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P61353 (RL27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L27
Gene names
Name:RPL27
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L27e family.

Contains 1 KOW domain.

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
   Technical term3D-structure
Complete proteome
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

translation

Non-traceable author statement PubMed 12962325. 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 PubMed 12962325. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

ribonucleoprotein complex

Inferred from direct assay PubMed 18809582. Source: MGI

ribosome

Traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

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

structural constituent of ribosome

Non-traceable author statement PubMed 12962325. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13613660S ribosomal protein L27
PRO_0000126077

Regions

Domain5 – 4036KOW

Amino acid modifications

Modified residue271N6-acetyllysine Ref.5
Modified residue931N6-acetyllysine Ref.5

Sequences

Sequence LengthMass (Da)Tools
P61353 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 73F4151495029A32

FASTA13615,798
        10         20         30         40         50         60 
MGKFMKPGKV VLVLAGRYSG RKAVIVKNID DGTSDRPYSH ALVAGIDRYP RKVTAAMGKK 

        70         80         90        100        110        120 
KIAKRSKIKS FVKVYNYNHL MPTRYSVDIP LDKTVVNKDV FRDPALKRKA RREAKVKFEE 

       130 
RYKTGKNKWF FQKLRF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of a full length cDNA encoding ribosomal protein L27 from human fetal kidney."
Gallagher R.A., McClean P.M., Malik A.N.
Biochim. Biophys. Acta 1217:329-332(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Bhat K.S.
Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Tissue: Blood, Brain, Eye and Skin.
[5]"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-27 AND LYS-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"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].
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19527 mRNA. Translation: AAA19815.1.
AB061851 Genomic DNA. Translation: BAB79492.1.
L05094 mRNA. Translation: AAC15857.1.
BC001700 mRNA. Translation: AAH01700.1.
BC002588 mRNA. Translation: AAH02588.1.
BC007273 mRNA. Translation: AAH07273.1.
BC010026 mRNA. Translation: AAH10026.1.
BC098560 mRNA. Translation: AAH98560.1.
PIRS43505.
RefSeqNP_000979.1. NM_000988.3.
UniGeneHs.514196.
Hs.660076.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00Z1-136[»]
ProteinModelPortalP61353.
SMRP61353. Positions 2-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112074. 71 interactions.
IntActP61353. 14 interactions.
MINTMINT-1145695.
STRING9606.ENSP00000253788.

PTM databases

PhosphoSiteP61353.

Polymorphism databases

DMDM47117772.

2D gel databases

SWISS-2DPAGEP61353.

Proteomic databases

PaxDbP61353.
PRIDEP61353.

Protocols and materials databases

DNASU6155.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253788; ENSP00000253788; ENSG00000131469.
ENST00000589037; ENSP00000467587; ENSG00000131469.
ENST00000589913; ENSP00000464813; ENSG00000131469.
GeneID6155.
KEGGhsa:6155.
UCSCuc002icj.3. human.

Organism-specific databases

CTD6155.
GeneCardsGC17P041150.
HGNCHGNC:10328. RPL27.
HPAHPA002649.
MIM607526. gene.
neXtProtNX_P61353.
PharmGKBPA34707.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2163.
HOGENOMHOG000210138.
HOVERGENHBG050005.
InParanoidP61353.
KOK02901.
OMAKIYKPGK.
OrthoDBEOG7J181Z.
PhylomeDBP61353.

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

BgeeP61353.
CleanExHS_RPL27.
GenevestigatorP61353.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
InterProIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR001141. Ribosomal_L27e.
IPR018262. Ribosomal_L27e_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERPTHR10497. PTHR10497. 1 hit.
PfamPF00467. KOW. 1 hit.
PF01777. Ribosomal_L27e. 1 hit.
[Graphical view]
ProDomPD009396. Ribosomal_L27e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMSSF50104. SSF50104. 1 hit.
PROSITEPS01107. RIBOSOMAL_L27E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL27. human.
GeneWikiRPL27.
GenomeRNAi6155.
NextBio23903.
PROP61353.
SOURCESearch...

Entry information

Entry nameRL27_HUMAN
AccessionPrimary (citable) accession number: P61353
Secondary accession number(s): P08526, Q4G0A9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
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 chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM