RL18A_HUMAN - dbPTM
RL18A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL18A_HUMAN
UniProt AC Q02543
Protein Name 60S ribosomal protein L18a
Gene Name RPL18A
Organism Homo sapiens (Human).
Sequence Length 176
Subcellular Localization
Protein Description
Protein Sequence MKASGTLREYKVVGRCLPTPKCHTPPLYRMRIFAPNHVVAKSRFWYFVSQLKKMKKSSGEIVYCGQVFEKSPLRVKNFGIWLRYDSRSGTHNMYREYRDLTTAGAVTQCYRDMGARHRARAHSIQIMKVEEIAASKCRRPAVKQFHDSKIKFPLPHRVLRRQHKPRFTTKRPNTFF
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
2Sumoylation------MKASGTLRE
------CCCCCCCEE
51.78-
2Ubiquitination------MKASGTLRE
------CCCCCCCEE
51.7824816145
2Sumoylation------MKASGTLRE
------CCCCCCCEE
51.78-
2Methylation------MKASGTLRE
------CCCCCCCEE
51.7872592333
4Phosphorylation----MKASGTLREYK
----CCCCCCCEEEE
27.1320068231
6Phosphorylation--MKASGTLREYKVV
--CCCCCCCEEEEEE
21.8320068231
8MethylationMKASGTLREYKVVGR
CCCCCCCEEEEEEEE
45.07115491815
10PhosphorylationASGTLREYKVVGRCL
CCCCCEEEEEEEEEC
11.5829496907
11UbiquitinationSGTLREYKVVGRCLP
CCCCEEEEEEEEECC
26.2023000965
11AcetylationSGTLREYKVVGRCLP
CCCCEEEEEEEEECC
26.2025953088
11SumoylationSGTLREYKVVGRCLP
CCCCEEEEEEEEECC
26.2025218447
11SumoylationSGTLREYKVVGRCLP
CCCCEEEEEEEEECC
26.20-
21UbiquitinationGRCLPTPKCHTPPLY
EEECCCCCCCCCCEE
40.9223000965
21AcetylationGRCLPTPKCHTPPLY
EEECCCCCCCCCCEE
40.9225953088
24PhosphorylationLPTPKCHTPPLYRMR
CCCCCCCCCCEEEEE
35.7517192257
28PhosphorylationKCHTPPLYRMRIFAP
CCCCCCEEEEEEECC
14.2428985074
30SulfoxidationHTPPLYRMRIFAPNH
CCCCEEEEEEECCCC
2.1428183972
31MethylationTPPLYRMRIFAPNHV
CCCEEEEEEECCCCE
16.33115491823
412-HydroxyisobutyrylationAPNHVVAKSRFWYFV
CCCCEEEHHHHHHHH
30.47-
41AcetylationAPNHVVAKSRFWYFV
CCCCEEEHHHHHHHH
30.4725953088
41UbiquitinationAPNHVVAKSRFWYFV
CCCCEEEHHHHHHHH
30.4721906983
42PhosphorylationPNHVVAKSRFWYFVS
CCCEEEHHHHHHHHH
23.9928152594
46PhosphorylationVAKSRFWYFVSQLKK
EEHHHHHHHHHHHHH
7.4420090780
49PhosphorylationSRFWYFVSQLKKMKK
HHHHHHHHHHHHHHC
21.6421712546
52UbiquitinationWYFVSQLKKMKKSSG
HHHHHHHHHHHCCCC
43.0921963094
52AcetylationWYFVSQLKKMKKSSG
HHHHHHHHHHHCCCC
43.0925953088
53UbiquitinationYFVSQLKKMKKSSGE
HHHHHHHHHHCCCCC
65.6222817900
54SulfoxidationFVSQLKKMKKSSGEI
HHHHHHHHHCCCCCE
6.7228183972
55UbiquitinationVSQLKKMKKSSGEIV
HHHHHHHHCCCCCEE
59.3822817900
56AcetylationSQLKKMKKSSGEIVY
HHHHHHHCCCCCEEE
46.4826051181
56UbiquitinationSQLKKMKKSSGEIVY
HHHHHHHCCCCCEEE
46.4821963094
562-HydroxyisobutyrylationSQLKKMKKSSGEIVY
HHHHHHHCCCCCEEE
46.48-
57PhosphorylationQLKKMKKSSGEIVYC
HHHHHHCCCCCEEEE
37.7523927012
58PhosphorylationLKKMKKSSGEIVYCG
HHHHHCCCCCEEEEC
49.6923927012
63PhosphorylationKSSGEIVYCGQVFEK
CCCCCEEEECEEEEC
9.1223927012
64GlutathionylationSSGEIVYCGQVFEKS
CCCCEEEECEEEECC
1.8122555962
64S-nitrosylationSSGEIVYCGQVFEKS
CCCCEEEECEEEECC
1.8118335467
64S-nitrosocysteineSSGEIVYCGQVFEKS
CCCCEEEECEEEECC
1.81-
702-HydroxyisobutyrylationYCGQVFEKSPLRVKN
EECEEEECCCEEEEE
46.00-
70UbiquitinationYCGQVFEKSPLRVKN
EECEEEECCCEEEEE
46.0023000965
70AcetylationYCGQVFEKSPLRVKN
EECEEEECCCEEEEE
46.0026051181
71PhosphorylationCGQVFEKSPLRVKNF
ECEEEECCCEEEEEE
23.2023927012
76SumoylationEKSPLRVKNFGIWLR
ECCCEEEEEEEEEEE
39.87-
76AcetylationEKSPLRVKNFGIWLR
ECCCEEEEEEEEEEE
39.8725825284
76SuccinylationEKSPLRVKNFGIWLR
ECCCEEEEEEEEEEE
39.87-
76SuccinylationEKSPLRVKNFGIWLR
ECCCEEEEEEEEEEE
39.8721890473
76UbiquitinationEKSPLRVKNFGIWLR
ECCCEEEEEEEEEEE
39.8723000965
84PhosphorylationNFGIWLRYDSRSGTH
EEEEEEEEECCCCCC
18.9929214152
86PhosphorylationGIWLRYDSRSGTHNM
EEEEEEECCCCCCHH
21.2930624053
88PhosphorylationWLRYDSRSGTHNMYR
EEEEECCCCCCHHHH
52.5820068231
90PhosphorylationRYDSRSGTHNMYREY
EEECCCCCCHHHHHH
16.0120068231
93SulfoxidationSRSGTHNMYREYRDL
CCCCCCHHHHHHHHC
2.3130846556
94PhosphorylationRSGTHNMYREYRDLT
CCCCCHHHHHHHHCC
12.9527080861
101PhosphorylationYREYRDLTTAGAVTQ
HHHHHHCCHHHHHHH
20.9121712546
101O-linked_GlycosylationYREYRDLTTAGAVTQ
HHHHHHCCHHHHHHH
20.9128510447
102PhosphorylationREYRDLTTAGAVTQC
HHHHHCCHHHHHHHH
30.3228152594
107PhosphorylationLTTAGAVTQCYRDMG
CCHHHHHHHHHHHHC
16.6428152594
109GlutathionylationTAGAVTQCYRDMGAR
HHHHHHHHHHHHCHH
1.8822555962
109S-palmitoylationTAGAVTQCYRDMGAR
HHHHHHHHHHHHCHH
1.8829575903
110PhosphorylationAGAVTQCYRDMGARH
HHHHHHHHHHHCHHH
10.3828152594
110NitrationAGAVTQCYRDMGARH
HHHHHHHHHHHCHHH
10.38-
123PhosphorylationRHRARAHSIQIMKVE
HHHHHHCEEEEEEHH
18.4029255136
127SulfoxidationRAHSIQIMKVEEIAA
HHCEEEEEEHHHHHH
1.9730846556
128AcetylationAHSIQIMKVEEIAAS
HCEEEEEEHHHHHHH
48.3926051181
128MethylationAHSIQIMKVEEIAAS
HCEEEEEEHHHHHHH
48.3982988953
128SumoylationAHSIQIMKVEEIAAS
HCEEEEEEHHHHHHH
48.3928112733
128SumoylationAHSIQIMKVEEIAAS
HCEEEEEEHHHHHHH
48.39-
128UbiquitinationAHSIQIMKVEEIAAS
HCEEEEEEHHHHHHH
48.3921963094
135PhosphorylationKVEEIAASKCRRPAV
EHHHHHHHCCCCHHH
24.2229255136
1362-HydroxyisobutyrylationVEEIAASKCRRPAVK
HHHHHHHCCCCHHHH
27.34-
136AcetylationVEEIAASKCRRPAVK
HHHHHHHCCCCHHHH
27.3425953088
136UbiquitinationVEEIAASKCRRPAVK
HHHHHHHCCCCHHHH
27.3423000965
1432-HydroxyisobutyrylationKCRRPAVKQFHDSKI
CCCCHHHHHHCCCCC
49.72-
143AcetylationKCRRPAVKQFHDSKI
CCCCHHHHHHCCCCC
49.7226051181
143UbiquitinationKCRRPAVKQFHDSKI
CCCCHHHHHHCCCCC
49.7223000965
149SumoylationVKQFHDSKIKFPLPH
HHHHCCCCCCCCCCH
56.84-
149AcetylationVKQFHDSKIKFPLPH
HHHHCCCCCCCCCCH
56.8419809653
149UbiquitinationVKQFHDSKIKFPLPH
HHHHCCCCCCCCCCH
56.8423000965
149SumoylationVKQFHDSKIKFPLPH
HHHHCCCCCCCCCCH
56.84-
1512-HydroxyisobutyrylationQFHDSKIKFPLPHRV
HHCCCCCCCCCCHHH
44.67-
151AcetylationQFHDSKIKFPLPHRV
HHCCCCCCCCCCHHH
44.6725953088
151UbiquitinationQFHDSKIKFPLPHRV
HHCCCCCCCCCCHHH
44.6723000965
151SumoylationQFHDSKIKFPLPHRV
HHCCCCCCCCCCHHH
44.67-
151SumoylationQFHDSKIKFPLPHRV
HHCCCCCCCCCCHHH
44.67-
164UbiquitinationRVLRRQHKPRFTTKR
HHHHHCCCCCCCCCC
29.5623000965
168PhosphorylationRQHKPRFTTKRPNTF
HCCCCCCCCCCCCCC
32.4622817900
169PhosphorylationQHKPRFTTKRPNTFF
CCCCCCCCCCCCCCC
23.5022817900
170AcetylationHKPRFTTKRPNTFF-
CCCCCCCCCCCCCC-
63.9025953088
170SumoylationHKPRFTTKRPNTFF-
CCCCCCCCCCCCCC-
63.9028112733
170UbiquitinationHKPRFTTKRPNTFF-
CCCCCCCCCCCCCC-
63.9023000965
1702-HydroxyisobutyrylationHKPRFTTKRPNTFF-
CCCCCCCCCCCCCC-
63.90-
170SumoylationHKPRFTTKRPNTFF-
CCCCCCCCCCCCCC-
63.90-

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 RL18A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL18A_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 RL18A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LIPL_HUMANLPLphysical
16169070
MK_HUMANMDKphysical
16169070
RL36_HUMANRPL36physical
16169070
RL18_HUMANRPL18physical
22939629
RL19_HUMANRPL19physical
22939629
RL21_HUMANRPL21physical
22939629
RL23A_HUMANRPL23Aphysical
22939629
RL23_HUMANRPL23physical
22939629
RL24_HUMANRPL24physical
22939629
RL30_HUMANRPL30physical
22939629
RL31_HUMANRPL31physical
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
RS11_HUMANRPS11physical
22939629
RS12_HUMANRPS12physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RS16_HUMANRPS16physical
22939629
RS19_HUMANRPS19physical
22939629
RS20_HUMANRPS20physical
22939629
RS23_HUMANRPS23physical
22939629
RS26_HUMANRPS26physical
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
RS24_HUMANRPS24physical
22939629
RS13_HUMANRPS13physical
22939629
RL37A_HUMANRPL37Aphysical
22939629
RS14_HUMANRPS14physical
22939629
RL22_HUMANRPL22physical
22939629
RLA0_HUMANRPLP0physical
22939629
RS27A_HUMANRPS27Aphysical
22939629
RS21_HUMANRPS21physical
22939629
RL32_HUMANRPL32physical
22939629
U2AF2_HUMANU2AF2physical
22939629
SPB1_HUMANFTSJ3physical
22939629
RRS1_HUMANRRS1physical
22939629
TPR_HUMANTPRphysical
22939629
TCP4_HUMANSUB1physical
22939629
CAZA2_HUMANCAPZA2physical
22863883
BRX1_HUMANBRIX1physical
26344197
DDX27_HUMANDDX27physical
26344197
DDX56_HUMANDDX56physical
26344197
EF1A1_HUMANEEF1A1physical
26344197
IF6_HUMANEIF6physical
26344197
MK67I_HUMANNIFKphysical
26344197
NOC2L_HUMANNOC2Lphysical
26344197
NOP2_HUMANNOP2physical
26344197
PESC_HUMANPES1physical
26344197
RL10_HUMANRPL10physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL10L_HUMANRPL10Lphysical
26344197
RL11_HUMANRPL11physical
26344197
RL12_HUMANRPL12physical
26344197
RL13_HUMANRPL13physical
26344197
RL13A_HUMANRPL13Aphysical
26344197
RL15_HUMANRPL15physical
26344197
RL19_HUMANRPL19physical
26344197
RL22_HUMANRPL22physical
26344197
RL23_HUMANRPL23physical
26344197
RL23A_HUMANRPL23Aphysical
26344197
RL27_HUMANRPL27physical
26344197
RL27A_HUMANRPL27Aphysical
26344197
RL30_HUMANRPL30physical
26344197
RL31_HUMANRPL31physical
26344197
RL32_HUMANRPL32physical
26344197
RL35_HUMANRPL35physical
26344197
RL35A_HUMANRPL35Aphysical
26344197
RL36_HUMANRPL36physical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL38_HUMANRPL38physical
26344197
RL3L_HUMANRPL3Lphysical
26344197
RL5_HUMANRPL5physical
26344197
RL7_HUMANRPL7physical
26344197
RL7A_HUMANRPL7Aphysical
26344197
RL8_HUMANRPL8physical
26344197
RL9_HUMANRPL9physical
26344197
RLA0_HUMANRPLP0physical
26344197
RLA1_HUMANRPLP1physical
26344197
RS10_HUMANRPS10physical
26344197
RS11_HUMANRPS11physical
26344197
RS12_HUMANRPS12physical
26344197
RS13_HUMANRPS13physical
26344197
RS14_HUMANRPS14physical
26344197
RS15A_HUMANRPS15Aphysical
26344197
RS18_HUMANRPS18physical
26344197
RS19_HUMANRPS19physical
26344197
RS23_HUMANRPS23physical
26344197
RS25_HUMANRPS25physical
26344197
RS26_HUMANRPS26physical
26344197
RS3A_HUMANRPS3Aphysical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS5_HUMANRPS5physical
26344197
RS6_HUMANRPS6physical
26344197
RS7_HUMANRPS7physical
26344197
RS8_HUMANRPS8physical
26344197
RS9_HUMANRPS9physical
26344197
RSSA_HUMANRPSAphysical
26344197
SF3B3_HUMANSF3B3physical
26344197
RL40_HUMANUBA52physical
26344197
PUM3_HUMANKIAA0020physical
28514442
TAF1D_HUMANTAF1Dphysical
28514442
TSYL2_HUMANTSPYL2physical
28514442
RRP5_HUMANPDCD11physical
28514442
RRP8_HUMANRRP8physical
28514442
CENPU_HUMANCENPUphysical
28514442
NOC2L_HUMANNOC2Lphysical
28514442
NPA1P_HUMANURB1physical
28514442
DDX24_HUMANDDX24physical
28514442
CEBPZ_HUMANCEBPZphysical
28514442
RRP7A_HUMANRRP7Aphysical
28514442
WDR36_HUMANWDR36physical
28514442
BRX1_HUMANBRIX1physical
28514442
TAF1C_HUMANTAF1Cphysical
28514442
DDX31_HUMANDDX31physical
28514442
NOC3L_HUMANNOC3Lphysical
28514442
ZN689_HUMANZNF689physical
28514442
ZCCHV_HUMANZC3HAV1physical
28514442
DDX54_HUMANDDX54physical
28514442
REXO4_HUMANREXO4physical
28514442
TRM1L_HUMANTRMT1Lphysical
28514442
DHX30_HUMANDHX30physical
28514442
RBM28_HUMANRBM28physical
28514442
RL30_HUMANRPL30physical
28514442
NOG2_HUMANGNL2physical
28514442
SRBD1_HUMANSRBD1physical
28514442
DDX51_HUMANDDX51physical
28514442
TTF1_HUMANTTF1physical
28514442
RL32_HUMANRPL32physical
28514442
NOP53_HUMANGLTSCR2physical
28514442
RL3_HUMANRPL3physical
28514442
NOL6_HUMANNOL6physical
28514442
BMS1_HUMANBMS1physical
28514442
NGDN_HUMANNGDNphysical
28514442
DDX56_HUMANDDX56physical
28514442
TSYL1_HUMANTSPYL1physical
28514442
SRP68_HUMANSRP68physical
28514442
RPP29_HUMANPOP4physical
28514442
BBX_HUMANBBXphysical
28514442
DDX10_HUMANDDX10physical
28514442
RPF1_HUMANRPF1physical
28514442
CH033_HUMANC8orf33physical
28514442
TUT7_HUMANZCCHC6physical
28514442
NEPRO_HUMANC3orf17physical
28514442
IMP4_HUMANIMP4physical
28514442
EXOSX_HUMANEXOSC10physical
28514442
NAT10_HUMANNAT10physical
28514442
SDA1_HUMANSDAD1physical
28514442
RBM34_HUMANRBM34physical
28514442
NOP2_HUMANNOP2physical
28514442
RSBN1_HUMANRSBN1physical
28514442
GLYR1_HUMANGLYR1physical
28514442
MBB1A_HUMANMYBBP1Aphysical
28514442
YTDC2_HUMANYTHDC2physical
28514442
STAU1_HUMANSTAU1physical
28514442
URB2_HUMANURB2physical
28514442
SPB1_HUMANFTSJ3physical
28514442
RFC1_HUMANRFC1physical
28514442
PATZ1_HUMANPATZ1physical
28514442
NOG1_HUMANGTPBP4physical
28514442
RL4_HUMANRPL4physical
28514442
RL7A_HUMANRPL7Aphysical
28514442
SRRM1_HUMANSRRM1physical
28514442
DDX27_HUMANDDX27physical
28514442
RBM4_HUMANRBM4physical
28514442
DKC1_HUMANDKC1physical
28514442
RL23A_HUMANRPL23Aphysical
28514442
PRKRA_HUMANPRKRAphysical
28514442
RIOX2_HUMANMINAphysical
28514442
RRP1B_HUMANRRP1Bphysical
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 RL18A_HUMAN

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Related Literatures of Post-Translational Modification
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-71, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, 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-71 AND SER-123, AND MASSSPECTROMETRY.
"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 THR-24; SER-71 AND SER-123,AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63, AND MASSSPECTROMETRY.

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