FYB

FYN binding protein

PDB rendering based on 1ri9.

Available structures
PDB	1RI9, 2GTJ, 2GTO

Identifiers

Symbols

FYB; ADAP; PRO0823; SLAP-130

External IDs

OMIM: 602731 MGI: 1346327 HomoloGene: 22664 GeneCards: FYB Gene

Gene Ontology
Molecular function	• protein binding
Cellular component	• nucleus • cytoplasm • cytosol • cytosol
Biological process	• protein phosphorylation • NLS-bearing substrate import into nucleus • immune response • signal transduction • intracellular protein kinase cascade • cell junction assembly • T cell receptor signaling pathway
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 5:
39.11 – 39.27 Mb

Chr 15:
6.53 – 6.61 Mb

PubMed search

[1]

[2]

FYN binding protein (FYB-120/130), also known as FYB, ADAP (Adhesion- and Degranulation-promoting Adapter Protein), and SLAP-130 (SLP-76-associated phosphoprotein of 130 kDa) is a protein that in humans is encoded by the FYB gene.^[1]

Interactions

FYB has been shown to interact with FYN^[2]^[3], SKAP1^[3]^[4], and SLP-76 (Lymphocyte cytosolic protein 2)^[5].

References

^ "Entrez Gene: FYB FYN binding protein (FYB-120/130)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2533.
^ da Silva, A J; Janssen O, Rudd C E (Dec. 1993). "T cell receptor zeta/CD3-p59fyn(T)-associated p120/130 binds to the SH2 domain of p59fyn(T)". J. Exp. Med. (UNITED STATES) 178 (6): 2107–13. doi:10.1084/jem.178.6.2107. ISSN 0022-1007. PMC 2191307. PMID 7504057. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2191307.
^ ^a ^b Marie-Cardine, A; Hendricks-Taylor L R, Boerth N J, Zhao H, Schraven B, Koretzky G A (Oct. 1998). "Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130". J. Biol. Chem. (UNITED STATES) 273 (40): 25789–95. doi:10.1074/jbc.273.40.25789. ISSN 0021-9258. PMID 9748251.
^ Liu, J; Kang H, Raab M, da Silva A J, Kraeft S K, Rudd C E (Jul. 1998). "FYB (FYN binding protein) serves as a binding partner for lymphoid protein and FYN kinase substrate SKAP55 and a SKAP55-related protein in T cells". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (15): 8779–84. doi:10.1073/pnas.95.15.8779. ISSN 0027-8424. PMC 21153. PMID 9671755. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21153.
^ Musci MA, Hendricks-Taylor LR, Motto DG, et al. (1997). "Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases.". J. Biol. Chem. 272 (18): 11674–7. doi:10.1074/jbc.272.18.11674. PMID 9115214.

da Silva AJ, Janssen O, Rudd CE (1993). "T cell receptor zeta/CD3-p59fyn(T)-associated p120/130 binds to the SH2 domain of p59fyn(T).". J. Exp. Med. 178 (6): 2107–13. doi:10.1084/jem.178.6.2107. PMC 2191307. PMID 7504057. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2191307.
Musci MA, Hendricks-Taylor LR, Motto DG, et al. (1997). "Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases.". J. Biol. Chem. 272 (18): 11674–7. doi:10.1074/jbc.272.18.11674. PMID 9115214.
da Silva AJ, Li Z, de Vera C, et al. (1997). "Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production.". Proc. Natl. Acad. Sci. U.S.A. 94 (14): 7493–8. doi:10.1073/pnas.94.14.7493. PMC 23849. PMID 9207119. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=23849.
Liu J, Kang H, Raab M, et al. (1998). "FYB (FYN binding protein) serves as a binding partner for lymphoid protein and FYN kinase substrate SKAP55 and a SKAP55-related protein in T cells.". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8779–84. doi:10.1073/pnas.95.15.8779. PMC 21153. PMID 9671755. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21153.
Marie-Cardine A, Hendricks-Taylor LR, Boerth NJ, et al. (1998). "Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130.". J. Biol. Chem. 273 (40): 25789–95. doi:10.1074/jbc.273.40.25789. PMID 9748251.
Marie-Cardine A, Verhagen AM, Eckerskorn C, Schraven B (1998). "SKAP-HOM, a novel adaptor protein homologous to the FYN-associated protein SKAP55.". FEBS Lett. 435 (1): 55–60. doi:10.1016/S0014-5793(98)01040-0. PMID 9755858.
Veale M, Raab M, Li Z, et al. (1999). "Novel isoform of lymphoid adaptor FYN-T-binding protein (FYB-130) interacts with SLP-76 and up-regulates interleukin 2 production.". J. Biol. Chem. 274 (40): 28427–35. doi:10.1074/jbc.274.40.28427. PMID 10497204.
Hamid N, Gustavsson A, Andersson K, et al. (1999). "YopH dephosphorylates Cas and Fyn-binding protein in macrophages.". Microb. Pathog. 27 (4): 231–42. doi:10.1006/mpat.1999.0301. PMID 10502464.
Geng L, Raab M, Rudd CE (1999). "Cutting edge: SLP-76 cooperativity with FYB/FYN-T in the Up-regulation of TCR-driven IL-2 transcription requires SLP-76 binding to FYB at Tyr595 and Tyr651.". J. Immunol. 163 (11): 5753–7. PMID 10570256.
Krause M, Sechi AS, Konradt M, et al. (2000). "Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton.". J. Cell Biol. 149 (1): 181–94. doi:10.1083/jcb.149.1.181. PMC 2175102. PMID 10747096. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2175102.
Kang H, Freund C, Duke-Cohan JS, et al. (2000). "SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55.". EMBO J. 19 (12): 2889–99. doi:10.1093/emboj/19.12.2889. PMC 203341. PMID 10856234. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=203341.
Asazuma N, Wilde JI, Berlanga O, et al. (2000). "Interaction of linker for activation of T cells with multiple adapter proteins in platelets activated by the glycoprotein VI-selective ligand, convulxin.". J. Biol. Chem. 275 (43): 33427–34. doi:10.1074/jbc.M001439200. PMID 10942756.
Li C, Iosef C, Jia CY, et al. (2003). "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. 278 (6): 3852–9. doi:10.1074/jbc.M206649200. PMID 12458214.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
Heuer K, Arbuzova A, Strauss H, et al. (2005). "The helically extended SH3 domain of the T cell adaptor protein ADAP is a novel lipid interaction domain.". J. Mol. Biol. 348 (4): 1025–35. doi:10.1016/j.jmb.2005.02.069. PMID 15843031.
Huang Y, Norton DD, Precht P, et al. (2005). "Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T cells.". J. Biol. Chem. 280 (25): 23576–83. doi:10.1074/jbc.M413201200. PMID 15849195.
Koga S, Yogo K, Yoshikawa K, et al. (2005). "Physical and functional association of c-Src and adhesion and degranulation promoting adaptor protein (ADAP) in osteoclastogenesis in vitro.". J. Biol. Chem. 280 (36): 31564–71. doi:10.1074/jbc.M502703200. PMID 16020549.
Duke-Cohan JS, Kang H, Liu H, Rudd CE (2006). "Regulation and function of SKAP-55 non-canonical motif binding to the SH3c domain of adhesion and degranulation-promoting adaptor protein.". J. Biol. Chem. 281 (19): 13743–50. doi:10.1074/jbc.M508774200. PMID 16461356.

PDB gallery

1ri9: Structure of a helically extended SH3 domain of the T cell adapter protein ADAP

2gtj: Reduced form of ADAP hSH3-N-domain

2gto: Oxidized form of ADAP hSH3-N

FYB

Interactions

References

Further reading