http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID188725

Outgoing Links

Predicate Object
abstract The fourth LIM domain of the Paxillin-like protein family. The fourth 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 LIM4_Paxillin_like
isDiscussedBy http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18680030
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7226009
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30161373
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24684046
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12425074
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23281369
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16486584
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21995544
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21410568
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16589021
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8601479
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14016594
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5792562
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14486530
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26209648
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27357395
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11900404
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7762499
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4939642
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16506366
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24179217
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4742729
type http://purl.obolibrary.org/obo/SO_0000417

Incoming Links

Predicate Subject
has component http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ55BI0

Total number of triples: 26.