cgenetic
27708008
ERG2_YEASTERG2genetic
27708008
DOM34_YEASTDOM34genetic
27708008
YO13A_YEASTYOL013W-Agenetic
27708008
ERP4_YEASTERP4genetic
27708008
CTF4_YEASTCTF4genetic
27708008
PDXH_YEASTYPR172Wgenetic
27708008
OPT2_YEASTOPT2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS24B_YEAST

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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: PROTEIN SEQUENCE OF 2-16, 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-14, AND MASSSPECTROMETRY.
"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-14, AND MASSSPECTROMETRY.

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