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Showing Protein Signaling lymphocytic activation molecule (HMDBP13732)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP13732
Secondary Accession Numbers None
Name Signaling lymphocytic activation molecule
Synonyms
  1. CDw150
  2. IPO-3
  3. SLAM family member 1
Gene Name SLAMF1
Protein Type Unknown
Biological Properties
General Function Not Available
Specific 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-alpha 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).(Microbial infection) Acts as a receptor for Measles virus; also including isoform 4.
Pathways
  • Measles
Reactions Not Available
GO Classification
Biological Process
lymphocyte activation
myeloid dendritic cell activation involved in immune response
negative regulation of CD40 signaling pathway
positive regulation of cell proliferation
phagocytosis
cell adhesion
negative regulation of tumor necrosis factor production
positive regulation of ERK1 and ERK2 cascade
innate immune response
adaptive immune response
negative regulation of interleukin-6 production
positive regulation of JNK cascade
negative regulation of interleukin-12 production
Cellular Component
cell surface
extracellular vesicular exosome
plasma membrane
integral to membrane
Molecular Function
viral receptor activity
SH2 domain binding
antigen binding
transmembrane signaling receptor activity
identical protein binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 335
Molecular Weight 37230.64
Theoretical pI 8.46
Pfam Domain Function
Signals
  • 1-20;
Transmembrane Regions
  • 238-258;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q13291
UniProtKB/Swiss-Prot Entry Name SLAF1_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
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  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed:16959974 ]
  4. Chan B, Lanyi A, Song HK, Griesbach J, Simarro-Grande M, Poy F, Howie D, Sumegi J, Terhorst C, Eck MJ: SAP couples Fyn to SLAM immune receptors. Nat Cell Biol. 2003 Feb;5(2):155-60. [PubMed:12545174 ]
  5. Mikhalap SV, Shlapatska LM, Berdova AG, Law CL, Clark EA, Sidorenko SP: CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis. J Immunol. 1999 May 15;162(10):5719-27. [PubMed:10229804 ]
  6. Cocks BG, Chang CC, Carballido JM, Yssel H, de Vries JE, Aversa G: A novel receptor involved in T-cell activation. Nature. 1995 Jul 20;376(6537):260-3. doi: 10.1038/376260a0. [PubMed:7617038 ]
  7. Romanets-Korbut O, Najakshin AM, Yurchenko M, Malysheva TA, Kovalevska L, Shlapatska LM, Zozulya YA, Taranin AV, Horvat B, Sidorenko SP: Expression of CD150 in tumors of the central nervous system: identification of a novel isoform. PLoS One. 2015 Feb 24;10(2):e0118302. doi: 10.1371/journal.pone.0118302. eCollection 2015. [PubMed:25710480 ]
  8. Ferrand V, Li C, Romeo G, Yin L: Absence of SLAM mutations in EBV-associated lymphoproliferative disease patients. J Med Virol. 2003 May;70(1):131-6. doi: 10.1002/jmv.10373. [PubMed:12629654 ]
  9. Punnonen J, Cocks BG, Carballido JM, Bennett B, Peterson D, Aversa G, de Vries JE: Soluble and membrane-bound forms of signaling lymphocytic activation molecule (SLAM) induce proliferation and Ig synthesis by activated human B lymphocytes. J Exp Med. 1997 Mar 17;185(6):993-1004. doi: 10.1084/jem.185.6.993. [PubMed:9091591 ]
  10. Sayos J, Wu C, Morra M, Wang N, Zhang X, Allen D, van Schaik S, Notarangelo L, Geha R, Roncarolo MG, Oettgen H, De Vries JE, Aversa G, Terhorst C: The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM. Nature. 1998 Oct 1;395(6701):462-9. doi: 10.1038/26683. [PubMed:9774102 ]
  11. Tatsuo H, Ono N, Tanaka K, Yanagi Y: SLAM (CDw150) is a cellular receptor for measles virus. Nature. 2000 Aug 24;406(6798):893-7. doi: 10.1038/35022579. [PubMed:10972291 ]
  12. Howie D, Simarro M, Sayos J, Guirado M, Sancho J, Terhorst C: Molecular dissection of the signaling and costimulatory functions of CD150 (SLAM): CD150/SAP binding and CD150-mediated costimulation. Blood. 2002 Feb 1;99(3):957-65. doi: 10.1182/blood.v99.3.957. [PubMed:11806999 ]
  13. Li C, Iosef C, Jia CY, Han VK, Li SS: Dual functional roles for the X-linked lymphoproliferative syndrome gene product SAP/SH2D1A in signaling through the signaling lymphocyte activation molecule (SLAM) family of immune receptors. J Biol Chem. 2003 Feb 7;278(6):3852-9. doi: 10.1074/jbc.M206649200. Epub 2002 Nov 27. [PubMed:12458214 ]
  14. Rethi B, Gogolak P, Szatmari I, Veres A, Erdos E, Nagy L, Rajnavolgyi E, Terhorst C, Lanyi A: SLAM/SLAM interactions inhibit CD40-induced production of inflammatory cytokines in monocyte-derived dendritic cells. Blood. 2006 Apr 1;107(7):2821-9. doi: 10.1182/blood-2005-06-2265. Epub 2005 Nov 29. [PubMed:16317102 ]
  15. Yurchenko MY, Kovalevska LM, Shlapatska LM, Berdova GG, Clark EA, Sidorenko SP: CD150 regulates JNK1/2 activation in normal and Hodgkin's lymphoma B cells. Immunol Cell Biol. 2010 Jul;88(5):565-74. doi: 10.1038/icb.2010.14. Epub 2010 Mar 16. [PubMed:20231852 ]
  16. Berger SB, Romero X, Ma C, Wang G, Faubion WA, Liao G, Compeer E, Keszei M, Rameh L, Wang N, Boes M, Regueiro JR, Reinecker HC, Terhorst C: SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages. Nat Immunol. 2010 Oct;11(10):920-7. doi: 10.1038/ni.1931. Epub 2010 Sep 5. [PubMed:20818396 ]
  17. Morra M, Lu J, Poy F, Martin M, Sayos J, Calpe S, Gullo C, Howie D, Rietdijk S, Thompson A, Coyle AJ, Denny C, Yaffe MB, Engel P, Eck MJ, Terhorst C: Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells. EMBO J. 2001 Nov 1;20(21):5840-52. doi: 10.1093/emboj/20.21.5840. [PubMed:11689425 ]
  18. Hwang PM, Li C, Morra M, Lillywhite J, Muhandiram DR, Gertler F, Terhorst C, Kay LE, Pawson T, Forman-Kay JD, Li SC: A "three-pronged" binding mechanism for the SAP/SH2D1A SH2 domain: structural basis and relevance to the XLP syndrome. EMBO J. 2002 Feb 1;21(3):314-23. doi: 10.1093/emboj/21.3.314. [PubMed:11823424 ]