40S ribosomal protein S21

RPS21
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4UG0, 4V6X, 5A2Q, 5AJ0, 5FLX, 3J7R, 4D61, 4D5L, 4UJD, 3J7P, 4UJE, 4UJC
Identifiers
Aliases	RPS21 , HLDF, S21, ribosomal protein S21
External IDs	OMIM: 180477 MGI: 1913731 HomoloGene: 90915 GeneCards: RPS21
Gene location (Human) Chr. Chromosome 20 (human) [1] Band 20q13.33 Start 62,387,116 bp [1] End 62,388,520 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band n/a Start 180,257,377 bp [2] End 180,258,445 bp [2]
RNA expression pattern Bgee Top expressed in thyroid gland material anatomical entity ovary bone marrow endometrium appendix synovial membrane cerebral cortex nipple More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein N-terminus binding structural constituent of ribosome RNA binding Cellular component small ribosomal subunit intracellular anatomical structure cytosol cytosolic small ribosomal subunit ribosome nucleoplasm cytoplasm endoplasmic reticulum rough endoplasmic reticulum polysomal ribosome synapse Biological process endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) translational initiation SRP-dependent cotranslational protein targeting to membrane nuclear-transcribed mRNA catabolic process, nonsense-mediated decay viral transcription protein biosynthesis rRNA processing cytoplasmic translation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6227	66481
Ensembl	ENSG00000171858	ENSMUSG00000039001
UniProt	P63220	Q9CQR2
RefSeq (mRNA)	NM_001024	NM_025587
RefSeq (protein)	NP_001015	NP_079863 NP_001342445 NP_001342446 NP_001342447 NP_001342449 NP_001342450
Location (UCSC)	Chr 20: 62.39 – 62.39 Mb	Chr 2: 180.26 – 180.26 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

40S ribosomal protein S21 is a protein, encoded in humans by the RPS21 gene. ^{[5] [6] [7]}

Function

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 S21E family of ribosomal proteins.

It is located in the cytoplasm. Alternative splice variants that encode different protein isoforms have been described, but their existence has not been verified. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. ^[7]

Interactions

RPS21 has been shown to interact with Ribosomal protein SA. ^{[8] [9]}

References

1. GRCh38: Ensembl release 89: ENSG00000171858 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000039001 - 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. Bhat KS, Morrison SG (Jun 1993). "Primary structure of human ribosomal protein S21". Nucleic Acids Research. 21 (12): 2939. doi:10.1093/nar/21.12.2939. PMC   309688 . PMID   8332502.
6. Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (May 1998). "A map of 75 human ribosomal protein genes". Genome Research. 8 (5): 509–23. doi: 10.1101/gr.8.5.509 . PMID   9582194.
7. "Entrez Gene: RPS21 ribosomal protein S21".
8. Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl: 11858/00-001M-0000-0010-8592-0 . PMID   16169070. S2CID   8235923.
9. Sato M, Saeki Y, Tanaka K, Kaneda Y (Mar 1999). "Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system". Biochemical and Biophysical Research Communications. 256 (2): 385–90. doi:10.1006/bbrc.1999.0343. PMID   10079194.

Further reading

• Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochemistry and Cell Biology. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID   8722009.
• Kostanian IA, Astapova MV, Starovoĭtova EV, Dranitsyna SM, Lipkin VM (Apr 1995). "[A new differentiation factor from culture media of the HL-60 cell line treated with retinoic acid. Isolation and primary structure determination]". Bioorganicheskaia Khimiia. 21 (4): 243–8. PMID   7786314.
• Kostanyan IA, Astapova MV, Starovoytova EV, Dranitsina SM, Lipkin VM (Dec 1994). "A new human leukemia cell 8.2 kDa differentiation factor: isolation and primary structure". FEBS Letters. 356 (2–3): 327–9. doi: 10.1016/0014-5793(94)01306-3 . PMID   7805865. S2CID   43322576.
• Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, Wittmann-Liebold B, Otto A (Jul 1996). "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry". European Journal of Biochemistry. 239 (1): 144–9. doi: 10.1111/j.1432-1033.1996.0144u.x . PMID   8706699.
• Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi: 10.1101/gr.6.9.791 . PMID   8889548.
• Sato M, Saeki Y, Tanaka K, Kaneda Y (Mar 1999). "Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system". Biochemical and Biophysical Research Communications. 256 (2): 385–90. doi:10.1006/bbrc.1999.0343. PMID   10079194.
• Smirnova EV, Rakitina TV, Evtodienko A, Kostanian IA, Lipkin VM (May 2000). "Cloning and characterization of the human ribosomal protein S21 gene [". Bioorganicheskaia Khimiia. 26 (5): 392–6. PMID   10900511.
• Yoshihama M, Uechi T, Asakawa S, Kawasaki K, Kato S, Higa S, Maeda N, Minoshima S, Tanaka T, Shimizu N, Kenmochi N (Mar 2002). "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes". Genome Research. 12 (3): 379–90. doi:10.1101/gr.214202. PMC   155282 . PMID   11875025.
• Yu Y, Ji H, Doudna JA, Leary JA (Jun 2005). "Mass spectrometric analysis of the human 40S ribosomal subunit: native and HCV IRES-bound complexes". Protein Science. 14 (6): 1438–46. doi:10.1110/ps.041293005. PMC   2253395 . PMID   15883184.
• Oh JH, Yang JO, Hahn Y, Kim MR, Byun SS, Jeon YJ, Kim JM, Song KS, Noh SM, Kim S, Yoo HS, Kim YS, Kim NS (Dec 2005). "Transcriptome analysis of human gastric cancer". Mammalian Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID   16341674. S2CID   69278.