Anillin
| Anillin | ||
|---|---|---|
| Andere Namen |
ANLN, scra, FSGS8, Scraps | |
| Eigenschaften des menschlichen Proteins | ||
| Masse/Länge Primärstruktur | 1.124 Aminosäuren, 124.199 Da | |
| Bezeichner | ||
| Externe IDs | ||
| Vorkommen | ||
| Homologie-Familie | Hovergen | |
| Orthologe | ||
| Mensch | Hausmaus | |
| Entrez | 54443 | 68743 |
| Ensembl | ENSG00000011426 | |
| UniProt | Q9NQW6 | Q8K298 |
| Refseq (mRNA) | NM_001284301.3 | |
| Refseq (Protein) | NP_001271230.1 | |
| Genlocus | ||
| PubMed-Suche | 54443 | 68743
|
Anillin ist ein Protein aus Tieren, das am Zellwachstum und an der Zytokinese[1] beteiligt ist. Es ist nicht zu verwechseln mit dem Aminobenzol Anilin.
Eigenschaften
Anillin ist ein Aktin-bindendes Protein. Es reguliert das Zytoskelett in Podozyten der Niere.[2] Manche Mutationen des Anillins führen zur fokal segmentalen Glomerulosklerose des Typs 8.[3] Durch alternatives Spleißen werden verschiedene Isoformen des Anillins gebildet.[3] Während der Metaphase und der Anaphase der Mitose ist Anillin an der Bildung von Blebs beteiligt.[4]
Einzelnachweise
- ↑ W. M. 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. Band 280, Nummer 39, September 2005, S. 33516–33524, doi:10.1074/jbc.M504657200, PMID 16040610.
- ↑ R. A. Gbadegesin, G. Hall, A. Adeyemo, N. Hanke, I. Tossidou, J. Burchette, G. Wu, A. Homstad, M. A. Sparks, J. Gomez, R. Jiang, A. Alonso, P. Lavin, P. Conlon, R. Korstanje, M. C. Stander, G. Shamsan, M. Barua, R. Spurney, P. C. Singhal, J. B. Kopp, H. Haller, D. Howell, M. R. Pollak, A. S. Shaw, M. Schiffer, M. P. Winn: Mutations in the gene that encodes the F-actin binding protein anillin cause FSGS. In: Journal of the American Society of Nephrology. Band 25, Nummer 9, September 2014, S. 1991–2002, doi:10.1681/ASN.2013090976, PMID 24676636, PMC 4147982 (freier Volltext).
- ↑ a b 54443 - Gene ResultANLN anillin actin binding protein (human). In: ncbi.nlm.nih.gov. Abgerufen am 14. August 2019 (englisch).
- ↑ T. Kiyomitsu, I. M. Cheeseman: Cortical dynein and asymmetric membrane elongation coordinately position the spindle in anaphase. In: Cell. Band 154, Nummer 2, Juli 2013, S. 391–402, doi:10.1016/j.cell.2013.06.010, PMID 23870127, PMC 4177044 (freier Volltext).
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