UniProt functional annotation for P29350



	UniProt functional annotation for P29350

UniProt code: P29350.

Organism: Homo sapiens (Human).

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

Function: Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis. {ECO:0000269|PubMed:11266449}.

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:0000255|PROSITE- ProRule:PRU10044};

Subunit: Monomer. Interacts with MTUS1 (By similarity). Interacts with MILR1 (tyrosine-phosphorylated) (By similarity). Interacts with KIT (By similarity). Interacts with SIRPA/PTPNS1 (PubMed:9712903). Interacts with LILRB1 and LILRB2 (PubMed:9285411, PubMed:9842885). Interacts with FCRL2 and FCRL4 (PubMed:11162587, PubMed:14597715). Interacts with FCRL3 and FCRL6 (tyrosine phosphorylated form) (PubMed:20933011, PubMed:11162587, PubMed:19843936). Interacts with CD84 (PubMed:11414741). Interacts with CD300LF (PubMed:15184070). Interacts with CDK2 (PubMed:21262353). Interacts with KIR2DL1; the interaction is enhanced by ARRB2 (PubMed:18604210). Interacts (via SH2 1 domain) with ROS1; the interaction is direct and promotes ROS1 dephosphorylation (PubMed:11266449). Interacts with EGFR; inhibits EGFR-dependent activation of MAPK/ERK (PubMed:21258366). Interacts with LYN (PubMed:10574931). Interacts with the tyrosine phosphorylated form of PDPK1 (PubMed:19591923). Interacts with CEACAM1 (via cytoplasmic domain); this interaction depends on the monomer/dimer equilibrium and is phosphorylation-dependent (By similarity). Interacts with MPIG6B (via ITIM motif) (PubMed:23112346). Interacts with moesin/MSN. {ECO:0000250|UniProtKB:P29351, ECO:0000250|UniProtKB:P81718, ECO:0000269|PubMed:10574931, ECO:0000269|PubMed:11162587, ECO:0000269|PubMed:11266449, ECO:0000269|PubMed:11414741, ECO:0000269|PubMed:14597715, ECO:0000269|PubMed:15184070, ECO:0000269|PubMed:18604210, ECO:0000269|PubMed:19591923, ECO:0000269|PubMed:19843936, ECO:0000269|PubMed:20933011, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:23112346, ECO:0000269|PubMed:9285411, ECO:0000269|PubMed:9712903, ECO:0000269|PubMed:9842885}.

Subcellular location: Cytoplasm. Nucleus. Note=In neurons, translocates into the nucleus after treatment with angiotensin II (By similarity). Shuttles between the cytoplasm and nucleus via its association with PDPK1. {ECO:0000250}.

Tissue specificity: Isoform 1 is expressed in hematopoietic cells. Isoform 2 is expressed in non-hematopoietic cells.

Domain: The N-terminal SH2 domain functions as an auto-inhibitory domain, blocking the catalytic domain in the ligand-free close conformation. {ECO:0000269|PubMed:12482860, ECO:0000269|PubMed:21465528}.

Ptm: Phosphorylated on tyrosine residues. Binding of KITLG/SCF to KIT increases tyrosine phosphorylation (By similarity). Phosphorylation at Tyr-564 enhances phosphatase activity. {ECO:0000250, ECO:0000269|PubMed:10574931, ECO:0000269|PubMed:7781604}.

Similarity: Belongs to the protein-tyrosine phosphatase family. Non- receptor class 2 subfamily. {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:		Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis. {ECO:0000269\|PubMed:11266449}.


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:0000255\|PROSITE- ProRule:PRU10044};
Subunit:		Monomer. Interacts with MTUS1 (By similarity). Interacts with MILR1 (tyrosine-phosphorylated) (By similarity). Interacts with KIT (By similarity). Interacts with SIRPA/PTPNS1 (PubMed:9712903). Interacts with LILRB1 and LILRB2 (PubMed:9285411, PubMed:9842885). Interacts with FCRL2 and FCRL4 (PubMed:11162587, PubMed:14597715). Interacts with FCRL3 and FCRL6 (tyrosine phosphorylated form) (PubMed:20933011, PubMed:11162587, PubMed:19843936). Interacts with CD84 (PubMed:11414741). Interacts with CD300LF (PubMed:15184070). Interacts with CDK2 (PubMed:21262353). Interacts with KIR2DL1; the interaction is enhanced by ARRB2 (PubMed:18604210). Interacts (via SH2 1 domain) with ROS1; the interaction is direct and promotes ROS1 dephosphorylation (PubMed:11266449). Interacts with EGFR; inhibits EGFR-dependent activation of MAPK/ERK (PubMed:21258366). Interacts with LYN (PubMed:10574931). Interacts with the tyrosine phosphorylated form of PDPK1 (PubMed:19591923). Interacts with CEACAM1 (via cytoplasmic domain); this interaction depends on the monomer/dimer equilibrium and is phosphorylation-dependent (By similarity). Interacts with MPIG6B (via ITIM motif) (PubMed:23112346). Interacts with moesin/MSN. {ECO:0000250\|UniProtKB:P29351, ECO:0000250\|UniProtKB:P81718, ECO:0000269\|PubMed:10574931, ECO:0000269\|PubMed:11162587, ECO:0000269\|PubMed:11266449, ECO:0000269\|PubMed:11414741, ECO:0000269\|PubMed:14597715, ECO:0000269\|PubMed:15184070, ECO:0000269\|PubMed:18604210, ECO:0000269\|PubMed:19591923, ECO:0000269\|PubMed:19843936, ECO:0000269\|PubMed:20933011, ECO:0000269\|PubMed:21258366, ECO:0000269\|PubMed:21262353, ECO:0000269\|PubMed:23112346, ECO:0000269\|PubMed:9285411, ECO:0000269\|PubMed:9712903, ECO:0000269\|PubMed:9842885}.
Subcellular location:		Cytoplasm. Nucleus. Note=In neurons, translocates into the nucleus after treatment with angiotensin II (By similarity). Shuttles between the cytoplasm and nucleus via its association with PDPK1. {ECO:0000250}.
Tissue specificity:		Isoform 1 is expressed in hematopoietic cells. Isoform 2 is expressed in non-hematopoietic cells.
Domain:		The N-terminal SH2 domain functions as an auto-inhibitory domain, blocking the catalytic domain in the ligand-free close conformation. {ECO:0000269\|PubMed:12482860, ECO:0000269\|PubMed:21465528}.
Ptm:		Phosphorylated on tyrosine residues. Binding of KITLG/SCF to KIT increases tyrosine phosphorylation (By similarity). Phosphorylation at Tyr-564 enhances phosphatase activity. {ECO:0000250, ECO:0000269\|PubMed:10574931, ECO:0000269\|PubMed:7781604}.
Similarity:		Belongs to the protein-tyrosine phosphatase family. Non- receptor class 2 subfamily. {ECO:0000305}.