RL1B_YEAST - dbPTM
RL1B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL1B_YEAST
UniProt AC P0CX44
Protein Name 60S ribosomal protein L1-B {ECO:0000303|PubMed:9559554}
Gene Name RPL1B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 217
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. uL1 forms part of the L1 stalk, a mobile element that plays a role in evacuating the exit-site tRNA..
Protein Sequence MSKITSSQVREHVKELLKYSNETKKRNFLETVELQVGLKNYDPQRDKRFSGSLKLPNCPRPNMSICIFGDAFDVDRAKSCGVDAMSVDDLKKLNKNKKLIKKLSKKYNAFIASEVLIKQVPRLLGPQLSKAGKFPTPVSHNDDLYGKVTDVRSTIKFQLKKVLCLAVAVGNVEMEEDVLVNQILMSVNFFVSLLKKNWQNVGSLVVKSSMGPAFRLY
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------MSKITSSQV
------CCCCCHHHH		32.5310601260
5Phosphorylation---MSKITSSQVREH
---CCCCCHHHHHHH		26.5119823750
6Phosphorylation--MSKITSSQVREHV
--CCCCCHHHHHHHH		23.4219823750
7Phosphorylation-MSKITSSQVREHVK
-CCCCCHHHHHHHHH		24.8419823750
14UbiquitinationSQVREHVKELLKYSN
HHHHHHHHHHHHCCH		44.5522817900
18UbiquitinationEHVKELLKYSNETKK
HHHHHHHHCCHHHHC		60.2923749301
39UbiquitinationVELQVGLKNYDPQRD
EEEEEECCCCCCCCC		47.7515699485
47MethylationNYDPQRDKRFSGSLK
CCCCCCCCCCCCCCC		58.4921460220
54UbiquitinationKRFSGSLKLPNCPRP
CCCCCCCCCCCCCCC		64.6923749301
64PhosphorylationNCPRPNMSICIFGDA
CCCCCCCEEEEECCC		22.4321440633
78UbiquitinationAFDVDRAKSCGVDAM
CCCHHHHHHCCCCCC		47.3623749301
79PhosphorylationFDVDRAKSCGVDAMS
CCHHHHHHCCCCCCC		18.3417330950
86PhosphorylationSCGVDAMSVDDLKKL
HCCCCCCCHHHHHHH		24.9021440633
91UbiquitinationAMSVDDLKKLNKNKK
CCCHHHHHHHHHCHH		63.3115699485
92UbiquitinationMSVDDLKKLNKNKKL
CCHHHHHHHHHCHHH		65.6715699485
105UbiquitinationKLIKKLSKKYNAFIA
HHHHHHHHHHHHHHH		70.4817644757
106UbiquitinationLIKKLSKKYNAFIAS
HHHHHHHHHHHHHHH		40.1217644757
118UbiquitinationIASEVLIKQVPRLLG
HHHHHHHHHHHHHHC		40.8717644757
129PhosphorylationRLLGPQLSKAGKFPT
HHHCHHHHHCCCCCC		18.4028152593
130UbiquitinationLLGPQLSKAGKFPTP
HHCHHHHHCCCCCCC		70.5223749301
133UbiquitinationPQLSKAGKFPTPVSH
HHHHHCCCCCCCCCC		53.6924961812
147UbiquitinationHNDDLYGKVTDVRST
CCCCCCCCCCCHHHH		28.5323749301
196UbiquitinationFFVSLLKKNWQNVGS
HHHHHHHHHHCCHHH		64.4915699485
207UbiquitinationNVGSLVVKSSMGPAF
CHHHHEEECCCCCCC		29.3615699485
208PhosphorylationVGSLVVKSSMGPAFR
HHHHEEECCCCCCCC		17.5921440633
209PhosphorylationGSLVVKSSMGPAFRL
HHHEEECCCCCCCCC		23.2621440633
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 RL1B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL1B_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 RL1B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS41_YEASTVPS41genetic
20093466
HSP78_YEASTHSP78genetic
20093466
RPOM_YEASTRPO41genetic
20093466
GCN20_YEASTGCN20genetic
20093466
YG35_YEASTYGR125Wgenetic
20093466
PHB1_YEASTPHB1genetic
20093466
PUT2_YEASTPUT2genetic
20093466
RPN10_YEASTRPN10genetic
20093466
AIM21_YEASTAIM21genetic
20093466
YJY1_YEASTYJR011Cgenetic
20093466
NNK1_YEASTNNK1genetic
20093466
EF1G2_YEASTTEF4genetic
20093466
DYHC_YEASTDYN1genetic
20093466
YCT1_YEASTYCT1genetic
20093466
LDB18_YEASTLDB18genetic
20093466
RL8B_YEASTRPL8Bgenetic
20093466
COX12_YEASTCOX12genetic
20093466
MSC3_YEASTMSC3genetic
20093466
VIP1_YEASTVIP1genetic
20093466
SIW14_YEASTSIW14genetic
20093466
DIA2_YEASTDIA2genetic
20093466
LSM1_YEASTLSM1genetic
20876302
PAT1_YEASTPAT1genetic
20876302
XRN1_YEASTXRN1genetic
20876302
GBLP_YEASTASC1genetic
20876302
UBC4_YEASTUBC4genetic
20876302
RPN4_YEASTRPN4genetic
20876302
UBP6_YEASTUBP6genetic
20876302
PSA3_YEASTPRE9genetic
20876302
CUE3_YEASTCUE3genetic
20876302
DOA1_YEASTDOA1genetic
20876302
RPN10_YEASTRPN10genetic
20876302
RUP1_YEASTRUP1genetic
20876302
SEM1_YEASTSEM1genetic
20876302
UBI4P_YEASTUBI4genetic
20876302
UBP2_YEASTUBP2genetic
20876302
UBP8_YEASTUBP8genetic
20876302
UBA4_YEASTUBA4genetic
20876302
ULS1_YEASTULS1genetic
20876302
URM1_YEASTURM1genetic
20876302
RV161_YEASTRVS161genetic
20876302
RV167_YEASTRVS167genetic
20876302
EAF7_YEASTEAF7genetic
20876302
BEM1_YEASTBEM1genetic
20876302
SGF11_YEASTSGF11genetic
20876302
STB5_YEASTSTB5genetic
20876302
NNK1_YEASTNNK1genetic
22282571
HRR25_YEASTHRR25genetic
27708008
NIP7_YEASTNIP7genetic
27708008
IWS1_YEASTSPN1genetic
27708008
SEC23_YEASTSEC23genetic
27708008
SNT1_YEASTSNT1genetic
27708008
UME6_YEASTUME6genetic
27708008
YEY6_YEASTYER156Cgenetic
27708008
MOG1_YEASTMOG1genetic
27708008
SCS7_YEASTSCS7genetic
27708008
BUD21_YEASTBUD21genetic
27708008
OPY2_YEASTOPY2genetic
27708008
VPS4_YEASTVPS4genetic
27708008
ERD2_YEASTERD2genetic
27708008
EXO84_YEASTEXO84genetic
27708008
ERF3_YEASTSUP35genetic
27708008
SMT3_YEASTSMT3genetic
27708008
PSB3_YEASTPUP3genetic
27708008
GDI1_YEASTGDI1genetic
27708008
ACT_YEASTACT1genetic
27708008
SMD1_YEASTSMD1genetic
27708008
RPN1_YEASTRPN1genetic
27708008
YHS2_YEASTCIA2genetic
27708008
SMC3_YEASTSMC3genetic
27708008
EXO70_YEASTEXO70genetic
27708008
KRE9_YEASTKRE9genetic
27708008
CDC11_YEASTCDC11genetic
27708008
PRS7_YEASTRPT1genetic
27708008
NSE1_YEASTNSE1genetic
27708008
NOP56_YEASTNOP56genetic
27708008
SEN1_YEASTSEN1genetic
27708008
CAP_YEASTSRV2genetic
27708008
PSA7_YEASTPRE10genetic
27708008
HIR1_YEASTHIR1genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
SSH1_YEASTSSH1genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
RPN4_YEASTRPN4genetic
27708008
VAM6_YEASTVAM6genetic
27708008
ARO1_YEASTARO1genetic
27708008
NUM1_YEASTNUM1genetic
27708008
NBP2_YEASTNBP2genetic
27708008
DHSD_YEASTSDH4genetic
27708008
HEL2_YEASTHEL2genetic
27708008
PAL1_YEASTPAL1genetic
27708008
MRB1_YEASTPHO92genetic
27708008
SNF1_YEASTSNF1genetic
27708008
PAC11_YEASTPAC11genetic
27708008
BOI2_YEASTBOI2genetic
27708008
SODM_YEASTSOD2genetic
27708008
STB5_YEASTSTB5genetic
27708008
VPS53_YEASTVPS53genetic
27708008
RAV1_YEASTRAV1genetic
27708008
VPS55_YEASTVPS55genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
STE24_YEASTSTE24genetic
27708008
HIR3_YEASTHIR3genetic
27708008
CAPZA_YEASTCAP1genetic
27708008
VPS24_YEASTVPS24genetic
27708008
APE2_YEASTAPE2genetic
27708008
IRS4_YEASTIRS4genetic
27708008
DBP7_YEASTDBP7genetic
27708008
SHB17_YEASTSHB17genetic
27708008
ERG3_YEASTERG3genetic
27708008
ALAM_YEASTALT1genetic
27708008
COG8_YEASTCOG8genetic
27708008
TSL1_YEASTTSL1genetic
27708008
PKR1_YEASTPKR1genetic
27708008
YM22_YEASTYMR144Wgenetic
27708008
DYN3_YEASTDYN3genetic
27708008
COG6_YEASTCOG6genetic
27708008
EAF7_YEASTEAF7genetic
27708008
LSM7_YEASTLSM7genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
AGA1_YEASTAGA1genetic
27708008
YN93_YEASTYNR064Cgenetic
27708008
AIF1_YEASTAIF1genetic
27708008
PHO80_YEASTPHO80genetic
27708008
TLG2_YEASTTLG2genetic
27708008
PEX15_YEASTPEX15genetic
27708008
VPS68_YEASTVPS68genetic
27708008
FRE7_YEASTFRE7genetic
27708008
INP53_YEASTINP53genetic
27708008
COQ7_YEASTCAT5genetic
27708008
SWT1_YEASTSWT1genetic
27708008
ULS1_YEASTULS1genetic
27708008
HRK1_YEASTHRK1genetic
27708008
LIS1_YEASTPAC1genetic
27708008
VPH1_YEASTVPH1genetic
27708008
MBF1_YEASTMBF1genetic
27708008
BUD7_YEASTBUD7genetic
27708008
MNE1_YEASTMNE1genetic
27708008
GDS1_YEASTGDS1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL1B_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 ACETYLATION AT SER-2 BY NATA.
Methylation
ReferencePubMed
"The ribosomal L1 protuberance in yeast is methylated on a lysineresidue catalyzed by a seven beta-strand methyltransferase.";
Webb K.J., Al-Hadid Q., Zurita-Lopez C.I., Young B.D., Lipson R.S.,Clarke S.G.;
J. Biol. Chem. 286:18405-18413(2011).
Cited for: METHYLATION AT LYS-47, AND MASS SPECTROMETRY.
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-7 AND SER-86, 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-7, AND MASSSPECTROMETRY.
"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-79, AND MASSSPECTROMETRY.

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