UniProt functional annotation for Q9Z200



	UniProt functional annotation for Q9Z200

UniProt code: Q9Z200.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

Function: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis (By similarity). Involved in stimulation of glucose uptake by insulin. Involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Induces cytoskeletal reorganization and neurite outgrowth in cultured neurons. {ECO:0000250, ECO:0000269|PubMed:10854852, ECO:0000269|PubMed:11997497, ECO:0000269|PubMed:15031295, ECO:0000269|PubMed:9856458}.

Subunit: Homodimer. Interacts with KIT/c-KIT, SHC1, EPOR, PDGFR, VAV1 and VAV3. Interacts (via N-terminal region) with SHC1. Interacts (via the phosphorylated C-terminus) with GRB2. Interacts (via its SH2 domain) with EPOR, INSR and KIT. Interacts with GRB2 after B-cell antigen receptor stimulation. Interacts (via PH domain) with VAV3 (By similarity). Interacts with NTRK1, NTRK2 and NTRK3 (phosphorylated); after stimulation of the receptor by its extracellular ligand and subsequent autophosphorylation of the receptor. Binds INSR, GRB2, ASB6 and CAP. Insulin stimulation leads to dissociation of CAP. Binds CBS only when SH2B2/APS has become phosphorylated. INSR binding does not depend on the phosphorylation of SH2B2/APS. {ECO:0000250, ECO:0000269|PubMed:10854852, ECO:0000269|PubMed:11997497, ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:15031295, ECO:0000269|PubMed:15231829, ECO:0000269|PubMed:9856458}.

Subcellular location: Cytoplasm. Membrane. Note=Recruited to the membrane by binding to an autophosphorylated receptor after receptor stimulation by its extracellular ligand.

Tissue specificity: Detected in embryonic brain, spinal cord and cortical neurons. {ECO:0000269|PubMed:9856458}.

Ptm: Phosphorylated on a tyrosine residue by NTRK1, NTRK2, NTRK3 and INSR after stimulation of the receptor by its extracellular ligand. Tyrosine phosphorylated by JAK2, KIT and other kinases activated by B- cell receptor in response to stimulation with cytokines, IL3, IL5, PDGF, IGF1, IGF2, CSF2/GM-CSF and cross-linking of the B-cell receptor complex (By similarity). {ECO:0000250}.

Similarity: Belongs to the SH2B adapter family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



Function:		Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis (By similarity). Involved in stimulation of glucose uptake by insulin. Involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Induces cytoskeletal reorganization and neurite outgrowth in cultured neurons. {ECO:0000250, ECO:0000269\|PubMed:10854852, ECO:0000269\|PubMed:11997497, ECO:0000269\|PubMed:15031295, ECO:0000269\|PubMed:9856458}.


Subunit:		Homodimer. Interacts with KIT/c-KIT, SHC1, EPOR, PDGFR, VAV1 and VAV3. Interacts (via N-terminal region) with SHC1. Interacts (via the phosphorylated C-terminus) with GRB2. Interacts (via its SH2 domain) with EPOR, INSR and KIT. Interacts with GRB2 after B-cell antigen receptor stimulation. Interacts (via PH domain) with VAV3 (By similarity). Interacts with NTRK1, NTRK2 and NTRK3 (phosphorylated); after stimulation of the receptor by its extracellular ligand and subsequent autophosphorylation of the receptor. Binds INSR, GRB2, ASB6 and CAP. Insulin stimulation leads to dissociation of CAP. Binds CBS only when SH2B2/APS has become phosphorylated. INSR binding does not depend on the phosphorylation of SH2B2/APS. {ECO:0000250, ECO:0000269\|PubMed:10854852, ECO:0000269\|PubMed:11997497, ECO:0000269\|PubMed:14690593, ECO:0000269\|PubMed:15031295, ECO:0000269\|PubMed:15231829, ECO:0000269\|PubMed:9856458}.
Subcellular location:		Cytoplasm. Membrane. Note=Recruited to the membrane by binding to an autophosphorylated receptor after receptor stimulation by its extracellular ligand.
Tissue specificity:		Detected in embryonic brain, spinal cord and cortical neurons. {ECO:0000269\|PubMed:9856458}.
Ptm:		Phosphorylated on a tyrosine residue by NTRK1, NTRK2, NTRK3 and INSR after stimulation of the receptor by its extracellular ligand. Tyrosine phosphorylated by JAK2, KIT and other kinases activated by B- cell receptor in response to stimulation with cytokines, IL3, IL5, PDGF, IGF1, IGF2, CSF2/GM-CSF and cross-linking of the B-cell receptor complex (By similarity). {ECO:0000250}.
Similarity:		Belongs to the SH2B adapter family. {ECO:0000305}.