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P46777 (RL5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L5
Gene names
Name:RPL5
ORF Names:MSTP030
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for rRNA maturation and formation of the 60S ribosomal subunits. This protein binds 5S RNA. Ref.10

Subcellular location

Cytoplasm. Nucleusnucleolus Ref.7.

Involvement in disease

Diamond-Blackfan anemia 6 (DBA6) [MIM:612561]: 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.10 Ref.16

Sequence similarities

Belongs to the ribosomal protein L18P family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   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

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.6. 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_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay Ref.6. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 9687515. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay PubMed 18809582. Source: MGI

   Molecular_function5S rRNA binding

Inferred from electronic annotation. Source: InterPro

RNA binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12054647PubMed 16648475PubMed 9465063PubMed 9687515. Source: UniProtKB

structural constituent of ribosome

Non-traceable author statement Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DCCP431467EBI-358018,EBI-1222919
DccQ631554EBI-358018,EBI-1798965From a different organism.
MDM2Q009875EBI-358018,EBI-389668

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.14
Chain2 – 29729660S ribosomal protein L5 HAMAP-Rule MF_01337_A
PRO_0000131431

Amino acid modifications

Modified residue21N-acetylglycine Ref.14
Modified residue51N6-acetyllysine Ref.11
Modified residue481N6-acetyllysine Ref.11
Modified residue2201N6-acetyllysine By similarity
Modified residue2721Phosphoserine Ref.13

Natural variations

Natural variant1401G → S in DBA6. Ref.10
VAR_055450
Natural variant2101Y → C. Ref.5
Corresponds to variant rs11540832 [ dbSNP | Ensembl ].
VAR_052009
Natural variant2851A → V in DBA6. Ref.16
VAR_055451

Experimental info

Sequence conflict781A → R in AAA85654. Ref.1
Sequence conflict1761S → R Ref.9
Sequence conflict2641K → E in BAD96324. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P46777 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 07CA9FBA842BD2A3

FASTA29734,363
        10         20         30         40         50         60 
MGFVKVVKNK AYFKRYQVKF RRRREGKTDY YARKRLVIQD KNKYNTPKYR MIVRVTNRDI 

        70         80         90        100        110        120 
ICQIAYARIE GDMIVCAAYA HELPKYGVKV GLTNYAAAYC TGLLLARRLL NRFGMDKIYE 

       130        140        150        160        170        180 
GQVEVTGDEY NVESIDGQPG AFTCYLDAGL ARTTTGNKVF GALKGAVDGG LSIPHSTKRF 

       190        200        210        220        230        240 
PGYDSESKEF NAEVHRKHIM GQNVADYMRY LMEEDEDAYK KQFSQYIKNS VTPDMMEEMY 

       250        260        270        280        290 
KKAHAAIREN PVYEKKPKKE VKKKRWNRPK MSLAQKKDRV AQKKASFLRA QERAAES 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs."
Frigerio J.-M., Dagorn J.-C., Iovanna J.L.
Biochim. Biophys. Acta 1262:64-68(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Colon.
[2]Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., Liu L.S., Ding J.F. expand/collapse author list , Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Aorta.
[3]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Coronary arterial endothelium.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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], VARIANT CYS-210.
Tissue: Lung.
[6]"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: PROTEIN SEQUENCE OF 2-12, IDENTIFICATION BY MASS SPECTROMETRY.
[7]Bienvenut W.V.
Submitted (AUG-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 69-85; 159-188 AND 222-228, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"Interaction of the beta subunit of casein kinase II with the ribosomal protein L5."
Kim J.-M., Cha J.-Y., Marshak D.R., Bae Y.-S.
Biochem. Biophys. Res. Commun. 226:180-186(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 153-297.
[9]"U21, a novel small nucleolar RNA with a 13 nt. complementarity to 28S rRNA, is encoded in an intron of ribosomal protein L5 gene in chicken and mammals."
Qu L.H., Nicoloso M., Michot B., Azum M.C., Caizergues-Ferrer M., Renalier M.H., Bachellerie J.-P.
Nucleic Acids Res. 22:4073-4081(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-176.
[10]"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 DBA6 SER-140.
[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-5 AND LYS-48, 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]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, 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 GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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 DBA6 VAL-285.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14966 mRNA. Translation: AAA85654.1.
AF113210 mRNA. Translation: AAG39281.1.
AK222604 mRNA. Translation: BAD96324.1.
AL162740 Genomic DNA. Translation: CAI22505.1.
BC109370 mRNA. Translation: AAI09371.1.
U76609 mRNA. Translation: AAB18361.1.
Z35312 Genomic DNA. No translation available.
CCDSCCDS741.1.
PIRS55912.
RefSeqNP_000960.2. NM_000969.3.
UniGeneHs.532359.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00D1-297[»]
ProteinModelPortalP46777.
SMRP46777. Positions 9-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112045. 164 interactions.
DIPDIP-31152N.
IntActP46777. 23 interactions.
MINTMINT-1034099.
STRING9606.ENSP00000359345.

PTM databases

PhosphoSiteP46777.

Polymorphism databases

DMDM81175191.

Proteomic databases

MaxQBP46777.
PaxDbP46777.
PRIDEP46777.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370321; ENSP00000359345; ENSG00000122406.
GeneID6125.
KEGGhsa:6125.
UCSCuc001doz.3. human.

Organism-specific databases

CTD6125.
GeneCardsGC01P093297.
GeneReviewsRPL5.
HGNCHGNC:10360. RPL5.
HPAHPA043717.
HPA054444.
MIM603634. gene.
612561. phenotype.
neXtProtNX_P46777.
Orphanet124. Blackfan-Diamond anemia.
PharmGKBPA34755.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0256.
HOVERGENHBG009347.
InParanoidP46777.
KOK02932.
OMAVICAAYS.
OrthoDBEOG7VB2FW.
PhylomeDBP46777.
TreeFamTF300044.

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

ArrayExpressP46777.
BgeeP46777.
CleanExHS_RPL5.
GenevestigatorP46777.

Family and domain databases

HAMAPMF_01337_A. Ribosomal_L18_A.
InterProIPR005485. Rbsml_L5_euk/L18_arc.
IPR025607. Rbsml_L5e/L18P_C.
IPR005484. Ribosomal_L18/L5.
[Graphical view]
PANTHERPTHR23410. PTHR23410. 1 hit.
PfamPF14204. Ribosomal_L18_c. 1 hit.
PF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
PRINTSPR00058. RIBOSOMALL5.
ProtoNetSearch...

Other

ChiTaRSRPL5. human.
GeneWikiRibosomal_protein_L5.
GenomeRNAi6125.
NextBio23791.
PROP46777.
SOURCESearch...

Entry information

Entry nameRL5_HUMAN
AccessionPrimary (citable) accession number: P46777
Secondary accession number(s): Q32LZ3, Q53HH6, Q9H3F4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 139 of the entry and version 3 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