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Signaling lymphocytic activation molecule (SLAM family member 1) (CD antigen CD150)

 SLAF1_MOUSE             Reviewed;         343 AA.
Q9QUM4; Q9QXZ3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 140.
RecName: Full=Signaling lymphocytic activation molecule;
AltName: Full=SLAM family member 1;
AltName: CD_antigen=CD150;
Flags: Precursor;
Name=Slamf1; Synonyms=Slam;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
STRAIN=BALB/cJ;
PubMed=10570270;
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.;
"Molecular and functional characterization of mouse signaling
lymphocytic activation molecule (SLAM): differential expression and
responsiveness in Th1 and Th2 cells.";
J. Immunol. 163:5860-5870(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG), AND FUNCTION.
PubMed=15123745; DOI=10.1084/jem.20031835;
Wang N., Satoskar A., Faubion W., Howie D., Okamoto S., Feske S.,
Gullo C., Clarke K., Sosa M.R., Sharpe A.H., Terhorst C.;
"The cell surface receptor SLAM controls T cell and macrophage
functions.";
J. Exp. Med. 199:1255-1264(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Wu C., Wang N., Sayos J., Terhorst C.;
"Genomic organization of murine Slam.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION.
PubMed=9126961;
Aversa G., Chang C.C., Carballido J.M., Cocks B.G., de Vries J.E.;
"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.";
J. Immunol. 158:4036-4044(1997).
[5]
INTERACTION WITH SH2D1A.
PubMed=9774102; DOI=10.1038/26683;
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.;
"The X-linked lymphoproliferative-disease gene product SAP regulates
signals induced through the co-receptor SLAM.";
Nature 395:462-469(1998).
[6]
INTERACTION WITH SH2D1B.
PubMed=11689425; DOI=10.1093/emboj/20.21.5840;
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.;
"Structural basis for the interaction of the free SH2 domain EAT-2
with SLAM receptors in hematopoietic cells.";
EMBO J. 20:5840-5852(2001).
[7]
FUNCTION, PHOSPHORYLATION, INTERACTION WITH SH2D1A AND FYN, AND
MUTAGENESIS OF TYR-288; TYR-315 AND TYR-335.
PubMed=11477403; DOI=10.1038/90615;
Latour S., Gish G., Helgason C.D., Humphries R.K., Pawson T.,
Veillette A.;
"Regulation of SLAM-mediated signal transduction by SAP, the X-linked
lymphoproliferative gene product.";
Nat. Immunol. 2:681-690(2001).
[8]
FUNCTION.
PubMed=12351401; DOI=10.1182/blood-2002-02-0445;
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.;
"The role of SAP in murine CD150 (SLAM)-mediated T-cell proliferation
and interferon gamma production.";
Blood 100:2899-2907(2002).
[9]
FUNCTION.
PubMed=15315965; DOI=10.1182/blood-2004-04-1273;
Mikhalap S.V., Shlapatska L.M., Yurchenko O.V., Yurchenko M.Y.,
Berdova G.G., Nichols K.E., Clark E.A., Sidorenko S.P.;
"The adaptor protein SH2D1A regulates signaling through CD150 (SLAM)
in B cells.";
Blood 104:4063-4070(2004).
[10]
FUNCTION.
PubMed=15539155; DOI=10.1016/j.immuni.2004.09.012;
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.;
"SAP regulates T(H)2 differentiation and PKC-theta-mediated activation
of NF-kappaB1.";
Immunity 21:693-706(2004).
[11]
FUNCTION.
PubMed=16528012; DOI=10.1165/rcmb.2005-0294OC;
Wang N., Campo M., Ting L., Fleming C., Terhorst C., Finn P.W.;
"The costimulatory molecule SLAM is critical for pulmonary allergic
responses.";
Am. J. Respir. Cell Mol. Biol. 35:206-210(2006).
[12]
INTERACTION WITH SH2D1A AND FYN.
PubMed=16847311; DOI=10.1128/MCB.00357-06;
Chen R., Latour S., Shi X., Veillette A.;
"Association between SAP and FynT: Inducible SH3 domain-mediated
interaction controlled by engagement of the SLAM receptor.";
Mol. Cell. Biol. 26:5559-5568(2006).
[13]
FUNCTION.
PubMed=18031695; DOI=10.1016/j.immuni.2007.08.020;
Griewank K., Borowski C., Rietdijk S., Wang N., Julien A., Wei D.G.,
Mamchak A.A., Terhorst C., Bendelac A.;
"Homotypic interactions mediated by Slamf1 and Slamf6 receptors
control NKT cell lineage development.";
Immunity 27:751-762(2007).
[14]
FUNCTION.
PubMed=18606638; DOI=10.4049/jimmunol.181.2.869;
Baev D.V., Caielli S., Ronchi F., Coccia M., Facciotti F.,
Nichols K.E., Falcone M.;
"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.";
J. Immunol. 181:869-877(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
FUNCTION.
PubMed=20525889; DOI=10.4049/jimmunol.0903505;
Yusuf I., Kageyama R., Monticelli L., Johnston R.J., Ditoro D.,
Hansen K., Barnett B., Crotty S.;
"Germinal center T follicular helper cell IL-4 production is dependent
on signaling lymphocytic activation molecule receptor (CD150).";
J. Immunol. 185:190-202(2010).
[17]
FUNCTION.
PubMed=20818396; DOI=10.1038/ni.1931;
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.;
"SLAM is a microbial sensor that regulates bacterial phagosome
functions in macrophages.";
Nat. Immunol. 11:920-927(2010).
[18]
FUNCTION, AND INTERACTION WITH PIK3C3; BECN1 AND UVRAG.
PubMed=22493499; DOI=10.1074/jbc.M112.367060;
Ma C., Wang N., Detre C., Wang G., O'Keeffe M., Terhorst C.;
"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.";
J. Biol. Chem. 287:18359-18365(2012).
[19]
FUNCTION.
PubMed=25926831; DOI=10.3389/fimmu.2015.00158;
Wang N., Halibozek P.J., Yigit B., Zhao H., O'Keeffe M.S., Sage P.,
Sharpe A., Terhorst C.;
"Negative regulation of humoral immunity due to interplay between the
SLAMF1, SLAMF5, and SLAMF6 receptors.";
Front. Immunol. 6:158-158(2015).
-!- 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 (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). {ECO:0000250|UniProtKB:Q13291,
ECO:0000269|PubMed:11477403, ECO:0000269|PubMed:15123745,
ECO:0000269|PubMed:15315965, ECO:0000269|PubMed:15539155,
ECO:0000269|PubMed:16528012, ECO:0000269|PubMed:16847311,
ECO:0000269|PubMed:18031695, ECO:0000269|PubMed:18606638,
ECO:0000269|PubMed:25926831, ECO:0000269|PubMed:9126961}.
-!- FUNCTION: (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 PdtIns(3)P and NOX2 activity in the
phagosomes (PubMed:20818396, PubMed:22493499).
{ECO:0000269|PubMed:20818396, ECO:0000305|PubMed:22493499}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:Q13291, ECO:0000269|PubMed:11477403,
ECO:0000269|PubMed:11689425, ECO:0000269|PubMed:16847311,
ECO:0000269|PubMed:20525889, ECO:0000269|PubMed:22493499,
ECO:0000269|PubMed:9774102}.
-!- INTERACTION:
Q14457:BECN1 (xeno); NbExp=8; IntAct=EBI-7910086, EBI-949378;
P39688:Fyn; NbExp=4; IntAct=EBI-7910086, EBI-524514;
O88890:Sh2d1a; NbExp=3; IntAct=EBI-7910086, EBI-7910438;
Q9P2Y5:UVRAG (xeno); NbExp=6; IntAct=EBI-7910086, EBI-2952704;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q13291}; 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. {ECO:0000250|UniProtKB:Q13291}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q9QUM4-1; Sequence=Displayed;
Name=Short;
IsoId=Q9QUM4-2; Sequence=VSP_002570;
-!- DOMAIN: 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. {ECO:0000250|UniProtKB:Q13291}.
-!- PTM: Phosphorylated on tyrosine residues by FYN (By similarity).
{ECO:0000250|UniProtKB:Q13291, ECO:0000269|PubMed:11477403}.
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EMBL; AF149791; AAF22231.1; -; mRNA.
EMBL; AF149792; AAF22232.1; -; mRNA.
EMBL; AF164523; AAF13818.1; -; Genomic_DNA.
EMBL; AF164519; AAF13818.1; JOINED; Genomic_DNA.
EMBL; AF164520; AAF13818.1; JOINED; Genomic_DNA.
EMBL; AF164521; AAF13818.1; JOINED; Genomic_DNA.
EMBL; AF164522; AAF13818.1; JOINED; Genomic_DNA.
EMBL; AF160990; AAF14535.1; -; mRNA.
CCDS; CCDS15502.1; -. [Q9QUM4-1]
RefSeq; NP_038758.2; NM_013730.4. [Q9QUM4-1]
UniGene; Mm.103648; -.
ProteinModelPortal; Q9QUM4; -.
BioGrid; 205139; 2.
CORUM; Q9QUM4; -.
IntAct; Q9QUM4; 11.
MINT; MINT-205762; -.
STRING; 10090.ENSMUSP00000015460; -.
iPTMnet; Q9QUM4; -.
PhosphoSitePlus; Q9QUM4; -.
PaxDb; Q9QUM4; -.
PRIDE; Q9QUM4; -.
Ensembl; ENSMUST00000015460; ENSMUSP00000015460; ENSMUSG00000015316. [Q9QUM4-1]
GeneID; 27218; -.
KEGG; mmu:27218; -.
UCSC; uc007dpc.1; mouse. [Q9QUM4-1]
CTD; 6504; -.
MGI; MGI:1351314; Slamf1.
eggNOG; ENOG410IFKK; Eukaryota.
eggNOG; ENOG4111DAM; LUCA.
GeneTree; ENSGT00510000048858; -.
HOGENOM; HOG000125310; -.
HOVERGEN; HBG054224; -.
InParanoid; Q9QUM4; -.
KO; K06536; -.
OMA; NIYICTV; -.
OrthoDB; EOG091G0EOO; -.
PhylomeDB; Q9QUM4; -.
TreeFam; TF334964; -.
PRO; PR:Q9QUM4; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000015316; -.
ExpressionAtlas; Q9QUM4; baseline and differential.
Genevisible; Q9QUM4; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IDA:MGI.
GO; GO:0004872; F:receptor activity; IDA:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; IMP:MGI.
GO; GO:0002277; P:myeloid dendritic cell activation involved in immune response; ISO:MGI.
GO; GO:0001779; P:natural killer cell differentiation; IMP:UniProtKB.
GO; GO:0001787; P:natural killer cell proliferation; IMP:UniProtKB.
GO; GO:2000349; P:negative regulation of CD40 signaling pathway; ISO:MGI.
GO; GO:1902714; P:negative regulation of interferon-gamma secretion; IDA:UniProtKB.
GO; GO:0032695; P:negative regulation of interleukin-12 production; ISO:MGI.
GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:MGI.
GO; GO:0002725; P:negative regulation of T cell cytokine production; IDA:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:UniProtKB.
GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:1902715; P:positive regulation of interferon-gamma secretion; IDA:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:MGI.
GO; GO:0050790; P:regulation of catalytic activity; IMP:MGI.
GO; GO:0031338; P:regulation of vesicle fusion; IMP:MGI.
GO; GO:0035744; P:T-helper 1 cell cytokine production; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR010407; Sig_lymph_act_molc_N.
Pfam; PF06214; SLAM; 1.
ProDom; PD090491; Sig_lymph_act_molc_N; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Innate immunity; Membrane; Phagocytosis;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 343 Signaling lymphocytic activation
molecule.
/FTId=PRO_0000014960.
TOPO_DOM 25 242 Extracellular. {ECO:0000255}.
TRANSMEM 243 265 Helical. {ECO:0000255}.
TOPO_DOM 266 343 Cytoplasmic. {ECO:0000255}.
DOMAIN 29 138 Ig-like V-type.
DOMAIN 145 228 Ig-like C2-type.
MOTIF 286 291 ITSM 1. {ECO:0000250|UniProtKB:Q13291}.
MOTIF 313 318 SH2-binding. {ECO:0000255}.
MOTIF 333 338 ITSM 2. {ECO:0000250|UniProtKB:Q13291}.
MOD_RES 288 288 Phosphotyrosine; by FYN.
{ECO:0000250|UniProtKB:Q13291}.
MOD_RES 315 315 Phosphotyrosine; by FYN.
{ECO:0000250|UniProtKB:Q13291}.
MOD_RES 335 335 Phosphotyrosine; by FYN.
{ECO:0000250|UniProtKB:Q13291}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 161 232 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 167 212 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 296 343 PQEKKLHDALTDQDPCTTIYVAATEPAPESVQEPNPTTVYA
SVTLPES -> VRSMPHLAGVSVIFRTGFLIAALHTTMVLQ
GLLE (in isoform Short).
{ECO:0000303|PubMed:10570270}.
/FTId=VSP_002570.
MUTAGEN 288 288 Y->A: Greatly reduces SLAMF1:SH2D1A-
mediated intracellular tyrosine
phosphorylation.
{ECO:0000269|PubMed:11477403}.
MUTAGEN 315 315 Y->A: Abolishes SLAMF1:SH2D1A-mediated
intracellular tyrosine phosphorylation,
no effect on interaction with SH2D1A;
when associated with A-335.
{ECO:0000269|PubMed:11477403}.
MUTAGEN 335 335 Y->A: Abolishes SLAMF1:SH2D1A-mediated
intracellular tyrosine phosphorylation,
no effect on interaction with SH2D1A;
when associated with A-315.
{ECO:0000269|PubMed:11477403}.
SEQUENCE 343 AA; 38094 MW; 7980470157E834C4 CRC64;
MDPKGSLSWR ILLFLSLAFE LSYGTGGGVM DCPVILQKLG QDTWLPLTNE HQINKSVNKS
VRILVTMATS PGSKSNKKIV SFDLSKGSYP DHLEDGYHFQ SKNLSLKILG NRRESEGWYL
VSVEENVSVQ QFCKQLKLYE QVSPPEIKVL NKTQENENGT CSLLLACTVK KGDHVTYSWS
DEAGTHLLSR ANRSHLLHIT LSNQHQDSIY NCTASNPVSS ISRTFNLSSQ ACKQESSSES
SPWMQYTLVP LGVVIIFILV FTAIIMMKRQ GKSNHCQPPV EEKSLTIYAQ VQKSGPQEKK
LHDALTDQDP CTTIYVAATE PAPESVQEPN PTTVYASVTL PES


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6249 Signaling lymphocytic activation molecule family member 2 0.1 mg
6251 Signaling lymphocytic activation molecule family member 3 0.1 mg
6247 Signaling lymphocytic activation molecule family member 1 0.1 mg
6249 Signaling lymphocytic activation molecule family member 2 0.5 mg
6251 Signaling lymphocytic activation molecule family member 3 0.5 mg
6247 Signaling lymphocytic activation molecule family member 1 0.5 mg
6253 Signaling lymphocytic activation molecule family member 4 0.5 mg
CF76 Human Signaling Lymphocytic Activation Molecule SLAM 50
C292 Human Signaling Lymphocytic Activation Molecule SLAM l0
EIAAB38622 Mouse,Mus musculus,Signaling lymphocytic activation molecule,Slam,Slamf1
H0973 Signaling Lymphocytic Activation Molecule Family, Member 7 (SLAMF7), Human, ELISA Kit 96T
QY-E00804 Human Signaling Lymphocytic Activation Molecule Family, Member 7(SLAMF7)ELISA Kit 96T
UB-E00804 Human Signaling Lymphocytic Activation Molecule Family, Member 7(SLAMF7)ELISA Kit 96T
201-12-4949 Human Signaling Lymphocytic Activation Molecule Family, Member 7(SLAMF7)ELISA Kit 96T
YSRTMCA2251XZ CD150, Signalling Lymphocytic Activation Molecule (SLAM), Clone A12, Mab anti_Human, azide_free; flow_IP_functional studies (induces proliferation) 1 mg.


 

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