40S ribosomal protein S9

Protein-coding gene in the species Homo sapiens
RPS9
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4UG0, 4V6X, 5A2Q, 5AJ0, 4KZY, 3J7R, 4D61, 4KZX, 4D5L, 5FLX, 4UJD, 3J7P, 4KZZ, 4UJE, 4UJC

Identifiers
AliasesRPS9, S9, ribosomal protein S9
External IDsOMIM: 603631; MGI: 1924096; HomoloGene: 68145; GeneCards: RPS9; OMA:RPS9 - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for RPS9
Genomic location for RPS9
Band19q13.42Start54,200,809 bp[1]
End54,249,003 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for RPS9
Genomic location for RPS9
Band7|7 A1Start3,706,992 bp[2]
End3,709,896 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • monocyte

  • left ovary

  • right ovary

  • right uterine tube

  • skin of abdomen

  • canal of the cervix

  • skin of leg

  • lymph node

  • appendix

  • gallbladder
Top expressed in
  • medial ganglionic eminence

  • ventricular zone

  • transitional epithelium of urinary bladder

  • efferent ductule

  • blastocyst

  • fetal liver hematopoietic progenitor cell

  • thymus

  • maxillary prominence

  • lip

  • mandibular prominence
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • rRNA binding
  • structural constituent of ribosome
  • translation regulator activity
  • protein binding
  • RNA binding
Cellular component
  • cytoplasm
  • cytosol
  • ribosome
  • membrane
  • focal adhesion
  • intracellular anatomical structure
  • nucleolus
  • small ribosomal subunit
  • extracellular exosome
  • nucleus
  • nucleoplasm
  • cytosolic small ribosomal subunit
  • synapse
  • ribonucleoprotein complex
Biological process
  • positive regulation of translational fidelity
  • viral transcription
  • SRP-dependent cotranslational protein targeting to membrane
  • positive regulation of cell population proliferation
  • translational initiation
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
  • protein biosynthesis
  • rRNA processing
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6203

76846

Ensembl
ENSG00000274646
ENSG00000277359
ENSG00000274950
ENSG00000274626
ENSG00000275323

ENSG00000278270
ENSG00000278081
ENSG00000274005
ENSG00000277079
ENSG00000170889

ENSMUSG00000006333

UniProt

P46781

Q6ZWN5

RefSeq (mRNA)
NM_001013
NM_001321701
NM_001321702
NM_001321704
NM_001321705

NM_001321706

NM_029767

RefSeq (protein)
NP_001004
NP_001308630
NP_001308631
NP_001308633
NP_001308634

NP_001308635

NP_084043

Location (UCSC)Chr 19: 54.2 – 54.25 MbChr 7: 3.71 – 3.71 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

40S ribosomal protein S9 is a protein that in humans is encoded by the RPS9 gene.[5][6][7]

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S4P family of ribosomal proteins. It is located in the cytoplasm. Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found. As is typical for genes encoding ribosomal proteins, multiple processed pseudogenes derived from this gene are dispersed through the genome.[7]

References

  1. ^ a b c ENSG00000277359, ENSG00000274950, ENSG00000274626, ENSG00000275323, ENSG00000278270, ENSG00000278081, ENSG00000274005, ENSG00000277079, ENSG00000170889 GRCh38: Ensembl release 89: ENSG00000274646, ENSG00000277359, ENSG00000274950, ENSG00000274626, ENSG00000275323, ENSG00000278270, ENSG00000278081, ENSG00000274005, ENSG00000277079, ENSG00000170889 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000006333 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Frigerio JM, Dagorn JC, Iovanna JL (Jul 1995). "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs". Biochim Biophys Acta. 1262 (1): 64–8. doi:10.1016/0167-4781(95)00045-i. PMID 7772601.
  6. ^ Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (Aug 1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
  7. ^ a b "Entrez Gene: RPS9 ribosomal protein S9".

Further reading

  • Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID 8722009.
  • Mundus DA, Bulygin KN, Yamkovoy VI, et al. (1993). "Structural arrangement of the codon-anticodon interaction area in human placenta ribosomes. Affinity labelling of the 40S subunits by derivatives of oligoribonucleotides containing the AUG codon". Biochim. Biophys. Acta. 1173 (3): 273–82. doi:10.1016/0167-4781(93)90124-v. PMID 8318536.
  • Vladimirov SN, Ivanov AV, Karpova GG, et al. (1996). "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry". Eur. J. Biochem. 239 (1): 144–9. doi:10.1111/j.1432-1033.1996.0144u.x. PMID 8706699.
  • Yu Z, Ford BN, Glickman BW (2000). "Identification of genes responsive to BPDE treatment in HeLa cells using cDNA expression assays". Environ. Mol. Mutagen. 36 (3): 201–5. doi:10.1002/1098-2280(2000)36:3<201::AID-EM3>3.0.CO;2-1. PMID 11044901. S2CID 19391792.
  • Bortoluzzi S, d'Alessi F, Romualdi C, Danieli GA (2002). "Differential expression of genes coding for ribosomal proteins in different human tissues". Bioinformatics. 17 (12): 1152–7. doi:10.1093/bioinformatics/17.12.1152. PMID 11751223.
  • Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
  • Yoshihama M, Uechi T, Asakawa S, et al. (2002). "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes". Genome Res. 12 (3): 379–90. doi:10.1101/gr.214202. PMC 155282. PMID 11875025.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Dubois T, Zemlickova E, Howell S, Aitken A (2003). "Centaurin-alpha 1 associates in vitro and in vivo with nucleolin". Biochem. Biophys. Res. Commun. 301 (2): 502–8. doi:10.1016/S0006-291X(02)03010-3. PMID 12565890.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
  • Yu Y, Ji H, Doudna JA, Leary JA (2005). "Mass spectrometric analysis of the human 40S ribosomal subunit: native and HCV IRES-bound complexes". Protein Sci. 14 (6): 1438–46. doi:10.1110/ps.041293005. PMC 2253395. PMID 15883184.
  • Tu LC, Yan X, Hood L, Lin B (2007). "Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells". Mol. Cell. Proteomics. 6 (4): 575–88. doi:10.1074/mcp.M600249-MCP200. PMID 17220478.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.


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  • t
  • e
Proteins
Initiation factor
Bacterial
Mitochondrial
Archaeal
  • aIF1
  • aIF2
  • aIF5
  • aIF6
Eukaryotic
eIF1
eIF2
eIF3
eIF4
eIF5
eIF6
Elongation factor
Bacterial/​Mitochondrial
Archaeal/​Eukaryotic
Release factor
Ribosomal Proteins
Cytoplasmic
60S subunit
40S subunit
Mitochondrial
39S subunit
28S subunit
Other concepts


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