Anillin
| Anillin | ||
|---|---|---|
| other names |
ANLN, scra, FSGS8, scraps |
|
| Properties of human protein | ||
| Mass / length primary structure | 1,124 amino acids , 124,199 Da | |
| Identifier | ||
| External IDs | ||
| Orthologue | ||
| human | House mouse | |
| Entrez | 54443 | 68743 |
| Ensemble | ENSG00000011426 | |
| UniProt | Q9NQW6 | Q8K298 |
| Refseq (mRNA) | NM_001284301.3 | |
| Refseq (protein) | NP_001271230.1 | |
| Gene locus | ||
| PubMed search | 54443 |
68743
|
Anillin is a protein from animals that is involved in cell growth and cytokinesis . It is not to be confused with the aminobenzene aniline .
properties
Anillin is an actin- binding protein. It regulates the cytoskeleton in podocytes of the kidney . Some mutations of anillin lead to focal segmental glomerulosclerosis of type 8. Alternative splicing creates different isoforms of anillin. During the metaphase and anaphase of mitosis , anillin is involved in the formation of blebs .
Individual evidence
- ↑ WM Zhao, G. Fang: Anillin is a substrate of anaphase-promoting complex / cyclosome (APC / C) that controls spatial contractility of myosin during late cytokinesis. In: Journal of Biological Chemistry . Volume 280, Number 39, September 2005, pp. 33516-33524, doi : 10.1074 / jbc.M504657200 , PMID 16040610 .
- ↑ RA Gbadegesin, G. Hall, A. Adeyemo, N. Hanke, I. Tossidou, J. Burchette, G. Wu, A. Homstad, MA Sparks, J. Gomez, R. Jiang, A. Alonso, P. Lavin , P. Conlon, R. Korstanje, MC Stander, G. Shamsan, M. Barua, R. Spurney, PC Singhal, JB Kopp, H. Haller, D. Howell, MR Pollak, AS Shaw, M. Schiffer, MP Winn : Mutations in the gene that encodes the F-actin binding protein anillin cause FSGS. In: Journal of the American Society of Nephrology . Volume 25, number 9, September 2014, pp. 1991-2002, doi : 10.1681 / ASN.2013090976 , PMID 24676636 , PMC 4147982 (free full text).
- ↑ a b 54443 - Gene ResultANLN anillin actin binding protein (human). In: ncbi.nlm.nih.gov. Retrieved on August 14, 2019 .
- ↑ T. Kiyomitsu, IM Cheeseman: Cortical dynein and asymmetric membrane elongation coordinately position the spindle in anaphase. In: Cell . Volume 154, number 2, July 2013, pp. 391-402, doi : 10.1016 / j.cell.2013.06.010 , PMID 23870127 , PMC 4177044 (free full text).