UniProt functional annotation for P49023



	UniProt functional annotation for P49023

UniProt code: P49023.

Organism: Homo sapiens (Human).

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

Function: Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).

Subunit: Interacts in vitro with VCL/vinculin as well as to the SH3 domain of SRC and, when tyrosine phosphorylated, to the SH2 domain of CRK (PubMed:7534286). Interacts with GIT1 (PubMed:10938112). Interacts with NUDT16L1/SDOS (By similarity). Interacts with PTK2/FAK1 (PubMed:14527389). Interacts with PTK2B/PYK2 (PubMed:19358827). Interacts with ASAP2 (PubMed:10749932). Interacts with unphosphorylated ITGA4 (PubMed:10604475). Interacts with RNF5 (PubMed:12861019). Interacts with PDCD10 (PubMed:20489202). Interacts with NEK3, the interaction is prolactin-dependent (PubMed:17297458). Interacts with PTK6 (PubMed:15572663). Interacts with TGFB1I1 (By similarity). Interacts with SORBS1 (PubMed:17462669). Interacts with PARVB (PubMed:22869380). Interacts (via LD motif 4) with PARVA/PARVIN (PubMed:15817463, PubMed:18508764, PubMed:18940607). Interacts (via LD motif 4) with ILK (PubMed:15817463, PubMed:18508764, PubMed:18940607). Interacts (via cytoplasmic domain) with CEACAM1; the interaction is phosphotyrosyl-dependent (PubMed:11035932). Interacts with LIMA1; this complex stabilizes actin dynamics (PubMed:24694988). Interacts with CD36 (via C-terminus) (PubMed:20037584). {ECO:0000250|UniProtKB:Q66H76, ECO:0000250|UniProtKB:Q8VI36, ECO:0000269|PubMed:10604475, ECO:0000269|PubMed:10749932, ECO:0000269|PubMed:10938112, ECO:0000269|PubMed:11035932, ECO:0000269|PubMed:12861019, ECO:0000269|PubMed:14527389, ECO:0000269|PubMed:15572663, ECO:0000269|PubMed:15817463, ECO:0000269|PubMed:17297458, ECO:0000269|PubMed:17462669, ECO:0000269|PubMed:18508764, ECO:0000269|PubMed:18940607, ECO:0000269|PubMed:19358827, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:20489202, ECO:0000269|PubMed:22869380, ECO:0000269|PubMed:24694988, ECO:0000269|PubMed:7534286}.

Subunit: [Isoform Beta]: Interacts strongly with PTK2/FAK1 and weakly with VCL/vinculin. {ECO:0000269|PubMed:9054445}.

Subunit: [Isoform Gamma]: Interacts strongly with VCL/vinculin but only weakly with PTK2/FAK1. {ECO:0000269|PubMed:9054445}.

Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20489202}. Cell junction, focal adhesion {ECO:0000269|PubMed:20489202, ECO:0000269|PubMed:23128389}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q8VI36}. Note=Colocalizes with integrins at the cell periphery. Colocalize with PXN to membrane ruffles and the leading edge of migrating cells (PubMed:23128389). {ECO:0000250, ECO:0000269|PubMed:23128389}.

Ptm: Phosphorylated by MAPK1/ERK2 (By similarity). Phosphorylated on tyrosine residues during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens. Phosphorylation at Ser-244 by CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation. Phosphorylation at Tyr-31 and Tyr-118 by PTK6 promote the activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion. Phosphorylation at Ser-250 by SLK is required for PXN redistribution and cell motility (PubMed:23128389). {ECO:0000250, ECO:0000269|PubMed:11774284, ECO:0000269|PubMed:15572663, ECO:0000269|PubMed:18042622, ECO:0000269|PubMed:23128389}.

Similarity: Belongs to the paxillin family. {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:		Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).


Subunit:		Interacts in vitro with VCL/vinculin as well as to the SH3 domain of SRC and, when tyrosine phosphorylated, to the SH2 domain of CRK (PubMed:7534286). Interacts with GIT1 (PubMed:10938112). Interacts with NUDT16L1/SDOS (By similarity). Interacts with PTK2/FAK1 (PubMed:14527389). Interacts with PTK2B/PYK2 (PubMed:19358827). Interacts with ASAP2 (PubMed:10749932). Interacts with unphosphorylated ITGA4 (PubMed:10604475). Interacts with RNF5 (PubMed:12861019). Interacts with PDCD10 (PubMed:20489202). Interacts with NEK3, the interaction is prolactin-dependent (PubMed:17297458). Interacts with PTK6 (PubMed:15572663). Interacts with TGFB1I1 (By similarity). Interacts with SORBS1 (PubMed:17462669). Interacts with PARVB (PubMed:22869380). Interacts (via LD motif 4) with PARVA/PARVIN (PubMed:15817463, PubMed:18508764, PubMed:18940607). Interacts (via LD motif 4) with ILK (PubMed:15817463, PubMed:18508764, PubMed:18940607). Interacts (via cytoplasmic domain) with CEACAM1; the interaction is phosphotyrosyl-dependent (PubMed:11035932). Interacts with LIMA1; this complex stabilizes actin dynamics (PubMed:24694988). Interacts with CD36 (via C-terminus) (PubMed:20037584). {ECO:0000250\|UniProtKB:Q66H76, ECO:0000250\|UniProtKB:Q8VI36, ECO:0000269\|PubMed:10604475, ECO:0000269\|PubMed:10749932, ECO:0000269\|PubMed:10938112, ECO:0000269\|PubMed:11035932, ECO:0000269\|PubMed:12861019, ECO:0000269\|PubMed:14527389, ECO:0000269\|PubMed:15572663, ECO:0000269\|PubMed:15817463, ECO:0000269\|PubMed:17297458, ECO:0000269\|PubMed:17462669, ECO:0000269\|PubMed:18508764, ECO:0000269\|PubMed:18940607, ECO:0000269\|PubMed:19358827, ECO:0000269\|PubMed:20037584, ECO:0000269\|PubMed:20489202, ECO:0000269\|PubMed:22869380, ECO:0000269\|PubMed:24694988, ECO:0000269\|PubMed:7534286}.
Subunit:		[Isoform Beta]: Interacts strongly with PTK2/FAK1 and weakly with VCL/vinculin. {ECO:0000269\|PubMed:9054445}.
Subunit:		[Isoform Gamma]: Interacts strongly with VCL/vinculin but only weakly with PTK2/FAK1. {ECO:0000269\|PubMed:9054445}.
Subcellular location:		Cytoplasm, cytoskeleton {ECO:0000269\|PubMed:20489202}. Cell junction, focal adhesion {ECO:0000269\|PubMed:20489202, ECO:0000269\|PubMed:23128389}. Cytoplasm, cell cortex {ECO:0000250\|UniProtKB:Q8VI36}. Note=Colocalizes with integrins at the cell periphery. Colocalize with PXN to membrane ruffles and the leading edge of migrating cells (PubMed:23128389). {ECO:0000250, ECO:0000269\|PubMed:23128389}.
Ptm:		Phosphorylated by MAPK1/ERK2 (By similarity). Phosphorylated on tyrosine residues during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens. Phosphorylation at Ser-244 by CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation. Phosphorylation at Tyr-31 and Tyr-118 by PTK6 promote the activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion. Phosphorylation at Ser-250 by SLK is required for PXN redistribution and cell motility (PubMed:23128389). {ECO:0000250, ECO:0000269\|PubMed:11774284, ECO:0000269\|PubMed:15572663, ECO:0000269\|PubMed:18042622, ECO:0000269\|PubMed:23128389}.
Similarity:		Belongs to the paxillin family. {ECO:0000305}.