60S ribosomal protein L28

Protein found in humans
RPL28
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

5AJ0, 4UG0, 4V6X, 4UJD, 4D67, 4D5Y, 4UJE, 4UJC

Identifiers
AliasesRPL28, L28, ribosomal protein L28
External IDsOMIM: 603638; MGI: 101839; HomoloGene: 768; GeneCards: RPL28; OMA:RPL28 - orthologs
EC number3.6.5.3
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for RPL28
Genomic location for RPL28
Band19q13.42Start55,385,932 bp[1]
End55,403,250 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for RPL28
Genomic location for RPL28
Band7 A1|7 2.77 cMStart4,795,873 bp[2]
End4,798,065 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • superficial temporal artery

  • oral cavity

  • trabecular bone

  • lower lobe of lung

  • human penis

  • caput epididymis

  • corpus epididymis

  • vulva

  • stromal cell of endometrium

  • right uterine tube
Top expressed in
  • urinary bladder

  • yolk sac

  • adrenal gland

  • white adipose tissue

  • bone marrow

  • uterus

  • thymus

  • spleen

  • ganglionic eminence

  • islet of Langerhans
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein binding
  • RNA binding
  • structural constituent of ribosome
Cellular component
  • cell body
  • cytosol
  • ribosome
  • membrane
  • intracellular anatomical structure
  • dendrite
  • cytoplasmic ribonucleoprotein granule
  • cytosolic large ribosomal subunit
  • extracellular exosome
Biological process
  • positive regulation of protein targeting to mitochondrion
  • viral transcription
  • SRP-dependent cotranslational protein targeting to membrane
  • regulation of autophagy of mitochondrion
  • translational initiation
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
  • rRNA processing
  • protein biosynthesis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6158

19943

Ensembl

ENSG00000108107

ENSMUSG00000030432

UniProt

P46779

P41105

RefSeq (mRNA)
NM_000991
NM_001136134
NM_001136135
NM_001136136
NM_001136137

NM_001363697

NM_009081

RefSeq (protein)
NP_000982
NP_001129606
NP_001129607
NP_001129608
NP_001129609

NP_001350626

NP_033107

Location (UCSC)Chr 19: 55.39 – 55.4 MbChr 7: 4.8 – 4.8 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

60S ribosomal protein L28 is a protein that in humans is encoded by the RPL28 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 60S subunit. The protein belongs to the L28E family of ribosomal proteins. 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]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000108107 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030432 – 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. ^ Frigerio JM, Dagorn JC, Iovanna JL (Jul 1995). "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs". Biochim Biophys Acta. 1262 (1): 64–8. doi:10.1016/0167-4781(95)00045-i. PMID 7772601.
  6. ^ 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.
  7. ^ a b "Entrez Gene: RPL28 ribosomal protein L28".

External links

  • Human RPL28 genome location and RPL28 gene details page in the UCSC Genome Browser.
  • PDBe-KB provides an overview of all the structure information available in the PDB for Human 60S ribosomal protein L28

Further reading

  • Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID 8722009.
  • Brown JR, Daar IO, Krug JR, Maquat LE (1985). "Characterization of the functional gene and several processed pseudogenes in the human triosephosphate isomerase gene family". Mol. Cell. Biol. 5 (7): 1694–706. doi:10.1128/mcb.5.7.1694. PMC 367288. PMID 4022011.
  • Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
  • Bortoluzzi S, d'Alessi F, Romualdi C, Danieli GA (2002). "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.
  • Mammalian Gene Collection Program Team, Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences. 99 (26): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Kasai H, Nadano D, Hidaka E, et al. (2003). "Differential expression of ribosomal proteins in human normal and neoplastic colorectum". J. Histochem. Cytochem. 51 (5): 567–74. doi:10.1177/002215540305100502. PMID 12704204. S2CID 25865715.
  • Odintsova TI, Müller EC, Ivanov AV, et al. (2004). "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing". J. Protein Chem. 22 (3): 249–58. doi:10.1023/A:1025068419698. PMID 12962325. S2CID 10710245.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Villacé P, Marión RM, Ortín J (2004). "The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs". Nucleic Acids Res. 32 (8): 2411–20. doi:10.1093/nar/gkh552. PMC 419443. PMID 15121898.
  • Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 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
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Elongation factor
Bacterial/​Mitochondrial
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Release factor
Ribosomal Proteins
Cytoplasmic
60S subunit
40S subunit
Mitochondrial
39S subunit
28S subunit
Other concepts
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