60S ribosomal protein L13
RPL13 | ||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| ||||||||||||||||||||||||||||||||||||||||
| ||||||||||||||||||||||||||||||||||||||||
Wikidata | ||||||||||||||||||||||||||||||||||||||||
|
60S ribosomal protein L13 is a protein that in humans is encoded by the RPL13 gene.[5][6]
Function
Interactions
RPL13 has been shown to
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
- ^ a b c GRCh38: Ensembl release 89: ENSG00000167526 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000059776 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 9582194.
- ^ a b "Entrez Gene: RPL13 ribosomal protein L13".
- PMID 11101529.
- ^ "BBC1 | SGD". www.yeastgenome.org. Retrieved 2020-01-09.
- ^ PMID 11901111.
- S2CID 11363803.
- ^ a b "Pombase". www.pombase.org. Retrieved 2020-01-09.
- PMID 20603077.
- PMID 28218250.
- 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. 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. 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. 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. 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. 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. 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. 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. PMID 16786168.
External links
- PDBe-KB provides an overview of all the structure information available in the PDB for Human 60S ribosomal protein L13