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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

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 similarity

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. RNA binding Source: ProtInc
  3. rRNA binding Source: UniProtKB-KW
  4. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  4. protein localization to nucleus Source: UniProtKB
  5. protein targeting Source: UniProtKB
  6. ribosomal large subunit biogenesis Source: UniProtKB
  7. rRNA processing Source: UniProtKB
  8. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  9. translation Source: UniProtKB
  10. translational elongation Source: Reactome
  11. translational initiation Source: Reactome
  12. translational termination Source: Reactome
  13. viral life cycle Source: Reactome
  14. viral process Source: Reactome
  15. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10301. RPL11.

Subcellular locationi

Nucleusnucleolus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic large ribosomal subunit Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB
  5. nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Diamond-Blackfan anemia 72 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201L → H in DBA7. 1 Publication
VAR_055448
Natural varianti161 – 1611Missing in DBA7. 1 Publication
VAR_055449

Keywords - Diseasei

Diamond-Blackfan anemia, Disease mutation

Organism-specific databases

MIMi612562. phenotype.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34664.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 17817760S ribosomal protein L11PRO_0000125082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei44 – 441Phosphothreonine1 Publication
Modified residuei52 – 521N6-acetyllysine1 Publication
Modified residuei85 – 851N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62913.
PaxDbiP62913.
PRIDEiP62913.

2D gel databases

SWISS-2DPAGEP62913.

PTM databases

PhosphoSiteiP62913.

Miscellaneous databases

PMAP-CutDBP62913.

Expressioni

Gene expression databases

BgeeiP62913.
CleanExiHS_RPL11.
ExpressionAtlasiP62913. baseline and differential.
GenevestigatoriP62913.

Organism-specific databases

HPAiHPA002734.

Interactioni

Subunit structurei

Interacts with PML and MDM2.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM2Q0098711EBI-354380,EBI-389668
MYCP011063EBI-354380,EBI-447544
NEDD8Q158434EBI-354380,EBI-716247

Protein-protein interaction databases

BioGridi112055. 151 interactions.
IntActiP62913. 32 interactions.
MINTiMINT-1140097.
STRINGi9606.ENSP00000363676.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CJ1-178[»]
ProteinModelPortaliP62913.
SMRiP62913. Positions 9-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L5P family.Curated

Phylogenomic databases

eggNOGiCOG0094.
HOGENOMiHOG000231312.
HOVERGENiHBG055214.
InParanoidiP62913.
KOiK02868.
OMAiFGMDVAI.
OrthoDBiEOG7ZPNMB.
PhylomeDBiP62913.
TreeFamiTF300017.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERiPTHR11994. PTHR11994. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311D → G in CAA55816 (PubMed:7748210).Curated
Sequence conflicti73 – 731T → A in CAA55816 (PubMed:7748210).Curated
Sequence conflicti92 – 921Y → L in CAA55816 (PubMed:7748210).Curated
Sequence conflicti118 – 1181K → E in CAA55816 (PubMed:7748210).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201L → H in DBA7. 1 Publication
VAR_055448
Natural varianti161 – 1611Missing in DBA7. 1 Publication
VAR_055449

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3 – 31Missing in isoform 2. 1 PublicationVSP_008320

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.
UCSCiuc001bhk.3. human.
uc001bhl.3. human. [P62913-2]

Polymorphism databases

DMDMi51702795.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CJ1-178[»]
ProteinModelPortaliP62913.
SMRiP62913. Positions 9-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112055. 151 interactions.
IntActiP62913. 32 interactions.
MINTiMINT-1140097.
STRINGi9606.ENSP00000363676.

PTM databases

PhosphoSiteiP62913.

Polymorphism databases

DMDMi51702795.

2D gel databases

SWISS-2DPAGEP62913.

Proteomic databases

MaxQBiP62913.
PaxDbiP62913.
PRIDEiP62913.

Protocols and materials databases

DNASUi6135.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374550; ENSP00000363676; ENSG00000142676. [P62913-1]
GeneIDi6135.
KEGGihsa:6135.
UCSCiuc001bhk.3. human.
uc001bhl.3. human. [P62913-2]

Organism-specific databases

CTDi6135.
GeneCardsiGC01P024018.
GeneReviewsiRPL11.
HGNCiHGNC:10301. RPL11.
HPAiHPA002734.
MIMi604175. gene.
612562. phenotype.
neXtProtiNX_P62913.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34664.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0094.
HOGENOMiHOG000231312.
HOVERGENiHBG055214.
InParanoidiP62913.
KOiK02868.
OMAiFGMDVAI.
OrthoDBiEOG7ZPNMB.
PhylomeDBiP62913.
TreeFamiTF300017.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiRPL11. human.
GeneWikiiRPL11.
GenomeRNAii6135.
NextBioi23831.
PMAP-CutDBP62913.
PROiP62913.
SOURCEiSearch...

Gene expression databases

BgeeiP62913.
CleanExiHS_RPL11.
ExpressionAtlasiP62913. baseline and differential.
GenevestigatoriP62913.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERiPTHR11994. PTHR11994. 1 hit.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and determination of the primary structure of DNA complementary to the mRNA of human ribosomal protein L11."
    Mishin V.P., Filipenko M.L., Muravlev A.I., Karpova G.G., Mertvetsov N.P.
    Bioorg. Khim. 21:158-160(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Expressed sequence tags from a human cell line."
    Bhat K.S.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Structural and functional analysis of the human ribosomal protein L11 gene."
    Voronina E.N., Kolokol'tsova T.D., Nechaeva E.A., Filipenko M.L.
    Mol. Biol. (Mosk.) 37:425-435(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Tonsil.
  5. Quadroni M., Bienvenut W.V.
    Submitted (NOV-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 89-95; 119-145 AND 157-164, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  6. "Identification of novel tumor antigens in CLL by SEREX: assessment of their potential as targets for immunotherapeutic approaches."
    Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-178 (ISOFORM 1).
  7. "A map of 75 human ribosomal protein genes."
    Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
    Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-52.
  8. "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
  9. Cited for: FUNCTION, VARIANT DBA7 GLU-161 DEL.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
  17. "Identification of mutations in the ribosomal protein L5 (RPL5) and ribosomal protein L11 (RPL11) genes in Czech patients with Diamond-Blackfan anemia."
    Cmejla R., Cmejlova J., Handrkova H., Petrak J., Petrtylova K., Mihal V., Stary J., Cerna Z., Jabali Y., Pospisilova D.
    Hum. Mutat. 30:321-327(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DBA7 HIS-20.

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: March 4, 2015
This is version 111 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

External Data

Dasty 3

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 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.