RL6_HUMAN - dbPTM
RL6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL6_HUMAN
UniProt AC Q02878
Protein Name 60S ribosomal protein L6
Gene Name RPL6
Organism Homo sapiens (Human).
Sequence Length 288
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.; (Microbial infection) Specifically binds to domain C of the Tax-responsive enhancer element in the long terminal repeat of HTLV-I. [PubMed: 8457378]
Protein Sequence MAGEKVEKPDTKEKKPEAKKVDAGGKVKKGNLKAKKPKKGKPHCSRNPVLVRGIGRYSRSAMYSRKAMYKRKYSAAKSKVEKKKKEKVLATVTKPVGGDKNGGTRVVKLRKMPRYYPTEDVPRKLLSHGKKPFSQHVRKLRASITPGTILIILTGRHRGKRVVFLKQLASGLLLVTGPLVLNRVPLRRTHQKFVIATSTKIDISNVKIPKHLTDAYFKKKKLRKPRHQEGEIFDTEKEKYEITEQRKIDQKAVDSQILPKIKAIPQLQGYLRSVFALTNGIYPHKLVF
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------MAGEKVEKP
------CCCCCCCCC
34.55-
5Ubiquitination---MAGEKVEKPDTK
---CCCCCCCCCCCC
55.5719608861
5Sumoylation---MAGEKVEKPDTK
---CCCCCCCCCCCC
55.5728112733
5Acetylation---MAGEKVEKPDTK
---CCCCCCCCCCCC
55.5719608861
8UbiquitinationMAGEKVEKPDTKEKK
CCCCCCCCCCCCCCC
51.70-
11PhosphorylationEKVEKPDTKEKKPEA
CCCCCCCCCCCCCCC
50.0220068231
26AcetylationKKVDAGGKVKKGNLK
CCCCCCCCCCCCCCC
50.3825953088
26UbiquitinationKKVDAGGKVKKGNLK
CCCCCCCCCCCCCCC
50.38-
52MethylationSRNPVLVRGIGRYSR
CCCCCCHHCCCCCCH
27.1816226847
57PhosphorylationLVRGIGRYSRSAMYS
CHHCCCCCCHHHHHC
11.8328102081
58PhosphorylationVRGIGRYSRSAMYSR
HHCCCCCCHHHHHCH
20.5628102081
59MethylationRGIGRYSRSAMYSRK
HCCCCCCHHHHHCHH
21.35115492231
60PhosphorylationGIGRYSRSAMYSRKA
CCCCCCHHHHHCHHH
16.0828102081
63PhosphorylationRYSRSAMYSRKAMYK
CCCHHHHHCHHHHHH
12.6828102081
64PhosphorylationYSRSAMYSRKAMYKR
CCHHHHHCHHHHHHH
17.7728102081
74PhosphorylationAMYKRKYSAAKSKVE
HHHHHHHHHHHHHHH
25.4524719451
77UbiquitinationKRKYSAAKSKVEKKK
HHHHHHHHHHHHHHH
50.99-
87AcetylationVEKKKKEKVLATVTK
HHHHHHHCEEEEEEC
51.9725953088
87UbiquitinationVEKKKKEKVLATVTK
HHHHHHHCEEEEEEC
51.97-
87MalonylationVEKKKKEKVLATVTK
HHHHHHHCEEEEEEC
51.9726320211
872-HydroxyisobutyrylationVEKKKKEKVLATVTK
HHHHHHHCEEEEEEC
51.97-
91PhosphorylationKKEKVLATVTKPVGG
HHHCEEEEEECCCCC
25.2521406692
93PhosphorylationEKVLATVTKPVGGDK
HCEEEEEECCCCCCC
25.8521406692
94AcetylationKVLATVTKPVGGDKN
CEEEEEECCCCCCCC
33.1125953088
94UbiquitinationKVLATVTKPVGGDKN
CEEEEEECCCCCCCC
33.11-
94SuccinylationKVLATVTKPVGGDKN
CEEEEEECCCCCCCC
33.11-
94MalonylationKVLATVTKPVGGDKN
CEEEEEECCCCCCCC
33.1126320211
100AcetylationTKPVGGDKNGGTRVV
ECCCCCCCCCCEEEE
61.8525953088
100UbiquitinationTKPVGGDKNGGTRVV
ECCCCCCCCCCEEEE
61.8521906983
1002-HydroxyisobutyrylationTKPVGGDKNGGTRVV
ECCCCCCCCCCEEEE
61.85-
115PhosphorylationKLRKMPRYYPTEDVP
EECCCCCCCCCCCCC
14.1328152594
116PhosphorylationLRKMPRYYPTEDVPR
ECCCCCCCCCCCCCH
12.6428152594
118PhosphorylationKMPRYYPTEDVPRKL
CCCCCCCCCCCCHHH
28.7928152594
124UbiquitinationPTEDVPRKLLSHGKK
CCCCCCHHHHHCCCC
47.94-
1242-HydroxyisobutyrylationPTEDVPRKLLSHGKK
CCCCCCHHHHHCCCC
47.94-
127PhosphorylationDVPRKLLSHGKKPFS
CCCHHHHHCCCCCHH
40.4020068231
130UbiquitinationRKLLSHGKKPFSQHV
HHHHHCCCCCHHHHH
52.4221906983
131AcetylationKLLSHGKKPFSQHVR
HHHHCCCCCHHHHHH
56.7526051181
131UbiquitinationKLLSHGKKPFSQHVR
HHHHCCCCCHHHHHH
56.7521906983
134PhosphorylationSHGKKPFSQHVRKLR
HCCCCCHHHHHHHHH
28.0923312004
143PhosphorylationHVRKLRASITPGTIL
HHHHHHHCCCCCEEE
22.1428450419
145PhosphorylationRKLRASITPGTILII
HHHHHCCCCCEEEEE
17.1128450419
148PhosphorylationRASITPGTILIILTG
HHCCCCCEEEEEEEC
17.5128450419
154PhosphorylationGTILIILTGRHRGKR
CEEEEEEECCCCCCE
23.04-
166MethylationGKRVVFLKQLASGLL
CCEEHHHHHHHHCCE
31.6230993971
170PhosphorylationVFLKQLASGLLLVTG
HHHHHHHHCCEEEEC
38.2720068231
176PhosphorylationASGLLLVTGPLVLNR
HHCCEEEECCEECCC
32.8120068231
192UbiquitinationPLRRTHQKFVIATST
CCCCCCCCEEEEECC
33.71-
1922-HydroxyisobutyrylationPLRRTHQKFVIATST
CCCCCCCCEEEEECC
33.71-
192AcetylationPLRRTHQKFVIATST
CCCCCCCCEEEEECC
33.7125825284
198PhosphorylationQKFVIATSTKIDISN
CCEEEEECCEEEHHC
20.7721712546
199PhosphorylationKFVIATSTKIDISNV
CEEEEECCEEEHHCC
27.8821712546
200UbiquitinationFVIATSTKIDISNVK
EEEEECCEEEHHCCC
37.84-
204PhosphorylationTSTKIDISNVKIPKH
ECCEEEHHCCCCCHH
31.6421815630
207AcetylationKIDISNVKIPKHLTD
EEEHHCCCCCHHHHH
58.5023236377
207SuccinylationKIDISNVKIPKHLTD
EEEHHCCCCCHHHHH
58.5021906983
207UbiquitinationKIDISNVKIPKHLTD
EEEHHCCCCCHHHHH
58.50-
210AcetylationISNVKIPKHLTDAYF
HHCCCCCHHHHHHHH
55.5125825284
2102-HydroxyisobutyrylationISNVKIPKHLTDAYF
HHCCCCCHHHHHHHH
55.51-
210MalonylationISNVKIPKHLTDAYF
HHCCCCCHHHHHHHH
55.5126320211
210UbiquitinationISNVKIPKHLTDAYF
HHCCCCCHHHHHHHH
55.5119608861
213PhosphorylationVKIPKHLTDAYFKKK
CCCCHHHHHHHHHHH
20.5028152594
216PhosphorylationPKHLTDAYFKKKKLR
CHHHHHHHHHHHCCC
20.8128152594
218MethylationHLTDAYFKKKKLRKP
HHHHHHHHHHCCCCC
51.5119608861
218UbiquitinationHLTDAYFKKKKLRKP
HHHHHHHHHHCCCCC
51.5121906983
2182-HydroxyisobutyrylationHLTDAYFKKKKLRKP
HHHHHHHHHHCCCCC
51.51-
218AcetylationHLTDAYFKKKKLRKP
HHHHHHHHHHCCCCC
51.5119608861
219UbiquitinationLTDAYFKKKKLRKPR
HHHHHHHHHCCCCCC
45.29-
220UbiquitinationTDAYFKKKKLRKPRH
HHHHHHHHCCCCCCC
58.59-
224UbiquitinationFKKKKLRKPRHQEGE
HHHHCCCCCCCCCCC
57.76-
237AcetylationGEIFDTEKEKYEITE
CCCCCCHHHHEECCC
62.6925953088
237UbiquitinationGEIFDTEKEKYEITE
CCCCCCHHHHEECCC
62.6921906983
239AcetylationIFDTEKEKYEITEQR
CCCCHHHHEECCCHH
60.2919608861
239MethylationIFDTEKEKYEITEQR
CCCCHHHHEECCCHH
60.2919608861
239UbiquitinationIFDTEKEKYEITEQR
CCCCHHHHEECCCHH
60.2921906983
240NitrationFDTEKEKYEITEQRK
CCCHHHHEECCCHHC
17.41-
247UbiquitinationYEITEQRKIDQKAVD
EECCCHHCCCHHHHH
50.78-
251AcetylationEQRKIDQKAVDSQIL
CHHCCCHHHHHCCHH
46.7823236377
251UbiquitinationEQRKIDQKAVDSQIL
CHHCCCHHHHHCCHH
46.7821906983
251SumoylationEQRKIDQKAVDSQIL
CHHCCCHHHHHCCHH
46.78-
255PhosphorylationIDQKAVDSQILPKIK
CCHHHHHCCHHHHHH
16.7221712546
2602-HydroxyisobutyrylationVDSQILPKIKAIPQL
HHCCHHHHHHHHHHH
54.09-
260SuccinylationVDSQILPKIKAIPQL
HHCCHHHHHHHHHHH
54.0927452117
260UbiquitinationVDSQILPKIKAIPQL
HHCCHHHHHHHHHHH
54.09-
260AcetylationVDSQILPKIKAIPQL
HHCCHHHHHHHHHHH
54.0926051181
262MalonylationSQILPKIKAIPQLQG
CCHHHHHHHHHHHHH
46.5226320211
2622-HydroxyisobutyrylationSQILPKIKAIPQLQG
CCHHHHHHHHHHHHH
46.52-
262UbiquitinationSQILPKIKAIPQLQG
CCHHHHHHHHHHHHH
46.52-
262SumoylationSQILPKIKAIPQLQG
CCHHHHHHHHHHHHH
46.52-
270PhosphorylationAIPQLQGYLRSVFAL
HHHHHHHHHHHHHHH
5.9828152594
272MethylationPQLQGYLRSVFALTN
HHHHHHHHHHHHHHC
23.45115492223
273PhosphorylationQLQGYLRSVFALTNG
HHHHHHHHHHHHHCC
20.9921712546
278PhosphorylationLRSVFALTNGIYPHK
HHHHHHHHCCCCCCC
28.1528442448
282PhosphorylationFALTNGIYPHKLVF-
HHHHCCCCCCCCCC-
10.7328152594
285UbiquitinationTNGIYPHKLVF----
HCCCCCCCCCC----
41.6721906983

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 RL6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL6_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 RL6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FGF2_HUMANFGF2physical
9826564
RL7A_HUMANRPL7Aphysical
22939629
RL7_HUMANRPL7physical
22939629
RS13_HUMANRPS13physical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RS3_HUMANRPS3physical
22939629
RS11_HUMANRPS11physical
22939629
RLA0_HUMANRPLP0physical
22939629
RL8_HUMANRPL8physical
22939629
RS9_HUMANRPS9physical
22939629
RL9_HUMANRPL9physical
22939629
RS12_HUMANRPS12physical
22939629
RS14_HUMANRPS14physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RS15_HUMANRPS15physical
22939629
RS16_HUMANRPS16physical
22939629
RS17_HUMANRPS17physical
22939629
RS19_HUMANRPS19physical
22939629
RS20_HUMANRPS20physical
22939629
RS23_HUMANRPS23physical
22939629
RS24_HUMANRPS24physical
22939629
RS25_HUMANRPS25physical
22939629
RS26_HUMANRPS26physical
22939629
RS2_HUMANRPS2physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS5_HUMANRPS5physical
22939629
RS6_HUMANRPS6physical
22939629
RS7_HUMANRPS7physical
22939629
RS8_HUMANRPS8physical
22939629
RSSA_HUMANRPSAphysical
22939629
RS28_HUMANRPS28physical
22939629
RLA1_HUMANRPLP1physical
22939629
RS21_HUMANRPS21physical
22939629
RS27A_HUMANRPS27Aphysical
22939629
SRP14_HUMANSRP14physical
22939629
U2AF2_HUMANU2AF2physical
22939629
SYEP_HUMANEPRSphysical
22939629
RS27L_HUMANRPS27Lphysical
22939629
RRS1_HUMANRRS1physical
22939629
SPB1_HUMANFTSJ3physical
22939629
TPR_HUMANTPRphysical
22939629
IL7RA_HUMANIL7Rphysical
23151878
SE1L1_HUMANSEL1Lphysical
21988832
MDM2_HUMANMDM2physical
24174547
LARP7_HUMANLARP7physical
26186194
RL26L_HUMANRPL26L1physical
26186194
YBOX1_HUMANYBX1physical
26186194
RT09_HUMANMRPS9physical
26186194
SPB1_HUMANFTSJ3physical
26186194
NGRN_HUMANNGRNphysical
26186194
RT26_HUMANMRPS26physical
26186194
DCAF1_HUMANVPRBPphysical
26186194
PTCD1_HUMANPTCD1physical
26186194
RENT1_HUMANUPF1physical
26186194
PTCD3_HUMANPTCD3physical
26186194
STAU2_HUMANSTAU2physical
26186194
PABP4_HUMANPABPC4physical
26186194
RT23_HUMANMRPS23physical
26186194
RM46_HUMANMRPL46physical
26186194
RT27_HUMANMRPS27physical
26186194
RRP12_HUMANRRP12physical
26186194
KRI1_HUMANKRI1physical
26186194
MTEF3_HUMANMTERF3physical
26186194
RT34_HUMANMRPS34physical
26186194
RT29_HUMANDAP3physical
26186194
SURF6_HUMANSURF6physical
26186194
NPM_HUMANNPM1physical
26186194
RT05_HUMANMRPS5physical
26186194
RT07_HUMANMRPS7physical
26186194
RT22_HUMANMRPS22physical
26186194
RM24_HUMANMRPL24physical
26186194
LARP1_HUMANLARP1physical
26186194
RT31_HUMANMRPS31physical
26186194
LN28B_HUMANLIN28Bphysical
26186194
KRR1_HUMANKRR1physical
26186194
NOP2_HUMANNOP2physical
26186194
RT02_HUMANMRPS2physical
26186194
MOV10_HUMANMOV10physical
26186194
RM27_HUMANMRPL27physical
26186194
RT11_HUMANMRPS11physical
26186194
SIR1_HUMANSIRT1physical
26186194
CLH2_HUMANCLTCL1physical
26186194
RM47_HUMANMRPL47physical
26186194
RT24_HUMANMRPS24physical
26186194
RALY_HUMANRALYphysical
26186194
ZBT11_HUMANZBTB11physical
26186194
RM38_HUMANMRPL38physical
26186194
RM15_HUMANMRPL15physical
26186194
ILF2_HUMANILF2physical
26186194
RT14_HUMANMRPS14physical
26186194
RM13_HUMANMRPL13physical
26186194
RT33_HUMANMRPS33physical
26186194
RM09_HUMANMRPL9physical
26186194
ICT1_HUMANICT1physical
26186194
RM30_HUMANMRPL30physical
26186194
GZF1_HUMANGZF1physical
26186194
RT18A_HUMANMRPS18Aphysical
26186194
RM42_HUMANMRPL42physical
26186194
RT30_HUMANMRPS30physical
26186194
RT18C_HUMANMRPS18Cphysical
26186194
SRS10_HUMANSRSF10physical
26186194
RM34_HUMANMRPL34physical
26186194
RT21_HUMANMRPS21physical
26186194
UIF_HUMANFYTTD1physical
26186194
ABCF2_HUMANABCF2physical
26344197
AL1B1_HUMANALDH1B1physical
26344197
APT_HUMANAPRTphysical
26344197
BRD4_HUMANBRD4physical
26344197
BRX1_HUMANBRIX1physical
26344197
NOG1_HUMANGTPBP4physical
26344197
HNRPC_HUMANHNRNPCphysical
26344197
IF2B3_HUMANIGF2BP3physical
26344197
PININ_HUMANPNNphysical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL12_HUMANRPL12physical
26344197
RL15_HUMANRPL15physical
26344197
RL18A_HUMANRPL18Aphysical
26344197
RL19_HUMANRPL19physical
26344197
RL22_HUMANRPL22physical
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
RL37A_HUMANRPL37Aphysical
26344197
RL38_HUMANRPL38physical
26344197
RL4_HUMANRPL4physical
26344197
RL7_HUMANRPL7physical
26344197
RL7A_HUMANRPL7Aphysical
26344197
RL8_HUMANRPL8physical
26344197
RL9_HUMANRPL9physical
26344197
RLA1_HUMANRPLP1physical
26344197
RLA2_HUMANRPLP2physical
26344197
RS10_HUMANRPS10physical
26344197
RS12_HUMANRPS12physical
26344197
RS14_HUMANRPS14physical
26344197
RS15_HUMANRPS15physical
26344197
RS16_HUMANRPS16physical
26344197
RS18_HUMANRPS18physical
26344197
RS19_HUMANRPS19physical
26344197
RS2_HUMANRPS2physical
26344197
RS23_HUMANRPS23physical
26344197
RS25_HUMANRPS25physical
26344197
RS26_HUMANRPS26physical
26344197
RS3_HUMANRPS3physical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS5_HUMANRPS5physical
26344197
RS6_HUMANRPS6physical
26344197
RS7_HUMANRPS7physical
26344197
RL26L_HUMANRPL26L1physical
28514442
PTCD1_HUMANPTCD1physical
28514442
RT09_HUMANMRPS9physical
28514442
RALY_HUMANRALYphysical
28514442
RT22_HUMANMRPS22physical
28514442
YBOX3_HUMANYBX3physical
28514442
LARP1_HUMANLARP1physical
28514442
NGRN_HUMANNGRNphysical
28514442
RT18A_HUMANMRPS18Aphysical
28514442
SIR1_HUMANSIRT1physical
28514442
RT05_HUMANMRPS5physical
28514442
RENT1_HUMANUPF1physical
28514442
UIF_HUMANFYTTD1physical
28514442
PTCD3_HUMANPTCD3physical
28514442
MOV10_HUMANMOV10physical
28514442
SURF6_HUMANSURF6physical
28514442
RT02_HUMANMRPS2physical
28514442
CLH2_HUMANCLTCL1physical
28514442
RT18C_HUMANMRPS18Cphysical
28514442
RT29_HUMANDAP3physical
28514442
RM38_HUMANMRPL38physical
28514442
RM24_HUMANMRPL24physical
28514442
RBM34_HUMANRBM34physical
28514442
DCAF1_HUMANVPRBPphysical
28514442
RM13_HUMANMRPL13physical
28514442
MTEF3_HUMANMTERF3physical
28514442
ZBT11_HUMANZBTB11physical
28514442
RT21_HUMANMRPS21physical
28514442
RT14_HUMANMRPS14physical
28514442
RT35_HUMANMRPS35physical
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 RL6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-5; LYS-210 AND LYS-239, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND MASSSPECTROMETRY.

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