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Protein

60S ribosomal protein L11

Gene

RPL11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

GO - Biological processi

  • negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • negative regulation of protein neddylation Source: CAFA
  • negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: CAFA
  • negative regulation of ubiquitin protein ligase activity Source: CAFA
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • positive regulation of gene expression Source: CAFA
  • positive regulation of protein binding Source: CAFA
  • positive regulation of signal transduction by p53 class mediator Source: UniProtKB
  • protein localization to nucleus Source: UniProtKB
  • protein stabilization Source: CAFA
  • protein targeting Source: UniProtKB
  • ribosomal large subunit assembly Source: UniProtKB
  • ribosomal large subunit biogenesis Source: UniProtKB
  • rRNA processing Source: UniProtKB
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • translation Source: GO_Central
  • translational initiation Source: Reactome
  • viral transcription Source: Reactome

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-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.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10301. RPL11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • protein complex Source: CAFA

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.
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
Modified residuei44PhosphothreonineCombined sources1
Modified residuei47PhosphothreonineCombined sources1
Modified residuei52N6-acetyllysineCombined sources1
Modified residuei85N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62913.
PaxDbiP62913.
PeptideAtlasiP62913.
PRIDEiP62913.
TopDownProteomicsiP62913-1. [P62913-1]

2D gel databases

SWISS-2DPAGEiP62913.

PTM databases

iPTMnetiP62913.
PhosphoSitePlusiP62913.
SwissPalmiP62913.

Miscellaneous databases

PMAP-CutDBiP62913.

Expressioni

Gene expression databases

BgeeiENSG00000142676.
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

Show more details

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: CAFA

Protein-protein interaction databases

BioGridi112055. 190 interactors.
IntActiP62913. 55 interactors.
MINTiMINT-1140097.
STRINGi9606.ENSP00000363676.

Structurei

Secondary structure

1178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 25Combined sources10
Beta strandi27 – 30Combined sources4
Helixi31 – 44Combined sources14
Beta strandi49 – 52Combined sources4
Helixi58 – 60Combined sources3
Beta strandi67 – 74Combined sources8
Helixi76 – 89Combined sources14
Turni90 – 92Combined sources3
Beta strandi93 – 95Combined sources3
Helixi96 – 98Combined sources3
Beta strandi105 – 110Combined sources6
Helixi112 – 115Combined sources4
Turni121 – 123Combined sources3
Beta strandi128 – 135Combined sources8
Helixi159 – 169Combined sources11
Beta strandi173 – 175Combined sources3

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[»]
ProteinModelPortaliP62913.
SMRiP62913.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0397. Eukaryota.
COG0094. LUCA.
GeneTreeiENSGT00390000013411.
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_domain.
IPR031310. Ribosomal_L5_N.
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

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

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.
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. [P62913-1]
GeneIDi6135.
KEGGihsa:6135.

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

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: July 5, 2017
This is version 138 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. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families