RL6B_YEAST - dbPTM
RL6B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL6B_YEAST
UniProt AC P05739
Protein Name 60S ribosomal protein L6-B {ECO:0000303|PubMed:9559554}
Gene Name RPL6B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 176
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 MTAQQAPKWYPSEDVAAPKKTRKAVRPQKLRASLVPGTVLILLAGRFRGKRVVYLKHLEDNTLLVTGPFKVNGVPLRRVNARYVIATSTKVSVEGVNVEKFNVEYFAKEKLTKKEKKEANLFPEQQTKEIKTERVEDQKVVDKALLAEIKKTPLLKQYLSASFSLKNGDKPHLLKF
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
8SuccinylationMTAQQAPKWYPSEDV
CCCCCCCCCCCCCCC		63.4823954790
8UbiquitinationMTAQQAPKWYPSEDV
CCCCCCCCCCCCCCC		63.4824961812
12PhosphorylationQAPKWYPSEDVAAPK
CCCCCCCCCCCCCCC		30.6325752575
19UbiquitinationSEDVAAPKKTRKAVR
CCCCCCCCCCCCCCC		63.1523749301
19AcetylationSEDVAAPKKTRKAVR
CCCCCCCCCCCCCCC		63.1524489116
19SuccinylationSEDVAAPKKTRKAVR
CCCCCCCCCCCCCCC		63.1523954790
20UbiquitinationEDVAAPKKTRKAVRP
CCCCCCCCCCCCCCC		53.1322817900
23UbiquitinationAAPKKTRKAVRPQKL
CCCCCCCCCCCCHHH		57.3722817900
29UbiquitinationRKAVRPQKLRASLVP
CCCCCCHHHHHHCCC		42.4923749301
33PhosphorylationRPQKLRASLVPGTVL
CCHHHHHHCCCCCEE		24.3822369663
38PhosphorylationRASLVPGTVLILLAG
HHHCCCCCEEEEEEE		13.1822369663
56UbiquitinationGKRVVYLKHLEDNTL
CEEEEEEEECCCCEE		28.5817644757
56AcetylationGKRVVYLKHLEDNTL
CEEEEEEEECCCCEE		28.5824489116
70AcetylationLLVTGPFKVNGVPLR
EEEECCEEECCEECC		37.6124489116
70UbiquitinationLLVTGPFKVNGVPLR
EEEECCEEECCEECC		37.6117644757
90UbiquitinationYVIATSTKVSVEGVN
EEEEECEEEEEECCC		32.0723749301
92PhosphorylationIATSTKVSVEGVNVE
EEECEEEEEECCCHH		18.9230377154
100UbiquitinationVEGVNVEKFNVEYFA
EECCCHHHEEHHHHH		37.6523749301
100AcetylationVEGVNVEKFNVEYFA
EECCCHHHEEHHHHH		37.6524489116
108SuccinylationFNVEYFAKEKLTKKE
EEHHHHHHHHCCHHH		45.5423954790
108UbiquitinationFNVEYFAKEKLTKKE
EEHHHHHHHHCCHHH		45.5423749301
108AcetylationFNVEYFAKEKLTKKE
EEHHHHHHHHCCHHH		45.5424489116
1082-HydroxyisobutyrylationFNVEYFAKEKLTKKE
EEHHHHHHHHCCHHH		45.54-
110UbiquitinationVEYFAKEKLTKKEKK
HHHHHHHHCCHHHHH		61.8322817900
113UbiquitinationFAKEKLTKKEKKEAN
HHHHHCCHHHHHHHC		70.1722817900
114UbiquitinationAKEKLTKKEKKEANL
HHHHCCHHHHHHHCC		70.3222817900
116UbiquitinationEKLTKKEKKEANLFP
HHCCHHHHHHHCCCC		65.8722817900
117UbiquitinationKLTKKEKKEANLFPE
HCCHHHHHHHCCCCH		64.2523749301
128AcetylationLFPEQQTKEIKTERV
CCCHHHHHHHHHCCC		53.7724489116
128UbiquitinationLFPEQQTKEIKTERV
CCCHHHHHHHHHCCC		53.7723749301
131SuccinylationEQQTKEIKTERVEDQ
HHHHHHHHHCCCCCH		45.4823954790
131UbiquitinationEQQTKEIKTERVEDQ
HHHHHHHHHCCCCCH		45.4822817900
139UbiquitinationTERVEDQKVVDKALL
HCCCCCHHHHCHHHH		57.4523749301
139SuccinylationTERVEDQKVVDKALL
HCCCCCHHHHCHHHH		57.4523954790
139AcetylationTERVEDQKVVDKALL
HCCCCCHHHHCHHHH		57.4524489116
1392-HydroxyisobutyrylationTERVEDQKVVDKALL
HCCCCCHHHHCHHHH		57.45-
143UbiquitinationEDQKVVDKALLAEIK
CCHHHHCHHHHHHHH		29.3523749301
143SuccinylationEDQKVVDKALLAEIK
CCHHHHCHHHHHHHH		29.3523954790
143AcetylationEDQKVVDKALLAEIK
CCHHHHCHHHHHHHH		29.3524489116
1432-HydroxyisobutyrylationEDQKVVDKALLAEIK
CCHHHHCHHHHHHHH		29.35-
1502-HydroxyisobutyrylationKALLAEIKKTPLLKQ
HHHHHHHHCCHHHHH		41.94-
150SuccinylationKALLAEIKKTPLLKQ
HHHHHHHHCCHHHHH		41.9423954790
150AcetylationKALLAEIKKTPLLKQ
HHHHHHHHCCHHHHH		41.9424489116
150UbiquitinationKALLAEIKKTPLLKQ
HHHHHHHHCCHHHHH		41.9423749301
151UbiquitinationALLAEIKKTPLLKQY
HHHHHHHCCHHHHHH		62.1222817900
156UbiquitinationIKKTPLLKQYLSASF
HHCCHHHHHHHHHHE		44.5823749301
160PhosphorylationPLLKQYLSASFSLKN
HHHHHHHHHHEECCC		19.5522369663
162PhosphorylationLKQYLSASFSLKNGD
HHHHHHHHEECCCCC		16.4022369663
164PhosphorylationQYLSASFSLKNGDKP
HHHHHHEECCCCCCC		35.6222369663
166UbiquitinationLSASFSLKNGDKPHL
HHHHEECCCCCCCCE		58.6523749301
170UbiquitinationFSLKNGDKPHLLKF-
EECCCCCCCCEECC-		35.4222817900
175AcetylationGDKPHLLKF------
CCCCCEECC------		56.2224489116
175UbiquitinationGDKPHLLKF------
CCCCCEECC------		56.2223749301
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 RL6B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL6B_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 RL6B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCN4_YEASTGCN4genetic
18423200
ADT2_YEASTPET9genetic
19160490
PHB1_YEASTPHB1genetic
19160490
YME1_YEASTYME1genetic
19160490
RL23A_YEASTRPL23Agenetic
27708008
RL23B_YEASTRPL23Agenetic
27708008
TCM62_YEASTTCM62genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
ASK10_YEASTASK10genetic
27708008
CDK1_YEASTCDC28genetic
27708008
APC11_YEASTAPC11genetic
27708008
RPN5_YEASTRPN5genetic
27708008
DAD1_YEASTDAD1genetic
27708008
HEM6_YEASTHEM13genetic
27708008
ERF3_YEASTSUP35genetic
27708008
RMRP_YEASTSNM1genetic
27708008
PSB3_YEASTPUP3genetic
27708008
RPN11_YEASTRPN11genetic
27708008
PRS8_YEASTRPT6genetic
27708008
PRP18_YEASTPRP18genetic
27708008
TFC4_YEASTTFC4genetic
27708008
RPN1_YEASTRPN1genetic
27708008
MED14_YEASTRGR1genetic
27708008
MPPB_YEASTMAS1genetic
27708008
GSP1_YEASTGSP1genetic
27708008
MED11_YEASTMED11genetic
27708008
ERG8_YEASTERG8genetic
27708008
DPOA_YEASTPOL1genetic
27708008
PSA7_YEASTPRE10genetic
27708008
PSB5_YEASTPRE2genetic
27708008
RPN7_YEASTRPN7genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
YBQ6_YEASTYBR056Wgenetic
27708008
UBC4_YEASTUBC4genetic
27708008
SGF29_YEASTSGF29genetic
27708008
RPN4_YEASTRPN4genetic
27708008
GPR1_YEASTGPR1genetic
27708008
VAM6_YEASTVAM6genetic
27708008
NUM1_YEASTNUM1genetic
27708008
SEM1_YEASTSEM1genetic
27708008
RV167_YEASTRVS167genetic
27708008
UBP6_YEASTUBP6genetic
27708008
MRM2_YEASTMRM2genetic
27708008
XRN1_YEASTXRN1genetic
27708008
RS25A_YEASTRPS25Agenetic
27708008
YHJ5_YEASTNEL1genetic
27708008
HTD2_YEASTHTD2genetic
27708008
THP2_YEASTTHP2genetic
27708008
FIS1_YEASTFIS1genetic
27708008
FMC1_YEASTFMC1genetic
27708008
ILM1_YEASTILM1genetic
27708008
POM33_YEASTPOM33genetic
27708008
LDB18_YEASTLDB18genetic
27708008
SIC1_YEASTSIC1genetic
27708008
COA4_YEASTCOA4genetic
27708008
PSP2_YEASTPSP2genetic
27708008
GTR1_YEASTGTR1genetic
27708008
GBLP_YEASTASC1genetic
27708008
DIA1_YEASTDIA1genetic
27708008
COQ7_YEASTCAT5genetic
27708008
VPS17_YEASTVPS17genetic
27708008
PUS7_YEASTPUS7genetic
27708008
VTS1_YEASTVTS1genetic
27708008
MTHR1_YEASTMET12genetic
27708008
SUR1_YEASTSUR1genetic
27708008
KES1_YEASTKES1genetic
27708008
DAP1_YEASTDAP1genetic
27708008
RU2A_YEASTLEA1genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL6B_YEAST

loading...

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-162, 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-162, AND MASSSPECTROMETRY.

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