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Protein

60S ribosomal protein L27

Gene

RPL27

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. 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. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  5. translation Source: UniProtKB
  6. translational elongation Source: Reactome
  7. translational initiation Source: Reactome
  8. translational termination Source: Reactome
  9. viral life cycle Source: Reactome
  10. viral process Source: Reactome
  11. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

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 L27
Gene namesi
Name:RPL27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:10328. RPL27.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic large ribosomal subunit Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. membrane Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. ribonucleoprotein complex Source: MGI
  8. ribosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34707.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13613660S ribosomal protein L27PRO_0000126077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271N6-acetyllysine1 Publication
Modified residuei93 – 931N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP61353.
PaxDbiP61353.
PRIDEiP61353.

2D gel databases

SWISS-2DPAGEP61353.

PTM databases

PhosphoSiteiP61353.

Expressioni

Gene expression databases

BgeeiP61353.
CleanExiHS_RPL27.
ExpressionAtlasiP61353. baseline and differential.
GenevestigatoriP61353.

Organism-specific databases

HPAiHPA002649.

Interactioni

Protein-protein interaction databases

BioGridi112074. 72 interactions.
IntActiP61353. 14 interactions.
MINTiMINT-1145695.
STRINGi9606.ENSP00000253788.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CZ1-136[»]
ProteinModelPortaliP61353.
SMRiP61353. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 4036KOWAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein L27e family.Curated
Contains 1 KOW domain.Curated

Phylogenomic databases

eggNOGiCOG2163.
GeneTreeiENSGT00390000010721.
HOGENOMiHOG000210138.
HOVERGENiHBG050005.
InParanoidiP61353.
KOiK02901.
OMAiKIYKPGK.
OrthoDBiEOG7J181Z.
PhylomeDBiP61353.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR001141. Ribosomal_L27e.
IPR018262. Ribosomal_L27e_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR10497. PTHR10497. 1 hit.
PfamiPF00467. KOW. 1 hit.
PF01777. Ribosomal_L27e. 1 hit.
[Graphical view]
ProDomiPD009396. Ribosomal_L27e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
PROSITEiPS01107. RIBOSOMAL_L27E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P61353-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKFMKPGKV VLVLAGRYSG RKAVIVKNID DGTSDRPYSH ALVAGIDRYP
60 70 80 90 100
RKVTAAMGKK KIAKRSKIKS FVKVYNYNHL MPTRYSVDIP LDKTVVNKDV
110 120 130
FRDPALKRKA RREAKVKFEE RYKTGKNKWF FQKLRF
Length:136
Mass (Da):15,798
Last modified:January 23, 2007 - v2
Checksum:i73F4151495029A32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11449.1.
PIRiS43505.
RefSeqiNP_000979.1. NM_000988.3.
UniGeneiHs.514196.
Hs.660076.

Genome annotation databases

EnsembliENST00000253788; ENSP00000253788; ENSG00000131469.
ENST00000589037; ENSP00000467587; ENSG00000131469.
ENST00000589913; ENSP00000464813; ENSG00000131469.
GeneIDi6155.
KEGGihsa:6155.
UCSCiuc002icj.3. human.

Polymorphism databases

DMDMi47117772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11449.1.
PIRiS43505.
RefSeqiNP_000979.1. NM_000988.3.
UniGeneiHs.514196.
Hs.660076.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CZ1-136[»]
ProteinModelPortaliP61353.
SMRiP61353. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112074. 72 interactions.
IntActiP61353. 14 interactions.
MINTiMINT-1145695.
STRINGi9606.ENSP00000253788.

PTM databases

PhosphoSiteiP61353.

Polymorphism databases

DMDMi47117772.

2D gel databases

SWISS-2DPAGEP61353.

Proteomic databases

MaxQBiP61353.
PaxDbiP61353.
PRIDEiP61353.

Protocols and materials databases

DNASUi6155.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000253788; ENSP00000253788; ENSG00000131469.
ENST00000589037; ENSP00000467587; ENSG00000131469.
ENST00000589913; ENSP00000464813; ENSG00000131469.
GeneIDi6155.
KEGGihsa:6155.
UCSCiuc002icj.3. human.

Organism-specific databases

CTDi6155.
GeneCardsiGC17P041150.
HGNCiHGNC:10328. RPL27.
HPAiHPA002649.
MIMi607526. gene.
neXtProtiNX_P61353.
PharmGKBiPA34707.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2163.
GeneTreeiENSGT00390000010721.
HOGENOMiHOG000210138.
HOVERGENiHBG050005.
InParanoidiP61353.
KOiK02901.
OMAiKIYKPGK.
OrthoDBiEOG7J181Z.
PhylomeDBiP61353.

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

ChiTaRSiRPL27. human.
GeneWikiiRPL27.
GenomeRNAii6155.
NextBioi23903.
PROiP61353.
SOURCEiSearch...

Gene expression databases

BgeeiP61353.
CleanExiHS_RPL27.
ExpressionAtlasiP61353. baseline and differential.
GenevestigatoriP61353.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR001141. Ribosomal_L27e.
IPR018262. Ribosomal_L27e_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR10497. PTHR10497. 1 hit.
PfamiPF00467. KOW. 1 hit.
PF01777. Ribosomal_L27e. 1 hit.
[Graphical view]
ProDomiPD009396. Ribosomal_L27e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
PROSITEiPS01107. RIBOSOMAL_L27E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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.
  9. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL27_HUMAN
AccessioniPrimary (citable) accession number: P61353
Secondary accession number(s): P08526, Q4G0A9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
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, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. 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.