Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

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).By similarity1 Publication

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • protein localization to nucleus Source: UniProtKB
  • protein targeting Source: UniProtKB
  • ribosomal large subunit assembly Source: GO_Central
  • ribosomal large subunit biogenesis Source: UniProtKB
  • rRNA processing Source: UniProtKB
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • translation Source: UniProtKB
  • translational initiation Source: Reactome
  • viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000142676-MONOMER.
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
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
Complete GO annotation...

Keywords - Cellular componenti

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.

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-2DPAGEP62913.

PTM databases

iPTMnetiP62913.
PhosphoSitePlusiP62913.
SwissPalmiP62913.

Miscellaneous databases

PMAP-CutDBP62913.

Expressioni

Gene expression databases

BgeeiENSG00000142676.
CleanExiHS_RPL11.
ExpressionAtlasiP62913. baseline and differential.
GenevisibleiP62913. HS.

Organism-specific databases

HPAiHPA002734.

Interactioni

Subunit structurei

Interacts with PML and MDM2.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CAMK2BQ135543EBI-354380,EBI-1058722
KRT40Q6A1623EBI-354380,EBI-10171697
KRTAP10-7P604093EBI-354380,EBI-10172290
MDM2Q0098711EBI-354380,EBI-389668
MYCP011063EBI-354380,EBI-447544
NEDD8Q158434EBI-354380,EBI-716247

Protein-protein interaction databases

BioGridi112055. 187 interactors.
IntActiP62913. 53 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[»]
ProteinModelPortaliP62913.
SMRiP62913.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L5P family.Curated

Phylogenomic databases

eggNOGiKOG0397. Eukaryota.
COG0094. LUCA.
GeneTreeiENSGT00390000013411.
HOGENOMiHOG000231312.
HOVERGENiHBG055214.
InParanoidiP62913.
KOiK02868.
OMAiEHTEFPS.
OrthoDBiEOG091G0LSV.
PhylomeDBiP62913.
TreeFamiTF300017.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
[Graphical view]
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]

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

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

Protein-protein interaction databases

BioGridi112055. 187 interactors.
IntActiP62913. 53 interactors.
MINTiMINT-1140097.
STRINGi9606.ENSP00000363676.

PTM databases

iPTMnetiP62913.
PhosphoSitePlusiP62913.
SwissPalmiP62913.

Polymorphism and mutation databases

BioMutaiRPL11.
DMDMi51702795.

2D gel databases

SWISS-2DPAGEP62913.

Proteomic databases

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

Protocols and materials databases

DNASUi6135.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374550; ENSP00000363676; ENSG00000142676. [P62913-1]
GeneIDi6135.
KEGGihsa:6135.

Organism-specific databases

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

Phylogenomic databases

eggNOGiKOG0397. Eukaryota.
COG0094. LUCA.
GeneTreeiENSGT00390000013411.
HOGENOMiHOG000231312.
HOVERGENiHBG055214.
InParanoidiP62913.
KOiK02868.
OMAiEHTEFPS.
OrthoDBiEOG091G0LSV.
PhylomeDBiP62913.
TreeFamiTF300017.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000142676-MONOMER.
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.

Miscellaneous databases

ChiTaRSiRPL11. human.
GeneWikiiRPL11.
GenomeRNAii6135.
PMAP-CutDBP62913.
PROiP62913.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000142676.
CleanExiHS_RPL11.
ExpressionAtlasiP62913. baseline and differential.
GenevisibleiP62913. HS.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
[Graphical view]
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL11_HUMAN
AccessioniPrimary (citable) accession number: P62913
Secondary accession number(s): P25121
, P39026, Q8TDH2, Q9Y674
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 131 of the entry and version 2 of the sequence. [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

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.