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P62841 (RS15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S15
Alternative name(s):
RIG protein
Gene names
Name:RPS15
Synonyms:RIG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length145 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein S19P family.

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
   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 small subunit assembly

Inferred from electronic annotation. Source: Ensembl

ribosomal small subunit biogenesis

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

ribosomal small subunit export from nucleus

Inferred from mutant phenotype PubMed 16037817. Source: UniProtKB

translation

Inferred by curator PubMed 15883184Ref.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_componentcytosol

Traceable author statement. Source: Reactome

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.6. Source: UniProtKB

nucleoplasm

Non-traceable author statement PubMed 16037817. Source: UniProtKB

nucleus

Non-traceable author statement Ref.2Ref.1. Source: UniProtKB

   Molecular_functionDNA binding

Non-traceable author statement Ref.2Ref.1. Source: UniProtKB

poly(A) RNA binding

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

structural constituent of ribosome

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UPF2Q9HAU51EBI-372635,EBI-372073

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 14514440S ribosomal protein S15 HAMAP-Rule MF_00531
PRO_0000130027

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.9

Sequences

Sequence LengthMass (Da)Tools
P62841 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CA2C682302C7B387

FASTA14517,040
        10         20         30         40         50         60 
MAEVEQKKKR TFRKFTYRGV DLDQLLDMSY EQLMQLYSAR QRRRLNRGLR RKQHSLLKRL 

        70         80         90        100        110        120 
RKAKKEAPPM EKPEVVKTHL RDMIILPEMV GSMVGVYNGK TFNQVEIKPE MIGHYLGEFS 

       130        140 
ITYKPVKHGR PGIGATHSSR FIPLK 

« Hide

References

« Hide 'large scale' references
[1]"Evolutionary conservation of the insulinoma gene rig and its possible function."
Inoue C., Shiga K., Takasawa S., Kitagawa M., Yamamoto H., Okamoto H.
Proc. Natl. Acad. Sci. U.S.A. 84:6659-6662(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and characterization of the human homologue of rig and its pseudogenes: the functional gene has features characteristic of housekeeping genes."
Shiga K., Yamamoto H., Okamoto H.
Proc. Natl. Acad. Sci. U.S.A. 87:3594-3598(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning and characterization of human insulinoma protein."
Yu L., Zhao S.Y.
Submitted (APR-1999) 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: Pancreas.
[5]"Progressive spastic myelopathy in a patient co-infected with HIV-1 and HTLV-II: autoantibodies to the human homologue of rig in blood and cerebrospinal fluid."
Rosenblatt J.D., Tomkins P., Rosenthal M., Kacena A., Chan G., Valderama R., Harrington W. Jr., Saxton E., Diagne A., Zhao J.-Q., Mitsuyasu R.T., Weisbart R.H.
AIDS 6:1151-1158(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-145.
Tissue: Brain.
[6]"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 101-116.
Tissue: Placenta.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"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].
[9]"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].
[10]"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
J02984 mRNA. Translation: AAA36036.1.
M32405 Genomic DNA. Translation: AAA36568.1.
AF145025 mRNA. Translation: AAP97277.1.
BC064908 mRNA. Translation: AAH64908.1.
BC105810 mRNA. Translation: AAI05811.1.
BC141832 mRNA. Translation: AAI41833.1.
PIRR3HU15. A35908.
RefSeqNP_001009.1. NM_001018.3.
UniGeneHs.406683.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZKQelectron microscopy8.70s1-145[»]
3J3Aelectron microscopy5.00P1-145[»]
ProteinModelPortalP62841.
SMRP62841. Positions 4-130.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112123. 77 interactions.
IntActP62841. 9 interactions.
MINTMINT-5004408.
STRING9606.ENSP00000233609.

PTM databases

PhosphoSiteP62841.

Polymorphism databases

DMDM51338641.

Proteomic databases

PaxDbP62841.
PRIDEP62841.

Protocols and materials databases

DNASU6209.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000586686; ENSP00000467676; ENSG00000115268.
GeneID6209.
KEGGhsa:6209.
UCSCuc002lsp.1. human.

Organism-specific databases

CTD6209.
GeneCardsGC19P001438.
HGNCHGNC:10388. RPS15.
HPAHPA054510.
HPA057793.
MIM180535. gene.
neXtProtNX_P62841.
PharmGKBPA34787.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0185.
HOGENOMHOG000111561.
HOVERGENHBG000709.
InParanoidP62841.
KOK02958.
OrthoDBEOG780RPS.
PhylomeDBP62841.

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

BgeeP62841.
CleanExHS_RPS15.
GenevestigatorP62841.

Family and domain databases

Gene3D3.30.860.10. 1 hit.
HAMAPMF_00531. Ribosomal_S19.
InterProIPR002222. Ribosomal_S19.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
IPR005713. Ribosomal_S19A/S15e.
[Graphical view]
PANTHERPTHR11880. PTHR11880. 1 hit.
PfamPF00203. Ribosomal_S19. 1 hit.
[Graphical view]
PIRSFPIRSF002144. Ribosomal_S19. 1 hit.
PRINTSPR00975. RIBOSOMALS19.
SUPFAMSSF54570. SSF54570. 1 hit.
TIGRFAMsTIGR01025. rpsS_arch. 1 hit.
PROSITEPS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62841.
GeneWikiRPS15.
GenomeRNAi6209.
NextBio24119.
PMAP-CutDBP62841.
PROP62841.
SOURCESearch...

Entry information

Entry nameRS15_HUMAN
AccessionPrimary (citable) accession number: P62841
Secondary accession number(s): A5D8V9 expand/collapse secondary AC list , P11174, Q3KRA1, Q9UDC2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 106 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 19

Human chromosome 19: entries, gene names and cross-references to MIM