RL18_HUMAN - dbPTM
RL18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL18_HUMAN
UniProt AC Q07020
Protein Name 60S ribosomal protein L18
Gene Name RPL18
Organism Homo sapiens (Human).
Sequence Length 188
Subcellular Localization Cytoplasm, cytosol . Cytoplasm . Rough endoplasmic reticulum . Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity).
Protein Description Component of the large ribosomal subunit..
Protein Sequence MGVDIRHNKDRKVRRKEPKSQDIYLRLLVKLYRFLARRTNSTFNQVVLKRLFMSRTNRPPLSLSRMIRKMKLPGRENKTAVVVGTITDDVRVQEVPKLKVCALRVTSRARSRILRAGGKILTFDQLALDSPKGCGTVLLSGPRKGREVYRHFGKAPGTPHSHTKPYVRSKGRKFERARGRRASRGYKN
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
6Methylation--MGVDIRHNKDRKV
--CCCCCCCCCCCCC
23.90115491775
19AcetylationKVRRKEPKSQDIYLR
CCCCCCCCCHHHHHH
62.9427452117
19UbiquitinationKVRRKEPKSQDIYLR
CCCCCCCCCHHHHHH
62.94-
20UbiquitinationVRRKEPKSQDIYLRL
CCCCCCCCHHHHHHH
43.74-
26MethylationKSQDIYLRLLVKLYR
CCHHHHHHHHHHHHH
14.70115491785
30AcetylationIYLRLLVKLYRFLAR
HHHHHHHHHHHHHHH
39.5125825284
302-HydroxyisobutyrylationIYLRLLVKLYRFLAR
HHHHHHHHHHHHHHH
39.51-
30UbiquitinationIYLRLLVKLYRFLAR
HHHHHHHHHHHHHHH
39.5121906983
39PhosphorylationYRFLARRTNSTFNQV
HHHHHHHCCCCHHHH
28.1528450419
41PhosphorylationFLARRTNSTFNQVVL
HHHHHCCCCHHHHHH
33.4928450419
42PhosphorylationLARRTNSTFNQVVLK
HHHHCCCCHHHHHHH
28.7728450419
49AcetylationTFNQVVLKRLFMSRT
CHHHHHHHHHHHCCC
35.1326051181
49UbiquitinationTFNQVVLKRLFMSRT
CHHHHHHHHHHHCCC
35.1321890473
62PhosphorylationRTNRPPLSLSRMIRK
CCCCCCCCHHHHHHH
30.0328450419
64PhosphorylationNRPPLSLSRMIRKMK
CCCCCCHHHHHHHCC
19.2028450419
65MethylationRPPLSLSRMIRKMKL
CCCCCHHHHHHHCCC
29.82115491805
78UbiquitinationKLPGRENKTAVVVGT
CCCCCCCCEEEEEEE
32.8621906983
79PhosphorylationLPGRENKTAVVVGTI
CCCCCCCEEEEEEEE
35.9423911959
85PhosphorylationKTAVVVGTITDDVRV
CEEEEEEEECCCCCH
14.75-
87PhosphorylationAVVVGTITDDVRVQE
EEEEEEECCCCCHHC
26.4522210691
91MethylationGTITDDVRVQEVPKL
EEECCCCCHHCCCCC
31.25115491795
97UbiquitinationVRVQEVPKLKVCALR
CCHHCCCCCEEEEEH
67.1421906983
97AcetylationVRVQEVPKLKVCALR
CCHHCCCCCEEEEEH
67.1425953088
972-HydroxyisobutyrylationVRVQEVPKLKVCALR
CCHHCCCCCEEEEEH
67.14-
99UbiquitinationVQEVPKLKVCALRVT
HHCCCCCEEEEEHHH
41.2021906983
99AcetylationVQEVPKLKVCALRVT
HHCCCCCEEEEEHHH
41.2027452117
106PhosphorylationKVCALRVTSRARSRI
EEEEEHHHHHHHHHH
13.1820363803
111PhosphorylationRVTSRARSRILRAGG
HHHHHHHHHHHHCCC
23.7620363803
1192-HydroxyisobutyrylationRILRAGGKILTFDQL
HHHHCCCEEEEEEEE
33.36-
119SumoylationRILRAGGKILTFDQL
HHHHCCCEEEEEEEE
33.3628112733
119UbiquitinationRILRAGGKILTFDQL
HHHHCCCEEEEEEEE
33.3621906983
119AcetylationRILRAGGKILTFDQL
HHHHCCCEEEEEEEE
33.3623236377
122PhosphorylationRAGGKILTFDQLALD
HCCCEEEEEEEECCC
28.7423403867
125AcetylationGKILTFDQLALDSPK
CEEEEEEEECCCCCC
25.1719608861
130PhosphorylationFDQLALDSPKGCGTV
EEEECCCCCCCCCEE
29.3919664994
132UbiquitinationQLALDSPKGCGTVLL
EECCCCCCCCCEEEE
71.44-
132AcetylationQLALDSPKGCGTVLL
EECCCCCCCCCEEEE
71.4426051181
134S-palmitoylationALDSPKGCGTVLLSG
CCCCCCCCCEEEECC
5.2929575903
134GlutathionylationALDSPKGCGTVLLSG
CCCCCCCCCEEEECC
5.2922555962
136PhosphorylationDSPKGCGTVLLSGPR
CCCCCCCEEEECCCC
16.4424732914
140PhosphorylationGCGTVLLSGPRKGRE
CCCEEEECCCCCCHH
42.4625159151
150MethylationRKGREVYRHFGKAPG
CCCHHHHHHCCCCCC
24.67115491765
154AcetylationEVYRHFGKAPGTPHS
HHHHHCCCCCCCCCC
50.9219608861
154UbiquitinationEVYRHFGKAPGTPHS
HHHHHCCCCCCCCCC
50.9219608861
158PhosphorylationHFGKAPGTPHSHTKP
HCCCCCCCCCCCCCH
19.4423927012
161PhosphorylationKAPGTPHSHTKPYVR
CCCCCCCCCCCHHCC
33.7723927012
163PhosphorylationPGTPHSHTKPYVRSK
CCCCCCCCCHHCCCC
36.4129496963
164SumoylationGTPHSHTKPYVRSKG
CCCCCCCCHHCCCCC
29.0028112733
164AcetylationGTPHSHTKPYVRSKG
CCCCCCCCHHCCCCC
29.0025825284
164UbiquitinationGTPHSHTKPYVRSKG
CCCCCCCCHHCCCCC
29.00-
166PhosphorylationPHSHTKPYVRSKGRK
CCCCCCHHCCCCCHH
15.2828152594
183PhosphorylationRARGRRASRGYKN--
HHHHHHHCCCCCC--
25.1523882029

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 RL18_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL18_HUMAN !!

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 RL18_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL19_HUMANRPL19physical
22939629
RL21_HUMANRPL21physical
22939629
RL22_HUMANRPL22physical
22939629
RL23_HUMANRPL23physical
22939629
RL24_HUMANRPL24physical
22939629
RL27A_HUMANRPL27Aphysical
22939629
RL31_HUMANRPL31physical
22939629
RL37A_HUMANRPL37Aphysical
22939629
RL3_HUMANRPL3physical
22939629
RL4_HUMANRPL4physical
22939629
RL5_HUMANRPL5physical
22939629
RL6_HUMANRPL6physical
22939629
RL7A_HUMANRPL7Aphysical
22939629
RL7_HUMANRPL7physical
22939629
RL8_HUMANRPL8physical
22939629
RL9_HUMANRPL9physical
22939629
RS13_HUMANRPS13physical
22939629
RS14_HUMANRPS14physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RS16_HUMANRPS16physical
22939629
RS19_HUMANRPS19physical
22939629
RS23_HUMANRPS23physical
22939629
RS25_HUMANRPS25physical
22939629
RS26_HUMANRPS26physical
22939629
RS28_HUMANRPS28physical
22939629
RS2_HUMANRPS2physical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RS3_HUMANRPS3physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS5_HUMANRPS5physical
22939629
RS6_HUMANRPS6physical
22939629
RS7_HUMANRPS7physical
22939629
RS8_HUMANRPS8physical
22939629
RSSA_HUMANRPSAphysical
22939629
RL23A_HUMANRPL23Aphysical
22939629
RL30_HUMANRPL30physical
22939629
RS24_HUMANRPS24physical
22939629
RS12_HUMANRPS12physical
22939629
RS20_HUMANRPS20physical
22939629
RS11_HUMANRPS11physical
22939629
RLA0_HUMANRPLP0physical
22939629
RL36_HUMANRPL36physical
22939629
RL27_HUMANRPL27physical
22939629
RS9_HUMANRPS9physical
22939629
RL35_HUMANRPL35physical
22939629
RS17_HUMANRPS17physical
22939629
RL38_HUMANRPL38physical
22939629
RL32_HUMANRPL32physical
22939629
RS21_HUMANRPS21physical
22939629
RS27A_HUMANRPS27Aphysical
22939629
U2AF2_HUMANU2AF2physical
22939629
RS27L_HUMANRPS27Lphysical
22939629
TEBP_HUMANPTGES3physical
22939629
TBA1B_HUMANTUBA1Bphysical
22939629
RM12_HUMANMRPL12physical
22939629
IL7RA_HUMANIL7Rphysical
23151878
MCA3_HUMANEEF1E1physical
22863883
UBIM_HUMANFAUphysical
22863883
SYIC_HUMANIARSphysical
22863883
CPSF5_HUMANNUDT21physical
22863883
RL13_HUMANRPL13physical
22863883
RL23A_HUMANRPL23Aphysical
22863883
RL24_HUMANRPL24physical
22863883
RLA0_HUMANRPLP0physical
22863883
HNRPU_HUMANHNRNPUphysical
26344197
HNRL2_HUMANHNRNPUL2physical
26344197
PABP1_HUMANPABPC1physical
26344197
PABP4_HUMANPABPC4physical
26344197
RL10_HUMANRPL10physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL12_HUMANRPL12physical
26344197
RL13_HUMANRPL13physical
26344197
RL13A_HUMANRPL13Aphysical
26344197
RL14_HUMANRPL14physical
26344197
RL15_HUMANRPL15physical
26344197
RL17_HUMANRPL17physical
26344197
RL18A_HUMANRPL18Aphysical
26344197
RL19_HUMANRPL19physical
26344197
RL23_HUMANRPL23physical
26344197
RL26_HUMANRPL26physical
26344197
RL27_HUMANRPL27physical
26344197
RL27A_HUMANRPL27Aphysical
26344197
RL30_HUMANRPL30physical
26344197
RL31_HUMANRPL31physical
26344197
RL32_HUMANRPL32physical
26344197
RL34_HUMANRPL34physical
26344197
RL35_HUMANRPL35physical
26344197
RL35A_HUMANRPL35Aphysical
26344197
RL36_HUMANRPL36physical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL38_HUMANRPL38physical
26344197
RL5_HUMANRPL5physical
26344197
RL6_HUMANRPL6physical
26344197
RL7_HUMANRPL7physical
26344197
RL7A_HUMANRPL7Aphysical
26344197
RL9_HUMANRPL9physical
26344197
RLA2_HUMANRPLP2physical
26344197
RS10_HUMANRPS10physical
26344197
RS12_HUMANRPS12physical
26344197
RS13_HUMANRPS13physical
26344197
RS14_HUMANRPS14physical
26344197
RS15_HUMANRPS15physical
26344197
RS18_HUMANRPS18physical
26344197
RS23_HUMANRPS23physical
26344197
RS25_HUMANRPS25physical
26344197
RS26_HUMANRPS26physical
26344197
RS5_HUMANRPS5physical
26344197
RS6_HUMANRPS6physical
26344197
RS7_HUMANRPS7physical
26344197
RS8_HUMANRPS8physical
26344197
RS9_HUMANRPS9physical
26344197
RSSA_HUMANRPSAphysical
26344197
CEBPZ_HUMANCEBPZphysical
28514442
RRP5_HUMANPDCD11physical
28514442
FNTB_HUMANFNTBphysical
28514442
DCAF1_HUMANVPRBPphysical
28514442
UBE2O_HUMANUBE2Ophysical
28514442
NOC2L_HUMANNOC2Lphysical
28514442
RRP8_HUMANRRP8physical
28514442
NLE1_HUMANNLE1physical
28514442
NSUN4_HUMANNSUN4physical
28514442
PUM3_HUMANKIAA0020physical
28514442
RIOX2_HUMANMINAphysical
28514442
NOG2_HUMANGNL2physical
28514442
CENPC_HUMANCENPCphysical
28514442
REXO4_HUMANREXO4physical
28514442
TTC19_HUMANTTC19physical
28514442
RBM34_HUMANRBM34physical
28514442
NOL8_HUMANNOL8physical
28514442
NP1L1_HUMANNAP1L1physical
28514442
NOG1_HUMANGTPBP4physical
28514442
RBM28_HUMANRBM28physical
28514442
ZC3HA_HUMANZC3H10physical
28514442
SPT2_HUMANSPTY2D1physical
28514442
DKC1_HUMANDKC1physical
28514442
DDX10_HUMANDDX10physical
28514442
C1QBP_HUMANC1QBPphysical
28514442
SPB1_HUMANFTSJ3physical
28514442
RM48_HUMANMRPL48physical
28514442
DDX27_HUMANDDX27physical
28514442
FNTA_HUMANFNTAphysical
28514442
BRX1_HUMANBRIX1physical
28514442
NP1L4_HUMANNAP1L4physical
28514442
ZN512_HUMANZNF512physical
28514442
RL26L_HUMANRPL26L1physical
28514442
RT31_HUMANMRPS31physical
28514442
DDX51_HUMANDDX51physical
28514442
ZNF22_HUMANZNF22physical
28514442
ZCCHV_HUMANZC3HAV1physical
28514442
DDX24_HUMANDDX24physical
28514442
DDX52_HUMANDDX52physical
28514442
RM16_HUMANMRPL16physical
28514442
RRP7A_HUMANRRP7Aphysical
28514442
NOP56_HUMANNOP56physical
28514442
RT33_HUMANMRPS33physical
28514442
RM28_HUMANMRPL28physical
28514442
ZN644_HUMANZNF644physical
28514442
RL10A_HUMANRPL10Aphysical
28514442
HERC5_HUMANHERC5physical
28514442
MBB1A_HUMANMYBBP1Aphysical
28514442
RT09_HUMANMRPS9physical
28514442
FCF1_HUMANFCF1physical
28514442
RM13_HUMANMRPL13physical
28514442
RT18C_HUMANMRPS18Cphysical
28514442
RM32_HUMANMRPL32physical
28514442
RT35_HUMANMRPS35physical
28514442
RBM19_HUMANRBM19physical
28514442
DDX54_HUMANDDX54physical
28514442
NOC3L_HUMANNOC3Lphysical
28514442
RL3_HUMANRPL3physical
28514442
RM47_HUMANMRPL47physical
28514442
NPA1P_HUMANURB1physical
28514442
DDX56_HUMANDDX56physical
28514442
RL18A_HUMANRPL18Aphysical
28514442
DHX30_HUMANDHX30physical
28514442
RRP1_HUMANRRP1physical
28514442
ZN771_HUMANZNF771physical
28514442
BUD13_HUMANBUD13physical
28514442
RPF2_HUMANRPF2physical
28514442
PK1IP_HUMANPAK1IP1physical
28514442
RM27_HUMANMRPL27physical
28514442
RM24_HUMANMRPL24physical
28514442
RL8_HUMANRPL8physical
28514442
NSA2_HUMANNSA2physical
28514442
DDX18_HUMANDDX18physical
28514442
NEPRO_HUMANC3orf17physical
28514442
RM20_HUMANMRPL20physical
28514442
NOP2_HUMANNOP2physical
28514442
RM17_HUMANMRPL17physical
28514442
RT05_HUMANMRPS5physical
28514442
RM03_HUMANMRPL3physical
28514442
SAS10_HUMANUTP3physical
28514442
GNL3_HUMANGNL3physical
28514442
RL30_HUMANRPL30physical
28514442
RT10_HUMANMRPS10physical
28514442
RM51_HUMANMRPL51physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL18_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-154, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND THR-158, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY.

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