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Protein

40S ribosomal protein S15a

Gene

RPS15A

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

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
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_1979. Translation initiation complex formation.
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_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S15a
Gene namesi
Name:RPS15A
ORF Names:OK/SW-cl.82
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:10389. RPS15A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • cytosolic small ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34788.

Polymorphism and mutation databases

BioMutaiRPS15A.
DMDMi50403624.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 13012940S ribosomal protein S15aPRO_0000126602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881N6-succinyllysineBy similarity

Proteomic databases

MaxQBiP62244.
PaxDbiP62244.
PeptideAtlasiP62244.
PRIDEiP62244.

2D gel databases

SWISS-2DPAGEP62244.

PTM databases

PhosphoSiteiP62244.

Miscellaneous databases

PMAP-CutDBP62244.

Expressioni

Gene expression databases

BgeeiP62244.
CleanExiHS_RPS15A.
ExpressionAtlasiP62244. baseline and differential.
GenevisibleiP62244. HS.

Organism-specific databases

HPAiHPA047103.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX39BQ138381EBI-347895,EBI-348622

Protein-protein interaction databases

BioGridi112124. 138 interactions.
IntActiP62244. 16 interactions.
MINTiMINT-1036414.
STRINGi9606.ENSP00000318646.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AW1-130[»]
5AJ0electron microscopy3.50BW1-130[»]
ProteinModelPortaliP62244.
SMRiP62244. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S8P family.Curated

Phylogenomic databases

eggNOGiCOG0096.
GeneTreeiENSGT00390000003021.
HOGENOMiHOG000204097.
HOVERGENiHBG056618.
InParanoidiP62244.
KOiK02957.
OMAiTHEVTPA.
OrthoDBiEOG77Q4ZM.
PhylomeDBiP62244.
TreeFamiTF300067.

Family and domain databases

HAMAPiMF_01302_A. Ribosomal_S8_A.
InterProiIPR000630. Ribosomal_S8.
[Graphical view]
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiPF00410. Ribosomal_S8. 1 hit.
[Graphical view]
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiPS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRMNVLADA LKSINNAEKR GKRQVLIRPC SKVIVRFLTV MMKHGYIGEF
60 70 80 90 100
EIIDDHRAGK IVVNLTGRLN KCGVISPRFD VQLKDLEKWQ NNLLPSRQFG
110 120 130
FIVLTTSAGI MDHEEARRKH TGGKILGFFF
Length:130
Mass (Da):14,840
Last modified:January 23, 2007 - v2
Checksum:iD4AC1E8864E3A184
GO

Sequence cautioni

The sequence CAA44568.1 differs from that shown. Reason: Frameshift at positions 24 and 37. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31R → C AA sequence (PubMed:8706699).Curated
Sequence conflicti40 – 401V → L in CAA59127 (Ref. 2) Curated
Sequence conflicti79 – 791F → S in AAH01697 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62691 mRNA. Translation: CAA44568.1. Frameshift.
X84407 mRNA. Translation: CAA59127.1.
AY208299 mRNA. Translation: AAO48936.1.
AB062400 mRNA. Translation: BAB93487.1.
BC001697 mRNA. Translation: AAH01697.1.
BC030569 mRNA. Translation: AAH30569.1.
BC046113 mRNA. Translation: AAH46113.1.
BC105273 mRNA. Translation: AAI05274.1.
BC105292 mRNA. Translation: AAI05293.1.
AB007154 Genomic DNA. Translation: BAA28592.1.
CCDSiCCDS10571.1.
PIRiS52339.
RefSeqiNP_001010.2. NM_001019.4.
NP_001025180.1. NM_001030009.1.
UniGeneiHs.370504.

Genome annotation databases

EnsembliENST00000322989; ENSP00000318646; ENSG00000134419.
ENST00000563390; ENSP00000457000; ENSG00000134419.
ENST00000565420; ENSP00000458115; ENSG00000134419.
ENST00000572008; ENSP00000458528; ENSG00000134419.
GeneIDi6210.
KEGGihsa:6210.
UCSCiuc002dfh.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62691 mRNA. Translation: CAA44568.1. Frameshift.
X84407 mRNA. Translation: CAA59127.1.
AY208299 mRNA. Translation: AAO48936.1.
AB062400 mRNA. Translation: BAB93487.1.
BC001697 mRNA. Translation: AAH01697.1.
BC030569 mRNA. Translation: AAH30569.1.
BC046113 mRNA. Translation: AAH46113.1.
BC105273 mRNA. Translation: AAI05274.1.
BC105292 mRNA. Translation: AAI05293.1.
AB007154 Genomic DNA. Translation: BAA28592.1.
CCDSiCCDS10571.1.
PIRiS52339.
RefSeqiNP_001010.2. NM_001019.4.
NP_001025180.1. NM_001030009.1.
UniGeneiHs.370504.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AW1-130[»]
5AJ0electron microscopy3.50BW1-130[»]
ProteinModelPortaliP62244.
SMRiP62244. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112124. 138 interactions.
IntActiP62244. 16 interactions.
MINTiMINT-1036414.
STRINGi9606.ENSP00000318646.

PTM databases

PhosphoSiteiP62244.

Polymorphism and mutation databases

BioMutaiRPS15A.
DMDMi50403624.

2D gel databases

SWISS-2DPAGEP62244.

Proteomic databases

MaxQBiP62244.
PaxDbiP62244.
PeptideAtlasiP62244.
PRIDEiP62244.

Protocols and materials databases

DNASUi6210.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322989; ENSP00000318646; ENSG00000134419.
ENST00000563390; ENSP00000457000; ENSG00000134419.
ENST00000565420; ENSP00000458115; ENSG00000134419.
ENST00000572008; ENSP00000458528; ENSG00000134419.
GeneIDi6210.
KEGGihsa:6210.
UCSCiuc002dfh.1. human.

Organism-specific databases

CTDi6210.
GeneCardsiGC16M018701.
H-InvDBHIX0033054.
HGNCiHGNC:10389. RPS15A.
HPAiHPA047103.
MIMi603674. gene.
neXtProtiNX_P62244.
PharmGKBiPA34788.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0096.
GeneTreeiENSGT00390000003021.
HOGENOMiHOG000204097.
HOVERGENiHBG056618.
InParanoidiP62244.
KOiK02957.
OMAiTHEVTPA.
OrthoDBiEOG77Q4ZM.
PhylomeDBiP62244.
TreeFamiTF300067.

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
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_1979. Translation initiation complex formation.
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_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiRPS15A. human.
GeneWikiiRPS15A.
GenomeRNAii6210.
NextBioi24123.
PMAP-CutDBP62244.
PROiP62244.
SOURCEiSearch...

Gene expression databases

BgeeiP62244.
CleanExiHS_RPS15A.
ExpressionAtlasiP62244. baseline and differential.
GenevisibleiP62244. HS.

Family and domain databases

HAMAPiMF_01302_A. Ribosomal_S8_A.
InterProiIPR000630. Ribosomal_S8.
[Graphical view]
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiPF00410. Ribosomal_S8. 1 hit.
[Graphical view]
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiPS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Schwabe G.
    Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Mays G., Burchert-Graeve M.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Carcinoma.
  3. "Human S15a expression is up-regulated by HBV X protein."
    Lian Z., Liu J., Li L., Li X., Tufan S.N.L., Wu M.-C., Wang H., Arbuthnot P., Kew M.K., Feitelson M.M.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon adenocarcinoma.
  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].
    Tissue: Eye, Lung and Skin.
  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 2-17 AND 33-60.
    Tissue: Placenta.
  7. "A map of 75 human ribosomal protein genes."
    Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
    Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-54.
  8. Cited for: PARTIAL PROTEIN SEQUENCE.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS15A_HUMAN
AccessioniPrimary (citable) accession number: P62244
Secondary accession number(s): P39027
, P39031, Q3MHD9, Q8C023, Q9BV24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 122 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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.