RPL13
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesRPL13, BBC1, D16S444E, D16S44E, L13, ribosomal protein L13, SEMDIST
External IDsOMIM: 113703 MGI: 3642685 HomoloGene: 5568 GeneCards: RPL13
Orthologs
SpeciesHumanMouse
Entrez

6137

100040416

Ensembl

ENSG00000167526

ENSMUSG00000059776

UniProt

P26373

n/a

RefSeq (mRNA)

NM_033251
NM_000977
NM_001243130
NM_001243131

XM_036163486

RefSeq (protein)

NP_000968
NP_001230060
NP_150254

n/a

Location (UCSC)Chr 16: 89.56 – 89.56 MbChr 3: 58.89 – 58.9 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

60S ribosomal protein L13 is a protein that in humans is encoded by the RPL13 gene.[5][6]

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 L13E family of ribosomal proteins. It is located in the cytoplasm. This gene is expressed at significantly higher levels in benign breast lesions than in breast carcinomas. Transcript variants derived from alternative splicing and/or alternative polyadenylation exist; these variants encode the same protein. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[6]

Interactions

RPL13 has been shown to interact with CDC5L.[7]

Bbc1

Bbc1 (Mti1p) is a protein expressed in yeasts that is thought to associate with actin networks. Bbc1 is short for Bni1 synthetic lethal and Bee1 (las17) complex member.[8] The alternate name, Mti1p, is short for Myosin tail region-interacting protein.[9] Bbc1 is involved in cytoskeletal regulation during endocytosis. Budding yeast Bbc1 inhibits the activator of the Arp2/3 complex Las17 (WASp homolog).[10] The protein also interacts with the tail of Myosin 1 proteins.[9]

In fission yeast, Bbc1 is considered a WIP family cytoskeletal protein. Bbc1 localizes to actin cortical patches, cell division sites, the cell tip, and the cytosol. Cells with bbc1 gene deletion are viable.[11] Bbc1 is affinity captured by the Nebulin-family actin filament anchoring protein Cyk3[12] and the SMARCAD1 family ATP-dependent DNA helicase Fft3.[11][13] Bbc1 competes with WIP homolog Vrp1 to bind the Myosin 1 tail to regulate actin assembly at endocytic sites.[14]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000167526 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000059776 - 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. ↑ Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (August 1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
  6. 1 2 "Entrez Gene: RPL13 ribosomal protein L13".
  7. ↑ Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (December 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". EMBO J. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846. PMID 11101529.
  8. ↑ "BBC1 | SGD". www.yeastgenome.org. Retrieved 2020-01-09.
  9. 1 2 Mochida J, Yamamoto T, Fujimura-Kamada K, Tanaka K (March 2002). "The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae". Genetics. 160 (3): 923–34. doi:10.1093/genetics/160.3.923. OCLC 678661938. PMC 1462009. PMID 11901111.
  10. ↑ Rodal AA, Manning AL, Goode BL, Drubin DG (June 2003). "Negative regulation of yeast WASp by two SH3 domain-containing proteins". Current Biology. 13 (12): 1000–8. doi:10.1016/s0960-9822(03)00383-x. PMID 12814545. S2CID 11363803.
  11. 1 2 "Pombase". www.pombase.org. Retrieved 2020-01-09.
  12. ↑ Roberts-Galbraith RH, Ohi MD, Ballif BA, Chen JS, McLeod I, McDonald WH, et al. (July 2010). "Dephosphorylation of F-BAR protein Cdc15 modulates its conformation and stimulates its scaffolding activity at the cell division site". Molecular Cell. 39 (1): 86–99. doi:10.1016/j.molcel.2010.06.012. PMC 2916701. PMID 20603077.
  13. ↑ Lee J, Choi ES, Seo HD, Kang K, Gilmore JM, Florens L, et al. (February 2017). "Fft3 induces nucleosome disassembly to facilitate RNA polymerase II elongation". Nature Communications. 8: 14527. Bibcode:2017NatCo...814527L. doi:10.1038/ncomms14527. PMC 5321744. PMID 28218250.
  14. ↑ MacQuarrie CD, Mangione MC, Carroll R, James M, Gould KL, Sirotkin V (September 2019). "S. pombe adaptor protein Bbc1 regulates localization of Wsp1 and Vrp1 during endocytic actin patch assembly". Journal of Cell Science. 132 (17): jcs233502. doi:10.1242/jcs.233502. PMC 6771142. PMID 31391237.

Further reading

  • PDBe-KB provides an overview of all the structure information available in the PDB for Human 60S ribosomal protein L13


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