RL8_HUMAN - dbPTM
RL8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL8_HUMAN
UniProt AC P62917
Protein Name 60S ribosomal protein L8
Gene Name RPL8
Organism Homo sapiens (Human).
Sequence Length 257
Subcellular Localization Cytoplasm .
Protein Description Component of the large ribosomal subunit..
Protein Sequence MGRVIRGQRKGAGSVFRAHVKHRKGAARLRAVDFAERHGYIKGIVKDIIHDPGRGAPLAKVVFRDPYRFKKRTELFIAAEGIHTGQFVYCGKKAQLNIGNVLPVGTMPEGTIVCCLEEKPGDRGKLARASGNYATVISHNPETKKTRVKLPSGSKKVISSANRAVVGVVAGGGRIDKPILKAGRAYHKYKAKRNCWPRVRGVAMNPVEHPFGGGNHQHIGKPSTIRRDAPAGRKVGLIAARRTGRLRGTKTVQEKEN
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
10SumoylationRVIRGQRKGAGSVFR
CEECCCCCCCCHHHH
45.27-
10UbiquitinationRVIRGQRKGAGSVFR
CEECCCCCCCCHHHH
45.2724816145
10SumoylationRVIRGQRKGAGSVFR
CEECCCCCCCCHHHH
45.27-
14PhosphorylationGQRKGAGSVFRAHVK
CCCCCCCHHHHHHHC
19.9723911959
37MethylationRAVDFAERHGYIKGI
HHHHHHHHHCCCHHH
25.71115492307
40PhosphorylationDFAERHGYIKGIVKD
HHHHHHCCCHHHHHH
8.0428152594
422-HydroxyisobutyrylationAERHGYIKGIVKDII
HHHHCCCHHHHHHHH
33.82-
42SuccinylationAERHGYIKGIVKDII
HHHHCCCHHHHHHHH
33.8223954790
42UbiquitinationAERHGYIKGIVKDII
HHHHCCCHHHHHHHH
33.8223000965
42SumoylationAERHGYIKGIVKDII
HHHHCCCHHHHHHHH
33.8228112733
42AcetylationAERHGYIKGIVKDII
HHHHCCCHHHHHHHH
33.8226051181
46UbiquitinationGYIKGIVKDIIHDPG
CCCHHHHHHHHCCCC
41.0923000965
46SuccinylationGYIKGIVKDIIHDPG
CCCHHHHHHHHCCCC
41.0923954790
462-HydroxyisobutyrylationGYIKGIVKDIIHDPG
CCCHHHHHHHHCCCC
41.09-
46AcetylationGYIKGIVKDIIHDPG
CCCHHHHHHHHCCCC
41.0923749302
54MethylationDIIHDPGRGAPLAKV
HHHCCCCCCCCCHHE
43.41115492315
602-HydroxyisobutyrylationGRGAPLAKVVFRDPY
CCCCCCHHEEECCCC
46.76-
60UbiquitinationGRGAPLAKVVFRDPY
CCCCCCHHEEECCCC
46.7623000965
60NeddylationGRGAPLAKVVFRDPY
CCCCCCHHEEECCCC
46.7632015554
67PhosphorylationKVVFRDPYRFKKRTE
HEEECCCCCCCCCEE
32.7328152594
73PhosphorylationPYRFKKRTELFIAAE
CCCCCCCEEEEEEEE
46.0120068231
84PhosphorylationIAAEGIHTGQFVYCG
EEEECCCCCCEEECC
30.6628152594
89PhosphorylationIHTGQFVYCGKKAQL
CCCCCEEECCCCEEE
9.2128152594
92AcetylationGQFVYCGKKAQLNIG
CCEEECCCCEEEECC
41.1825953088
922-HydroxyisobutyrylationGQFVYCGKKAQLNIG
CCEEECCCCEEEECC
41.18-
92UbiquitinationGQFVYCGKKAQLNIG
CCEEECCCCEEEECC
41.1821963094
932-HydroxyisobutyrylationQFVYCGKKAQLNIGN
CEEECCCCEEEECCC
27.01-
93UbiquitinationQFVYCGKKAQLNIGN
CEEECCCCEEEECCC
27.0122817900
106PhosphorylationGNVLPVGTMPEGTIV
CCEECCEECCCCEEE
29.77-
107SulfoxidationNVLPVGTMPEGTIVC
CEECCEECCCCEEEE
2.0430846556
111PhosphorylationVGTMPEGTIVCCLEE
CEECCCCEEEEECCC
14.47-
114S-palmitoylationMPEGTIVCCLEEKPG
CCCCEEEEECCCCCC
1.6119801377
119AcetylationIVCCLEEKPGDRGKL
EEEECCCCCCCCCHH
44.9525953088
119UbiquitinationIVCCLEEKPGDRGKL
EEEECCCCCCCCCHH
44.9521906983
125UbiquitinationEKPGDRGKLARASGN
CCCCCCCHHHHHCCC
39.6123503661
130PhosphorylationRGKLARASGNYATVI
CCHHHHHCCCEEEEE
23.2428152594
133PhosphorylationLARASGNYATVISHN
HHHHCCCEEEEEECC
13.7425159151
133NitrationLARASGNYATVISHN
HHHHCCCEEEEEECC
13.74-
135PhosphorylationRASGNYATVISHNPE
HHCCCEEEEEECCCC
14.1728442448
138PhosphorylationGNYATVISHNPETKK
CCEEEEEECCCCCCC
16.9328442448
143PhosphorylationVISHNPETKKTRVKL
EEECCCCCCCEEEEC
38.8124117733
144UbiquitinationISHNPETKKTRVKLP
EECCCCCCCEEEECC
50.9521906983
144SumoylationISHNPETKKTRVKLP
EECCCCCCCEEEECC
50.95-
1442-HydroxyisobutyrylationISHNPETKKTRVKLP
EECCCCCCCEEEECC
50.95-
144AcetylationISHNPETKKTRVKLP
EECCCCCCCEEEECC
50.9523236377
145UbiquitinationSHNPETKKTRVKLPS
ECCCCCCCEEEECCC
49.3221963094
149SumoylationETKKTRVKLPSGSKK
CCCCEEEECCCCCCE
51.9228112733
1492-HydroxyisobutyrylationETKKTRVKLPSGSKK
CCCCEEEECCCCCCE
51.92-
149AcetylationETKKTRVKLPSGSKK
CCCCEEEECCCCCCE
51.9226051181
149UbiquitinationETKKTRVKLPSGSKK
CCCCEEEECCCCCCE
51.9227667366
152PhosphorylationKTRVKLPSGSKKVIS
CEEEECCCCCCEEHH
67.1620860994
154O-linked_GlycosylationRVKLPSGSKKVISSA
EEECCCCCCEEHHCC
33.3731492838
154PhosphorylationRVKLPSGSKKVISSA
EEECCCCCCEEHHCC
33.3723312004
155AcetylationVKLPSGSKKVISSAN
EECCCCCCEEHHCCC
55.3625953088
155UbiquitinationVKLPSGSKKVISSAN
EECCCCCCEEHHCCC
55.3624816145
156UbiquitinationKLPSGSKKVISSANR
ECCCCCCEEHHCCCC
46.6427667366
1562-HydroxyisobutyrylationKLPSGSKKVISSANR
ECCCCCCEEHHCCCC
46.64-
159PhosphorylationSGSKKVISSANRAVV
CCCCEEHHCCCCEEE
26.7821406692
160PhosphorylationGSKKVISSANRAVVG
CCCEEHHCCCCEEEE
20.5921406692
177UbiquitinationAGGGRIDKPILKAGR
ECCCCCCHHHHHCHH
31.4223000965
177SumoylationAGGGRIDKPILKAGR
ECCCCCCHHHHHCHH
31.42-
177SumoylationAGGGRIDKPILKAGR
ECCCCCCHHHHHCHH
31.42-
177AcetylationAGGGRIDKPILKAGR
ECCCCCCHHHHHCHH
31.4226822725
181UbiquitinationRIDKPILKAGRAYHK
CCCHHHHHCHHHHHH
49.9023000965
181AcetylationRIDKPILKAGRAYHK
CCCHHHHHCHHHHHH
49.9026051181
188UbiquitinationKAGRAYHKYKAKRNC
HCHHHHHHHHCCCCC
35.4521906983
190UbiquitinationGRAYHKYKAKRNCWP
HHHHHHHHCCCCCCC
52.8422817900
192UbiquitinationAYHKYKAKRNCWPRV
HHHHHHCCCCCCCCC
39.7422817900
192MethylationAYHKYKAKRNCWPRV
HHHHHHCCCCCCCCC
39.74116252491
216HydroxylationHPFGGGNHQHIGKPS
CCCCCCCCCCCCCCC
24.7023103944
2342-HydroxyisobutyrylationRDAPAGRKVGLIAAR
CCCCCCCCEEEEEEH
39.47-
234SumoylationRDAPAGRKVGLIAAR
CCCCCCCCEEEEEEH
39.4728112733
234UbiquitinationRDAPAGRKVGLIAAR
CCCCCCCCEEEEEEH
39.4727667366
234SumoylationRDAPAGRKVGLIAAR
CCCCCCCCEEEEEEH
39.47-
242MethylationVGLIAARRTGRLRGT
EEEEEEHHCCCCCCC
36.4824376817
242DimethylationVGLIAARRTGRLRGT
EEEEEEHHCCCCCCC
36.48-
250UbiquitinationTGRLRGTKTVQEKEN
CCCCCCCCCHHHCCC
49.9124816145
250SumoylationTGRLRGTKTVQEKEN
CCCCCCCCCHHHCCC
49.9128112733
255UbiquitinationGTKTVQEKEN-----
CCCCHHHCCC-----
45.5333845483

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
130SPhosphorylationKinaseAURKBQ96GD4
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
216HHydroxylation

23103944

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 RL8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS13_HUMANRPS13physical
22939629
RL9_HUMANRPL9physical
22939629
RS16_HUMANRPS16physical
22939629
RS23_HUMANRPS23physical
22939629
RS2_HUMANRPS2physical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RS3_HUMANRPS3physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS6_HUMANRPS6physical
22939629
RS8_HUMANRPS8physical
22939629
RSSA_HUMANRPSAphysical
22939629
RS26_HUMANRPS26physical
22939629
RS20_HUMANRPS20physical
22939629
RS9_HUMANRPS9physical
22939629
RS17_HUMANRPS17physical
22939629
RLA0_HUMANRPLP0physical
22939629
RM23_HUMANMRPL23physical
22939629
THIOM_HUMANTXN2physical
22939629
TBA1C_HUMANTUBA1Cphysical
22939629
IL7RA_HUMANIL7Rphysical
23151878
RL28_HUMANRPL28physical
22863883
RS25_HUMANRPS25physical
22863883
RL26L_HUMANRPL26L1physical
26186194
RLA2_HUMANRPLP2physical
26186194
RL4_HUMANRPL4physical
26186194
CC137_HUMANCCDC137physical
26186194
RBM28_HUMANRBM28physical
26186194
POP1_HUMANPOP1physical
26186194
DDX24_HUMANDDX24physical
26186194
SPB1_HUMANFTSJ3physical
26186194
RLA0_HUMANRPLP0physical
26186194
ZN668_HUMANZNF668physical
26186194
DKC1_HUMANDKC1physical
26186194
STAU2_HUMANSTAU2physical
26186194
STAU1_HUMANSTAU1physical
26186194
RL6_HUMANRPL6physical
26186194
DDX27_HUMANDDX27physical
26186194
RL15_HUMANRPL15physical
26186194
GLYR1_HUMANGLYR1physical
26186194
REXO4_HUMANREXO4physical
26186194
RS3A_HUMANRPS3Aphysical
26186194
RL18_HUMANRPL18physical
26186194
NSD2_HUMANWHSC1physical
26186194
CG050_HUMANC7orf50physical
26186194
RRP8_HUMANRRP8physical
26186194
PAPD5_HUMANPAPD5physical
26186194
ZCCHV_HUMANZC3HAV1physical
26186194
NOP2_HUMANNOP2physical
26186194
NOG2_HUMANGNL2physical
26186194
CCD86_HUMANCCDC86physical
26186194
RBM34_HUMANRBM34physical
26186194
RIOX2_HUMANMINAphysical
26186194
LN28B_HUMANLIN28Bphysical
26186194
RS8_HUMANRPS8physical
26186194
PUM3_HUMANKIAA0020physical
26186194
RL13A_HUMANRPL13Aphysical
26186194
RL37A_HUMANRPL37Aphysical
26186194
RSBNL_HUMANRSBN1Lphysical
26186194
RPF2_HUMANRPF2physical
26186194
RS24_HUMANRPS24physical
26186194
ZN770_HUMANZNF770physical
26186194
IF6_HUMANEIF6physical
26344197
PESC_HUMANPES1physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL11_HUMANRPL11physical
26344197
RL12_HUMANRPL12physical
26344197
RL13_HUMANRPL13physical
26344197
RL14_HUMANRPL14physical
26344197
RL15_HUMANRPL15physical
26344197
RL17_HUMANRPL17physical
26344197
RL18_HUMANRPL18physical
26344197
RL22_HUMANRPL22physical
26344197
RL23_HUMANRPL23physical
26344197
RL23A_HUMANRPL23Aphysical
26344197
RL24_HUMANRPL24physical
26344197
RL26_HUMANRPL26physical
26344197
RL26L_HUMANRPL26L1physical
26344197
RL27A_HUMANRPL27Aphysical
26344197
RL3_HUMANRPL3physical
26344197
RL31_HUMANRPL31physical
26344197
RL32_HUMANRPL32physical
26344197
RL34_HUMANRPL34physical
26344197
RL35A_HUMANRPL35Aphysical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL38_HUMANRPL38physical
26344197
RL3L_HUMANRPL3Lphysical
26344197
RL5_HUMANRPL5physical
26344197
RL9_HUMANRPL9physical
26344197
RLA2_HUMANRPLP2physical
26344197
RS11_HUMANRPS11physical
26344197
RS14_HUMANRPS14physical
26344197
RS15_HUMANRPS15physical
26344197
RS15A_HUMANRPS15Aphysical
26344197
RS16_HUMANRPS16physical
26344197
RS18_HUMANRPS18physical
26344197
RS19_HUMANRPS19physical
26344197
RS20_HUMANRPS20physical
26344197
RS23_HUMANRPS23physical
26344197
RS25_HUMANRPS25physical
26344197
RS26_HUMANRPS26physical
26344197
RS29_HUMANRPS29physical
26344197
RS3A_HUMANRPS3Aphysical
26344197
RS6_HUMANRPS6physical
26344197
RS7_HUMANRPS7physical
26344197
RS8_HUMANRPS8physical
26344197
RS9_HUMANRPS9physical
26344197
RSSA_HUMANRPSAphysical
26344197
TBB4B_HUMANTUBB4Bphysical
26344197
PUM3_HUMANKIAA0020physical
28514442
ZCCHV_HUMANZC3HAV1physical
28514442
RBM34_HUMANRBM34physical
28514442
RRP8_HUMANRRP8physical
28514442
GLYR1_HUMANGLYR1physical
28514442
RL26L_HUMANRPL26L1physical
28514442
NOG2_HUMANGNL2physical
28514442
STAU1_HUMANSTAU1physical
28514442
RLA0_HUMANRPLP0physical
28514442
NSD2_HUMANWHSC1physical
28514442
RL18A_HUMANRPL18Aphysical
28514442
RLA2_HUMANRPLP2physical
28514442
REXO4_HUMANREXO4physical
28514442
RS24_HUMANRPS24physical
28514442
ZN512_HUMANZNF512physical
28514442
NOP2_HUMANNOP2physical
28514442
RS8_HUMANRPS8physical
28514442
CC137_HUMANCCDC137physical
28514442
NPM_HUMANNPM1physical
28514442
ZBT24_HUMANZBTB24physical
28514442
RL4_HUMANRPL4physical
28514442
SPB1_HUMANFTSJ3physical
28514442
PAPD5_HUMANPAPD5physical
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 RL8_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-46, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-133, AND MASSSPECTROMETRY.

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