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Protein

40S ribosomal protein S26

Gene

RPS26

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

Functioni

GO - Molecular functioni

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

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 S26
Gene namesi
Name:RPS26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:10414. RPS26.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Diamond-Blackfan anemia 10 (DBA10)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies.

See also OMIM:613309
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331D → N in DBA10. 1 Publication
VAR_063580
Natural varianti115 – 1151M → T in DBA10. 1 Publication
VAR_063581

Keywords - Diseasei

Diamond-Blackfan anemia, Disease mutation

Organism-specific databases

MIMi613309. phenotype.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34818.

Polymorphism and mutation databases

BioMutaiRPS26.
DMDMi51338650.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11511440S ribosomal protein S26PRO_0000204509Add
BLAST

Proteomic databases

MaxQBiP62854.
PaxDbiP62854.
PRIDEiP62854.

PTM databases

PhosphoSiteiP62854.

Expressioni

Gene expression databases

BgeeiP62854.
CleanExiHS_RPS26.
ExpressionAtlasiP62854. baseline.
GenevisibleiP62854. HS.

Organism-specific databases

HPAiHPA043961.
HPA055803.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TSR2Q969E88EBI-353438,EBI-746981

Protein-protein interaction databases

BioGridi112145. 119 interactions.
IntActiP62854. 16 interactions.
MINTiMINT-4824850.
STRINGi9606.ENSP00000348849.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Aa1-115[»]
5AJ0electron microscopy3.50Ba1-115[»]
ProteinModelPortaliP62854.
SMRiP62854. Positions 2-97.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S26e family.Curated

Phylogenomic databases

eggNOGiCOG4830.
GeneTreeiENSGT00390000002517.
HOGENOMiHOG000108824.
HOVERGENiHBG079147.
InParanoidiP62854.
KOiK02976.
OMAiCSRCVGK.
OrthoDBiEOG7B31Q7.
PhylomeDBiP62854.
TreeFamiTF300234.

Family and domain databases

InterProiIPR000892. Ribosomal_S26e.
[Graphical view]
PANTHERiPTHR12538. PTHR12538. 1 hit.
PfamiPF01283. Ribosomal_S26e. 1 hit.
[Graphical view]
PROSITEiPS00733. RIBOSOMAL_S26E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62854-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKKRRNNGR AKKGRGHVQP IRCTNCARCV PKDKAIKKFV IRNIVEAAAV
60 70 80 90 100
RDISEASVFD AYVLPKLYVK LHYCVSCAIH SKVVRNRSRE ARKDRTPPPR
110
FRPAGAAPRP PPKPM
Length:115
Mass (Da):13,015
Last modified:January 23, 2007 - v3
Checksum:iF60DF98F8900D968
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781A → V in CAA54808 (PubMed:7945460).Curated
Sequence conflicti109 – 1091R → A in CAA49345 (PubMed:8464749).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331D → N in DBA10. 1 Publication
VAR_063580
Natural varianti115 – 1151M → T in DBA10. 1 Publication
VAR_063581

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69654 mRNA. Translation: CAA49345.1.
X77770 mRNA. Translation: CAA54808.1.
X79236 Genomic DNA. Translation: CAA55818.1.
U41448 Genomic DNA. Translation: AAC26987.1.
BC002604 mRNA. Translation: AAH02604.1.
BC015832 mRNA. Translation: AAH15832.1.
BC070220 mRNA. Translation: AAH70220.1.
BC105276 mRNA. Translation: AAI05277.1.
BC105798 mRNA. Translation: AAI05799.1.
CCDSiCCDS31832.1.
PIRiS55545.
T50824.
RefSeqiNP_001020.2. NM_001029.3.
XP_005276741.1. XM_005276684.2.
UniGeneiHs.447562.
Hs.567235.
Hs.711461.

Genome annotation databases

EnsembliENST00000356464; ENSP00000348849; ENSG00000197728.
ENST00000552361; ENSP00000450339; ENSG00000197728.
GeneIDi101929876.
6231.
KEGGihsa:101929876.
hsa:6231.
UCSCiuc001sjf.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69654 mRNA. Translation: CAA49345.1.
X77770 mRNA. Translation: CAA54808.1.
X79236 Genomic DNA. Translation: CAA55818.1.
U41448 Genomic DNA. Translation: AAC26987.1.
BC002604 mRNA. Translation: AAH02604.1.
BC015832 mRNA. Translation: AAH15832.1.
BC070220 mRNA. Translation: AAH70220.1.
BC105276 mRNA. Translation: AAI05277.1.
BC105798 mRNA. Translation: AAI05799.1.
CCDSiCCDS31832.1.
PIRiS55545.
T50824.
RefSeqiNP_001020.2. NM_001029.3.
XP_005276741.1. XM_005276684.2.
UniGeneiHs.447562.
Hs.567235.
Hs.711461.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Aa1-115[»]
5AJ0electron microscopy3.50Ba1-115[»]
ProteinModelPortaliP62854.
SMRiP62854. Positions 2-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112145. 119 interactions.
IntActiP62854. 16 interactions.
MINTiMINT-4824850.
STRINGi9606.ENSP00000348849.

PTM databases

PhosphoSiteiP62854.

Polymorphism and mutation databases

BioMutaiRPS26.
DMDMi51338650.

Proteomic databases

MaxQBiP62854.
PaxDbiP62854.
PRIDEiP62854.

Protocols and materials databases

DNASUi6231.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356464; ENSP00000348849; ENSG00000197728.
ENST00000552361; ENSP00000450339; ENSG00000197728.
GeneIDi101929876.
6231.
KEGGihsa:101929876.
hsa:6231.
UCSCiuc001sjf.3. human.

Organism-specific databases

CTDi6231.
GeneCardsiGC12P056438.
GeneReviewsiRPS26.
H-InvDBHIX0161895.
HGNCiHGNC:10414. RPS26.
HPAiHPA043961.
HPA055803.
MIMi603701. gene.
613309. phenotype.
neXtProtiNX_P62854.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34818.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4830.
GeneTreeiENSGT00390000002517.
HOGENOMiHOG000108824.
HOVERGENiHBG079147.
InParanoidiP62854.
KOiK02976.
OMAiCSRCVGK.
OrthoDBiEOG7B31Q7.
PhylomeDBiP62854.
TreeFamiTF300234.

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

GeneWikiiRPS26.
NextBioi24189.
PROiP62854.
SOURCEiSearch...

Gene expression databases

BgeeiP62854.
CleanExiHS_RPS26.
ExpressionAtlasiP62854. baseline.
GenevisibleiP62854. HS.

Family and domain databases

InterProiIPR000892. Ribosomal_S26e.
[Graphical view]
PANTHERiPTHR12538. PTHR12538. 1 hit.
PfamiPF01283. Ribosomal_S26e. 1 hit.
[Graphical view]
PROSITEiPS00733. RIBOSOMAL_S26E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "S26 ribosomal protein RNA: an invariant control for gene regulation experiments in eucaryotic cells and tissues."
    Vincent S., Marty L., Fort P.
    Nucleic Acids Res. 21:1498-1498(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning cDNA of human S26 ribosomal protein and determination of its primary structure."
    Filipenko M.L., Vladimirov S.N., Muravlev A.I., Karpova G.G., Mertvetsov N.P.
    Bioorg. Khim. 20:644-649(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  3. "Isolation, structural analysis and mapping of the functional gene of human ribosomal protein S26."
    Filipenko M.L., Vinichenko N.A., Karpova G.G., Mertvetsov N.P., Amaldi F.
    Gene 211:287-292(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  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: Brain, Lymph and Prostate.
  5. "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 2-11.
  6. "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: 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).
  10. Cited for: VARIANTS DBA10 ASN-33 AND THR-115.

Entry informationi

Entry nameiRS26_HUMAN
AccessioniPrimary (citable) accession number: P62854
Secondary accession number(s): P02383
, P70394, Q06722, Q3MHD8, Q6IRY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 114 of the entry and version 3 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. 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.