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O43294 Proteins LIM zinc-binding domain Repeats

Uniprot ID:O43294	Protein name: Transforming growth factor beta-1-induced transcript 1 protein	Gene : TGFB1I1 ARA55
Protein Family:Paxillin family	Squence Length : 461

Sequnce	>O43294 462 MEDLDALLSDLETTTSHMPRSGAPKERPAEPLTPPPSYGHQPQTGSGESSGASGDKDHLYSTVCKPRSPKPAAPAAPPFSSSSGVLGTGLCELDRLLQELNATQFNITDEIMSQFPSSKVASGEQKEDQSEDKKRPSLPSSPSPGLPKASATSATLELDRLMASLSDFRVQNHLPASGPTQPPVVSSTNEGSPSPPEPTGKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFVCGGCSTALGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPFGDEGFHEREGRPYCRRDFLQLFAPRCQGCQGPILDNYISALSALWHPDCFVCRECFAPFSGGSFFEHEGRPLCENHFHARRGSLCATCGLPVTGRCVSALGRRFHPDHFTCTFCLRPLTKGSFQERAGKPYCQPCFLKLFG
Domains	DOMAIN 226 285 LIM zinc-binding 1 DOMAIN 286 343 LIM zinc-binding 2 DOMAIN 344 403 LIM zinc-binding 3 DOMAIN 404 461 LIM zinc-binding 4
LIM zinc-binding sequence regions	226 - 285 CGSCNKPIAGQVVTALGRAWHPEHFVCGGCSTALGGSSFFEKDGAPFCPECYFERFSPRC 286 - 343 GFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPFGDEGFHEREGRPYCRRDFLQLFAPR 344 - 403 CQGCQGPILDNYISALSALWHPDCFVCRECFAPFSGGSFFEHEGRPLCENHFHARRGSLC 404 - 461 ATCGLPVTGRCVSALGRRFHPDHFTCTFCLRPLTKGSFQERAGKPYCQPCFLKLFG
Function	"Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity"
Motifs	MOTIF 3 15 LD motif 1. MOTIF 92 104 LD motif 2. MOTIF 157 168 LD motif 3. MOTIF 203 215 LD motif 4
Mutation	60 60 Y->F: Prevents phosphorylation by FAK2 and FYN 287 287 C->A: Abolishes interaction with CBLC and enhancement of CBLC E3 ubiquitin-protein ligase activity 313 313 C->A: No effect on interaction with CBLC 338 342 FLQLF->ALQAA: Loss of interaction with AR when associated with 456-A--A-460 369 369 C->S: Loss of AR coactivation when associated with S-372 372 372 C->S: Loss of AR coactivation when associated with S-369 428 428 H->S: Loss of AR coactivation when associated with S-431 431 431 C->S: Loss of AR coactivation when associated with S-428 456 460 FLKLF->ALKAA: Loss of interaction with AR when associated with 338-A--A-342