RL13A_YEAST - dbPTM
RL13A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL13A_YEAST
UniProt AC Q12690
Protein Name 60S ribosomal protein L13-A {ECO:0000303|PubMed:9559554}
Gene Name RPL13A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 199
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 MAISKNLPILKNHFRKHWQERVKVHFDQAGKKVSRRNARATRAAKIAPRPLDLLRPVVRAPTVKYNRKVRAGRGFTLAEVKAAGLTAAYARTIGIAVDHRRQNRNQEIFDANVQRLKEYQSKIIVFPRNGKAPEAEQVLSAAATFPIAQPATDVEARAVQDNGESAFRTLRLARSEKKFRGIREKRAREKAEAEAEKKK
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
5Ubiquitination---MAISKNLPILKN
---CCCCCCCHHHHH		57.2924961812
31UbiquitinationVHFDQAGKKVSRRNA
HHHHHHCCHHHHHHH		53.6822817900
32UbiquitinationHFDQAGKKVSRRNAR
HHHHHCCHHHHHHHH		44.5222817900
45UbiquitinationARATRAAKIAPRPLD
HHHHHHHHHCCCCHH		38.1123749301
62PhosphorylationRPVVRAPTVKYNRKV
CCCCCCCCCCCCCEE		28.7520377248
64UbiquitinationVVRAPTVKYNRKVRA
CCCCCCCCCCCEECC		39.0123749301
68UbiquitinationPTVKYNRKVRAGRGF
CCCCCCCEECCCCCC		32.2222817900
76PhosphorylationVRAGRGFTLAEVKAA
ECCCCCCCHHHHHHH		28.0722369663
81UbiquitinationGFTLAEVKAAGLTAA
CCCHHHHHHHCHHHH		24.8323749301
86PhosphorylationEVKAAGLTAAYARTI
HHHHHCHHHHHHHHH		14.3421440633
89PhosphorylationAAGLTAAYARTIGIA
HHCHHHHHHHHHCHH		8.3121082442
117UbiquitinationDANVQRLKEYQSKII
HHHHHHHHHHHCCEE		57.4723749301
122UbiquitinationRLKEYQSKIIVFPRN
HHHHHHCCEEEECCC		22.4124961812
131UbiquitinationIVFPRNGKAPEAEQV
EEECCCCCCCHHHHH		65.4024961812
140PhosphorylationPEAEQVLSAAATFPI
CHHHHHHHHHHCCCC		19.6022369663
144PhosphorylationQVLSAAATFPIAQPA
HHHHHHHCCCCCCCC		25.8022890988
152PhosphorylationFPIAQPATDVEARAV
CCCCCCCCHHHHHHH		47.4622369663
165PhosphorylationAVQDNGESAFRTLRL
HHHCCHHHHHHHHHH		33.8224909858
169PhosphorylationNGESAFRTLRLARSE
CHHHHHHHHHHHHCH		15.1324961812
175PhosphorylationRTLRLARSEKKFRGI
HHHHHHHCHHHHHHH		48.4324961812
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 RL13A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL13A_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 RL13A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC4_YEASTUBC4genetic
20093466
MBA1_YEASTMBA1genetic
20093466
CHK1_YEASTCHK1genetic
20093466
RV161_YEASTRVS161genetic
20093466
RIM1_YEASTRIM1genetic
20093466
PAT1_YEASTPAT1genetic
20093466
ARF1_YEASTARF1genetic
20093466
PP4C_YEASTPPH3genetic
20093466
GNTK_YEASTYDR248Cgenetic
20093466
SEM1_YEASTSEM1genetic
20093466
LSM6_YEASTLSM6genetic
20093466
RV167_YEASTRVS167genetic
20093466
SPT3_YEASTSPT3genetic
20093466
IES5_YEASTIES5genetic
20093466
UBP6_YEASTUBP6genetic
20093466
HAP2_YEASTHAP2genetic
20093466
XRN1_YEASTXRN1genetic
20093466
AAKG_YEASTSNF4genetic
20093466
THP2_YEASTTHP2genetic
20093466
STB5_YEASTSTB5genetic
20093466
IST3_YEASTIST3genetic
20093466
PIR5_YEASTYJL160Cgenetic
20093466
LSM1_YEASTLSM1genetic
20093466
YJ24_YEASTKCH1genetic
20093466
PTK2_YEASTPTK2genetic
20093466
LDB18_YEASTLDB18genetic
20093466
SIC1_YEASTSIC1genetic
20093466
DPH5_YEASTDPH5genetic
20093466
YL271_YEASTYLR271Wgenetic
20093466
COQ11_YEASTYLR290Cgenetic
20093466
GTR1_YEASTGTR1genetic
20093466
GBLP_YEASTASC1genetic
20093466
AEP2_YEASTAEP2genetic
20093466
LSM7_YEASTLSM7genetic
20093466
EOS1_YEASTEOS1genetic
20093466
DOM34_YEASTDOM34genetic
20093466
COQ7_YEASTCAT5genetic
20093466
SRO7_YEASTSRO7genetic
20093466
SYT1_YEASTSYT1genetic
20093466
SIR2_YEASTSIR2genetic
21902802
RL13B_YEASTRPL13Bgenetic
22377630
CHK1_YEASTCHK1genetic
22282571
RS7B_YEASTRPS7Bgenetic
27708008
UBC4_YEASTUBC4genetic
27708008
MBA1_YEASTMBA1genetic
27708008
CHK1_YEASTCHK1genetic
27708008
RIM1_YEASTRIM1genetic
27708008
PAT1_YEASTPAT1genetic
27708008
DHSD_YEASTSDH4genetic
27708008
LSM6_YEASTLSM6genetic
27708008
YD541_YEASTYDR541Cgenetic
27708008
UBP6_YEASTUBP6genetic
27708008
SGF73_YEASTSGF73genetic
27708008
AAKG_YEASTSNF4genetic
27708008
XRN1_YEASTXRN1genetic
27708008
ASK10_YEASTASK10genetic
27708008
STB5_YEASTSTB5genetic
27708008
IST3_YEASTIST3genetic
27708008
LSM1_YEASTLSM1genetic
27708008
PIR5_YEASTYJL160Cgenetic
27708008
RAD7_YEASTRAD7genetic
27708008
YJ24_YEASTKCH1genetic
27708008
TCTP_YEASTTMA19genetic
27708008
MMM1_YEASTMMM1genetic
27708008
SIC1_YEASTSIC1genetic
27708008
YL271_YEASTYLR271Wgenetic
27708008
COQ11_YEASTYLR290Cgenetic
27708008
SRR1L_YEASTBER1genetic
27708008
YL415_YEASTYLR415Cgenetic
27708008
GTR1_YEASTGTR1genetic
27708008
MGR3_YEASTMGR3genetic
27708008
GBLP_YEASTASC1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
EOS1_YEASTEOS1genetic
27708008
SWS2_YEASTSWS2genetic
27708008
LSM7_YEASTLSM7genetic
27708008
ROD1_YEASTROD1genetic
27708008
GLO4_YEASTGLO4genetic
27708008
COQ7_YEASTCAT5genetic
27708008
ATG13_YEASTATG13genetic
27708008
QCR2_YEASTQCR2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL13A_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-140 AND THR-152, ANDMASS 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-140, AND MASSSPECTROMETRY.
"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-140, AND MASSSPECTROMETRY.

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