60S ribosomal protein L13

"Bbc1" redirects here. For other uses, see Bbc1 (disambiguation).

RPL13
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 4UG0, 4V6X, 5AJ0, 4UJD, 4D67, 4D5Y, 4UJE, 4UJC
Identifiers
Aliases	RPL13 , BBC1, D16S444E, D16S44E, L13, ribosomal protein L13, SEMDIST
External IDs	OMIM: 113703; MGI: 3642685; HomoloGene: 5568; GeneCards: RPL13; OMA:RPL13 - orthologs
Gene location (Human) Chr. Chromosome 16 (human) [1] Band 16q24.3|17p11.2 Start 89,560,677 bp [1] End 89,564,542 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3 D|3 28.88 cM Start 58,894,591 bp [2] End 58,895,226 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left ovary right ovary right uterine tube skin of abdomen skin of leg canal of the cervix ectocervix anterior pituitary body of uterus olfactory zone of nasal mucosa Top expressed in dentate gyrus of hippocampal formation granule cell embryo embryo morula blastocyst epiblast lens urinary bladder duodenum proximal tubule More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding structural constituent of ribosome RNA binding Cellular component cytosol ribosome cytosolic ribosome membrane intracellular anatomical structure cytosolic large ribosomal subunit nucleus nucleolus endoplasmic reticulum Biological process viral transcription SRP-dependent cotranslational protein targeting to membrane translational initiation nuclear-transcribed mRNA catabolic process, nonsense-mediated decay rRNA processing protein biosynthesis Sources:Amigo / QuickGO
Orthologs Species Human Mouse 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 Mb Chr 3: 58.89 – 58.9 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/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. GRCh38: Ensembl release 89: ENSG00000167526 – Ensembl, May 2017
2. 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. "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. 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. Bibcode:2003CBio...13.1000R. doi: 10.1016/s0960-9822(03)00383-x . PMID   12814545. S2CID   11363803.
11. "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

• 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 SM, Helps NR, Sharp MG, Brammar WJ, Walker RA, Varley JM (1993). "Isolation and characterization of a novel gene with differential expression in benign and malignant human breast tumours". Hum. Mol. Genet. 1 (2): 91–6. doi:10.1093/hmg/1.2.91. PMID   1301162.
• Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID   7821789.
• Yaseen NR, Blobel G (1997). "Cloning and characterization of human karyopherin beta3". Proc. Natl. Acad. Sci. U.S.A. 94 (9): 4451–6. Bibcode:1997PNAS...94.4451Y. doi: 10.1073/pnas.94.9.4451 . PMC   20743 . PMID   9114010.
• 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.
• Bi W, Yan J, Stankiewicz P, Park SS, Walz K, Boerkoel CF, Potocki L, Shaffer LG, Devriendt K, Nowaczyk MJ, Inoue K, Lupski JR (2002). "Genes in a refined Smith-Magenis syndrome critical deletion interval on chromosome 17p11.2 and the syntenic region of the mouse". Genome Res. 12 (5): 713–28. doi:10.1101/gr.73702. PMC   186594 . PMID   11997338.
• 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.
• Kobayashi T, Sasaki Y, Oshima Y, Yamamoto H, Mita H, Suzuki H, Toyota M, Tokino T, Itoh F, Imai K, Shinomura Y (2006). "Activation of the ribosomal protein L13 gene in human gastrointestinal cancer". Int. J. Mol. Med. 18 (1): 161–70. doi: 10.3892/ijmm.18.1.161 . PMID   16786168.

External links

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