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Protein

Signaling lymphocytic activation molecule

Gene

Slamf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). However, signaling is also regulated by SH2D1A which can simultaneously interact with and recruit FYN which subsequently phosphorylates and activates SLAMF1 (By similarity). Mediates IL-2-independent proliferation of activated T-cells during immune responses and induces IFN-gamma production (PubMed:9126961, PubMed:12351401). 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 (PubMed:11477403, PubMed:16847311, PubMed:15539155). Promotes T-cell receptor-induced IL-4 secretion by CD4+ cells (PubMed:15123745). Inhibits antigen receptor-mediated production of IFN-gamma, but not IL-2, in CD4-/CD8- T-cells (PubMed:11477403). Required for IL-4 production by germinal centers T follicular helper (T(Fh))cells (PubMed:20525889). May inhibit CD40-induced signal transduction in monocyte-derived dendritic cells (By similarity). May play a role in a allergic responses and may regulate allergen-induced Th2 cytokine and Th1 cytokine secretion (PubMed:16528012). 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 (PubMed:18031695). Involved in the peripheral differentiation of indifferent natural killer T (iNKT) cells toward a regulatory NKT2 type (PubMed:18606638). In macrophages involved in down-regulation of IL-12, TNF-alpha and nitric oxide in response to lipopolysaccharide (LPS) (PubMed:15123745). 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 (PubMed:15315965). In conjunction with CD84/SLAMF5 and SLAMF6 may be a negative regulator of the humoral immune response (PubMed:25926831).By similarity10 Publications
(Microbial infection) 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 accumulated of PdtIns3P and NOX2 activity in the phagosomes (PubMed:20818396, PubMed:22493499).1 Publication1 Publication

GO - Molecular functioni

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • myeloid dendritic cell activation involved in immune response Source: MGI
  • natural killer cell differentiation Source: UniProtKB
  • natural killer cell proliferation Source: UniProtKB
  • negative regulation of CD40 signaling pathway Source: MGI
  • negative regulation of interferon-gamma secretion Source: UniProtKB
  • negative regulation of interleukin-12 production Source: MGI
  • negative regulation of interleukin-6 production Source: MGI
  • negative regulation of T cell cytokine production Source: UniProtKB
  • negative regulation of tumor necrosis factor production Source: MGI
  • phagocytosis Source: UniProtKB-KW
  • positive regulation of activated T cell proliferation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: MGI
  • positive regulation of interferon-gamma secretion Source: UniProtKB
  • positive regulation of JNK cascade Source: MGI
  • regulation of catalytic activity Source: MGI
  • regulation of vesicle fusion Source: MGI
  • T-helper 1 cell cytokine production Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Adaptive immunity, Cell adhesion, Immunity, Innate immunity, Phagocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Signaling lymphocytic activation molecule
Alternative name(s):
SLAM family member 1
CD_antigen: CD150
Gene namesi
Name:Slamf1
Synonyms:Slam
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1351314. Slamf1.

Subcellular locationi

  • Cell membrane By similarity; 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.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 242218ExtracellularSequence analysisAdd
BLAST
Transmembranei243 – 26523HelicalSequence analysisAdd
BLAST
Topological domaini266 – 34378CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • external side of plasma membrane Source: MGI
  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • phagocytic vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi288 – 2881Y → A: Greatly reduces SLAMF1:SH2D1A-mediated intracellular tyrosine phosphorylation. 1 Publication
Mutagenesisi315 – 3151Y → A: Abolishes SLAMF1:SH2D1A-mediated intracellular tyrosine phosphorylation, no effect on interaction with SH2D1A; when associated with A-335. 1 Publication
Mutagenesisi335 – 3351Y → A: Abolishes SLAMF1:SH2D1A-mediated intracellular tyrosine phosphorylation, no effect on interaction with SH2D1A; when associated with A-315. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 343319Signaling lymphocytic activation moleculePRO_0000014960Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence analysis
Glycosylationi58 – 581N-linked (GlcNAc...)Sequence analysis
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence analysis
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence analysis
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence analysis
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence analysis
Disulfide bondi161 ↔ 232PROSITE-ProRule annotation
Disulfide bondi167 ↔ 212PROSITE-ProRule annotation
Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence analysis
Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence analysis
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence analysis
Modified residuei288 – 2881Phosphotyrosine; by FYNBy similarity
Modified residuei315 – 3151Phosphotyrosine; by FYNBy similarity
Modified residuei335 – 3351Phosphotyrosine; by FYNBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues by FYN (By similarity).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9QUM4.
MaxQBiQ9QUM4.
PaxDbiQ9QUM4.
PRIDEiQ9QUM4.

PTM databases

iPTMnetiQ9QUM4.
PhosphoSiteiQ9QUM4.

Expressioni

Gene expression databases

BgeeiQ9QUM4.
ExpressionAtlasiQ9QUM4. baseline and differential.
GenevisibleiQ9QUM4. MM.

Interactioni

Subunit structurei

Interacts (via cytoplasmic domain) with SH2D1A and SH2D1B; SH2D1A mediates association with FYN; SH2D1A binds to phosphorylated and not phosphorylated ITSM 1 (PubMed:9774102, PubMed:16847311, PubMed:11477403.) Interacts (via cytoplasmic domain phosphorylated on tyrosine residues) with INPP5D and PTPN11; presence of SH2D1A facilitates binding to INPP5D (By similarity). Interacts with MAP4K1 (By similarity). Interacts with PIK3C3, BECN1 and UVRAG; indicative for an association with PI3K complex II (PI3KC3-C2) (PubMed:22493499).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BECN1Q144578EBI-7910086,EBI-949378From a different organism.
FynP396884EBI-7910086,EBI-524514
Sh2d1aO888903EBI-7910086,EBI-7910438
UVRAGQ9P2Y56EBI-7910086,EBI-2952704From a different organism.

Protein-protein interaction databases

BioGridi205139. 2 interactions.
IntActiQ9QUM4. 10 interactions.
MINTiMINT-205762.
STRINGi10090.ENSMUSP00000015460.

Structurei

3D structure databases

ProteinModelPortaliQ9QUM4.
SMRiQ9QUM4. Positions 32-141, 162-221.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 138110Ig-like V-typeAdd
BLAST
Domaini145 – 22884Ig-like C2-typeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi286 – 2916ITSM 1By similarity
Motifi313 – 3186SH2-bindingSequence analysis
Motifi333 – 3386ITSM 2By similarity

Domaini

The ITSMs (immunoreceptor tyrosine-based switch motifs) with the consensus sequence T-X-Y-X-X-[VI] present in SLAM family receptors have overlapping specificity for activating and inhibitory SH2 domain-containing binding partners. Especially they mediate the interaction with the SH2 domain of SH2D1A and SH2D1B. For SLAMF1 a 'two-out-of-three-pronged' mechanism is proposed involving threonine (position -2), phosphorylated tyrosine (position 0) and valine/isoleucine (position +3). Binding is mediated by either three 'prongs' (for high affinity binding involving ITSM 1) or a combination of any two also including non-phosphorylated Tyr-288 of ITSM 1 thus providing a positive feedback loop implicating SH2D1A-dependent recruitment of activating FYN. ITSM 2 needs to be phosphorylated on Tyr-335 for SH2D1A binding.By similarity

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFKK. Eukaryota.
ENOG4111DAM. LUCA.
GeneTreeiENSGT00510000048858.
HOGENOMiHOG000125310.
HOVERGENiHBG054224.
InParanoidiQ9QUM4.
KOiK06536.
OMAiHFCLQLK.
OrthoDBiEOG7Q8CQJ.
PhylomeDBiQ9QUM4.
TreeFamiTF334964.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR010407. Sig_lymph_act_molc_N.
[Graphical view]
PfamiPF06214. SLAM. 1 hit.
[Graphical view]
ProDomiPD090491. Sig_lymph_act_molc_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q9QUM4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDPKGSLSWR ILLFLSLAFE LSYGTGGGVM DCPVILQKLG QDTWLPLTNE
60 70 80 90 100
HQINKSVNKS VRILVTMATS PGSKSNKKIV SFDLSKGSYP DHLEDGYHFQ
110 120 130 140 150
SKNLSLKILG NRRESEGWYL VSVEENVSVQ QFCKQLKLYE QVSPPEIKVL
160 170 180 190 200
NKTQENENGT CSLLLACTVK KGDHVTYSWS DEAGTHLLSR ANRSHLLHIT
210 220 230 240 250
LSNQHQDSIY NCTASNPVSS ISRTFNLSSQ ACKQESSSES SPWMQYTLVP
260 270 280 290 300
LGVVIIFILV FTAIIMMKRQ GKSNHCQPPV EEKSLTIYAQ VQKSGPQEKK
310 320 330 340
LHDALTDQDP CTTIYVAATE PAPESVQEPN PTTVYASVTL PES
Length:343
Mass (Da):38,094
Last modified:May 1, 2000 - v1
Checksum:i7980470157E834C4
GO
Isoform Short (identifier: Q9QUM4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     296-343: PQEKKLHDAL...VYASVTLPES → VRSMPHLAGVSVIFRTGFLIAALHTTMVLQGLLE

Show »
Length:329
Mass (Da):36,590
Checksum:i3F43476A7CD3686F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei296 – 34348PQEKK…TLPES → VRSMPHLAGVSVIFRTGFLI AALHTTMVLQGLLE in isoform Short. 1 PublicationVSP_002570Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149791 mRNA. Translation: AAF22231.1.
AF149792 mRNA. Translation: AAF22232.1.
AF164523
, AF164519, AF164520, AF164521, AF164522 Genomic DNA. Translation: AAF13818.1.
AF160990 mRNA. Translation: AAF14535.1.
CCDSiCCDS15502.1. [Q9QUM4-1]
RefSeqiNP_038758.2. NM_013730.4. [Q9QUM4-1]
UniGeneiMm.103648.

Genome annotation databases

EnsembliENSMUST00000015460; ENSMUSP00000015460; ENSMUSG00000015316. [Q9QUM4-1]
GeneIDi27218.
KEGGimmu:27218.
UCSCiuc007dpc.1. mouse. [Q9QUM4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149791 mRNA. Translation: AAF22231.1.
AF149792 mRNA. Translation: AAF22232.1.
AF164523
, AF164519, AF164520, AF164521, AF164522 Genomic DNA. Translation: AAF13818.1.
AF160990 mRNA. Translation: AAF14535.1.
CCDSiCCDS15502.1. [Q9QUM4-1]
RefSeqiNP_038758.2. NM_013730.4. [Q9QUM4-1]
UniGeneiMm.103648.

3D structure databases

ProteinModelPortaliQ9QUM4.
SMRiQ9QUM4. Positions 32-141, 162-221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205139. 2 interactions.
IntActiQ9QUM4. 10 interactions.
MINTiMINT-205762.
STRINGi10090.ENSMUSP00000015460.

PTM databases

iPTMnetiQ9QUM4.
PhosphoSiteiQ9QUM4.

Proteomic databases

EPDiQ9QUM4.
MaxQBiQ9QUM4.
PaxDbiQ9QUM4.
PRIDEiQ9QUM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015460; ENSMUSP00000015460; ENSMUSG00000015316. [Q9QUM4-1]
GeneIDi27218.
KEGGimmu:27218.
UCSCiuc007dpc.1. mouse. [Q9QUM4-1]

Organism-specific databases

CTDi6504.
MGIiMGI:1351314. Slamf1.

Phylogenomic databases

eggNOGiENOG410IFKK. Eukaryota.
ENOG4111DAM. LUCA.
GeneTreeiENSGT00510000048858.
HOGENOMiHOG000125310.
HOVERGENiHBG054224.
InParanoidiQ9QUM4.
KOiK06536.
OMAiHFCLQLK.
OrthoDBiEOG7Q8CQJ.
PhylomeDBiQ9QUM4.
TreeFamiTF334964.

Miscellaneous databases

NextBioi305116.
PROiQ9QUM4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QUM4.
ExpressionAtlasiQ9QUM4. baseline and differential.
GenevisibleiQ9QUM4. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR010407. Sig_lymph_act_molc_N.
[Graphical view]
PfamiPF06214. SLAM. 1 hit.
[Graphical view]
ProDomiPD090491. Sig_lymph_act_molc_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular and functional characterization of mouse signaling lymphocytic activation molecule (SLAM): differential expression and responsiveness in Th1 and Th2 cells."
    Castro A.G., Hauser T.M., Cocks B.G., Abrams J., Zurawski S., Churakova T., Zonin F., Robinson D., Tangye S.G., Aversa G., Nichols K.E., de Vries J.E., Lanier L.L., O'Garra A.
    J. Immunol. 163:5860-5870(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
    Strain: BALB/cJ.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG), FUNCTION.
  3. "Genomic organization of murine Slam."
    Wu C., Wang N., Sayos J., Terhorst C.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  4. "Engagement of the signaling lymphocytic activation molecule (SLAM) on activated T cells results in IL-2-independent, cyclosporin A-sensitive T cell proliferation and IFN-gamma production."
    Aversa G., Chang C.C., Carballido J.M., Cocks B.G., de Vries J.E.
    J. Immunol. 158:4036-4044(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM."
    Sayos J., Wu C., Morra M., Wang N., Zhang X., Allen D., van Schaik S., Notarangelo L., Geha R., Roncarolo M.G., Oettgen H., de Vries J.E., Aversa G., Terhorst C.
    Nature 395:462-469(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2D1A.
  6. "Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells."
    Morra M., Lu J., Poy F., Martin M., Sayos J., Calpe S., Gullo C., Howie D., Rietdijk S., Thompson A., Coyle A.J., Denny C., Yaffe M.B., Engel P., Eck M.J., Terhorst C.
    EMBO J. 20:5840-5852(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2D1B.
  7. "Regulation of SLAM-mediated signal transduction by SAP, the X-linked lymphoproliferative gene product."
    Latour S., Gish G., Helgason C.D., Humphries R.K., Pawson T., Veillette A.
    Nat. Immunol. 2:681-690(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH SH2D1A AND FYN, MUTAGENESIS OF TYR-288; TYR-315 AND TYR-335.
  8. "The role of SAP in murine CD150 (SLAM)-mediated T-cell proliferation and interferon gamma production."
    Howie D., Okamoto S., Rietdijk S., Clarke K., Wang N., Gullo C., Bruggeman J.P., Manning S., Coyle A.J., Greenfield E., Kuchroo V., Terhorst C.
    Blood 100:2899-2907(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "The adaptor protein SH2D1A regulates signaling through CD150 (SLAM) in B cells."
    Mikhalap S.V., Shlapatska L.M., Yurchenko O.V., Yurchenko M.Y., Berdova G.G., Nichols K.E., Clark E.A., Sidorenko S.P.
    Blood 104:4063-4070(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "SAP regulates T(H)2 differentiation and PKC-theta-mediated activation of NF-kappaB1."
    Cannons J.L., Yu L.J., Hill B., Mijares L.A., Dombroski D., Nichols K.E., Antonellis A., Koretzky G.A., Gardner K., Schwartzberg P.L.
    Immunity 21:693-706(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The costimulatory molecule SLAM is critical for pulmonary allergic responses."
    Wang N., Campo M., Ting L., Fleming C., Terhorst C., Finn P.W.
    Am. J. Respir. Cell Mol. Biol. 35:206-210(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Association between SAP and FynT: Inducible SH3 domain-mediated interaction controlled by engagement of the SLAM receptor."
    Chen R., Latour S., Shi X., Veillette A.
    Mol. Cell. Biol. 26:5559-5568(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2D1A AND FYN.
  13. "Homotypic interactions mediated by Slamf1 and Slamf6 receptors control NKT cell lineage development."
    Griewank K., Borowski C., Rietdijk S., Wang N., Julien A., Wei D.G., Mamchak A.A., Terhorst C., Bendelac A.
    Immunity 27:751-762(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Impaired SLAM-SLAM homotypic interaction between invariant NKT cells and dendritic cells affects differentiation of IL-4/IL-10-secreting NKT2 cells in nonobese diabetic mice."
    Baev D.V., Caielli S., Ronchi F., Coccia M., Facciotti F., Nichols K.E., Falcone M.
    J. Immunol. 181:869-877(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  16. "Germinal center T follicular helper cell IL-4 production is dependent on signaling lymphocytic activation molecule receptor (CD150)."
    Yusuf I., Kageyama R., Monticelli L., Johnston R.J., Ditoro D., Hansen K., Barnett B., Crotty S.
    J. Immunol. 185:190-202(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages."
    Berger S.B., Romero X., Ma C., Wang G., Faubion W.A., Liao G., Compeer E., Keszei M., Rameh L., Wang N., Boes M., Regueiro J.R., Reinecker H.C., Terhorst C.
    Nat. Immunol. 11:920-927(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Receptor signaling lymphocyte-activation molecule family 1 (Slamf1) regulates membrane fusion and NADPH oxidase 2 (NOX2) activity by recruiting a Beclin-1/Vps34/ultraviolet radiation resistance-associated gene (UVRAG) complex."
    Ma C., Wang N., Detre C., Wang G., O'Keeffe M., Terhorst C.
    J. Biol. Chem. 287:18359-18365(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PIK3C3; BECN1 AND UVRAG.
  19. "Negative regulation of humoral immunity due to interplay between the SLAMF1, SLAMF5, and SLAMF6 receptors."
    Wang N., Halibozek P.J., Yigit B., Zhao H., O'Keeffe M.S., Sage P., Sharpe A., Terhorst C.
    Front. Immunol. 6:158-158(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiSLAF1_MOUSE
AccessioniPrimary (citable) accession number: Q9QUM4
Secondary accession number(s): Q9QXZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.