Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P62913 (RL11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L11
Alternative name(s):
CLL-associated antigen KW-12
Gene names
Name:RPL11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.9

Subunit structure

Interacts with PML and MDM2 By similarity.

Subcellular location

Nucleusnucleolus By similarity.

Involvement in disease

Diamond-Blackfan anemia 7 (DBA7) [MIM:612562]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.16

Sequence similarities

Belongs to the ribosomal protein L5P family.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDiamond-Blackfan anemia
Disease mutation
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

protein localization to nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein targeting

Inferred from mutant phenotype PubMed 15195100. Source: UniProtKB

rRNA processing

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

ribosomal large subunit biogenesis

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

translation

Non-traceable author statement Ref.8. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay Ref.8. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleolus

Inferred from direct assay PubMed 15195100. Source: UniProtKB

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

rRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of ribosome

Non-traceable author statement Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P62913-1)

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.
Isoform 2 (identifier: P62913-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 17817760S ribosomal protein L11
PRO_0000125082

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.8 Ref.13 Ref.14
Modified residue441Phosphothreonine Ref.10
Modified residue521N6-acetyllysine Ref.11
Modified residue851N6-acetyllysine Ref.11

Natural variations

Alternative sequence31Missing in isoform 2.
VSP_008320
Natural variant201L → H in DBA7. Ref.16
VAR_055448
Natural variant1611Missing in DBA7. Ref.9
VAR_055449

Experimental info

Sequence conflict311D → G in CAA55816. Ref.1
Sequence conflict731T → A in CAA55816. Ref.1
Sequence conflict921Y → L in CAA55816. Ref.1
Sequence conflict1181K → E in CAA55816. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 26EC965C9239774E

FASTA17820,252
        10         20         30         40         50         60 
MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF SKARYTVRSF 

        70         80         90        100        110        120 
GIRRNEKIAV HCTVRGAKAE EILEKGLKVR EYELRKNNFS DTGNFGFGIQ EHIDLGIKYD 

       130        140        150        160        170 
PSIGIYGLDF YVVLGRPGFS IADKKRRTGC IGAKHRISKE EAMRWFQQKY DGIILPGK 

« Hide

Isoform 2 [UniParc] [UniParc].

Checksum: 534FC28B1D3CF195
Show »

FASTA17720,124

References

« Hide 'large scale' references
[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]"Ribosomal protein L5 and L11 mutations are associated with cleft palate and abnormal thumbs in Diamond-Blackfan anemia patients."
Gazda H.T., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.-F., Schneider H., Darras N., Hasman C., Sieff C.A., Newburger P.E., Ball S.E., Niewiadomska E., Matysiak M., Zaucha J.M., Glader B., Niemeyer C., Meerpohl J.J., Atsidaftos E. expand/collapse author list , Lipton J.M., Gleizes P.-E., Beggs A.H.
Am. J. Hum. Genet. 83:769-780(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
[16]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS45049.
RefSeqNP_000966.2. NM_000975.3.
NP_001186731.1. NM_001199802.1.
UniGeneHs.719951.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00J1-178[»]
ProteinModelPortalP62913.
SMRP62913. Positions 9-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112055. 150 interactions.
IntActP62913. 31 interactions.
MINTMINT-1140097.
STRING9606.ENSP00000363676.

PTM databases

PhosphoSiteP62913.

Polymorphism databases

DMDM51702795.

2D gel databases

SWISS-2DPAGEP62913.

Proteomic databases

PaxDbP62913.
PRIDEP62913.

Protocols and materials databases

DNASU6135.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374550; ENSP00000363676; ENSG00000142676. [P62913-1]
GeneID6135.
KEGGhsa:6135.
UCSCuc001bhk.3. human.
uc001bhl.3. human. [P62913-2]

Organism-specific databases

CTD6135.
GeneCardsGC01P024018.
HGNCHGNC:10301. RPL11.
HPAHPA002734.
MIM604175. gene.
612562. phenotype.
neXtProtNX_P62913.
Orphanet124. Blackfan-Diamond anemia.
PharmGKBPA34664.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0094.
HOGENOMHOG000231312.
HOVERGENHBG055214.
InParanoidP62913.
KOK02868.
OMAEDTMAWF.
OrthoDBEOG7ZPNMB.
PhylomeDBP62913.
TreeFamTF300017.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP62913.
BgeeP62913.
CleanExHS_RPL11.
GenevestigatorP62913.

Family and domain databases

Gene3D3.30.1440.10. 1 hit.
InterProIPR002132. Ribosomal_L5.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERPTHR11994. PTHR11994. 1 hit.
PfamPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMSSF55282. SSF55282. 1 hit.
PROSITEPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL11. human.
GeneWikiRPL11.
GenomeRNAi6135.
NextBio23831.
PMAP-CutDBP62913.
PROP62913.
SOURCESearch...

Entry information

Entry nameRL11_HUMAN
AccessionPrimary (citable) accession number: P62913
Secondary accession number(s): P25121 expand/collapse secondary AC list , P39026, Q8TDH2, Q9Y674
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM