RL8A_YEAST - dbPTM
RL8A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL8A_YEAST
UniProt AC P17076
Protein Name 60S ribosomal protein L8-A {ECO:0000303|PubMed:9559554}
Gene Name RPL8A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 256
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 MAPGKKVAPAPFGAKSTKSNKTRNPLTHSTPKNFGIGQAVQPKRNLSRYVKWPEYVRVQRQKKILSIRLKVPPTIAQFQYTLDRNTAAETFKLFNKYRPETAAEKKERLTKEAAAVAEGKSKQDASPKPYAVKYGLNHVVALIENKKAKLVLIANDVDPIELVVFLPALCKKMGVPYAIVKGKARLGTLVNQKTSAVAALTEVRAEDEAALAKLVSTIDANFADKYDEVKKHWGGGILGNKAQAKMDKRAKNSDSA
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
6Acetylation--MAPGKKVAPAPFG
--CCCCCCCCCCCCC		49.9325381059
6Ubiquitination--MAPGKKVAPAPFG
--CCCCCCCCCCCCC		49.9323749301
15UbiquitinationAPAPFGAKSTKSNKT
CCCCCCCCCCCCCCC		60.0622817900
15SuccinylationAPAPFGAKSTKSNKT
CCCCCCCCCCCCCCC		60.0623954790
15AcetylationAPAPFGAKSTKSNKT
CCCCCCCCCCCCCCC		60.0624489116
16PhosphorylationPAPFGAKSTKSNKTR
CCCCCCCCCCCCCCC		40.3028152593
17PhosphorylationAPFGAKSTKSNKTRN
CCCCCCCCCCCCCCC		37.4728152593
18UbiquitinationPFGAKSTKSNKTRNP
CCCCCCCCCCCCCCC		60.1522817900
18AcetylationPFGAKSTKSNKTRNP
CCCCCCCCCCCCCCC		60.1525381059
22PhosphorylationKSTKSNKTRNPLTHS
CCCCCCCCCCCCCCC		39.6722369663
27PhosphorylationNKTRNPLTHSTPKNF
CCCCCCCCCCCCCCC		18.2922369663
29PhosphorylationTRNPLTHSTPKNFGI
CCCCCCCCCCCCCCC		40.9622369663
30PhosphorylationRNPLTHSTPKNFGIG
CCCCCCCCCCCCCCC		30.5822369663
32AcetylationPLTHSTPKNFGIGQA
CCCCCCCCCCCCCCC		66.0624489116
32UbiquitinationPLTHSTPKNFGIGQA
CCCCCCCCCCCCCCC		66.0624961812
43SuccinylationIGQAVQPKRNLSRYV
CCCCCCCCCCHHHHC		36.5123954790
43AcetylationIGQAVQPKRNLSRYV
CCCCCCCCCCHHHHC		36.5124489116
43MethylationIGQAVQPKRNLSRYV
CCCCCCCCCCHHHHC		36.5120137074
43UbiquitinationIGQAVQPKRNLSRYV
CCCCCCCCCCHHHHC		36.5115699485
49PhosphorylationPKRNLSRYVKWPEYV
CCCCHHHHCCCHHHH		11.7321440633
51UbiquitinationRNLSRYVKWPEYVRV
CCHHHHCCCHHHHHH		48.3623749301
51AcetylationRNLSRYVKWPEYVRV
CCHHHHCCCHHHHHH		48.3624489116
66PhosphorylationQRQKKILSIRLKVPP
HHCCCEEEEEECCCC		14.7721440633
70UbiquitinationKILSIRLKVPPTIAQ
CEEEEEECCCCCEEE		42.7323749301
92SuccinylationNTAAETFKLFNKYRP
CCHHHHHHHHHHHCH		60.6423954790
92AcetylationNTAAETFKLFNKYRP
CCHHHHHHHHHHHCH		60.6424489116
92UbiquitinationNTAAETFKLFNKYRP
CCHHHHHHHHHHHCH		60.6423749301
96UbiquitinationETFKLFNKYRPETAA
HHHHHHHHHCHHHHH		34.9922817900
96AcetylationETFKLFNKYRPETAA
HHHHHHHHHCHHHHH		34.9924489116
105AcetylationRPETAAEKKERLTKE
CHHHHHHHHHHHHHH		56.0324489116
106UbiquitinationPETAAEKKERLTKEA
HHHHHHHHHHHHHHH		39.3022817900
111SuccinylationEKKERLTKEAAAVAE
HHHHHHHHHHHHHHC		50.3623954790
111AcetylationEKKERLTKEAAAVAE
HHHHHHHHHHHHHHC		50.3624489116
111UbiquitinationEKKERLTKEAAAVAE
HHHHHHHHHHHHHHC		50.3623749301
120UbiquitinationAAAVAEGKSKQDASP
HHHHHCCCCCCCCCC		46.0823749301
121PhosphorylationAAVAEGKSKQDASPK
HHHHCCCCCCCCCCC		46.5422369663
122UbiquitinationAVAEGKSKQDASPKP
HHHCCCCCCCCCCCC		56.5423749301
126PhosphorylationGKSKQDASPKPYAVK
CCCCCCCCCCCHHHH		41.5722369663
128AcetylationSKQDASPKPYAVKYG
CCCCCCCCCHHHHHC		48.4424489116
130PhosphorylationQDASPKPYAVKYGLN
CCCCCCCHHHHHCCH		30.1025521595
133AcetylationSPKPYAVKYGLNHVV
CCCCHHHHHCCHHHH		25.9824489116
146AcetylationVVALIENKKAKLVLI
HHHHHCCCCCEEEEE		41.1224489116
149UbiquitinationLIENKKAKLVLIAND
HHCCCCCEEEEEECC		48.2717644757
171UbiquitinationVFLPALCKKMGVPYA
HHHHHHHHHHCCCEE		46.7917644757
172UbiquitinationFLPALCKKMGVPYAI
HHHHHHHHHCCCEEE		39.6323749301
181AcetylationGVPYAIVKGKARLGT
CCCEEEEECCHHHHH		48.8924489116
188PhosphorylationKGKARLGTLVNQKTS
ECCHHHHHHHCCHHH		31.9321440633
193SuccinylationLGTLVNQKTSAVAAL
HHHHHCCHHHHHHHH		38.9623954790
193UbiquitinationLGTLVNQKTSAVAAL
HHHHHCCHHHHHHHH		38.9623749301
194PhosphorylationGTLVNQKTSAVAALT
HHHHCCHHHHHHHHH		16.5021440633
213UbiquitinationEDEAALAKLVSTIDA
HCHHHHHHHHHHHCH		50.7224961812
213AcetylationEDEAALAKLVSTIDA
HCHHHHHHHHHHHCH		50.7224489116
216PhosphorylationAALAKLVSTIDANFA
HHHHHHHHHHCHHHH		30.0417563356
217PhosphorylationALAKLVSTIDANFAD
HHHHHHHHHCHHHHH		18.5224961812
225SuccinylationIDANFADKYDEVKKH
HCHHHHHCHHHHHHH		51.6923954790
225AcetylationIDANFADKYDEVKKH
HCHHHHHCHHHHHHH		51.6924489116
225UbiquitinationIDANFADKYDEVKKH
HCHHHHHCHHHHHHH		51.6915699485
230UbiquitinationADKYDEVKKHWGGGI
HHCHHHHHHHCCCCC		36.5515699485
230AcetylationADKYDEVKKHWGGGI
HHCHHHHHHHCCCCC		36.5524489116
230SuccinylationADKYDEVKKHWGGGI
HHCHHHHHHHCCCCC		36.5523954790
231UbiquitinationDKYDEVKKHWGGGIL
HCHHHHHHHCCCCCC		50.1715699485
231AcetylationDKYDEVKKHWGGGIL
HCHHHHHHHCCCCCC		50.1722865919
241UbiquitinationGGGILGNKAQAKMDK
CCCCCCHHHHHHHHH		39.8315699485
241MethylationGGGILGNKAQAKMDK
CCCCCCHHHHHHHHH		39.8320137074
241AcetylationGGGILGNKAQAKMDK
CCCCCCHHHHHHHHH		39.8324489116
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 RL8A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL8A_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 RL8A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SKI2_YEASTSKI2genetic
7739557
RRP41_YEASTSKI6genetic
9566888
XRN1_YEASTXRN1genetic
6987655
SKI2_YEASTSKI2genetic
6987655
SKI3_YEASTSKI3genetic
6987655
CSL4_YEASTCSL4genetic
6987655
NMD3_YEASTNMD3physical
17015443
USA1_YEASTUSA1physical
18719252
SSB1_YEASTSSB1physical
19536198
UBC4_YEASTUBC4genetic
20093466
UBS1_YEASTUBS1genetic
20093466
PAT1_YEASTPAT1genetic
20093466
RPN4_YEASTRPN4genetic
20093466
VPS41_YEASTVPS41genetic
20093466
EAF1_YEASTEAF1genetic
20093466
SEM1_YEASTSEM1genetic
20093466
EMI2_YEASTEMI2genetic
20093466
SWI4_YEASTSWI4genetic
20093466
UBP6_YEASTUBP6genetic
20093466
DBP3_YEASTDBP3genetic
20093466
SGF73_YEASTSGF73genetic
20093466
SLX9_YEASTSLX9genetic
20093466
PSA3_YEASTPRE9genetic
20093466
G3P3_YEASTTDH3genetic
20093466
RPN10_YEASTRPN10genetic
20093466
FMC1_YEASTFMC1genetic
20093466
MGA2_YEASTMGA2genetic
20093466
LSM1_YEASTLSM1genetic
20093466
DOA1_YEASTDOA1genetic
20093466
RL14A_YEASTRPL14Agenetic
20093466
DYHC_YEASTDYN1genetic
20093466
RL8B_YEASTRPL8Bgenetic
20093466
ARP6_YEASTARP6genetic
20093466
RSC2_YEASTRSC2genetic
20093466
SAM37_YEASTSAM37genetic
20093466
UBX4_YEASTUBX4genetic
20093466
MED9_YEASTCSE2genetic
20093466
BUB3_YEASTBUB3genetic
20093466
VAM3_YEASTVAM3genetic
20093466
LCB4_YEASTLCB4genetic
20093466
ULS1_YEASTULS1genetic
20093466
PPQ1_YEASTPPQ1genetic
20093466
SUR1_YEASTSUR1genetic
20093466
YME1_YEASTYME1genetic
20093466
RL8B_YEASTRPL8Bgenetic
22377630
TCPZ_YEASTCCT6genetic
27708008
BOS1_YEASTBOS1genetic
27708008
MCM1_YEASTMCM1genetic
27708008
UBX4_YEASTUBX4genetic
27708008
EXO84_YEASTEXO84genetic
27708008
CDK1_YEASTCDC28genetic
27708008
CDC10_YEASTCDC10genetic
27708008
COPA_YEASTCOP1genetic
27708008
RPN5_YEASTRPN5genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TFB1_YEASTTFB1genetic
27708008
RPB7_YEASTRPB7genetic
27708008
PSB3_YEASTPUP3genetic
27708008
CDC4_YEASTCDC4genetic
27708008
ACT_YEASTACT1genetic
27708008
PMM_YEASTSEC53genetic
27708008
RPN11_YEASTRPN11genetic
27708008
PSB7_YEASTPRE4genetic
27708008
RPN12_YEASTRPN12genetic
27708008
PRS8_YEASTRPT6genetic
27708008
ALG2_YEASTALG2genetic
27708008
DAM1_YEASTDAM1genetic
27708008
PRP21_YEASTPRP21genetic
27708008
ESS1_YEASTESS1genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
ABF1_YEASTABF1genetic
27708008
PRS7_YEASTRPT1genetic
27708008
MED14_YEASTRGR1genetic
27708008
CDC3_YEASTCDC3genetic
27708008
IMB1_YEASTKAP95genetic
27708008
HMCS_YEASTERG13genetic
27708008
SGT1_YEASTSGT1genetic
27708008
PSB5_YEASTPRE2genetic
27708008
RPN7_YEASTRPN7genetic
27708008
UBC4_YEASTUBC4genetic
27708008
PER1_YEASTPER1genetic
27708008
PAT1_YEASTPAT1genetic
27708008
RPN4_YEASTRPN4genetic
27708008
VPS41_YEASTVPS41genetic
27708008
SGF73_YEASTSGF73genetic
27708008
PSA3_YEASTPRE9genetic
27708008
RPN10_YEASTRPN10genetic
27708008
FMC1_YEASTFMC1genetic
27708008
MGA2_YEASTMGA2genetic
27708008
LSM1_YEASTLSM1genetic
27708008
DOA1_YEASTDOA1genetic
27708008
SAM37_YEASTSAM37genetic
27708008
VAM3_YEASTVAM3genetic
27708008
ULS1_YEASTULS1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
PPQ1_YEASTPPQ1genetic
27708008
VPS4_YEASTVPS4genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL8A_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-126 AND SER-216, 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-216, 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-126, AND MASSSPECTROMETRY.

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