UniProt functional annotation for Q15654



	UniProt functional annotation for Q15654

UniProt code: Q15654.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF- kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor. {ECO:0000269|PubMed:14688263, ECO:0000269|PubMed:15489293, ECO:0000269|PubMed:16624523, ECO:0000269|PubMed:19017743}.

Subunit: Specifically interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone (PubMed:14688263). Interacts (via the third LIM domain and C-terminus) with PTPN13 (via the second PDZ domain) (PubMed:10400701, PubMed:17591779, PubMed:19017743, PubMed:10826496). Interacts (via the second LIM domain or via the third LIM domain plus C-terminus) with PDLIM4 (via PDZ domain) (PubMed:10826496). Found in a complex with PTPN13 and PDLIM4 (By similarity). Interacts with SVIL isoform 2 (PubMed:16880273). Interacts with LPAR2 but not other LPA receptors (PubMed:14688263). Interacts with PRKAA2 (PubMed:16624523). Interacts with MAGI1 (PubMed:19017743). Interacts with SCRIB (PubMed:16137684). In case of infection, interacts with S.typhimurium protein sseI (PubMed:17095609). {ECO:0000250|UniProtKB:Q9Z1Y4, ECO:0000269|PubMed:10400701, ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:14688263, ECO:0000269|PubMed:16137684, ECO:0000269|PubMed:16624523, ECO:0000269|PubMed:16880273, ECO:0000269|PubMed:17095609, ECO:0000269|PubMed:17591779, ECO:0000269|PubMed:19017743}.

Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16624523}. Cell junction, focal adhesion {ECO:0000269|PubMed:16624523}. Nucleus {ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:16624523}. Cytoplasm {ECO:0000269|PubMed:16624523}. Note=Shuttles between nucleus and cytoplasm (PubMed:16624523). Colocalizes with actin (PubMed:10826496). {ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:16624523}.

Tissue specificity: Abundantly expressed in kidney, liver and lung. Lower levels in heart, placenta and pancreas. Expressed in colonic epithelial cells. Up-regulated in colonic tumors. {ECO:0000269|PubMed:19017743}.

Domain: The LIM zinc-binding domains mediate interaction with LPAR2 and with S.typhimurium protein sseI.

Ptm: Phosphorylation at Tyr-55 by SRC is required for enhancement of lysophosphatidic acid-induced cell migration. Tyr-55 is dephosphorylated by PTPN13. {ECO:0000269|PubMed:15988003, ECO:0000269|PubMed:17591779}.

Similarity: Belongs to the zyxin/ajuba family. {ECO:0000305}.

Sequence caution: Sequence=AAC41740.1; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF- kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor. {ECO:0000269\|PubMed:14688263, ECO:0000269\|PubMed:15489293, ECO:0000269\|PubMed:16624523, ECO:0000269\|PubMed:19017743}.


Subunit:		Specifically interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone (PubMed:14688263). Interacts (via the third LIM domain and C-terminus) with PTPN13 (via the second PDZ domain) (PubMed:10400701, PubMed:17591779, PubMed:19017743, PubMed:10826496). Interacts (via the second LIM domain or via the third LIM domain plus C-terminus) with PDLIM4 (via PDZ domain) (PubMed:10826496). Found in a complex with PTPN13 and PDLIM4 (By similarity). Interacts with SVIL isoform 2 (PubMed:16880273). Interacts with LPAR2 but not other LPA receptors (PubMed:14688263). Interacts with PRKAA2 (PubMed:16624523). Interacts with MAGI1 (PubMed:19017743). Interacts with SCRIB (PubMed:16137684). In case of infection, interacts with S.typhimurium protein sseI (PubMed:17095609). {ECO:0000250\|UniProtKB:Q9Z1Y4, ECO:0000269\|PubMed:10400701, ECO:0000269\|PubMed:10826496, ECO:0000269\|PubMed:14688263, ECO:0000269\|PubMed:16137684, ECO:0000269\|PubMed:16624523, ECO:0000269\|PubMed:16880273, ECO:0000269\|PubMed:17095609, ECO:0000269\|PubMed:17591779, ECO:0000269\|PubMed:19017743}.
Subcellular location:		Cytoplasm, cytoskeleton {ECO:0000269\|PubMed:16624523}. Cell junction, focal adhesion {ECO:0000269\|PubMed:16624523}. Nucleus {ECO:0000269\|PubMed:10826496, ECO:0000269\|PubMed:16624523}. Cytoplasm {ECO:0000269\|PubMed:16624523}. Note=Shuttles between nucleus and cytoplasm (PubMed:16624523). Colocalizes with actin (PubMed:10826496). {ECO:0000269\|PubMed:10826496, ECO:0000269\|PubMed:16624523}.
Tissue specificity:		Abundantly expressed in kidney, liver and lung. Lower levels in heart, placenta and pancreas. Expressed in colonic epithelial cells. Up-regulated in colonic tumors. {ECO:0000269\|PubMed:19017743}.
Domain:		The LIM zinc-binding domains mediate interaction with LPAR2 and with S.typhimurium protein sseI.
Ptm:		Phosphorylation at Tyr-55 by SRC is required for enhancement of lysophosphatidic acid-induced cell migration. Tyr-55 is dephosphorylated by PTPN13. {ECO:0000269\|PubMed:15988003, ECO:0000269\|PubMed:17591779}.
Similarity:		Belongs to the zyxin/ajuba family. {ECO:0000305}.
Sequence caution:		Sequence=AAC41740.1; Type=Frameshift; Evidence={ECO:0000305};