http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID188724
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | The third LIM domain of the paxillin like protein family. The third LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. |
| title | LIM3_Paxillin_like |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4742729 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24179217 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16486584 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24684046 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8601479 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16589021 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27357395 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14016594 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7226009 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5792562 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30161373 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16506366 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12425074 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21995544 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18680030 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21410568 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4939642 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23281369 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14486530 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11900404 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26209648 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7762499 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 31.