60S ribosomal protein L3

Protein found in humans
RPL3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4UG0, 4V6X, 5AJ0

Identifiers
AliasesRPL3, ASC-1, L3, TARBP-B, ribosomal protein L3
External IDsOMIM: 604163; MGI: 1351605; HomoloGene: 747; GeneCards: RPL3; OMA:RPL3 - orthologs
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for RPL3
Genomic location for RPL3
Band22q13.1Start39,312,882 bp[1]
End39,320,389 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for RPL3
Genomic location for RPL3
Band15|15 E1Start79,961,992 bp[2]
End79,976,069 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • left ovary

  • right ovary

  • beta cell

  • ventricular zone

  • anterior pituitary

  • skin of arm

  • canal of the cervix

  • stromal cell of endometrium

  • ganglionic eminence

  • body of uterus
Top expressed in
  • ventricular zone

  • ovary

  • dentate gyrus of hippocampal formation granule cell

  • epiblast

  • hypothalamus

  • ganglionic eminence

  • lens

  • blastocyst

  • zone of skin

  • hippocampus proper
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • protein binding
  • 5S rRNA binding
  • RNA binding
  • structural constituent of ribosome
Cellular component
  • ribosome
  • focal adhesion
  • intracellular anatomical structure
  • extracellular exosome
  • nucleolus
  • nucleus
  • cytoplasm
  • cytosolic large ribosomal subunit
  • cytosol
  • protein-containing complex
  • synapse
Biological process
  • cellular response to interleukin-4
  • viral transcription
  • SRP-dependent cotranslational protein targeting to membrane
  • translational initiation
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
  • rRNA processing
  • ribosomal large subunit assembly
  • protein biosynthesis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6122

27367

Ensembl

ENSG00000100316

ENSMUSG00000060036

UniProt

P39023

P27659

RefSeq (mRNA)

NM_001033853
NM_000967

NM_013762

RefSeq (protein)

NP_000958
NP_001029025

NP_038790

Location (UCSC)Chr 22: 39.31 – 39.32 MbChr 15: 79.96 – 79.98 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

60S ribosomal protein L3 is a protein that in humans is encoded by the RPL3 gene.[5][6][7]

Function

Ribosomes, the complexes 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. The RPL3 gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L3P family of ribosomal proteins and it is located in the cytoplasm. The protein can bind to the HIV-1 TAR mRNA, and it has been suggested that the protein contributes to tat-mediated transactivation. This gene is co-transcribed with several small nucleolar RNA genes, which are located in several of this gene's introns. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. 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: ENSG00000100316 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000060036 – 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. ^ Ou JH, Yen TS, Wang YF, Kam WK, Rutter WJ (Jan 1988). "Cloning and characterization of a human ribosomal protein gene with enhanced expression in fetal and neoplastic cells". Nucleic Acids Res. 15 (21): 8919–34. doi:10.1093/nar/15.21.8919. PMC 306413. PMID 2891103.
  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): 509–523. doi:10.1101/gr.8.5.509. PMID 9582194.
  7. ^ a b "Entrez Gene: RPL3 ribosomal protein L3".

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.
  • Adams MD, Dubnick M, Kerlavage AR, Moreno R, Kelley JM, Utterback TR, Nagle JW, Fields C, Venter JC (1992). "Sequence identification of 2,375 human brain genes". Nature. 355 (6361): 632–4. Bibcode:1992Natur.355..632A. doi:10.1038/355632a0. PMID 1538749. S2CID 4234345.
  • Reddy TR, Suhasini M, Rappaport J, Looney DJ, Kraus G, Wong-Staal F (1995). "Molecular cloning and characterization of a TAR-binding nuclear factor from T cells". AIDS Res. Hum. Retroviruses. 11 (6): 663–9. doi:10.1089/aid.1995.11.663. PMID 7576925.
  • Matoba R, Okubo K, Hori N, Fukushima A, Matsubara K (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene. 146 (2): 199–207. doi:10.1016/0378-1119(94)90293-3. PMID 8076819.
  • Van Raay TJ, Connors TD, Klinger KW, Landes GM, Burn TC (1997). "A novel ribosomal protein L3-like gene (RPL3L) maps to the autosomal dominant polycystic kidney disease gene region". Genomics. 37 (2): 172–6. doi:10.1006/geno.1996.0538. PMID 8921388.
  • Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
  • Duga S, Asselta R, Malcovati M, Tenchini ML, Ronchi S, Simonic T (2000). "The intron-containing L3 ribosomal protein gene (RPL3): sequence analysis and identification of U43 and of two novel intronic small nucleolar RNAs". Biochim. Biophys. Acta. 1490 (3): 225–36. doi:10.1016/S0167-4781(99)00237-7. PMID 10684968.
  • Uechi T, Tanaka T, Kenmochi N (2001). "A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders". Genomics. 72 (3): 223–30. doi:10.1006/geno.2000.6470. PMID 11401437.
  • Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
  • Odintsova TI, Müller EC, Ivanov AV, Egorov TA, Bienert R, Vladimirov SN, Kostka S, Otto A, Wittmann-Liebold B, Karpova GG (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.
  • Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
  • Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
  • Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
  • Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
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Proteins
Initiation factor
Bacterial
Mitochondrial
Archaeal
  • aIF1
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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
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