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P61353

- RL27_HUMAN

UniProt

P61353 - RL27_HUMAN

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Protein
60S ribosomal protein L27
Gene
RPL27
Organism
Homo sapiens (Human)
Status
Reviewed - 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. RNA metabolic process Source: Reactome
  2. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  3. cellular protein metabolic process Source: Reactome
  4. gene expression Source: Reactome
  5. mRNA metabolic process Source: Reactome
  6. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  7. translation Source: UniProtKB
  8. translational elongation Source: Reactome
  9. translational initiation Source: Reactome
  10. translational termination Source: Reactome
  11. viral life cycle Source: Reactome
  12. viral process Source: Reactome
  13. 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: UniProt
  4. nucleus Source: UniProt
  5. ribonucleoprotein complex Source: MGI
  6. 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 L27
PRO_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.
GenevestigatoriP61353.

Organism-specific databases

HPAiHPA002649.

Interactioni

Protein-protein interaction databases

BioGridi112074. 65 interactions.
IntActiP61353. 14 interactions.
MINTiMINT-1145695.
STRINGi9606.ENSP00000253788.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00Z1-136[»]
ProteinModelPortaliP61353.
SMRiP61353. Positions 2-136.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 KOW domain.

Phylogenomic databases

eggNOGiCOG2163.
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

MGKFMKPGKV VLVLAGRYSG RKAVIVKNID DGTSDRPYSH ALVAGIDRYP    50
RKVTAAMGKK KIAKRSKIKS FVKVYNYNHL MPTRYSVDIP LDKTVVNKDV 100
FRDPALKRKA RREAKVKFEE RYKTGKNKWF FQKLRF 136
Length:136
Mass (Da):15,798
Last modified:January 23, 2007 - v2
Checksum:i73F4151495029A32
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11449.1.
PIRi S43505.
RefSeqi NP_000979.1. NM_000988.3.
UniGenei Hs.514196.
Hs.660076.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3B electron microscopy 5.00 Z 1-136 [» ]
ProteinModelPortali P61353.
SMRi P61353. Positions 2-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112074. 65 interactions.
IntActi P61353. 14 interactions.
MINTi MINT-1145695.
STRINGi 9606.ENSP00000253788.

PTM databases

PhosphoSitei P61353.

Polymorphism databases

DMDMi 47117772.

2D gel databases

SWISS-2DPAGE P61353.

Proteomic databases

MaxQBi P61353.
PaxDbi P61353.
PRIDEi P61353.

Protocols and materials databases

DNASUi 6155.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253788 ; ENSP00000253788 ; ENSG00000131469 .
ENST00000589037 ; ENSP00000467587 ; ENSG00000131469 .
ENST00000589913 ; ENSP00000464813 ; ENSG00000131469 .
GeneIDi 6155.
KEGGi hsa:6155.
UCSCi uc002icj.3. human.

Organism-specific databases

CTDi 6155.
GeneCardsi GC17P041150.
HGNCi HGNC:10328. RPL27.
HPAi HPA002649.
MIMi 607526. gene.
neXtProti NX_P61353.
PharmGKBi PA34707.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2163.
HOGENOMi HOG000210138.
HOVERGENi HBG050005.
InParanoidi P61353.
KOi K02901.
OMAi KIYKPGK.
OrthoDBi EOG7J181Z.
PhylomeDBi P61353.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi RPL27. human.
GeneWikii RPL27.
GenomeRNAii 6155.
NextBioi 23903.
PROi P61353.
SOURCEi Search...

Gene expression databases

Bgeei P61353.
CleanExi HS_RPL27.
Genevestigatori P61353.

Family and domain databases

Gene3Di 2.30.30.30. 1 hit.
InterProi IPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR001141. Ribosomal_L27e.
IPR018262. Ribosomal_L27e_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view ]
PANTHERi PTHR10497. PTHR10497. 1 hit.
Pfami PF00467. KOW. 1 hit.
PF01777. Ribosomal_L27e. 1 hit.
[Graphical view ]
ProDomi PD009396. Ribosomal_L27e. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00739. KOW. 1 hit.
[Graphical view ]
SUPFAMi SSF50104. SSF50104. 1 hit.
PROSITEi PS01107. RIBOSOMAL_L27E. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. 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: September 3, 2014
This is version 106 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

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