RPS7

RPS7

Ribosomal protein S7, also known as RPS7, is a human gene.cite web | title = Entrez Gene: RPS7 ribosomal protein S7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6201| accessdate = ]

PBB_Summary
section_title =
summary_text = 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 S7E family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.cite web | title = Entrez Gene: RPS7 ribosomal protein S7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6201| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Wool IG, Chan YL, Glück A |title=Structure and evolution of mammalian ribosomal proteins. |journal=Biochem. Cell Biol. |volume=73 |issue= 11-12 |pages= 933–47 |year= 1996 |pmid= 8722009 |doi=
*cite journal | author=Mundus DA, Bulygin KN, Yamkovoy VI, "et al." |title=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. |journal=Biochim. Biophys. Acta |volume=1173 |issue= 3 |pages= 273–82 |year= 1993 |pmid= 8318536 |doi=
*cite journal | author=Annilo T, Laan M, Stahl J, Metspalu A |title=The human ribosomal protein S7-encoding gene: isolation, structure and localization in 2p25. |journal=Gene |volume=165 |issue= 2 |pages= 297–302 |year= 1996 |pmid= 8522193 |doi=
*cite journal | author=Vladimirov SN, Ivanov AV, Karpova GG, "et al." |title=Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry. |journal=Eur. J. Biochem. |volume=239 |issue= 1 |pages= 144–9 |year= 1996 |pmid= 8706699 |doi=
*cite journal | author=Kenmochi N, Kawaguchi T, Rozen S, "et al." |title=A map of 75 human ribosomal protein genes. |journal=Genome Res. |volume=8 |issue= 5 |pages= 509–23 |year= 1998 |pmid= 9582194 |doi=
*cite journal | author=Jäkel S, Görlich D |title=Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells. |journal=EMBO J. |volume=17 |issue= 15 |pages= 4491–502 |year= 1998 |pmid= 9687515 |doi= 10.1093/emboj/17.15.4491
*cite journal | author=Gorbea C, Taillandier D, Rechsteiner M |title=Mapping subunit contacts in the regulatory complex of the 26 S proteasome. S2 and S5b form a tetramer with ATPase subunits S4 and S7. |journal=J. Biol. Chem. |volume=275 |issue= 2 |pages= 875–82 |year= 2000 |pmid= 10625621 |doi=
*cite journal | author=Jäkel S, Mingot JM, Schwarzmaier P, "et al." |title=Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains. |journal=EMBO J. |volume=21 |issue= 3 |pages= 377–86 |year= 2002 |pmid= 11823430 |doi= 10.1093/emboj/21.3.377
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Yu Y, Ji H, Doudna JA, Leary JA |title=Mass spectrometric analysis of the human 40S ribosomal subunit: native and HCV IRES-bound complexes. |journal=Protein Sci. |volume=14 |issue= 6 |pages= 1438–46 |year= 2005 |pmid= 15883184 |doi= 10.1110/ps.041293005
*cite journal | author=Tompkins V, Hagen J, Zediak VP, Quelle DE |title=Identification of novel ARF binding proteins by two-hybrid screening. |journal=Cell Cycle |volume=5 |issue= 6 |pages= 641–6 |year= 2006 |pmid= 16582619 |doi=
*cite journal | author=Chen D, Zhang Z, Li M, "et al." |title=Ribosomal protein S7 as a novel modulator of p53-MDM2 interaction: binding to MDM2, stabilization of p53 protein, and activation of p53 function. |journal=Oncogene |volume=26 |issue= 35 |pages= 5029–37 |year= 2007 |pmid= 17310983 |doi= 10.1038/sj.onc.1210327

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем сделать НИР

Look at other dictionaries:

  • Translation (biology) — Diagram showing the translation of mRNA and the synthesis of proteins by a ribosome. In molecular biology and genetics, translation is the third stage of protein biosynthesis (part of the overall process of gene expression). In translation,… …   Wikipedia

  • Ribosomal RNA — (rRNA) is the central component of the ribosome, the protein manufacturing machinery of all living cells. The function of the rRNA is to provide a mechanism for decoding mRNA into amino acids and to interact with the tRNAs during translation by… …   Wikipedia

  • Start codon — The start codon is generally defined as the point, sequence, at which a ribosome begins to translate a sequence of RNA into amino acids. When an RNA transcript is read from the 5 carbon to the 3 carbon by the ribosome the start codon (AUG) is the …   Wikipedia

  • Diamond–Blackfan anemia — Classification and external resources ICD 10 D61.0 ICD 9 284.01 …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”