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 L11  

UniProtKB / Swiss-Prot ID :  RL11_HUMAN

Gene Name (Synonyms) : 
RPL11  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus, nucleolus (By similarity). 

Protein Function :  Binds to 5S ribosomal RNA (By similarity). Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML (By similarity). 

Protein Sequence MAQDQGEKENPMRELRIRKLCLNICVGESGDRLTRAAKVLEQLTGQTPVFSKARYTVRSFGIRRNEKIAV...
Predicted Secondary Structure CCHHHCCCCCCEEECEEEEEEEECCCCHHHHHHHHHHHHHHHHHCCCCEEEEEEEECCCCCCCCCCEEEE...
Protein Variant
LocationDescription
20L -> H (in DBA7). VAR_055448
161Missing (in DBA7). VAR_055449
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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.---MAQDQG
---CCHHHC
22.96UniProtKB
Link-
8NeddyllysineDQGEKENPM
HHCCCCCCE
70.39Phosphositeplus
Link
19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LRIRKLCLN
CEEEEEEEE
40.98Phosphositeplus
Link
19NeddyllysineLRIRKLCLN
CEEEEEEEE
40.98Phosphositeplus
Link
38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TRAAKVLEQ
HHHHHHHHH
46.50Phosphositeplus
Link
38NeddyllysineTRAAKVLEQ
HHHHHHHHH
46.50Phosphositeplus
Link
44PhosphothreonineLEQLTGQTP
HHHHHCCCC
27.26HPRD
Link
44PhosphothreonineLEQLTGQTP
HHHHHCCCC
27.26Phosphositeplus
Link
44PhosphothreonineLEQLTGQTP
HHHHHCCCC
27.26SysPTM
Link
44Phosphothreonine.LEQLTGQTP
HHHHHCCCC
27.26UniProtKB
Link
47PhosphothreonineLTGQTPVFS
HHCCCCEEE
23.82HPRD
Link
47PhosphothreonineLTGQTPVFS
HHCCCCEEE
23.82Phosphositeplus
Link
47PhosphothreonineLTGQTPVFS
HHCCCCEEE
23.82SysPTM
Link
47Phosphothreonine.LTGQTPVFS
HHCCCCEEE
23.82UniProtKB
Link
52Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PVFSKARYT
CEEEEEEEE
25.97Phosphositeplus
Link
52N6-acetyllysinePVFSKARYT
CEEEEEEEE
25.97HPRD
Link
52N6-acetyllysinePVFSKARYT
CEEEEEEEE
25.97Phosphositeplus
Link
52N6-acetyllysine.PVFSKARYT
CEEEEEEEE
25.97UniProtKB
Link
52NeddyllysinePVFSKARYT
CEEEEEEEE
25.97Phosphositeplus
Link
67NeddyllysineRRNEKIAVH
CCCCEEEEE
39.24Phosphositeplus
Link
72S-nitrosocysteineIAVHCTVRG
EEEEEEECH
2.78dbSNO
Link
73PhosphothreonineAVHCTVRGA
EEEEEECHH
9.81HPRD
Link
73PhosphothreonineAVHCTVRGA
EEEEEECHH
9.81Phosphositeplus
Link
78Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VRGAKAEEI
ECHHHHHHH
60.19Phosphositeplus
Link
78NeddyllysineVRGAKAEEI
ECHHHHHHH
60.19Phosphositeplus
Link
85Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EILEKGLKV
HHHHCCEEE
67.13Phosphositeplus
Link
85N6-acetyllysineEILEKGLKV
HHHHCCEEE
67.13HPRD
Link
85N6-acetyllysineEILEKGLKV
HHHHCCEEE
67.13Phosphositeplus
Link
85N6-acetyllysine.EILEKGLKV
HHHHCCEEE
67.13UniProtKB
Link
85NeddyllysineEILEKGLKV
HHHHCCEEE
67.13Phosphositeplus
Link
88NeddyllysineEKGLKVREY
HCCEEEEEE
48.17Phosphositeplus
Link
96NeddyllysineYELRKNNFS
EEECCCCCC
69.72Phosphositeplus
Link
118NeddyllysineDLGIKYDPS
EECEEECCC
41.63Phosphositeplus
Link
140PhosphoserineRPGFSIADK
CCCHHHHHH
23.84Phosphositeplus
Link
144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SIADKKRRT
HHHHHHHHH
38.87Phosphositeplus
Link
144NeddyllysineSIADKKRRT
HHHHHHHHH
38.87Phosphositeplus
Link
145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IADKKRRTG
HHHHHHHHC
47.89Phosphositeplus
Link
145NeddyllysineIADKKRRTG
HHHHHHHHC
47.89Phosphositeplus
Link
150S-nitrosocysteineRRTGCIGAK
HHHCCCCCC
2.28dbSNO
Link
154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)CIGAKHRIS
CCCCCCCCC
28.36Phosphositeplus
Link
154NeddyllysineCIGAKHRIS
CCCCCCCCC
28.36Phosphositeplus
Link
159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HRISKEEAM
CCCCHHHHH
58.14Phosphositeplus
Link
159N6-acetyllysineHRISKEEAM
CCCCHHHHH
58.14HPRD
Link
159N6-acetyllysineHRISKEEAM
CCCCHHHHH
58.14Phosphositeplus
Link
159N6-acetyllysine.HRISKEEAM
CCCCHHHHH
58.14UniProtKB
Link
159NeddyllysineHRISKEEAM
CCCCHHHHH
58.14Phosphositeplus
Link
169Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)WFQQKYDGI
HHHHHCCEE
34.23Phosphositeplus
Link
169NeddyllysineWFQQKYDGI
HHHHHCCEE
34.23Phosphositeplus
Link
178NeddyllysineILPGK
EECCC
56.05Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
MYC_HUMANphysical interactionMINT-5208311MINT17599065
NFKB2_HUMANphysical interactionMINT-48766MINT14743216
M3K14_HUMANphysical interactionMINT-48866MINT14743216
NEMO_HUMANphysical interactionMINT-48234MINT14743216
MDM2_HUMANphysical interaction
physical interaction
EBI-1381121
EBI-1247215
intact17310983
17373842
PML_HUMANin vitro
in vivo
HPRD:10364HPRD15195100
MDM2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:10364HPRD14612427
12842086
BLMH_HUMANin vitro
yeast 2-hybrid
HPRD:10364HPRD10353821
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Disease Reference
Kegg disease
OMIM disease
612562Diamond-Blackfan anemia 7 (DBA7)
Drug Reference
There are no disease associations of PTM sites.
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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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-47, 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-52; LYS-85 AND LYS-159, ANDMASS SPECTROMETRY.
"Characterization and analysis of posttranslational modifications ofthe human large cytoplasmic ribosomal subunit proteins by massspectrometry and Edman sequencing.";
Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,Karpova G.G.;
J. Protein Chem. 22:249-258(2003).
Cited for: MASS SPECTROMETRY, AND ACETYLATION AT ALA-2.
Phosphorylation
ReferencePubMed
"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-44 AND THR-47, 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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-47, 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