CD84
entrez
8832
canonical
uniprot
Q9UIB8
canonical
ensembl
ENSG00000066294
resolver
ensp
ENSP00000312367
resolver
ensp
ENSP00000357027
resolver
ensp
ENSP00000357030
resolver
ensp
ENSP00000357033
resolver
ensp
ENSP00000442845
resolver
genesymbol
CD84
resolver
genesymbol_syn
SLAMF5
resolver
hgnc
HGNC:1704
resolver
uniprot
B2R8T1
resolver
uniprot
B7Z3R8
resolver
uniprot
O15430
resolver
uniprot
O95266
resolver
uniprot
O95660
resolver
uniprot
Q5H9R1
resolver
uniprot
Q6FHA8
resolver
uniprot
Q8WLP1
resolver
uniprot
Q8WWI8
resolver
uniprot
Q9UF04
resolver
uniprot
Q9UIB6
resolver
uniprot
Q9UIB7
resolver
uniprot
Q9UIT7
resolver
uniprot_entry
SLAF5_HUMAN
resolver
uniprot_sec
B2R8T1
resolver
uniprot_sec
B7Z3R8
resolver
uniprot_sec
O15430
resolver
uniprot_sec
O95266
resolver
uniprot_sec
O95660
resolver
uniprot_sec
Q5H9R1
resolver
uniprot_sec
Q6FHA8
resolver
uniprot_sec
Q8WLP1
resolver
uniprot_sec
Q8WWI8
resolver
uniprot_sec
Q9UF04
resolver
uniprot_sec
Q9UIB6
resolver
uniprot_sec
Q9UIB7
resolver
uniprot_sec
Q9UIT7
resolver
amino_acid_sequence
MAQHHLWILLLCLQTWPEAAGKDSEIFTVNGILGESVTFPVNIQEPRQVKIIAWTSKTSVAYVTPGDSETAPVVTVTHRNYYERIHALGPNYNLVISDLRMEDAGDYKADINTQADPYTTTKRYNLQIYRRLGKPKITQSLMASVNSTCNVTLTCSVEKEEKNVTYNWSPLGEEGNVLQIFQTPEDQELTYTCTAQNPVSNNSDSISARQLCADIAMGFRTHHTGLLSVLAMFFLLVLILSSVFLFRLFKRRQGRIFPEGSCLNTFTKNPYAASKKTIYTYIMASRNTQPAESRIYDEILQSKVLPSKEEPVNTVYSEVQFADKMGKASTQDSKPPGTSSYEIVI
uniprot
proteins
function
FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Can mediate natural killer (NK) cell cytotoxicity dependent on SH2D1A and SH2D1B (By similarity). Increases proliferative responses of activated T-cells and SH2D1A/SAP does not seem be required for this process. Homophilic interactions enhance interferon gamma/IFNG secretion in lymphocytes and induce platelet stimulation via a SH2D1A-dependent pathway. May serve as a marker for hematopoietic progenitor cells (PubMed:11564780, PubMed:12115647, PubMed:12928397, PubMed:12962726, PubMed:16037392) Required for a prolonged T-cell:B-cell contact, optimal T follicular helper function, and germinal center formation. In germinal centers involved in maintaining B-cell tolerance and in preventing autoimmunity (By similarity). In mast cells negatively regulates high affinity immunoglobulin epsilon receptor signaling; independent of SH2D1A and SH2D1B but implicating FES and PTPN6/SHP-1 (PubMed:22068234). In macrophages enhances LPS-induced MAPK phosphorylation and NF-kappaB activation and modulates LPS-induced cytokine secretion; involving ITSM 2 (By similarity). Positively regulates macroautophagy in primary dendritic cells via stabilization of IRF8; inhibits TRIM21-mediated proteasomal degradation of IRF8 (PubMed:29434592). {ECO:0000250|UniProtKB:Q18PI6, ECO:0000269|PubMed:11564780, ECO:0000269|PubMed:12115647, ECO:0000269|PubMed:12928397, ECO:0000269|PubMed:12962726, ECO:0000269|PubMed:16037392, ECO:0000269|PubMed:22068234, ECO:0000269|PubMed:29434592, ECO:0000305}.
uniprot
proteins
mass_dalton
38782
uniprot
proteins
mutagenesis
MUTAGEN 55; /note="T->A: Loss of dimerization."; /evidence="ECO:0000269|PubMed:17563375"; MUTAGEN 62; /note="Y->A: No effect."; /evidence="ECO:0000269|PubMed:17563375"; MUTAGEN 62; /note="Y->D: Loss of dimerization."; /evidence="ECO:0000269|PubMed:17563375"; MUTAGEN 77; /note="T->A: Loss of dimerization."; /evidence="ECO:0000269|PubMed:17563375"; MUTAGEN 78; /note="H->A: Loss of dimerization."; /evidence="ECO:0000269|PubMed:17563375"; MUTAGEN 110; /note="D->A: Loss of dimerization."; /evidence="ECO:0000269|PubMed:17563375"; MUTAGEN 112; /note="N->A: Loss of dimerization."; /evidence="ECO:0000269|PubMed:17563375"; MUTAGEN 119; /note="T->A: Loss of dimerization."; /evidence="ECO:0000269|PubMed:17563375"; MUTAGEN 279; /note="Y->F: Reduced tyrosine phosphorylation, reduced binding of SH2D1B and loss of binding of SH2D1A."; /evidence="ECO:0000269|PubMed:12928397"; MUTAGEN 316; /note="Y->F: Reduced tyrosine phosphorylation and reduced binding of SH2D1B. Loss of phosphorylation and loss of binding of SH2D1A and SH2D1B; when associated with F-279."; /evidence="ECO:0000269|PubMed:12928397
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by tyrosine-protein kinase LCK on tyrosine residues following ligation induced by agonist monoclonal antibody. The association with SH2D1A is dependent of tyrosine phosphorylation of its cytoplasmic domain. Phosphorylated on Tyr-296 and Tyr-316 following platelet aggregation. Phosphorylated on tyrosine residues upon high affinity immunoglobulin epsilon receptor aggregation in mast cells. {ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:12115647, ECO:0000269|PubMed:12928397, ECO:0000269|PubMed:16037392, ECO:0000269|PubMed:22068234}.; PTM: N-glycosylated. {ECO:0000269|PubMed:10698700, ECO:0000269|PubMed:9310491}.
uniprot
proteins
pubmed
10698700
uniprot
proteins
pubmed
10746783
uniprot
proteins
pubmed
11313386
uniprot
proteins
pubmed
11389028
uniprot
proteins
pubmed
11414741
uniprot
proteins
pubmed
11564780
uniprot
proteins
pubmed
12115647
uniprot
proteins
pubmed
12458214
uniprot
proteins
pubmed
12928397
uniprot
proteins
pubmed
12962726
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15245368
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16037392
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17563375
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
22068234
uniprot
proteins
pubmed
29434592
uniprot
proteins
pubmed
9310491
uniprot
proteins
sequence_length
345
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:12962726}; Single-pass type I membrane protein {ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:12962726}.
uniprot
proteins
transmembrane_region
TRANSMEM 226..246; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins