40S ribosomal protein S29

Protein-coding gene in the species Homo sapiens
RPS29
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4UG0, 4V6X, 5A2Q, 5AJ0, 4KZY, 4D61, 5FLX, 4KZX, 4D5L, 4V5Z, 4UJD, 4KZZ, 4UJE, 4UJC

Identifiers
AliasesRPS29, DBA13, S29, ribosomal protein S29, uS14
External IDsOMIM: 603633; MGI: 107681; HomoloGene: 83197; GeneCards: RPS29; OMA:RPS29 - orthologs
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for RPS29
Genomic location for RPS29
Band14q21.3Start49,570,984 bp[1]
End49,599,164 bp[1]
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[2]
Chromosome 12 (mouse)
Genomic location for RPS29
Genomic location for RPS29
Band12|12 C2Start69,204,496 bp[2]
End69,205,960 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
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
BioGPS
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
SpeciesHumanMouse
Entrez

6235

20090

Ensembl

ENSG00000213741

ENSMUSG00000034892

UniProt

P62273

P62274

RefSeq (mRNA)

NM_001032
NM_001030001
NM_001351375

NM_009093

RefSeq (protein)

NP_001023
NP_001025172
NP_001338304

NP_033119

Location (UCSC)Chr 14: 49.57 – 49.6 MbChr 12: 69.2 – 69.21 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000213741 – Ensembl, May 2017
  2. ^ a b c 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.
  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.
  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.
  7. ^ a b "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.

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.
  • 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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Proteins
Initiation factor
Bacterial
Mitochondrial
Archaeal
  • aIF1
  • aIF2
  • aIF5
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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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