http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID270694
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | Catalytic domain of Actin-Fragmin Kinase. AFK is found in slime molds, ciliates, and flowering plants. It catalyzes the transfer of the gamma-phosphoryl group from ATP specifically to threonine residues in the actin-fragmin complex. The phosphorylation sites are located at a minor contact site for DNase I and at an actin-actin contact site. Fragmin is an actin-binding protein that functions as a regulator of the microfilament system. It interferes with the growth of F-actin by severing actin filaments and capping their ends. The phosphorylation of the actin-fragmin complex inhibits its nucleation activity and results in calcium-dependent capping activity. Thus, AFK plays a role in regulating actin polymerization. The AFK catalytic domain is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. |
| title | AFK |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13850638 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26793021 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8411467 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/29472806 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
| Predicate | Subject |
|---|---|
| has component | http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP80197 |
Total number of triples: 8.