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UniProtKB - P62913 (RL11_HUMAN)

Protein

60S ribosomal protein L11

Gene

RPL11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs (PubMed:19061985, PubMed:12962325, PubMed:24120868). It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53 (PubMed:24120868). Promotes nucleolar location of PML (By similarity).By similarity3 Publications

GO - Molecular functioni

  • 5S rRNA binding Source: CAFA
  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: GO_Central
  • ubiquitin ligase inhibitor activity Source: CAFA
  • ubiquitin protein ligase binding Source: CAFA
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-HSA-156902 Peptide chain elongation
R-HSA-1799339 SRP-dependent cotranslational protein targeting to membrane
R-HSA-192823 Viral mRNA Translation
R-HSA-2408557 Selenocysteine synthesis
R-HSA-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-HSA-72689 Formation of a pool of free 40S subunits
R-HSA-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-HSA-72764 Eukaryotic Translation Termination
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
SIGNORiP62913

Protein family/group databases

MoonProtiP62913

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L11
Alternative name(s):
CLL-associated antigen KW-12
Large ribosomal subunit protein uL51 Publication
Gene namesi
Name:RPL11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000142676.12
HGNCiHGNC:10301 RPL11
MIMi604175 gene
neXtProtiNX_P62913

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Diamond-Blackfan anemia 7 (DBA7)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies.
See also OMIM:612562
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05544820L → H in DBA7. 1 Publication1
Natural variantiVAR_055449161Missing in DBA7. 1 Publication1

Keywords - Diseasei

Diamond-Blackfan anemia, Disease mutation

Organism-specific databases

DisGeNETi6135
GeneReviewsiRPL11
MalaCardsiRPL11
MIMi612562 phenotype
OpenTargetsiENSG00000142676
Orphaneti124 Blackfan-Diamond anemia
PharmGKBiPA34664

Chemistry databases

DrugBankiDB02494 Alpha-Hydroxy-Beta-Phenyl-Propionic Acid
DB07374 Anisomycin
DB08437 Puromycin

Polymorphism and mutation databases

BioMutaiRPL11
DMDMi51702795

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001250822 – 17860S ribosomal protein L11Add BLAST177

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources2 Publications1
Cross-linki38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei44PhosphothreonineCombined sources1
Modified residuei47PhosphothreonineCombined sources1
Modified residuei52N6-acetyllysine; alternateCombined sources1
Cross-linki52Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei85N6-acetyllysineCombined sources1
Cross-linki154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP62913
PaxDbiP62913
PeptideAtlasiP62913
PRIDEiP62913
ProteomicsDBi57452
57453 [P62913-2]
TopDownProteomicsiP62913-1 [P62913-1]

2D gel databases

SWISS-2DPAGEiP62913

PTM databases

iPTMnetiP62913
PhosphoSitePlusiP62913
SwissPalmiP62913

Miscellaneous databases

PMAP-CutDBiP62913

Expressioni

Gene expression databases

BgeeiENSG00000142676 Expressed in 232 organ(s), highest expression level in epithelium of bronchus
CleanExiHS_RPL11
ExpressionAtlasiP62913 baseline and differential
GenevisibleiP62913 HS

Organism-specific databases

HPAiHPA002734
HPA074839

Interactioni

Subunit structurei

Component of the large ribosomal subunit (LSU). Part of a LSU subcomplex, the 5S RNP which is composed of the 5S RNA, RPL5 and RPL11 (PubMed:24120868). Interacts with PML (By similarity). Interacts with MDM2; negatively regulates MDM2-mediated TP53 ubiquitination and degradation (PubMed:24120868). Interacts with NOP53; retains RPL11 into the nucleolus (PubMed:24556985, PubMed:27829214).By similarity3 Publications

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi112055, 270 interactors
CORUMiP62913
IntActiP62913, 63 interactors
MINTiP62913
STRINGi9606.ENSP00000363676

Structurei

Secondary structure

1178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP62913
SMRiP62913
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the universal ribosomal protein uL5 family.Curated

Phylogenomic databases

eggNOGiKOG0397 Eukaryota
COG0094 LUCA
GeneTreeiENSGT00910000144211
HOGENOMiHOG000231312
HOVERGENiHBG055214
InParanoidiP62913
KOiK02868
OMAiEDTMAWF
OrthoDBiEOG091G0LSV
PhylomeDBiP62913
TreeFamiTF300017

Family and domain databases

Gene3Di3.30.1440.10, 1 hit
InterProiView protein in InterPro
IPR002132 Ribosomal_L5
IPR031309 Ribosomal_L5_C
IPR020929 Ribosomal_L5_CS
IPR022803 Ribosomal_L5_dom_sf
IPR031310 Ribosomal_L5_N
PANTHERiPTHR11994 PTHR11994, 1 hit
PfamiView protein in Pfam
PF00281 Ribosomal_L5, 1 hit
PF00673 Ribosomal_L5_C, 1 hit
PIRSFiPIRSF002161 Ribosomal_L5, 1 hit
SUPFAMiSSF55282 SSF55282, 1 hit
PROSITEiView protein in PROSITE
PS00358 RIBOSOMAL_L5, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P62913-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF 
        60         70         80         90        100
SKARYTVRSF GIRRNEKIAV HCTVRGAKAE EILEKGLKVR EYELRKNNFS 
       110        120        130        140        150
DTGNFGFGIQ EHIDLGIKYD PSIGIYGLDF YVVLGRPGFS IADKKRRTGC 
       160        170 
IGAKHRISKE EAMRWFQQKY DGIILPGK
Length:178
Mass (Da):20,252
Last modified:January 23, 2007 - v2
Checksum:i26EC965C9239774E
GO
Isoform 2 (identifier: P62913-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3-3: Missing.

Show »
Length:177
Mass (Da):20,124
Checksum:i534FC28B1D3CF195
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5VVC8Q5VVC8_HUMAN
60S ribosomal protein L11
RPL11
167Annotation score:
A0A2R8Y447A0A2R8Y447_HUMAN
60S ribosomal protein L11
RPL11
44Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31D → G in CAA55816 (PubMed:7748210).Curated1
Sequence conflicti73T → A in CAA55816 (PubMed:7748210).Curated1
Sequence conflicti92Y → L in CAA55816 (PubMed:7748210).Curated1
Sequence conflicti118K → E in CAA55816 (PubMed:7748210).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05544820L → H in DBA7. 1 Publication1
Natural variantiVAR_055449161Missing in DBA7. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0083203Missing in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79234 mRNA Translation: CAA55816.1
L05092 mRNA Translation: AAC15856.1
AF101385 Genomic DNA Translation: AAD20460.3
BC018970 mRNA Translation: AAH18970.1
AF432212 mRNA Translation: AAL99919.1
AB007171 Genomic DNA Translation: BAA25831.1
CCDSiCCDS238.1
CCDS85940.1 [P62913-2]
PIRiS45049
RefSeqiNP_000966.2, NM_000975.3 [P62913-1]
NP_001186731.1, NM_001199802.1 [P62913-2]
UniGeneiHs.719951

Genome annotation databases

EnsembliENST00000374550; ENSP00000363676; ENSG00000142676 [P62913-2]
ENST00000643754; ENSP00000496250; ENSG00000142676 [P62913-1]
GeneIDi6135
KEGGihsa:6135

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Web resourcesi

Diamond-Blackfan Anemia mutation database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79234 mRNA Translation: CAA55816.1
L05092 mRNA Translation: AAC15856.1
AF101385 Genomic DNA Translation: AAD20460.3
BC018970 mRNA Translation: AAH18970.1
AF432212 mRNA Translation: AAL99919.1
AB007171 Genomic DNA Translation: BAA25831.1
CCDSiCCDS238.1
CCDS85940.1 [P62913-2]
PIRiS45049
RefSeqiNP_000966.2, NM_000975.3 [P62913-1]
NP_001186731.1, NM_001199802.1 [P62913-2]
UniGeneiHs.719951

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LJ1-178[»]
4V6Xelectron microscopy5.00CJ1-178[»]
4XXBX-ray2.40A1-178[»]
5AJ0electron microscopy3.50AJ1-178[»]
5LKSelectron microscopy3.60LJ1-178[»]
5T2Celectron microscopy3.60q1-178[»]
6EK0electron microscopy2.90LJ1-178[»]
ProteinModelPortaliP62913
SMRiP62913
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112055, 270 interactors
CORUMiP62913
IntActiP62913, 63 interactors
MINTiP62913
STRINGi9606.ENSP00000363676

Chemistry databases

DrugBankiDB02494 Alpha-Hydroxy-Beta-Phenyl-Propionic Acid
DB07374 Anisomycin
DB08437 Puromycin

Protein family/group databases

MoonProtiP62913

PTM databases

iPTMnetiP62913
PhosphoSitePlusiP62913
SwissPalmiP62913

Polymorphism and mutation databases

BioMutaiRPL11
DMDMi51702795

2D gel databases

SWISS-2DPAGEiP62913

Proteomic databases

EPDiP62913
PaxDbiP62913
PeptideAtlasiP62913
PRIDEiP62913
ProteomicsDBi57452
57453 [P62913-2]
TopDownProteomicsiP62913-1 [P62913-1]

Protocols and materials databases

DNASUi6135
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374550; ENSP00000363676; ENSG00000142676 [P62913-2]
ENST00000643754; ENSP00000496250; ENSG00000142676 [P62913-1]
GeneIDi6135
KEGGihsa:6135

Organism-specific databases

CTDi6135
DisGeNETi6135
EuPathDBiHostDB:ENSG00000142676.12
GeneCardsiRPL11
GeneReviewsiRPL11
HGNCiHGNC:10301 RPL11
HPAiHPA002734
HPA074839
MalaCardsiRPL11
MIMi604175 gene
612562 phenotype
neXtProtiNX_P62913
OpenTargetsiENSG00000142676
Orphaneti124 Blackfan-Diamond anemia
PharmGKBiPA34664
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0397 Eukaryota
COG0094 LUCA
GeneTreeiENSGT00910000144211
HOGENOMiHOG000231312
HOVERGENiHBG055214
InParanoidiP62913
KOiK02868
OMAiEDTMAWF
OrthoDBiEOG091G0LSV
PhylomeDBiP62913
TreeFamiTF300017

Enzyme and pathway databases

ReactomeiR-HSA-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-HSA-156902 Peptide chain elongation
R-HSA-1799339 SRP-dependent cotranslational protein targeting to membrane
R-HSA-192823 Viral mRNA Translation
R-HSA-2408557 Selenocysteine synthesis
R-HSA-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-HSA-72689 Formation of a pool of free 40S subunits
R-HSA-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-HSA-72764 Eukaryotic Translation Termination
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
SIGNORiP62913

Miscellaneous databases

ChiTaRSiRPL11 human
GeneWikiiRPL11
GenomeRNAii6135
PMAP-CutDBiP62913
PROiPR:P62913
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000142676 Expressed in 232 organ(s), highest expression level in epithelium of bronchus
CleanExiHS_RPL11
ExpressionAtlasiP62913 baseline and differential
GenevisibleiP62913 HS

Family and domain databases

Gene3Di3.30.1440.10, 1 hit
InterProiView protein in InterPro
IPR002132 Ribosomal_L5
IPR031309 Ribosomal_L5_C
IPR020929 Ribosomal_L5_CS
IPR022803 Ribosomal_L5_dom_sf
IPR031310 Ribosomal_L5_N
PANTHERiPTHR11994 PTHR11994, 1 hit
PfamiView protein in Pfam
PF00281 Ribosomal_L5, 1 hit
PF00673 Ribosomal_L5_C, 1 hit
PIRSFiPIRSF002161 Ribosomal_L5, 1 hit
SUPFAMiSSF55282 SSF55282, 1 hit
PROSITEiView protein in PROSITE
PS00358 RIBOSOMAL_L5, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRL11_HUMAN
AccessioniPrimary (citable) accession number: P62913
Secondary accession number(s): P25121
, P39026, Q8TDH2, Q9Y674
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 152 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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