40S ribosomal protein S2

The RPS2 gene is the gene which, in humans, encodes the 40S ribosomal protein S2.[5][6]

RPS2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRPS2, LLREP3, S2, ribosomal protein S2
External IDsOMIM: 603624 MGI: 105110 HomoloGene: 37714 GeneCards: RPS2
Gene location (Human)
Chr.Chromosome 16 (human)[1]
Band16p13.3Start1,962,058 bp[1]
End1,964,841 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

6187

16898

Ensembl

ENSG00000140988

ENSMUSG00000044533

UniProt

P15880

P25444

RefSeq (mRNA)

NM_002952

NM_008503

RefSeq (protein)

NP_002943

NP_032529

Location (UCSC)Chr 16: 1.96 – 1.96 MbChr 17: 24.72 – 24.72 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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 S5P family of ribosomal proteins. It is located in the cytoplasm. This gene shares sequence similarity with mouse LLRep3. It is co-transcribed with the small nucleolar RNA gene U64, which is located in its third intron. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[6]

Interactions

RPS2 has been shown to interact with PRMT3.[7]

gollark: > “This stuff is funny!” giggles your niece, squishing her fingers in the goop. “It’s all warm, gluey, and bouncy! Someone should be turning out this stuff for kids to play with, or as sticky putty to stick posters to walls, or whatever. You’ve got, like, an infinite supply of it, so that’s good economics, right?”
gollark: > “No! ElGr cells are a scientific miracle!” cries biologist Jack Ponta, jiggling a beaker full of purplish goop as he waves his arms in exasperation. “These cells have been a breakthrough; not only in testing cures for cancer, but also in understanding how cancer develops and functions! All these years later, these cells keep chugging along, outliving all the others! Who knows, with these cells, we might even one day unlock a path to immortality! Are you going to let bureaucracy get in the way of SCIENCE?”
gollark: > “We thought my poor grandmother’s remains had been buried in accordance with her wishes,” growls Elizabeth’s direct descendant, Catherine Gratwick. “Can’t you let her rest in peace? This is her body that you’re messing with. You can’t just irradiate and poison her; you must ask me first! How would you like it if your family’s remains were exhumed and mutilated? You must never use cells from deceased people without the explicit pre-mortem consent of the patient or their relatives. As for granny - I insist that all remaining samples of her be buried, and that you financially compensate her family for the pain and grief you have caused!”
gollark: > Two generations ago, scientists took a biopsy of a tumor from a cancer patient named Elizabeth Gratwick, who died soon after. Without her knowledge or consent, these cells were preserved in the laboratory and proved to be exceptionally stable in replication. As stable cancer cell lines are highly useful for medical research, “ElGr cells” have been sent to and used by scientists all over the world. However, objections are now being raised by Elizabeth’s descendants.
gollark: Now I need to answer a question!

References

  1. GRCh38: Ensembl release 89: ENSG00000140988 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000044533 - 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. 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.
  6. "Entrez Gene: RPS2 ribosomal protein S2".
  7. Choi, Seeyoung; Jung Cho-Rok; Kim Jin-Young; Im Dong-Soo (Sep 2008). "PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex". Biochim. Biophys. Acta. 1780 (9): 1062–9. doi:10.1016/j.bbagen.2008.05.010. ISSN 0006-3002. PMID 18573314.

Further reading

  • Overview of all the structural information available in the PDB for UniProt: P15880 (40S ribosomal protein S2) at the PDBe-KB.
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