O35324
uniprot
O35324
canonical
amino_acid_sequence
MDLPYYHGCLTKRECEALLLKGGVDGNFLIRDSESVPGALCLCVSFKKLVYSYRIFREKHGYYRIETDAHTPRTIFPNLQELVSKYGKPGQGLVVHLSNPIMRNNLCQRGRRMELELNVYENTDEEYVDVLP
uniprot
proteins
function
FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as CD84, SLAMF1, LY9 and CD244. In SLAM signaling seems to cooperate with SH2D1A/SAP. Plays a role in regulation of effector functions of natural killer (NK) cells by controlling signal transduction through CD244/2B4. However, conflicting results are reported which may reflect the use of different strain backgrounds. Proposed to act as an inhibitor of CD244-mediated NK cell function including cytotoxicity and IFN-gamma production, the latter found also by triggering KLRA4 and KLRK1 next to CD244 (PubMed:16127454). Seems to positively regulate CD244- and CD84-dependent NK cell functions implicating CD244-mediated phosphorylation of VAV1. Activation of SLAMF7-mediated NK cell function does not effect receptor tyrosine phosphorylation but distal signaling (PubMed:19151721, PubMed:20962259, PubMed:24687958). In the context of NK cell-mediated cytotoxicity does not enhance conjugate formation with target cells but stimulates polarization of the microtubule-organizing center and cytotoxic granules toward the NK cell synapse (PubMed:24687958). Negatively regulates CD40-induced cytokine production in dendritic cells downstream of SLAM family receptors probably by inducing activation of the PI3K pathway to inhibit p38 MAPK and JNK activation (PubMed:26432891). {ECO:0000250|UniProtKB:O14796, ECO:0000269|PubMed:16127454, ECO:0000269|PubMed:19151721, ECO:0000269|PubMed:20962259, ECO:0000269|PubMed:24687958, ECO:0000269|PubMed:26432891}.
uniprot
proteins
mass_dalton
15259
uniprot
proteins
mutagenesis
MUTAGEN 120; /note="Y->F: Abolishes tyrosine phosphorylation, no effect on interaction with SLAMF7 and CD244, abolishes SLAMF7-, CD244-, LY9- and CD8 mediated NK cell activation, fails to inhibit natural cytotoxicity and to suppress IFN-gamma secretion in response to ligation with CD244, FCGR3 or KLRB1C; when associated with F-127."; /evidence="ECO:0000269|PubMed:16127454, ECO:0000269|PubMed:19151721, ECO:0000269|PubMed:24687958"; MUTAGEN 127; /note="Y->F: Abolishes tyrosine phosphorylation, no effect on interaction with SLAMF7 and CD244, abolishes SLAMF7-, CD244-, LY9- and CD84-mediated NK cell activation, fails to inhibit natural cytotoxicity and to suppress IFN-gamma secretion in response to ligation with CD244, FCGR3 or KLRB1C; when associated with F-120."; /evidence="ECO:0000269|PubMed:16127454, ECO:0000269|PubMed:19151721, ECO:0000269|PubMed:24687958"; MUTAGEN 127; /note="Y->F: No stimulation of granule polarization during NK-mediated cytotoxicity."; /evidence="ECO:0000269|PubMed:24687958
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues; probably at Tyr-120 and/or Tyr-127. {ECO:0000269|PubMed:16127454}.
uniprot
proteins
pubmed
11689425
uniprot
proteins
pubmed
16127454
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16425036
uniprot
proteins
pubmed
19151721
uniprot
proteins
pubmed
20962259
uniprot
proteins
pubmed
21219180
uniprot
proteins
pubmed
24687958
uniprot
proteins
pubmed
26432891
uniprot
proteins
pubmed
9000139
uniprot
proteins
sequence_length
132
uniprot
proteins