FYB1_HUMAN
ID FYB1_HUMAN Reviewed; 783 AA.
AC O15117; A8K2Y8; B4DLN2; E9PBV9; O00359; Q9NZI9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=FYN-binding protein 1 {ECO:0000312|HGNC:HGNC:4036};
DE AltName: Full=Adhesion and degranulation promoting adaptor protein;
DE Short=ADAP;
DE AltName: Full=FYB-120/130;
DE Short=p120/p130;
DE AltName: Full=FYN-T-binding protein;
DE AltName: Full=SLAP-130;
DE AltName: Full=SLP-76-associated phosphoprotein;
GN Name=FYB1 {ECO:0000312|HGNC:HGNC:4036}; Synonyms=FYB, SLAP130;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-120), INTERACTION WITH FYN AND
RP LCP2, AND VARIANT PHE-672.
RC TISSUE=Tonsil;
RX PubMed=9207119; DOI=10.1073/pnas.94.14.7493;
RA da Silva A.J., Li Z., de Vera C., Canto E., Findell P., Rudd C.E.;
RT "Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-
RT containing leukocyte protein 76 and modulates interleukin 2 production.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7493-7498(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-120), PROTEIN SEQUENCE OF 363-370,
RP AND VARIANT PHE-672.
RX PubMed=9115214; DOI=10.1074/jbc.272.18.11674;
RA Musci M.A., Hendricks-Taylor L.R., Motto D.G., Paskind M., Kamens J.,
RA Turck C.W., Koretzky G.A.;
RT "Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T
RT cell antigen receptor-stimulated protein tyrosine kinases.";
RL J. Biol. Chem. 272:11674-11677(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-130), FUNCTION, INTERACTION WITH
RP EVL, AND VARIANT PHE-672.
RX PubMed=10747096; DOI=10.1083/jcb.149.1.181;
RA Krause M., Sechi A.S., Konradt M., Monner D., Gertler F.B., Wehland J.;
RT "Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP),
RT Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3
RT complex link T cell receptor (TCR) signaling to the actin cytoskeleton.";
RL J. Cell Biol. 149:181-194(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS FYB-130 AND 3), AND
RP VARIANT PHE-672.
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM FYB-130), AND VARIANT
RP PHE-672.
RC TISSUE=Cerebellum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH SKAP1 AND SKAP2.
RX PubMed=9755858; DOI=10.1016/s0014-5793(98)01040-0;
RA Marie-Cardine A., Verhagen A.M., Eckerskorn C., Schraven B.;
RT "SKAP-HOM, a novel adaptor protein homologous to the FYN-associated protein
RT SKAP55.";
RL FEBS Lett. 435:55-60(1998).
RN [9]
RP INTERACTION WITH SKAP1.
RX PubMed=9748251; DOI=10.1074/jbc.273.40.25789;
RA Marie-Cardine A., Hendricks-Taylor L.R., Boerth N.J., Zhao H., Schraven B.,
RA Koretzky G.A.;
RT "Molecular interaction between the Fyn-associated protein SKAP55 and the
RT SLP-76-associated phosphoprotein SLAP-130.";
RL J. Biol. Chem. 273:25789-25795(1998).
RN [10]
RP INTERACTION WITH SKAP1 AND SKAP2, AND SUBCELLULAR LOCATION.
RX PubMed=9671755; DOI=10.1073/pnas.95.15.8779;
RA Liu J., Kang H., Raab M., da Silva A.J., Kraeft S.-K., Rudd C.E.;
RT "FYB (FYN binding protein) serves as a binding partner for lymphoid protein
RT and FYN kinase substrate SKAP55 and a SKAP55-related protein in T cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8779-8784(1998).
RN [11]
RP INTERACTION WITH SKAP2.
RX PubMed=10942756; DOI=10.1074/jbc.m001439200;
RA Asazuma N., Wilde J.I., Berlanga O., Leduc M., Leo A., Schweighoffer E.,
RA Tybulewicz V., Bon C., Liu S.K., McGlade C.J., Schraven B., Watson S.P.;
RT "Interaction of linker for activation of T cells with multiple adapter
RT proteins in platelets activated by the glycoprotein VI-selective ligand,
RT convulxin.";
RL J. Biol. Chem. 275:33427-33434(2000).
RN [12]
RP INTERACTION WITH SKAP1.
RX PubMed=10856234; DOI=10.1093/emboj/19.12.2889;
RA Kang H., Freund C., Duke-Cohan J.S., Musacchio A., Wagner G., Rudd C.E.;
RT "SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY
RT motif in immune cell adaptor SKAP55.";
RL EMBO J. 19:2889-2899(2000).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [14]
RP INTERACTION WITH SKAP1 AND FYN, AND FUNCTION.
RX PubMed=15849195; DOI=10.1074/jbc.m413201200;
RA Huang Y., Norton D.D., Precht P., Martindale J.L., Burkhardt J.K.,
RA Wange R.L.;
RT "Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T cells.";
RL J. Biol. Chem. 280:23576-23583(2005).
RN [15]
RP INTERACTION WITH SKAP1.
RX PubMed=16461356; DOI=10.1074/jbc.m508774200;
RA Duke-Cohan J.S., Kang H., Liu H., Rudd C.E.;
RT "Regulation and function of SKAP-55 non-canonical motif binding to the SH3c
RT domain of adhesion and degranulation-promoting adaptor protein.";
RL J. Biol. Chem. 281:13743-13750(2006).
RN [16]
RP FUNCTION.
RX PubMed=16980616; DOI=10.1128/mcb.00331-06;
RA Kliche S., Breitling D., Togni M., Pusch R., Heuer K., Wang X., Freund C.,
RA Kasirer-Friede A., Menasche G., Koretzky G.A., Schraven B.;
RT "The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated
RT integrin activation through plasma membrane targeting of Rap1.";
RL Mol. Cell. Biol. 26:7130-7144(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [18]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-457; TYR-571; SER-573
RP AND TYR-651, VARIANT [LARGE SCALE ANALYSIS] PHE-672, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-225; SER-329 AND
RP SER-457, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP INVOLVEMENT IN THC3.
RX PubMed=25516138; DOI=10.1186/s12881-014-0135-0;
RA Hamamy H., Makrythanasis P., Al-Allawi N., Muhsin A.A., Antonarakis S.E.;
RT "Recessive thrombocytopenia likely due to a homozygous pathogenic variant
RT in the FYB gene: case report.";
RL BMC Med. Genet. 15:135-135(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP INVOLVEMENT IN THC3, AND VARIANT THC3 131-TRP--ASP-783 DEL.
RX PubMed=25876182; DOI=10.1111/jth.12966;
RA Levin C., Koren A., Pretorius E., Rosenberg N., Shenkman B., Hauschner H.,
RA Zalman L., Khayat M., Salama I., Elpeleg O., Shalev S.;
RT "Deleterious mutation in the FYB gene is associated with congenital
RT autosomal recessive small-platelet thrombocytopenia.";
RL J. Thromb. Haemost. 13:1285-1292(2015).
RN [25]
RP INTERACTION WITH LCP2; SKAP1; FYN AND LCK.
RX PubMed=27335501; DOI=10.4049/jimmunol.1501913;
RA Jung S.H., Yoo E.H., Yu M.J., Song H.M., Kang H.Y., Cho J.Y., Lee J.R.;
RT "ARAP, a novel adaptor protein, is required for TCR signaling and integrin-
RT mediated adhesion.";
RL J. Immunol. 197:942-952(2016).
RN [26]
RP STRUCTURE BY NMR OF 683-771.
RX PubMed=15062083; DOI=10.1016/j.str.2004.02.021;
RA Heuer K., Kofler M., Langdon G., Thiemke K., Freund C.;
RT "Structure of a helically extended SH3 domain of the T cell adapter protein
RT ADAP.";
RL Structure 12:603-610(2004).
CC -!- FUNCTION: Acts as an adapter protein of the FYN and LCP2 signaling
CC cascades in T-cells (By similarity). May play a role in linking T-cell
CC signaling to remodeling of the actin cytoskeleton (PubMed:10747096,
CC PubMed:16980616). Modulates the expression of IL2 (By similarity).
CC Involved in platelet activation (By similarity). Prevents the
CC degradation of SKAP1 and SKAP2 (PubMed:15849195). May be involved in
CC high affinity immunoglobulin epsilon receptor signaling in mast cells
CC (By similarity). {ECO:0000250|UniProtKB:D3ZIE4,
CC ECO:0000250|UniProtKB:O35601, ECO:0000269|PubMed:10747096,
CC ECO:0000269|PubMed:15849195, ECO:0000269|PubMed:16980616}.
CC -!- SUBUNIT: Part of a complex consisting of SKAP2, FYB1 and PTPNS1 (By
CC similarity). Part of a complex consisting of SKAP2, FYB1 and LILRB3 (By
CC similarity). Part of a complex consisting of SKAP1, FYB1 and CLNK (By
CC similarity). Interacts with CLNK (via its SH2 domain); this interaction
CC allows SKAP1 and FYB1 to recruit FYN to the complex, thus promoting the
CC phosphorylation of CLNK by FYN (By similarity). Interacts with FYN
CC (PubMed:9207119, PubMed:15849195, PubMed:27335501). Interacts with LCP2
CC (PubMed:9207119, PubMed:27335501). Interacts with SKAP1
CC (PubMed:9755858, PubMed:9748251, PubMed:9671755, PubMed:10856234,
CC PubMed:15849195, PubMed:16461356, PubMed:27335501). Interacts with
CC SKAP2 (PubMed:9755858, PubMed:9671755, PubMed:10942756). Interacts with
CC FASLG (PubMed:19807924). Interacts with EVL (PubMed:10747096).
CC Interacts with TMEM47 (By similarity). Interacts with LCK
CC (PubMed:27335501). {ECO:0000250|UniProtKB:D3ZIE4,
CC ECO:0000250|UniProtKB:O35601, ECO:0000269|PubMed:10747096,
CC ECO:0000269|PubMed:10856234, ECO:0000269|PubMed:10942756,
CC ECO:0000269|PubMed:15849195, ECO:0000269|PubMed:16461356,
CC ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:27335501,
CC ECO:0000269|PubMed:9207119, ECO:0000269|PubMed:9671755,
CC ECO:0000269|PubMed:9748251, ECO:0000269|PubMed:9755858}.
CC -!- INTERACTION:
CC O15117; P06241: FYN; NbExp=4; IntAct=EBI-1753267, EBI-515315;
CC O15117; Q13094: LCP2; NbExp=9; IntAct=EBI-1753267, EBI-346946;
CC O15117; P16333: NCK1; NbExp=3; IntAct=EBI-1753267, EBI-389883;
CC O15117; O43639: NCK2; NbExp=3; IntAct=EBI-1753267, EBI-713635;
CC O15117; Q86WV1: SKAP1; NbExp=6; IntAct=EBI-1753267, EBI-2477305;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9671755}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00768}. Cell junction
CC {ECO:0000250|UniProtKB:O35601}. Note=Colocalizes with TMEM47 at cell-
CC cell contacts in podocytes. {ECO:0000250|UniProtKB:O35601}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=FYB-120;
CC IsoId=O15117-1; Sequence=Displayed;
CC Name=FYB-130;
CC IsoId=O15117-2; Sequence=VSP_042309;
CC Name=3;
CC IsoId=O15117-3; Sequence=VSP_047288, VSP_042309;
CC -!- TISSUE SPECIFICITY: Expressed in hematopoietic tissues such as myeloid
CC and T-cells, spleen and thymus. Not expressed in B-cells, nor in non-
CC lymphoid tissues.
CC -!- PTM: T-cell receptor ligation leads to increased tyrosine
CC phosphorylation.
CC -!- DISEASE: Thrombocytopenia 3 (THC3) [MIM:273900]: A form of
CC thrombocytopenia, a hematologic disorder defined by a decrease in the
CC number of platelets in circulating blood, resulting in the potential
CC for increased bleeding and decreased ability for clotting. THC3 is an
CC autosomal recessive form characterized by onset in infancy.
CC {ECO:0000269|PubMed:25516138, ECO:0000269|PubMed:25876182}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; AF001862; AAB62226.1; -; mRNA.
DR EMBL; U93049; AAC51300.1; -; mRNA.
DR EMBL; AF198052; AAF62400.1; -; mRNA.
DR EMBL; AK290403; BAF83092.1; -; mRNA.
DR EMBL; AK297077; BAG59594.1; -; mRNA.
DR EMBL; AC008964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471119; EAW55984.1; -; Genomic_DNA.
DR EMBL; BC117449; AAI17450.1; -; mRNA.
DR EMBL; BC143645; AAI43646.1; -; mRNA.
DR CCDS; CCDS47200.1; -. [O15117-1]
DR CCDS; CCDS54848.1; -. [O15117-2]
DR CCDS; CCDS58945.1; -. [O15117-3]
DR RefSeq; NP_001230022.1; NM_001243093.1. [O15117-3]
DR RefSeq; NP_001456.3; NM_001465.4. [O15117-2]
DR RefSeq; NP_955367.1; NM_199335.3. [O15117-1]
DR RefSeq; XP_006714527.1; XM_006714464.2. [O15117-2]
DR RefSeq; XP_006714528.1; XM_006714465.2.
DR RefSeq; XP_006714529.1; XM_006714466.2. [O15117-2]
DR RefSeq; XP_011512310.1; XM_011514008.2. [O15117-3]
DR RefSeq; XP_011512311.1; XM_011514009.1. [O15117-2]
DR RefSeq; XP_011512312.1; XM_011514010.1. [O15117-2]
DR PDB; 1RI9; NMR; -; A=683-771.
DR PDB; 2GTJ; NMR; -; A=486-579.
DR PDB; 2GTO; NMR; -; A=486-579.
DR PDBsum; 1RI9; -.
DR PDBsum; 2GTJ; -.
DR PDBsum; 2GTO; -.
DR AlphaFoldDB; O15117; -.
DR BMRB; O15117; -.
DR SMR; O15117; -.
DR BioGRID; 108809; 18.
DR CORUM; O15117; -.
DR DIP; DIP-42204N; -.
DR ELM; O15117; -.
DR IntAct; O15117; 27.
DR MINT; O15117; -.
DR STRING; 9606.ENSP00000427114; -.
DR GlyGen; O15117; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; O15117; -.
DR PhosphoSitePlus; O15117; -.
DR BioMuta; FYB1; -.
DR OGP; O15117; -.
DR jPOST; O15117; -.
DR MassIVE; O15117; -.
DR MaxQB; O15117; -.
DR PeptideAtlas; O15117; -.
DR PRIDE; O15117; -.
DR ProteomicsDB; 4545; -.
DR ProteomicsDB; 48451; -. [O15117-1]
DR ProteomicsDB; 48452; -. [O15117-2]
DR Antibodypedia; 23110; 349 antibodies from 38 providers.
DR DNASU; 2533; -.
DR Ensembl; ENST00000351578.12; ENSP00000316460.7; ENSG00000082074.19. [O15117-1]
DR Ensembl; ENST00000512982.4; ENSP00000425845.3; ENSG00000082074.19. [O15117-2]
DR Ensembl; ENST00000515010.5; ENSP00000426346.1; ENSG00000082074.19. [O15117-1]
DR Ensembl; ENST00000646045.2; ENSP00000493623.1; ENSG00000082074.19. [O15117-3]
DR GeneID; 2533; -.
DR KEGG; hsa:2533; -.
DR MANE-Select; ENST00000512982.4; ENSP00000425845.3; NM_001465.6; NP_001456.3. [O15117-2]
DR UCSC; uc003jls.4; human. [O15117-1]
DR CTD; 2533; -.
DR DisGeNET; 2533; -.
DR GeneCards; FYB1; -.
DR HGNC; HGNC:4036; FYB1.
DR HPA; ENSG00000082074; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; FYB1; -.
DR MIM; 273900; phenotype.
DR MIM; 602731; gene.
DR neXtProt; NX_O15117; -.
DR OpenTargets; ENSG00000082074; -.
DR Orphanet; 566192; Congenital autosomal recessive small-platelet thrombocytopenia.
DR PharmGKB; PA28452; -.
DR VEuPathDB; HostDB:ENSG00000082074; -.
DR eggNOG; ENOG502QTTQ; Eukaryota.
DR GeneTree; ENSGT00530000063460; -.
DR HOGENOM; CLU_339375_0_0_1; -.
DR InParanoid; O15117; -.
DR OMA; KSSTWSW; -.
DR OrthoDB; 831692at2759; -.
DR PhylomeDB; O15117; -.
DR TreeFam; TF337003; -.
DR PathwayCommons; O15117; -.
DR Reactome; R-HSA-202433; Generation of second messenger molecules.
DR Reactome; R-HSA-391160; Signal regulatory protein family interactions.
DR SignaLink; O15117; -.
DR SIGNOR; O15117; -.
DR BioGRID-ORCS; 2533; 4 hits in 1074 CRISPR screens.
DR ChiTaRS; FYB; human.
DR EvolutionaryTrace; O15117; -.
DR GeneWiki; FYB; -.
DR GenomeRNAi; 2533; -.
DR Pharos; O15117; Tbio.
DR PRO; PR:O15117; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O15117; protein.
DR Bgee; ENSG00000082074; Expressed in monocyte and 180 other tissues.
DR ExpressionAtlas; O15117; baseline and differential.
DR Genevisible; O15117; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; TAS:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR CDD; cd11867; hSH3_ADAP; 1.
DR InterPro; IPR030635; FYB1.
DR InterPro; IPR043443; FYB1/2-like.
DR InterPro; IPR035540; FYB_hSH3.
DR InterPro; IPR029294; hSH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR16830; PTHR16830; 3.
DR PANTHER; PTHR16830:SF13; PTHR16830:SF13; 3.
DR Pfam; PF14603; hSH3; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell junction;
KW Coiled coil; Cytoplasm; Direct protein sequencing; Disease variant;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..783
FT /note="FYN-binding protein 1"
FT /id="PRO_0000087396"
FT DOMAIN 511..572
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 700..768
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..448
FT /note="Interaction with SKAP1"
FT REGION 598..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 456..507
FT /evidence="ECO:0000255"
FT MOTIF 462..465
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 469..505
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 595..598
FT /note="SH2-binding; to LCP2"
FT MOTIF 625..628
FT /note="SH2-binding; to FYN"
FT MOTIF 674..700
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..364
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35601"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 571
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35601"
FT MOD_RES 651
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1
FT /note="M -> MDGKADVKSLM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047288"
FT VAR_SEQ 636
FT /note="G -> GSTLQVQEKSNTWSWGILKMLKGKDDRKKSIREKPKVSDSDNNEGSS
FT (in isoform FYB-130 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10747096,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_042309"
FT VARIANT 51
FT /note="P -> L (in dbSNP:rs1642515)"
FT /id="VAR_056880"
FT VARIANT 131..783
FT /note="Missing (in THC3)"
FT /evidence="ECO:0000269|PubMed:25876182"
FT /id="VAR_078810"
FT VARIANT 332
FT /note="K -> R (in dbSNP:rs3749741)"
FT /id="VAR_056881"
FT VARIANT 672
FT /note="V -> F (in dbSNP:rs379707)"
FT /evidence="ECO:0000269|PubMed:10747096,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9115214, ECO:0000269|PubMed:9207119,
FT ECO:0007744|PubMed:19690332"
FT /id="VAR_060592"
FT CONFLICT 27
FT /note="N -> S (in Ref. 4; BAF83092)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="P -> L (in Ref. 2; AAC51300)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="L -> V (in Ref. 1; AAB62226)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="R -> C (in Ref. 4; BAF83092)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="K -> E (in Ref. 4; BAF83092)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="V -> A (in Ref. 4; BAF83092)"
FT /evidence="ECO:0000305"
FT HELIX 498..504
FT /evidence="ECO:0007829|PDB:2GTJ"
FT STRAND 514..520
FT /evidence="ECO:0007829|PDB:2GTJ"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:2GTO"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:2GTJ"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:2GTJ"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:2GTJ"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:2GTO"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:2GTJ"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:2GTJ"
FT HELIX 572..575
FT /evidence="ECO:0007829|PDB:2GTO"
FT HELIX 690..698
FT /evidence="ECO:0007829|PDB:1RI9"
FT STRAND 736..750
FT /evidence="ECO:0007829|PDB:1RI9"
FT TURN 751..753
FT /evidence="ECO:0007829|PDB:1RI9"
FT STRAND 754..759
FT /evidence="ECO:0007829|PDB:1RI9"
FT HELIX 760..762
FT /evidence="ECO:0007829|PDB:1RI9"
SQ SEQUENCE 783 AA; 85387 MW; 4EE28EF12AA0E457 CRC64;
MAKYNTGGNP TEDVSVNSRP FRVTGPNSSS GIQARKNLFN NQGNASPPAG PSNVPKFGSP
KPPVAVKPSS EEKPDKEPKP PFLKPTGAGQ RFGTPASLTT RDPEAKVGFL KPVGPKPINL
PKEDSKPTFP WPPGNKPSLH SVNQDHDLKP LGPKSGPTPP TSENEQKQAF PKLTGVKGKF
MSASQDLEPK PLFPKPAFGQ KPPLSTENSH EDESPMKNVS SSKGSPAPLG VRSKSGPLKP
AREDSENKDH AGEISSLPFP GVVLKPAASR GGPGLSKNGE EKKEDRKIDA AKNTFQSKIN
QEELASGTPP ARFPKAPSKL TVGGPWGQSQ EKEKGDKNSA TPKQKPLPPL FTLGPPPPKP
NRPPNVDLTK FHKTSSGNST SKGQTSYSTT SLPPPPPSHP ASQPPLPASH PSQPPVPSLP
PRNIKPPFDL KSPVNEDNQD GVTHSDGAGN LDEEQDSEGE TYEDIEASKE REKKREKEEK
KRLELEKKEQ KEKEKKEQEI KKKFKLTGPI QVIHLAKACC DVKGGKNELS FKQGEQIEII
RITDNPEGKW LGRTARGSYG YIKTTAVEID YDSLKLKKDS LGAPSRPIED DQEVYDDVAE
QDDISSHSQS GSGGIFPPPP DDDIYDGIEE EDADDGFPAP PKQLDMGDEV YDDVDTSDFP
VSSAEMSQGT NVGKAKTEEK DLKKLKKQEK EEKDFRKKFK YDGEIRVLYS TKVTTSITSK
KWGTRDLQVK PGESLEVIQT TDDTKVLCRN EEGKYGYVLR SYLADNDGEI YDDIADGCIY
DND
