This SAM (sterile alpha motif) domain repeat 2 of ANKS1 (also known as AIDA-1) is a protein-protein interaction domain.Proteins contain this domain include ANKS1A (also known as Odin) and ANKS1B (also known as AIDA-1 or EB-1). ANKS1A modulates EGF receptor recycling and stability []. ANKS1B may participate in the regulation of nucleoplasmic coilin protein interactions []. Structurally, ANKS1 consist of N-terminal ankyrin motifs followed by two tandem sterile alpha motif (SAM) domains and a carboxyl phosphotyrosine binding (PTB) domain []. SAM domains of ANKS1 can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor []. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. The second SAM domain may decouple from the first SAM domain to facilitate translocation of AIDA-1 to the nucleus [].
This SAM (sterile alpha motif) domain repeat 1 of ANKS1 (also known as AIDA-1) is a protein-protein interaction domain.Proteins contain this domain include ANKS1A (also known as Odin) and ANKS1B (also known as AIDA-1 or EB-1). ANKS1A modulates EGF receptor recycling and stability []. ANKS1B may participate in the regulation of nucleoplasmic coilin protein interactions []. Structurally, ANKS1 consist of N-terminal ankyrin motifs followed by two tandem sterile alpha motif (SAM) domains and a carboxyl phosphotyrosine binding (PTB) domain []. SAM domains of ANKS1 can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor []. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. The second SAM domain may decouple from the first SAM domain to facilitate translocation of AIDA-1 to the nucleus [].
