Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  40S ribosomal protein S11  

UniProtKB / Swiss-Prot ID :  RS11_HUMAN

Gene Name (Synonyms) : 
RPS11  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MADIQTERAYQKQPTIFQNKKRVLLGETGKEKLPRYYKNIGLGFKTPKEAIEGTYIDKKCPFTGNVSIRG...
Predicted Secondary Structure CCCCHHHHHHHHCCCEEECCCCCCCCCCCCCCCHHEEEECCCCCCCCHHHHCCCCCCCCCCCCCCEEECC...
Protein Variant -
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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
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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.---MADIQT
---CCCCHH
23.71UniProtKB
Link
10PhosphotyrosineTERAYQKQP
HHHHHHHCC
23.59Phosphositeplus
Link
10Phosphotyrosine.TERAYQKQP
HHHHHHHCC
23.59UniProtKB
Link
12Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RAYQKQPTI
HHHHHCCCE
45.64Phosphositeplus
Link
15PhosphothreonineQKQPTIFQN
HHCCCEEEC
31.75Phosphositeplus
Link
30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GETGKEKLP
CCCCCCCCH
60.12Phosphositeplus
Link
36PhosphotyrosineKLPRYYKNI
CCHHEEEEC
19.49Phosphositeplus
Link
36Phosphotyrosine.KLPRYYKNI
CCHHEEEEC
19.49UniProtKB
Link
37PhosphotyrosineLPRYYKNIG
CHHEEEECC
9.99Phosphositeplus
Link
37Phosphotyrosine.LPRYYKNIG
CHHEEEECC
9.99UniProtKB
Link
38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PRYYKNIGL
HHEEEECCC
32.90Phosphositeplus
Link
38N6-acetyllysinePRYYKNIGL
HHEEEECCC
32.90Phosphositeplus
Link
38N6-acetyllysine.PRYYKNIGL
HHEEEECCC
32.90UniProtKB
Link
45Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GLGFKTPKE
CCCCCCCHH
63.22Phosphositeplus
Link
45N6-acetyllysineGLGFKTPKE
CCCCCCCHH
63.22Phosphositeplus
Link
45N6-acetyllysine.GLGFKTPKE
CCCCCCCHH
63.22UniProtKB
Link
48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FKTPKEAIE
CCCCHHHHC
66.08Phosphositeplus
Link
55PhosphotyrosineIEGTYIDKK
HCCCCCCCC
20.27Phosphositeplus
Link
55Phosphotyrosine.IEGTYIDKK
HCCCCCCCC
20.27UniProtKB
Link
58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TYIDKKCPF
CCCCCCCCC
46.87Phosphositeplus
Link
59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YIDKKCPFT
CCCCCCCCC
43.31Phosphositeplus
Link
63PhosphothreonineKCPFTGNVS
CCCCCCCEE
17.00Phosphositeplus
Link
67PhosphoserineTGNVSIRGR
CCCEEECCE
15.57Phosphositeplus
Link
74PhosphoserineGRILSGVVT
CEEEEEEEE
27.46Phosphositeplus
Link
78PhosphothreonineSGVVTKMKM
EEEEEECCC
24.02Phosphositeplus
Link
79Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GVVTKMKMQ
EEEEECCCC
25.55Phosphositeplus
Link
92PhosphotyrosineIRRDYLHYI
EEEEEEEEC
8.12Phosphositeplus
Link
131S-nitrosocysteineTVGECRPLS
EEEEECCCC
4.46dbSNO
Link
131S-nitrosocysteineTVGECRPLS
EEEEECCCC
4.46HPRD
Link
131S-nitrosocysteineTVGECRPLS
EEEEECCCC
4.46SysPTM
Link
136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RPLSKTVRF
CCCCCCCEE
59.74Phosphositeplus
Link
144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FNVLKVTKA
EEEEEEEEC
43.50Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NFKB2_HUMANphysical interactionMINT-48729MINT14743216
M3K1_HUMANphysical interactionMINT-48309MINT14743216
M3K14_HUMANphysical interactionDIP:44924EDIP14743216
M3K14_HUMANin vitroHPRD:01599HPRD14743216
RS20_HUMANENSP00000270625STRING
RL18_HUMANENSP00000270625STRING
RS5_HUMANENSP00000270625STRING
RL6_HUMANENSP00000270625STRING
RS18_HUMANENSP00000270625STRING
EIF3D_HUMANENSP00000270625STRING
IF5_HUMANENSP00000270625STRING
EIF3E_HUMANENSP00000270625STRING
RS19_HUMANENSP00000270625STRING
RL18A_HUMANENSP00000270625STRING
RL19_HUMANENSP00000270625STRING
RS13_HUMANENSP00000270625STRING
RS12_HUMANENSP00000270625STRING
RS15_HUMANENSP00000270625STRING
RS25_HUMANENSP00000270625STRING
EIF3K_HUMANENSP00000270625STRING
RS4Y1_HUMANENSP00000270625STRING
RS16_HUMANENSP00000270625STRING
RL36_HUMANENSP00000270625STRING
IF2G_HUMANENSP00000270625STRING
EIF3G_HUMANENSP00000270625STRING
IF2A_HUMANENSP00000270625STRING
RL35_HUMANENSP00000270625STRING
EIF3J_HUMANENSP00000270625STRING
IF4B_HUMANENSP00000270625STRING
RL8_HUMANENSP00000270625STRING
RL31_HUMANENSP00000270625STRING
RL26L_HUMANENSP00000270625STRING
RL24_HUMANENSP00000270625STRING
IF4H_HUMANENSP00000270625STRING
RL3L_HUMANENSP00000270625STRING
RL13A_HUMANENSP00000270625STRING
RS27A_HUMANENSP00000270625STRING
UBIQ_HUMANENSP00000270625STRING
RL37_HUMANENSP00000270625STRING
EIF3H_HUMANENSP00000270625STRING
RS3_HUMANENSP00000270625STRING
UBIM_HUMANENSP00000270625STRING
RS30_HUMANENSP00000270625STRING
IF4E_HUMANENSP00000270625STRING
RL30_HUMANENSP00000270625STRING
IF2P_HUMANENSP00000270625STRING
RL26_HUMANENSP00000270625STRING
RL29_HUMANENSP00000270625STRING
RS23_HUMANENSP00000270625STRING
RS9_HUMANENSP00000270625STRING
RL13_HUMANENSP00000270625STRING
EF2_HUMANENSP00000270625STRING
RL38_HUMANENSP00000270625STRING
EIF3F_HUMANENSP00000270625STRING
EIF3F_HUMANENSP00000270625STRING
RS14_HUMANENSP00000270625STRING
RL4_HUMANENSP00000270625STRING
PABP1_HUMANENSP00000270625STRING
RS15A_HUMANENSP00000270625STRING
RLA2_HUMANENSP00000270625STRING
IF4G1_HUMANENSP00000270625STRING
IF4A2_HUMANENSP00000270625STRING
RL35A_HUMANENSP00000270625STRING
RL35A_HUMANENSP00000270625STRING
EIF3C_HUMANENSP00000270625STRING
RLA0_HUMANENSP00000270625STRING
RL32_HUMANENSP00000270625STRING
RS7_HUMANENSP00000270625STRING
RL7_HUMANENSP00000270625STRING
RL10_HUMANENSP00000270625STRING
RS2_HUMANENSP00000270625STRING
RL28_HUMANENSP00000270625STRING
RL3_HUMANENSP00000270625STRING
RL27A_HUMANENSP00000270625STRING
RLA1_HUMANENSP00000270625STRING
RL23_HUMANENSP00000270625STRING
RS17_HUMANENSP00000270625STRING
RS3A_HUMANENSP00000270625STRING
RSSA_HUMANENSP00000270625STRING
RL22_HUMANENSP00000270625STRING
RL15_HUMANENSP00000270625STRING
RL23A_HUMANENSP00000270625STRING
RS26_HUMANENSP00000270625STRING
RS28_HUMANENSP00000270625STRING
RL37A_HUMANENSP00000270625STRING
ERF1_HUMANENSP00000270625STRING
RL10A_HUMANENSP00000270625STRING
RL39_HUMANENSP00000270625STRING
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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-38 AND LYS-45, AND MASSSPECTROMETRY.
"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
"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 TYR-10; TYR-36; TYR-37 ANDTYR-55, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures