UniProt functional annotation for Q12923



	UniProt functional annotation for Q12923

UniProt code: Q12923.

Organism: Homo sapiens (Human).

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

Function: Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling (PubMed:15611135). May regulate phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of PIK3R2 (PubMed:23604317). {ECO:0000269|PubMed:15611135, ECO:0000269|PubMed:23604317}.

Catalytic activity: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:15611135, ECO:0000269|PubMed:19307596};

Subunit: Interacts (via the first PDZ domain) with PLEKHA1 and PLEKHA2 (PubMed:14516276). Interacts (via the second PDZ domain) with TNFRSF6 (Fas receptor) (via C-terminus) (PubMed:10704206). Interacts (via the second PDZ domain) with TRIP6 (via the third LIM domain and C-terminus) (PubMed:10826496, PubMed:10400701). Interacts (via the third PDZ domain) with NGFR (via C-terminal SVP motif) and PKN2 (via C-terminus) (PubMed:10544233, PubMed:11356191). Interacts (via the second or fourth PDZ domains) with PDLIM4 (via C-terminus only or via combined C- terminus and LIM domain, but not LIM domain only). Found in a complex with PDLIM4 and TRIP6 (By similarity). Interacts with PDLIM4; this interaction results in dephosphorylation of SRC 'Tyr-419' by this protein leading to its inactivation (PubMed:19307596). Interacts with BRD7 (By similarity). Interacts with RAPGEF6 (PubMed:12095257). Interacts with ARHGAP29 (PubMed:9305890). Interacts with PIK3R2; dephosphorylates PIK3R2 (PubMed:23604317). Interacts with FBXL2 (PubMed:23604317). Interacts (via the FERM domain) with ENTR1 (PubMed:23108400). Found in a complex with ENTR1, PTPN13 and GIT1 (PubMed:23108400). {ECO:0000250|UniProtKB:Q64512, ECO:0000269|PubMed:10400701, ECO:0000269|PubMed:10544233, ECO:0000269|PubMed:10704206, ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:11356191, ECO:0000269|PubMed:12095257, ECO:0000269|PubMed:14516276, ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:23604317, ECO:0000269|PubMed:9305890}.

Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11356191}. Nucleus {ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:11356191}. Cell projection, lamellipodium {ECO:0000269|PubMed:11356191}. Note=Colocalizes with F-actin (PubMed:10826496). Colocalizes with PKN2 in lamellipodia-like structure, regions of large actin turnover (PubMed:11356191). {ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:11356191}.

Tissue specificity: Expressed in keratinocytes (at protein level) (PubMed:29043977). Present in most tissues with the exception of the liver and skeletal muscle. Most abundant in lung, kidney and fetal brain. {ECO:0000269|PubMed:29043977}.

Miscellaneous: [Isoform 4]: May be due to a competing donor splice site. {ECO:0000305}.

Similarity: Belongs to the protein-tyrosine phosphatase family. Non- receptor class subfamily. {ECO:0000305}.

Sequence caution: Sequence=AAH39610.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; 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:		Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling (PubMed:15611135). May regulate phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of PIK3R2 (PubMed:23604317). {ECO:0000269\|PubMed:15611135, ECO:0000269\|PubMed:23604317}.


Catalytic activity:		Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269\|PubMed:15611135, ECO:0000269\|PubMed:19307596};
Subunit:		Interacts (via the first PDZ domain) with PLEKHA1 and PLEKHA2 (PubMed:14516276). Interacts (via the second PDZ domain) with TNFRSF6 (Fas receptor) (via C-terminus) (PubMed:10704206). Interacts (via the second PDZ domain) with TRIP6 (via the third LIM domain and C-terminus) (PubMed:10826496, PubMed:10400701). Interacts (via the third PDZ domain) with NGFR (via C-terminal SVP motif) and PKN2 (via C-terminus) (PubMed:10544233, PubMed:11356191). Interacts (via the second or fourth PDZ domains) with PDLIM4 (via C-terminus only or via combined C- terminus and LIM domain, but not LIM domain only). Found in a complex with PDLIM4 and TRIP6 (By similarity). Interacts with PDLIM4; this interaction results in dephosphorylation of SRC 'Tyr-419' by this protein leading to its inactivation (PubMed:19307596). Interacts with BRD7 (By similarity). Interacts with RAPGEF6 (PubMed:12095257). Interacts with ARHGAP29 (PubMed:9305890). Interacts with PIK3R2; dephosphorylates PIK3R2 (PubMed:23604317). Interacts with FBXL2 (PubMed:23604317). Interacts (via the FERM domain) with ENTR1 (PubMed:23108400). Found in a complex with ENTR1, PTPN13 and GIT1 (PubMed:23108400). {ECO:0000250\|UniProtKB:Q64512, ECO:0000269\|PubMed:10400701, ECO:0000269\|PubMed:10544233, ECO:0000269\|PubMed:10704206, ECO:0000269\|PubMed:10826496, ECO:0000269\|PubMed:11356191, ECO:0000269\|PubMed:12095257, ECO:0000269\|PubMed:14516276, ECO:0000269\|PubMed:19307596, ECO:0000269\|PubMed:23108400, ECO:0000269\|PubMed:23604317, ECO:0000269\|PubMed:9305890}.
Subcellular location:		Cytoplasm, cytoskeleton {ECO:0000269\|PubMed:11356191}. Nucleus {ECO:0000269\|PubMed:10826496, ECO:0000269\|PubMed:11356191}. Cell projection, lamellipodium {ECO:0000269\|PubMed:11356191}. Note=Colocalizes with F-actin (PubMed:10826496). Colocalizes with PKN2 in lamellipodia-like structure, regions of large actin turnover (PubMed:11356191). {ECO:0000269\|PubMed:10826496, ECO:0000269\|PubMed:11356191}.
Tissue specificity:		Expressed in keratinocytes (at protein level) (PubMed:29043977). Present in most tissues with the exception of the liver and skeletal muscle. Most abundant in lung, kidney and fetal brain. {ECO:0000269\|PubMed:29043977}.
Miscellaneous:		[Isoform 4]: May be due to a competing donor splice site. {ECO:0000305}.
Similarity:		Belongs to the protein-tyrosine phosphatase family. Non- receptor class subfamily. {ECO:0000305}.
Sequence caution:		Sequence=AAH39610.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};