SLAMF1
entrez
6504
canonical
uniprot
Q13291
canonical
ensembl
ENSG00000117090
resolver
ensp
ENSP00000306190
resolver
ensp
ENSP00000438406
resolver
ensp
ENSP00000548716
resolver
ensp
ENSP00000548717
resolver
ensp
ENSP00000647924
resolver
genesymbol
SLAMF1
resolver
genesymbol_syn
SLAM
resolver
hgnc
HGNC:10903
resolver
uniprot
B4E2E4
resolver
uniprot
Q5W172
resolver
uniprot
Q9HBE8
resolver
uniprot
W0HKK7
resolver
uniprot_entry
B4E2E4_HUMAN
resolver
uniprot_entry
SLAF1_HUMAN
resolver
uniprot_sec
Q5W172
resolver
uniprot_sec
Q9HBE8
resolver
uniprot_sec
W0HKK7
resolver
amino_acid_sequence
MDPKGLLSLTFVLFLSLAFGASYGTGGRMMNCPKILRQLGSKVLLPLTYERINKSMNKSIHIVVTMAKSLENSVENKIVSLDPSEAGPPRYLGDRYKFYLENLTLGIRESRKEDEGWYLMTLEKNVSVQRFCLQLRLYEQVSTPEIKVLNKTQENGTCTLILGCTVEKGDHVAYSWSEKAGTHPLNPANSSHLLSLTLGPQHADNIYICTVSNPISNNSQTFSPWPGCRTDPSETKPWAVYAGLLGGVIMILIMVVILQLRRRGKTNHYQTTVEKKSLTIYAQVQKPGPLQKKLDSFPAQDPCTTIYVAATEPVPESVQETNSITVYASVTLPES
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. SLAMF1-induced signal-transduction events in T-lymphocytes are different from those in B-cells. Two modes of SLAMF1 signaling seem to exist: one depending on SH2D1A (and perhaps SH2D1B) and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates. Initially it has been proposed that association with SH2D1A prevents binding to inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2 (PubMed:11806999). However, signaling is also regulated by SH2D1A which can simultaneously interact with and recruit FYN which subsequently phosphorylates and activates SLAMF1 (PubMed:12458214). Mediates IL-2-independent proliferation of activated T-cells during immune responses and induces IFN-gamma production (By similarity). Downstreaming signaling involves INPP5D, DOK1 and DOK2 leading to inhibited IFN-gamma production in T-cells, and PRKCQ, BCL10 and NFKB1 leading to increased T-cell activation and Th2 cytokine production (By similarity). Promotes T-cell receptor-induced IL-4 secretion by CD4(+) cells (By similarity). Inhibits antigen receptor-mediated production of IFN-gamma, but not IL-2, in CD4(-)/CD8(-) T-cells (By similarity). Required for IL-4 production by germinal centers T follicular helper (T(Fh))cells (By similarity). May inhibit CD40-induced signal transduction in monocyte-derived dendritic cells (PubMed:16317102). May play a role in allergic responses and may regulate allergen-induced Th2 cytokine and Th1 cytokine secretion (By similarity). In conjunction with SLAMF6 controls the transition between positive selection and the subsequent expansion and differentiation of the thymocytic natural killer T (NKT) cell lineage. Involved in the peripheral differentiation of indifferent natural killer T (iNKT) cells toward a regulatory NKT2 type (By similarity). In macrophages involved in down-regulation of IL-12, TNF and nitric oxide in response to lipopolysaccharide (LPS) (By similarity). In B-cells activates the ERK signaling pathway independently of SH2D1A but implicating both, SYK and INPP5D, and activates Akt signaling dependent on SYK and SH2D1A (By similarity). In B-cells also activates p38 MAPK and JNK1 and JNK2 (PubMed:20231852). In conjunction with CD84/SLAMF5 and SLAMF6 may be a negative regulator of the humoral immune response (By similarity). Involved in innate immune response against Gram-negative bacteria in macrophages; probably recognizes OmpC and/or OmpF on the bacterial surface, regulates phagosome maturation and recruitment of the PI3K complex II (PI3KC3-C2) leading to accumulation of PdtIns(3)P and NOX2 activity in the phagosomes (PubMed:20818396). {ECO:0000250|UniProtKB:Q9QUM4, ECO:0000269|PubMed:16317102, ECO:0000269|PubMed:20231852, ECO:0000269|PubMed:20818396, ECO:0000305|PubMed:11806999, ECO:0000305|PubMed:12458214}.; FUNCTION: (Microbial infection) Acts as a receptor for Measles virus; also including isoform 4. {ECO:0000269|PubMed:10972291, ECO:0000269|PubMed:21217702}.
uniprot
proteins
mass_dalton
37231
uniprot
proteins
mutagenesis
MUTAGEN 29; /note="M->S: Reduced infectivity."; /evidence="ECO:0000269|PubMed:32922371"; MUTAGEN 269; /note="Y->F: No effect on interaction with INPP5D/SHIP-1, PTPN11/SHP-2 and SH2D1A."; /evidence="ECO:0000269|PubMed:11313386"; MUTAGEN 279; /note="T->A: Disrupts interaction with SH2D1A; when associated with A-325."; /evidence="ECO:0000269|PubMed:11806999"; MUTAGEN 281; /note="Y->F: Disrupts interaction with INPP5D/SHIP-1 and PTPN11/SHP-2, no effect on interaction with SH2D1A."; /evidence="ECO:0000269|PubMed:11313386, ECO:0000269|PubMed:11806999"; MUTAGEN 281; /note="Y->F: Disrupts interaction with SH2D1A; when associated with F-327."; /evidence="ECO:0000269|PubMed:11806999"; MUTAGEN 307; /note="Y->F: No effect on interaction with PTPN11/SHP-2 and SH2D1A."; /evidence="ECO:0000269|PubMed:11313386"; MUTAGEN 325; /note="T->A: Disrupts interaction with SH2D1A; when associated with A-279."; /evidence="ECO:0000269|PubMed:11806999"; MUTAGEN 327; /note="Y->F: Disrupts interaction with INPP5D/SHIP-1 and PTPN11/SHP-2, no effect on interaction with SH2D1A."; /evidence="ECO:0000269|PubMed:11313386, ECO:0000269|PubMed:11806999"; MUTAGEN 327; /note="Y->F: Disrupts interaction with SH2D1A; when associated with F-281."; /evidence="ECO:0000269|PubMed:11806999
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues by FYN. {ECO:0000269|PubMed:11806999, ECO:0000269|PubMed:11823424}.
uniprot
proteins
pubmed
10229804
uniprot
proteins
pubmed
10972291
uniprot
proteins
pubmed
11313386
uniprot
proteins
pubmed
11689425
uniprot
proteins
pubmed
11806999
uniprot
proteins
pubmed
11823424
uniprot
proteins
pubmed
12458214
uniprot
proteins
pubmed
12545174
uniprot
proteins
pubmed
12629654
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16317102
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
20231852
uniprot
proteins
pubmed
20818396
uniprot
proteins
pubmed
21217702
uniprot
proteins
pubmed
25710480
uniprot
proteins
pubmed
32922371
uniprot
proteins
pubmed
7617038
uniprot
proteins
pubmed
9091591
uniprot
proteins
pubmed
9774102
uniprot
proteins
sequence_length
335
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11806999}; Single-pass type I membrane protein. Note=Present on the surface of B-cells and T-cells. Located at the plasma membrane contacts between neighboring T-cells (PubMed:11806999). {ECO:0000269|PubMed:11806999}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305|PubMed:7617038}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000305|PubMed:25710480}. Note=Overexpressed isoform 4 is detected on the cell surface. In glioma cell lines endogenous isoform 4 is detected predominantly in the cytoplasm and colocalized with endoplasmic reticulum and Golgi markers. {ECO:0000269|PubMed:25710480}.
uniprot
proteins
transmembrane_region
TRANSMEM 238..258; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins