RL5_YEAST - dbPTM
RL5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL5_YEAST
UniProt AC P26321
Protein Name 60S ribosomal protein L5 {ECO:0000303|PubMed:9559554}
Gene Name RPL5 {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 297
Subcellular Localization Cytoplasm . Nucleus . The SYO1-uL5-uL18 complex is transported into the nucleus by KAP104.
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 MAFQKDAKSSAYSSRFQTPFRRRREGKTDYYQRKRLVTQHKAKYNTPKYRLVVRFTNKDIICQIISSTITGDVVLAAAYSHELPRYGITHGLTNWAAAYATGLLIARRTLQKLGLDETYKGVEEVEGEYELTEAVEDGPRPFKVFLDIGLQRTTTGARVFGALKGASDGGLYVPHSENRFPGWDFETEEIDPELLRSYIFGGHVSQYMEELADDDEERFSELFKGYLADDIDADSLEDIYTSAHEAIRADPAFKPTEKKFTKEQYAAESKKYRQTKLSKEERAARVAAKIAALAGQQ
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
52-Hydroxyisobutyrylation---MAFQKDAKSSAY
---CCCCHHHHHHHH		53.88-
5Succinylation---MAFQKDAKSSAY
---CCCCHHHHHHHH		53.8823954790
8UbiquitinationMAFQKDAKSSAYSSR
CCCCHHHHHHHHHCC		55.8923749301
82-HydroxyisobutyrylationMAFQKDAKSSAYSSR
CCCCHHHHHHHHHCC		55.89-
8SuccinylationMAFQKDAKSSAYSSR
CCCCHHHHHHHHHCC		55.8923954790
8AcetylationMAFQKDAKSSAYSSR
CCCCHHHHHHHHHCC		55.8924489116
9PhosphorylationAFQKDAKSSAYSSRF
CCCHHHHHHHHHCCC		23.1723749301
10PhosphorylationFQKDAKSSAYSSRFQ
CCHHHHHHHHHCCCC		30.4427214570
27SuccinylationFRRRREGKTDYYQRK
CHHCCCCCCCHHHHH		33.2123954790
27AcetylationFRRRREGKTDYYQRK
CHHCCCCCCCHHHHH		33.2124489116
27UbiquitinationFRRRREGKTDYYQRK
CHHCCCCCCCHHHHH		33.2124961812
412-HydroxyisobutyrylationKRLVTQHKAKYNTPK
HHHHHHHHHHCCCCC		36.43-
41AcetylationKRLVTQHKAKYNTPK
HHHHHHHHHHCCCCC		36.4325381059
43UbiquitinationLVTQHKAKYNTPKYR
HHHHHHHHCCCCCEE		43.7823749301
43AcetylationLVTQHKAKYNTPKYR
HHHHHHHHCCCCCEE		43.7824489116
48AcetylationKAKYNTPKYRLVVRF
HHHCCCCCEEEEEEE		40.7524489116
482-HydroxyisobutyrylationKAKYNTPKYRLVVRF
HHHCCCCCEEEEEEE		40.75-
58UbiquitinationLVVRFTNKDIICQII
EEEEECCCCCHHHHH		47.4423749301
112AcetylationIARRTLQKLGLDETY
HHHHHHHHCCCCCCC		47.8624489116
1122-HydroxyisobutyrylationIARRTLQKLGLDETY
HHHHHHHHCCCCCCC		47.86-
112UbiquitinationIARRTLQKLGLDETY
HHHHHHHHCCCCCCC		47.8623749301
120UbiquitinationLGLDETYKGVEEVEG
CCCCCCCCCHHHCCC		64.9917644757
120AcetylationLGLDETYKGVEEVEG
CCCCCCCCCHHHCCC		64.9924489116
143UbiquitinationEDGPRPFKVFLDIGL
CCCCCCEEEEEEECC		34.4617644757
153PhosphorylationLDIGLQRTTTGARVF
EEECCCCCCCCCHHH		18.7517287358
154PhosphorylationDIGLQRTTTGARVFG
EECCCCCCCCCHHHH		25.9717287358
155PhosphorylationIGLQRTTTGARVFGA
ECCCCCCCCCHHHHH		28.3817287358
164AcetylationARVFGALKGASDGGL
CHHHHHHCCCCCCCE		52.4724489116
1642-HydroxyisobutyrylationARVFGALKGASDGGL
CHHHHHHCCCCCCCE		52.47-
164UbiquitinationARVFGALKGASDGGL
CHHHHHHCCCCCCCE		52.4723749301
164SuccinylationARVFGALKGASDGGL
CHHHHHHCCCCCCCE		52.4723954790
167PhosphorylationFGALKGASDGGLYVP
HHHHCCCCCCCEECC		45.5223749301
172PhosphorylationGASDGGLYVPHSENR
CCCCCCEECCCCCCC		18.4028889911
176PhosphorylationGGLYVPHSENRFPGW
CCEECCCCCCCCCCC		30.4223749301
226PhosphorylationFSELFKGYLADDIDA
HHHHHHHHHCCCCCH		10.1722369663
235PhosphorylationADDIDADSLEDIYTS
CCCCCHHHHHHHHHH		35.0722369663
240PhosphorylationADSLEDIYTSAHEAI
HHHHHHHHHHHHHHH		13.6322369663
241PhosphorylationDSLEDIYTSAHEAIR
HHHHHHHHHHHHHHH		21.5522369663
242PhosphorylationSLEDIYTSAHEAIRA
HHHHHHHHHHHHHHC		15.6220377248
254AcetylationIRADPAFKPTEKKFT
HHCCCCCCCCCCCCC		53.8124489116
2542-HydroxyisobutyrylationIRADPAFKPTEKKFT
HHCCCCCCCCCCCCC		53.81-
254SuccinylationIRADPAFKPTEKKFT
HHCCCCCCCCCCCCC		53.8123954790
256PhosphorylationADPAFKPTEKKFTKE
CCCCCCCCCCCCCHH		62.1122369663
2582-HydroxyisobutyrylationPAFKPTEKKFTKEQY
CCCCCCCCCCCHHHH		56.52-
258SuccinylationPAFKPTEKKFTKEQY
CCCCCCCCCCCHHHH		56.5223954790
258AcetylationPAFKPTEKKFTKEQY
CCCCCCCCCCCHHHH		56.5224489116
262AcetylationPTEKKFTKEQYAAES
CCCCCCCHHHHHHHH		46.0524489116
269PhosphorylationKEQYAAESKKYRQTK
HHHHHHHHHHHHHHH		29.7128889911
2702-HydroxyisobutyrylationEQYAAESKKYRQTKL
HHHHHHHHHHHHHHC		45.38-
270AcetylationEQYAAESKKYRQTKL
HHHHHHHHHHHHHHC		45.3825381059
270SuccinylationEQYAAESKKYRQTKL
HHHHHHHHHHHHHHC		45.3823954790
2762-HydroxyisobutyrylationSKKYRQTKLSKEERA
HHHHHHHHCCHHHHH		42.28-
2792-HydroxyisobutyrylationYRQTKLSKEERAARV
HHHHHCCHHHHHHHH		74.22-
289AcetylationRAARVAAKIAALAGQ
HHHHHHHHHHHHHCC		24.1224489116
289UbiquitinationRAARVAAKIAALAGQ
HHHHHHHHHHHHHCC		24.1223749301
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 RL5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL5_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 RL5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF6_YEASTTIF6physical
11805837
CIC1_YEASTCIC1physical
11805837
RRS1_YEASTRRS1physical
16100378
RPF2_YEASTRPF2physical
17938242
RL11A_YEASTRPL11Aphysical
17938242
SYO1_YEASTSYO1physical
23118189
RL11A_YEASTRPL11Aphysical
23118189
RS8A_YEASTRPS8Aphysical
24043628
RS8B_YEASTRPS8Aphysical
24043628
RL5_YEASTRPL5physical
24043628
FLO1_YEASTFLO1genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
RS14A_YEASTRPS14Agenetic
27708008
ATG15_YEASTATG15genetic
27708008
PHB1_YEASTPHB1genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
SSF1_YEASTSSF1genetic
27708008
SYG1_YEASTSYG1genetic
27708008
ICE2_YEASTICE2genetic
27708008
SAC1_YEASTSAC1genetic
27708008
COX8_YEASTCOX8genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
VPS9_YEASTVPS9genetic
27708008
MUB1_YEASTMUB1genetic
27708008
RS10B_YEASTRPS10Bgenetic
27708008
PET8_YEASTPET8genetic
27708008
SIN3_YEASTSIN3genetic
27708008
NOP12_YEASTNOP12genetic
27708008
RS28A_YEASTRPS28Agenetic
27708008
ULS1_YEASTULS1genetic
27708008
GIP4_YEASTGIP4genetic
27708008
KIN3_YEASTKIN3genetic
27708008
ECM15_YEASTECM15genetic
27708008
H4_YEASTHHF1genetic
27708008
H3_YEASTHHT1genetic
27708008
UBP14_YEASTUBP14genetic
27708008
RAD16_YEASTRAD16genetic
27708008
EF1A_YEASTTEF2genetic
27708008
SGF29_YEASTSGF29genetic
27708008
THRC_YEASTTHR4genetic
27708008
YCY0_YEASTYCR090Cgenetic
27708008
THI3_YEASTTHI3genetic
27708008
GYP7_YEASTGYP7genetic
27708008
AIM7_YEASTAIM7genetic
27708008
PP4C_YEASTPPH3genetic
27708008
VPS41_YEASTVPS41genetic
27708008
MKC7_YEASTMKC7genetic
27708008
GIR2_YEASTGIR2genetic
27708008
PLP1_YEASTPLP1genetic
27708008
MSN5_YEASTMSN5genetic
27708008
VPS74_YEASTVPS74genetic
27708008
FIT1_YEASTFIT1genetic
27708008
CAJ1_YEASTCAJ1genetic
27708008
RRT13_YEASTRRT13genetic
27708008
SWP82_YEASTSWP82genetic
27708008
DCV1_YEASTDCV1genetic
27708008
CGR1_YEASTCGR1genetic
27708008
TFS2_YEASTDST1genetic
27708008
HUR1_YEASTHUR1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
RS25A_YEASTRPS25Agenetic
27708008
YG1X_YEASTYGR050Cgenetic
27708008
SAY1_YEASTSAY1genetic
27708008
REXO1_YEASTRNH70genetic
27708008
YHC6_YEASTYHL026Cgenetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
STB5_YEASTSTB5genetic
27708008
YHY2_YEASTYHR182Wgenetic
27708008
ACA2_YEASTCST6genetic
27708008
AIR1_YEASTAIR1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
JJJ2_YEASTJJJ2genetic
27708008
ILM1_YEASTILM1genetic
27708008
TCTP_YEASTTMA19genetic
27708008
MCR1_YEASTMCR1genetic
27708008
XPOT_YEASTLOS1genetic
27708008
TRK2_YEASTTRK2genetic
27708008
SIS2_YEASTSIS2genetic
27708008
RNP1_YEASTRNP1genetic
27708008
ICT1_YEASTICT1genetic
27708008
TOP3_YEASTTOP3genetic
27708008
SEI1_YEASTFLD1genetic
27708008
SST2_YEASTSST2genetic
27708008
GIS4_YEASTGIS4genetic
27708008
STB4_YEASTSTB4genetic
27708008
GBLP_YEASTASC1genetic
27708008
YM71_YEASTYMR226Cgenetic
27708008
COX7_YEASTCOX7genetic
27708008
SCS7_YEASTSCS7genetic
27708008
AEP2_YEASTAEP2genetic
27708008
DOM34_YEASTDOM34genetic
27708008
HDA1_YEASTHDA1genetic
27708008
PMS1_YEASTPMS1genetic
27708008
KC12_YEASTYCK2genetic
27708008
YO029_YEASTYOL029Cgenetic
27708008
ADH1_YEASTADH1genetic
27708008
HMI1_YEASTHMI1genetic
27708008
RRP6_YEASTRRP6genetic
27708008
DIA2_YEASTDIA2genetic
27708008
WHI5_YEASTWHI5genetic
27708008
VAM3_YEASTVAM3genetic
27708008
AZF1_YEASTAZF1genetic
27708008
LCB4_YEASTLCB4genetic
27708008
DGK1_YEASTDGK1genetic
27708008
MRL1_YEASTMRL1genetic
27708008
CGS5_YEASTCLB5genetic
27708008
DBP10_YEASTDBP10physical
25404745
SPB1_YEASTSPB1physical
25404745
NOP2_YEASTNOP2physical
25404745
PESC_YEASTNOP7physical
25404745
NOG1_YEASTNOG1physical
25404745
ARX1_YEASTARX1physical
25404745
NUG1_YEASTNUG1physical
25404745
CIC1_YEASTCIC1physical
25404745
RL3_YEASTRPL3physical
25404745
RPF2_YEASTRPF2physical
25404745
RLP7_YEASTRLP7physical
25404745
RL4A_YEASTRPL4Aphysical
25404745
NSA2_YEASTNSA2physical
25404745
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL5_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-155 AND SER-235, ANDMASS SPECTROMETRY.
"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 THR-153; THR-154; THR-155AND SER-242, AND MASS SPECTROMETRY.
"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-235, AND MASSSPECTROMETRY.

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