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O15117

- FYB_HUMAN

UniProt

O15117 - FYB_HUMAN

Protein

FYN-binding protein

Gene

FYB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (24 Nov 2009)
      Previous versions | rss
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    Functioni

    Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells. Modulates the expression of interleukin-2 (IL-2). Involved in platelet activation. Prevents the degradation of SKAP1 and SKAP2. May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton.3 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. receptor binding Source: UniProtKB

    GO - Biological processi

    1. immune response Source: ProtInc
    2. intracellular signal transduction Source: ProtInc
    3. NLS-bearing protein import into nucleus Source: ProtInc
    4. protein phosphorylation Source: ProtInc
    5. signal transduction Source: ProtInc
    6. T cell receptor signaling pathway Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_12623. Generation of second messenger molecules.
    REACT_23916. Signal regulatory protein (SIRP) family interactions.
    SignaLinkiO15117.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FYN-binding protein
    Alternative name(s):
    Adhesion and degranulation promoting adaptor protein
    Short name:
    ADAP
    FYB-120/130
    Short name:
    p120/p130
    FYN-T-binding protein
    SLAP-130
    SLP-76-associated phosphoprotein
    Gene namesi
    Name:FYB
    Synonyms:SLAP130
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:4036. FYB.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28452.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 783782FYN-binding proteinPRO_0000087396Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei3 – 31N6-acetyllysine1 Publication
    Modified residuei28 – 281PhosphoserineBy similarity
    Modified residuei46 – 461Phosphoserine2 Publications
    Modified residuei457 – 4571Phosphoserine1 Publication
    Modified residuei571 – 5711Phosphotyrosine1 Publication
    Modified residuei573 – 5731Phosphoserine1 Publication
    Modified residuei651 – 6511Phosphotyrosine1 Publication

    Post-translational modificationi

    T-cell receptor ligation leads to increased tyrosine phosphorylation.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO15117.
    PaxDbiO15117.
    PRIDEiO15117.

    2D gel databases

    OGPiO15117.

    PTM databases

    PhosphoSiteiO15117.

    Miscellaneous databases

    PMAP-CutDBO15117.

    Expressioni

    Tissue specificityi

    Expressed in hematopoietic tissues such as myeloid and T-cells, spleen and thymus. Not expressed in B-cells, nor in non-lymphoid tissues.

    Gene expression databases

    ArrayExpressiO15117.
    BgeeiO15117.
    CleanExiHS_FYB.
    GenevestigatoriO15117.

    Organism-specific databases

    HPAiCAB025336.
    HPA026796.

    Interactioni

    Subunit structurei

    Part of a complex consisting of SKAP2, FYB and PTPNS1. Part of a complex consisting of SKAP2, FYB and LILRB3 By similarity. Interacts with FYN, LCP2, SKAP1 and SKAP2. Interacts with FASLG. Interacts with EVL.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FYNP062412EBI-1753267,EBI-515315
    LCP2Q130945EBI-1753267,EBI-346946
    NCK1P163333EBI-1753267,EBI-389883
    SKAP1Q86WV16EBI-1753267,EBI-2477305

    Protein-protein interaction databases

    BioGridi108809. 13 interactions.
    DIPiDIP-42204N.
    IntActiO15117. 26 interactions.
    MINTiMINT-1176058.
    STRINGi9606.ENSP00000316460.

    Structurei

    Secondary structure

    1
    783
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi498 – 5047
    Beta strandi514 – 5207
    Beta strandi526 – 5283
    Beta strandi537 – 5415
    Beta strandi546 – 5483
    Beta strandi551 – 5533
    Beta strandi559 – 5624
    Helixi564 – 5663
    Beta strandi567 – 5693
    Helixi572 – 5754
    Helixi690 – 6989
    Beta strandi736 – 75015
    Turni751 – 7533
    Beta strandi754 – 7596
    Helixi760 – 7623

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RI9NMR-A683-771[»]
    2GTJNMR-A486-579[»]
    2GTONMR-A486-579[»]
    ProteinModelPortaliO15117.
    SMRiO15117. Positions 506-579, 689-765.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15117.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini514 – 57057SH3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni348 – 448101Interaction with SKAP1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili456 – 50752Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi462 – 4654SH2-bindingSequence Analysis
    Motifi469 – 50537Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi595 – 5984SH2-binding; to LCP2
    Motifi625 – 6284SH2-binding; to FYN
    Motifi674 – 70027Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi355 – 3606Poly-Pro
    Compositional biasi393 – 3975Poly-Pro
    Compositional biasi617 – 6204Poly-Pro

    Sequence similaritiesi

    Contains 1 SH3 domain.Curated

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG18948.
    HOGENOMiHOG000008686.
    HOVERGENiHBG005774.
    KOiK17698.
    OMAiACCDVKG.
    OrthoDBiEOG70W3CP.
    PhylomeDBiO15117.
    TreeFamiTF337003.

    Family and domain databases

    InterProiIPR029294. hSH3.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF14603. hSH3. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 2 hits.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform FYB-120 (identifier: O15117-1) [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

    MAKYNTGGNP TEDVSVNSRP FRVTGPNSSS GIQARKNLFN NQGNASPPAG    50
    PSNVPKFGSP KPPVAVKPSS EEKPDKEPKP PFLKPTGAGQ RFGTPASLTT 100
    RDPEAKVGFL KPVGPKPINL PKEDSKPTFP WPPGNKPSLH SVNQDHDLKP 150
    LGPKSGPTPP TSENEQKQAF PKLTGVKGKF MSASQDLEPK PLFPKPAFGQ 200
    KPPLSTENSH EDESPMKNVS SSKGSPAPLG VRSKSGPLKP AREDSENKDH 250
    AGEISSLPFP GVVLKPAASR GGPGLSKNGE EKKEDRKIDA AKNTFQSKIN 300
    QEELASGTPP ARFPKAPSKL TVGGPWGQSQ EKEKGDKNSA TPKQKPLPPL 350
    FTLGPPPPKP NRPPNVDLTK FHKTSSGNST SKGQTSYSTT SLPPPPPSHP 400
    ASQPPLPASH PSQPPVPSLP PRNIKPPFDL KSPVNEDNQD GVTHSDGAGN 450
    LDEEQDSEGE TYEDIEASKE REKKREKEEK KRLELEKKEQ KEKEKKEQEI 500
    KKKFKLTGPI QVIHLAKACC DVKGGKNELS FKQGEQIEII RITDNPEGKW 550
    LGRTARGSYG YIKTTAVEID YDSLKLKKDS LGAPSRPIED DQEVYDDVAE 600
    QDDISSHSQS GSGGIFPPPP DDDIYDGIEE EDADDGFPAP PKQLDMGDEV 650
    YDDVDTSDFP VSSAEMSQGT NVGKAKTEEK DLKKLKKQEK EEKDFRKKFK 700
    YDGEIRVLYS TKVTTSITSK KWGTRDLQVK PGESLEVIQT TDDTKVLCRN 750
    EEGKYGYVLR SYLADNDGEI YDDIADGCIY DND 783
    Length:783
    Mass (Da):85,387
    Last modified:November 24, 2009 - v2
    Checksum:i4EE28EF12AA0E457
    GO
    Isoform FYB-130 (identifier: O15117-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         636-636: G → GSTLQVQEKSNTWSWGILKMLKGKDDRKKSIREKPKVSDSDNNEGSS

    Show »
    Length:829
    Mass (Da):90,606
    Checksum:iBDDEE1977674BC65
    GO
    Isoform 3 (identifier: O15117-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MDGKADVKSLM
         636-636: G → GSTLQVQEKSNTWSWGILKMLKGKDDRKKSIREKPKVSDSDNNEGSS

    Note: No experimental confirmation available.

    Show »
    Length:839
    Mass (Da):91,651
    Checksum:i3EB9A0C1FF816B6B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271N → S in BAF83092. (PubMed:14702039)Curated
    Sequence conflicti273 – 2731P → L in AAC51300. (PubMed:9115214)Curated
    Sequence conflicti275 – 2751L → V in AAB62226. (PubMed:9207119)Curated
    Sequence conflicti541 – 5411R → C in BAF83092. (PubMed:14702039)Curated
    Sequence conflicti674 – 6741K → E in BAF83092. (PubMed:14702039)Curated
    Sequence conflicti729 – 7291V → A in BAF83092. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511P → L.
    Corresponds to variant rs1642515 [ dbSNP | Ensembl ].
    VAR_056880
    Natural varianti332 – 3321K → R.
    Corresponds to variant rs3749741 [ dbSNP | Ensembl ].
    VAR_056881
    Natural varianti672 – 6721V → F.6 Publications
    Corresponds to variant rs379707 [ dbSNP | Ensembl ].
    VAR_060592

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MDGKADVKSLM in isoform 3. 1 PublicationVSP_047288
    Alternative sequencei636 – 6361G → GSTLQVQEKSNTWSWGILKM LKGKDDRKKSIREKPKVSDS DNNEGSS in isoform FYB-130 and isoform 3. 3 PublicationsVSP_042309

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001862 mRNA. Translation: AAB62226.1.
    U93049 mRNA. Translation: AAC51300.1.
    AF198052 mRNA. Translation: AAF62400.1.
    AK290403 mRNA. Translation: BAF83092.1.
    AK297077 mRNA. Translation: BAG59594.1.
    AC008964 Genomic DNA. No translation available.
    AC010633 Genomic DNA. No translation available.
    AC025471 Genomic DNA. No translation available.
    CH471119 Genomic DNA. Translation: EAW55984.1.
    BC117449 mRNA. Translation: AAI17450.1.
    BC143645 mRNA. Translation: AAI43646.1.
    CCDSiCCDS47200.1. [O15117-1]
    CCDS54848.1. [O15117-2]
    CCDS58945.1. [O15117-3]
    RefSeqiNP_001230022.1. NM_001243093.1. [O15117-3]
    NP_001456.3. NM_001465.4. [O15117-2]
    NP_955367.1. NM_199335.3. [O15117-1]
    XP_006714527.1. XM_006714464.1. [O15117-2]
    XP_006714528.1. XM_006714465.1. [O15117-2]
    XP_006714529.1. XM_006714466.1. [O15117-2]
    UniGeneiHs.370503.
    Hs.691768.

    Genome annotation databases

    EnsembliENST00000351578; ENSP00000316460; ENSG00000082074. [O15117-1]
    ENST00000505428; ENSP00000427114; ENSG00000082074. [O15117-2]
    ENST00000512982; ENSP00000425845; ENSG00000082074. [O15117-2]
    ENST00000515010; ENSP00000426346; ENSG00000082074. [O15117-1]
    GeneIDi2533.
    KEGGihsa:2533.
    UCSCiuc003jls.3. human. [O15117-1]
    uc003jlt.3. human. [O15117-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001862 mRNA. Translation: AAB62226.1 .
    U93049 mRNA. Translation: AAC51300.1 .
    AF198052 mRNA. Translation: AAF62400.1 .
    AK290403 mRNA. Translation: BAF83092.1 .
    AK297077 mRNA. Translation: BAG59594.1 .
    AC008964 Genomic DNA. No translation available.
    AC010633 Genomic DNA. No translation available.
    AC025471 Genomic DNA. No translation available.
    CH471119 Genomic DNA. Translation: EAW55984.1 .
    BC117449 mRNA. Translation: AAI17450.1 .
    BC143645 mRNA. Translation: AAI43646.1 .
    CCDSi CCDS47200.1. [O15117-1 ]
    CCDS54848.1. [O15117-2 ]
    CCDS58945.1. [O15117-3 ]
    RefSeqi NP_001230022.1. NM_001243093.1. [O15117-3 ]
    NP_001456.3. NM_001465.4. [O15117-2 ]
    NP_955367.1. NM_199335.3. [O15117-1 ]
    XP_006714527.1. XM_006714464.1. [O15117-2 ]
    XP_006714528.1. XM_006714465.1. [O15117-2 ]
    XP_006714529.1. XM_006714466.1. [O15117-2 ]
    UniGenei Hs.370503.
    Hs.691768.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RI9 NMR - A 683-771 [» ]
    2GTJ NMR - A 486-579 [» ]
    2GTO NMR - A 486-579 [» ]
    ProteinModelPortali O15117.
    SMRi O15117. Positions 506-579, 689-765.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108809. 13 interactions.
    DIPi DIP-42204N.
    IntActi O15117. 26 interactions.
    MINTi MINT-1176058.
    STRINGi 9606.ENSP00000316460.

    PTM databases

    PhosphoSitei O15117.

    2D gel databases

    OGPi O15117.

    Proteomic databases

    MaxQBi O15117.
    PaxDbi O15117.
    PRIDEi O15117.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351578 ; ENSP00000316460 ; ENSG00000082074 . [O15117-1 ]
    ENST00000505428 ; ENSP00000427114 ; ENSG00000082074 . [O15117-2 ]
    ENST00000512982 ; ENSP00000425845 ; ENSG00000082074 . [O15117-2 ]
    ENST00000515010 ; ENSP00000426346 ; ENSG00000082074 . [O15117-1 ]
    GeneIDi 2533.
    KEGGi hsa:2533.
    UCSCi uc003jls.3. human. [O15117-1 ]
    uc003jlt.3. human. [O15117-2 ]

    Organism-specific databases

    CTDi 2533.
    GeneCardsi GC05M039112.
    H-InvDB HIX0024785.
    HGNCi HGNC:4036. FYB.
    HPAi CAB025336.
    HPA026796.
    MIMi 602731. gene.
    neXtProti NX_O15117.
    PharmGKBi PA28452.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG18948.
    HOGENOMi HOG000008686.
    HOVERGENi HBG005774.
    KOi K17698.
    OMAi ACCDVKG.
    OrthoDBi EOG70W3CP.
    PhylomeDBi O15117.
    TreeFami TF337003.

    Enzyme and pathway databases

    Reactomei REACT_12623. Generation of second messenger molecules.
    REACT_23916. Signal regulatory protein (SIRP) family interactions.
    SignaLinki O15117.

    Miscellaneous databases

    EvolutionaryTracei O15117.
    GeneWikii FYB.
    GenomeRNAii 2533.
    NextBioi 9991.
    PMAP-CutDB O15117.
    PROi O15117.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15117.
    Bgeei O15117.
    CleanExi HS_FYB.
    Genevestigatori O15117.

    Family and domain databases

    InterProi IPR029294. hSH3.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF14603. hSH3. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production."
      da Silva A.J., Li Z., de Vera C., Canto E., Findell P., Rudd C.E.
      Proc. Natl. Acad. Sci. U.S.A. 94:7493-7498(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-120), INTERACTION WITH FYN AND LCP2, VARIANT PHE-672.
      Tissue: Tonsil.
    2. "Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases."
      Musci M.A., Hendricks-Taylor L.R., Motto D.G., Paskind M., Kamens J., Turck C.W., Koretzky G.A.
      J. Biol. Chem. 272:11674-11677(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-120), PROTEIN SEQUENCE OF 363-370, VARIANT PHE-672.
    3. "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."
      Krause M., Sechi A.S., Konradt M., Monner D., Gertler F.B., Wehland J.
      J. Cell Biol. 149:181-194(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-130), FUNCTION, INTERACTION WITH EVL, VARIANT PHE-672.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS FYB-130 AND 3), VARIANT PHE-672.
      Tissue: Umbilical cord blood.
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM FYB-130), VARIANT PHE-672.
      Tissue: Cerebellum.
    8. "SKAP-HOM, a novel adaptor protein homologous to the FYN-associated protein SKAP55."
      Marie-Cardine A., Verhagen A.M., Eckerskorn C., Schraven B.
      FEBS Lett. 435:55-60(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKAP1 AND SKAP2.
    9. "Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130."
      Marie-Cardine A., Hendricks-Taylor L.R., Boerth N.J., Zhao H., Schraven B., Koretzky G.A.
      J. Biol. Chem. 273:25789-25795(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKAP1.
    10. "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."
      Liu J., Kang H., Raab M., da Silva A.J., Kraeft S.-K., Rudd C.E.
      Proc. Natl. Acad. Sci. U.S.A. 95:8779-8784(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKAP1 AND SKAP2, SUBCELLULAR LOCATION.
    11. "Interaction of linker for activation of T cells with multiple adapter proteins in platelets activated by the glycoprotein VI-selective ligand, convulxin."
      Asazuma N., Wilde J.I., Berlanga O., Leduc M., Leo A., Schweighoffer E., Tybulewicz V., Bon C., Liu S.K., McGlade C.J., Schraven B., Watson S.P.
      J. Biol. Chem. 275:33427-33434(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKAP2.
    12. "SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55."
      Kang H., Freund C., Duke-Cohan J.S., Musacchio A., Wagner G., Rudd C.E.
      EMBO J. 19:2889-2899(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKAP1.
    13. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T cells."
      Huang Y., Norton D.D., Precht P., Martindale J.L., Burkhardt J.K., Wange R.L.
      J. Biol. Chem. 280:23576-23583(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKAP1 AND FYN, FUNCTION.
    15. "Regulation and function of SKAP-55 non-canonical motif binding to the SH3c domain of adhesion and degranulation-promoting adaptor protein."
      Duke-Cohan J.S., Kang H., Liu H., Rudd C.E.
      J. Biol. Chem. 281:13743-13750(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKAP1.
    16. "The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated integrin activation through plasma membrane targeting of Rap1."
      Kliche S., Breitling D., Togni M., Pusch R., Heuer K., Wang X., Freund C., Kasirer-Friede A., Menasche G., Koretzky G.A., Schraven B.
      Mol. Cell. Biol. 26:7130-7144(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    18. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-457; TYR-571; SER-573 AND TYR-651, VARIANT [LARGE SCALE ANALYSIS] PHE-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    21. "Structure of a helically extended SH3 domain of the T cell adapter protein ADAP."
      Heuer K., Kofler M., Langdon G., Thiemke K., Freund C.
      Structure 12:603-610(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 683-771.

    Entry informationi

    Entry nameiFYB_HUMAN
    AccessioniPrimary (citable) accession number: O15117
    Secondary accession number(s): A8K2Y8
    , B4DLN2, E9PBV9, O00359, Q9NZI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3