Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  60S ribosomal protein L6  

UniProtKB / Swiss-Prot ID :  RL6_HUMAN

Gene Name (Synonyms) : 
RPL6, TXREB1  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Specifically binds to domain C of the Tax-responsive enhancer element in the long terminal repeat of HTLV-I. 

Protein Sequence MAGEKVEKPDTKEKKPEAKKVDAGGKVKKGNLKAKKPKKGKPHCSRNPVLVRGIGRYSRSAMYSRKAMYK...
Predicted Secondary Structure CCCCCCCCCCCCCCCHHHHCCCCCCCCCHHHHHHHCCCCCCCCCCCCCCEEECCCHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
100K -> Q (in a colorectal cancer sample;somatic mutation).
227H -> R (in dbSNP:rs17851813). VAR_025313
237K -> E (in dbSNP:rs16942044). VAR_051810
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAGEKV
---CCCCCC
34.55UniProtKB
Link-
5N6-acetyllysineMAGEKVEKP
CCCCCCCCC
55.57HPRD
Link-
5N6-acetyllysineMAGEKVEKP
CCCCCCCCC
55.57Phosphositeplus
Link-
5N6-acetyllysine.MAGEKVEKP
CCCCCCCCC
55.57UniProtKB
Link-
11PhosphothreonineEKPDTKEKK
CCCCCCCCC
50.02HPRD
Link-
11PhosphothreonineEKPDTKEKK
CCCCCCCCC
50.02Phosphositeplus
Link-
94Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ATVTKPVGG
CCEEECCCC
33.11Phosphositeplus
Link
100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VGGDKNGGT
CCCCCCCCH
61.85Phosphositeplus
Link
127PhosphoserineRKLLSHGKK
HHHHHCCCC
40.40HPRD
Link
127Phosphoserine.RKLLSHGKK
HHHHHCCCC
40.40UniProtKB
Link
170PhosphoserineKQLASGLLL
EEECCCEEE
38.27HPRD
Link
170PhosphoserineKQLASGLLL
EEECCCEEE
38.27Phosphositeplus
Link
176PhosphothreonineLLLVTGPLV
EEEEECCCE
32.81HPRD
Link
176PhosphothreonineLLLVTGPLV
EEEEECCCE
32.81Phosphositeplus
Link
204PhosphoserineKIDISNVKI
EEEEECCCC
31.64HPRD
Link
204PhosphoserineKIDISNVKI
EEEEECCCC
31.64Phosphositeplus
Link
207Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ISNVKIPKH
EECCCCCHH
58.50Phosphositeplus
Link
210Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VKIPKHLTD
CCCCHHHHH
55.51Phosphositeplus
Link
210N6-acetyllysineVKIPKHLTD
CCCCHHHHH
55.51HPRD
Link
210N6-acetyllysineVKIPKHLTD
CCCCHHHHH
55.51Phosphositeplus
Link
210N6-acetyllysine.VKIPKHLTD
CCCCHHHHH
55.51UniProtKB
Link
218N6-acetyllysineDAYFKKKKL
HHHHHHHHH
51.51HPRD
Link
218N6-acetyllysineDAYFKKKKL
HHHHHHHHH
51.51Phosphositeplus
Link
237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FDTEKEKYE
CCCCCCHHC
62.69Phosphositeplus
Link
239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TEKEKYEIT
CCCCHHCCH
60.29Phosphositeplus
Link
239N6-acetyllysineTEKEKYEIT
CCCCHHCCH
60.29HPRD
Link
239N6-acetyllysineTEKEKYEIT
CCCCHHCCH
60.29Phosphositeplus
Link
239N6-acetyllysine.TEKEKYEIT
CCCCHHCCH
60.29UniProtKB
Link
251Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KIDQKAVDS
HHHHHHHHH
46.78Phosphositeplus
Link
262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LPKIKAIPQ
HHHHHCCHH
46.52Phosphositeplus
Link
282PhosphotyrosineTNGIYPHKL
CCCCCCEEC
10.73Phosphositeplus
Link
285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IYPHKLVF
CCCEECCC
41.67Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
M3K14_HUMANphysical interactionMINT-48004MINT14743216
M3K14_HUMANphysical interactionDIP:44922EDIP14743216
FGF2_HUMANin vitro
yeast 2-hybrid
HPRD:04745HPRD9826564
STAU1_HUMANin vitroHPRD:04745HPRD15121898
RL29_HUMANin vitroHPRD:04745HPRD6468376
M3K14_HUMANin vitroHPRD:04745HPRD14743216
RS20_HUMANENSP00000202773STRING
RL18_HUMANENSP00000202773STRING
RS5_HUMANENSP00000202773STRING
RS18_HUMANENSP00000202773STRING
RS19_HUMANENSP00000202773STRING
RL18A_HUMANENSP00000202773STRING
RL19_HUMANENSP00000202773STRING
RS13_HUMANENSP00000202773STRING
RS12_HUMANENSP00000202773STRING
RS15_HUMANENSP00000202773STRING
RS25_HUMANENSP00000202773STRING
RS4Y1_HUMANENSP00000202773STRING
RS16_HUMANENSP00000202773STRING
RL36_HUMANENSP00000202773STRING
RL35_HUMANENSP00000202773STRING
RL8_HUMANENSP00000202773STRING
RL31_HUMANENSP00000202773STRING
RL26L_HUMANENSP00000202773STRING
RL24_HUMANENSP00000202773STRING
RL3L_HUMANENSP00000202773STRING
RS11_HUMANENSP00000202773STRING
RL13A_HUMANENSP00000202773STRING
RS27A_HUMANENSP00000202773STRING
UBIQ_HUMANENSP00000202773STRING
RL37_HUMANENSP00000202773STRING
RS3_HUMANENSP00000202773STRING
UBIM_HUMANENSP00000202773STRING
RS30_HUMANENSP00000202773STRING
RL30_HUMANENSP00000202773STRING
IF2P_HUMANENSP00000202773STRING
RL26_HUMANENSP00000202773STRING
RL29_HUMANENSP00000202773STRING
RS23_HUMANENSP00000202773STRING
RS9_HUMANENSP00000202773STRING
RL13_HUMANENSP00000202773STRING
EF2_HUMANENSP00000202773STRING
RL38_HUMANENSP00000202773STRING
RS14_HUMANENSP00000202773STRING
RL4_HUMANENSP00000202773STRING
RS15A_HUMANENSP00000202773STRING
RLA2_HUMANENSP00000202773STRING
RL35A_HUMANENSP00000202773STRING
RL35A_HUMANENSP00000202773STRING
RLA0_HUMANENSP00000202773STRING
RL32_HUMANENSP00000202773STRING
RS7_HUMANENSP00000202773STRING
RL7_HUMANENSP00000202773STRING
RL10_HUMANENSP00000202773STRING
RS2_HUMANENSP00000202773STRING
RL28_HUMANENSP00000202773STRING
RL3_HUMANENSP00000202773STRING
RL27A_HUMANENSP00000202773STRING
RLA1_HUMANENSP00000202773STRING
RL23_HUMANENSP00000202773STRING
RS17_HUMANENSP00000202773STRING
RS3A_HUMANENSP00000202773STRING
RSSA_HUMANENSP00000202773STRING
RL22_HUMANENSP00000202773STRING
RL15_HUMANENSP00000202773STRING
RL23A_HUMANENSP00000202773STRING
RS26_HUMANENSP00000202773STRING
RS28_HUMANENSP00000202773STRING
RL37A_HUMANENSP00000202773STRING
ERF1_HUMANENSP00000202773STRING
RL10A_HUMANENSP00000202773STRING
RL39_HUMANENSP00000202773STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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-5; LYS-210 AND LYS-239, ANDMASS SPECTROMETRY.
"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.
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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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures