40S ribosomal protein S29

RPS29
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4UG0, 4V6X, 5A2Q, 5AJ0, 4KZY, 4D61, 5FLX, 4KZX, 4D5L, 4V5Z, 4UJD, 4KZZ, 4UJE, 4UJC
Identifiers
Aliases	RPS29, DBA13, S29, ribosomal protein S29, uS14
External IDs	OMIM: 603633; MGI: 107681; HomoloGene: 83197; GeneCards: RPS29; OMA:RPS29 - orthologs
Gene location (Human)
Chr.	Chromosome 14 (human)
End	49,599,164 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	69,205,960 bp
RNA expression pattern
	Top expressed in
	caput epididymis; ; human penis; ; parietal pleura; ; mucosa of sigmoid colon; ; superficial temporal artery; ; granulocyte; ; nipple; ; ganglionic eminence; ; corpus epididymis; ; mucosa of transverse colon;
	Top expressed in
	embryo; ; epiblast; ; uterus; ; yolk sac; ; embryo; ; blastocyst; ; neural tube; ; ganglionic eminence; ; ventricular zone; ; stomach;
	More reference expression data
	n/a
Gene ontology
Molecular function	structural constituent of ribosome; zinc ion binding; metal ion binding;
Cellular component	cytosol; ribosome; focal adhesion; intracellular anatomical structure; cytosolic small ribosomal subunit; small ribosomal subunit; extracellular exosome; nucleoplasm; cytoplasm; endoplasmic reticulum; rough endoplasmic reticulum; polysomal ribosome; cytoplasmic side of rough endoplasmic reticulum membrane;
Biological process	viral transcription; SRP-dependent cotranslational protein targeting to membrane; translational initiation; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; protein biosynthesis; rRNA processing; cytoplasmic translation;
	Sources:Amigo / QuickGO
Orthologs
	6235
	20090
	ENSG00000213741
	ENSMUSG00000034892
	P62273
	P62274
	NM_001032; NM_001030001; NM_001351375
	NM_009093
	NP_001023; NP_001025172; NP_001338304
	NP_033119
	Wikidata
View/Edit Human	View/Edit Mouse

40S ribosomal protein S29 is a protein that in humans is encoded by the RPS29 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 and a member of the S14P family of ribosomal proteins. The protein, which contains a C2-C2 zinc finger-like domain that can bind to zinc, can enhance the tumor suppressor activity of Ras-related protein 1A (KREV1). 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, there are multiple processed pseudogenes of this gene dispersed through the genome.^[7]

Clinical significance

Mutations in RPS29 cause Diamond–Blackfan anemia.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000213741 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000034892 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Kondoh N, Noda M, Fisher RJ, Schweinfest CW, Papas TS, Kondoh A, Samuel KP, Oikawa T (August 1996). "The S29 ribosomal protein increases tumor suppressor activity of K rev-1 gene on v-K ras-transformed NIH3T3 cells". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1313 (1): 41–6. doi:10.1016/0167-4889(96)00052-3. PMID 8781548.
^ Frigerio JM, Dagorn JC, Iovanna JL (May 1995). "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1262 (1): 64–8. doi:10.1016/0167-4781(95)00045-i. PMID 7772601.
^ ^a ^b "Entrez Gene: RPS29 ribosomal protein S29".
^ Mirabello L, Macari ER, Jessop L, Ellis SR, Myers T, Giri N, Taylor AM, McGrath KE, Humphries JM, Ballew BJ, Yeager M, Boland JF, He J, Hicks BD, Burdett L, Alter BP, Zon L, Savage SA (July 2014). "Whole-exome sequencing and functional studies identify RPS29 as a novel gene mutated in multicase Diamond-Blackfan anemia families". Blood. 124 (1): 24–32. doi:10.1182/blood-2013-11-540278. PMC 4125351. PMID 24829207.

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.
Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, Wittmann-Liebold B, Otto A (July 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.
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.
Coppock D, Kopman C, Gudas J, Cina-Poppe DA (March 2000). "Regulation of the quiescence-induced genes: quiescin Q6, decorin, and ribosomal protein S29". Biochemical and Biophysical Research Communications. 269 (2): 604–10. doi:10.1006/bbrc.2000.2324. PMID 10708601.
Bortoluzzi S, d'Alessi F, Romualdi C, Danieli GA (December 2001). "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.
Yoshihama M, Uechi T, Asakawa S, Kawasaki K, Kato S, Higa S, Maeda N, Minoshima S, Tanaka T, Shimizu N, Kenmochi N (March 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.
Zhou ZD, Bao L, Liu DG, Li MQ, Ge YZ, Huang YL, Liu WY (February 2003). "Low content of protein S29 in ribosomes of human lung cancer cell line a549: detected by two-dimensional electrophoresis". Protein and Peptide Letters. 10 (1): 91–7. doi:10.2174/0929866033408273. PMID 12625830.
Yu Y, Ji H, Doudna JA, Leary JA (June 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.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000213741 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000034892 – 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.

[pmid8781548-5] Kondoh N, Noda M, Fisher RJ, Schweinfest CW, Papas TS, Kondoh A, Samuel KP, Oikawa T (August 1996). "The S29 ribosomal protein increases tumor suppressor activity of K rev-1 gene on v-K ras-transformed NIH3T3 cells". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1313 (1): 41–6. doi:10.1016/0167-4889(96)00052-3. PMID 8781548.

[pmid7772601-6] Frigerio JM, Dagorn JC, Iovanna JL (May 1995). "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1262 (1): 64–8. doi:10.1016/0167-4781(95)00045-i. PMID 7772601.

[entrez-7] "Entrez Gene: RPS29 ribosomal protein S29".

[8] Mirabello L, Macari ER, Jessop L, Ellis SR, Myers T, Giri N, Taylor AM, McGrath KE, Humphries JM, Ballew BJ, Yeager M, Boland JF, He J, Hicks BD, Burdett L, Alter BP, Zon L, Savage SA (July 2014). "Whole-exome sequencing and functional studies identify RPS29 as a novel gene mutated in multicase Diamond-Blackfan anemia families". Blood. 124 (1): 24–32. doi:10.1182/blood-2013-11-540278. PMC 4125351. PMID 24829207.

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40S ribosomal protein S29

Function

Clinical significance

References

Further reading

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