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Q8C180

- FRS2_MOUSE

UniProt

Q8C180 - FRS2_MOUSE

Protein

Fibroblast growth factor receptor substrate 2

Gene

Frs2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Adapter protein that links activated FGR and NGF receptors to downstream signaling pathways. Plays an important role in the activation of MAP kinases and in the phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, in response to ligand-mediated activation of FGFR1. Modulates signaling via SHC1 by competing for a common binding site on NTRK1.5 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. transmembrane receptor protein tyrosine kinase adaptor activity Source: MGI

    GO - Biological processi

    1. activation of MAPK activity Source: MGI
    2. anterior/posterior axis specification, embryo Source: MGI
    3. fibroblast growth factor receptor signaling pathway Source: MGI
    4. forebrain development Source: MGI
    5. gastrulation with mouth forming second Source: MGI
    6. lens development in camera-type eye Source: MGI
    7. lens fiber cell development Source: MGI
    8. neuroblast proliferation Source: MGI
    9. optic placode formation involved in camera-type eye formation Source: MGI
    10. organ induction Source: MGI
    11. prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Source: MGI
    12. regulation of apoptotic process Source: MGI
    13. regulation of epithelial cell proliferation Source: MGI
    14. regulation of ERK1 and ERK2 cascade Source: MGI
    15. transmembrane receptor protein tyrosine kinase signaling pathway Source: MGI
    16. ventricular septum development Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_196455. Signaling by FGFR mutants.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198525. Negative regulation of FGFR signaling.
    REACT_223993. PI-3K cascade.
    REACT_226341. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibroblast growth factor receptor substrate 2
    Short name:
    FGFR substrate 2
    Alternative name(s):
    FGFR-signaling adaptor SNT
    FRS2-alpha
    Suc1-associated neurotrophic factor target 1
    Short name:
    SNT-1
    Gene namesi
    Name:Frs2
    Synonyms:Frs2a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1100860. Frs2.

    Subcellular locationi

    Membrane 1 Publication; Lipid-anchor 1 Publication

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. cytoplasm Source: MGI
    3. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Abolishes myristoylation and membrane association. 1 Publication
    Mutagenesisi196 – 1961Y → F: Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-306; F-349; F-392 and F-436. 1 Publication
    Mutagenesisi306 – 3061Y → F: Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-349; F-392 and F-436. 1 Publication
    Mutagenesisi349 – 3491Y → F: Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-306; F-392 and F-436. 1 Publication
    Mutagenesisi392 – 3921Y → F: Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-306; F-349 and F-436. 1 Publication
    Mutagenesisi436 – 4361Y → F: Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-306; F-349 and F-392. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedSequence Analysis
    Chaini2 – 508507Fibroblast growth factor receptor substrate 2PRO_0000087345Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Modified residuei196 – 1961Phosphotyrosine; by FGFR13 Publications
    Modified residuei211 – 2111Phosphoserine1 Publication
    Modified residuei221 – 2211PhosphoserineBy similarity
    Modified residuei306 – 3061Phosphotyrosine; by FGFR13 Publications
    Modified residuei349 – 3491Phosphotyrosine; by FGFR14 Publications
    Modified residuei392 – 3921Phosphotyrosine; by FGFR13 Publications
    Modified residuei436 – 4361Phosphotyrosine; by FGFR12 Publications
    Modified residuei471 – 4711Phosphotyrosine; by FGFR11 Publication

    Post-translational modificationi

    Phosphorylated on tyrosine residues upon stimulation by FGF2 or NGFB. Phosphorylated by ULK2 (in vitro). Phosphorylated on tyrosine residues by activated ALK and FGFR1. Phosphorylated on tyrosine residues upon activation of FGFR2 and FGFR3. Phosphorylated on threonine residues by MAP kinases; this inhibits tyrosine phosphorylation, and thereby down-regulates FRS2-mediated activation of MAP kinases.
    Ubiquitinated when tyrosine phosphorylated and in a complex with GRB2. The unphosphorylated form is not subject to ubiquitination.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ8C180.

    PTM databases

    PhosphoSiteiQ8C180.

    Expressioni

    Tissue specificityi

    Ubiquitous. Expression is highest in brain, kidney, lung and testis.1 Publication

    Gene expression databases

    BgeeiQ8C180.
    CleanExiMM_FRS2.
    GenevestigatoriQ8C180.

    Interactioni

    Subunit structurei

    Part of a complex containing FRS2, GRB2, GAB1, PIK3R1 and SOS1. Part of a complex containing GRB2 and CBL. Binds ALK, CKS2, FGFR1, RET, MAPK1/ERK2, MAPK3/ERK1 and SRC. The tyrosine-phosphorylated protein binds the SH2 domains of GRB2 and PTPN11. Interacts with NTRK1, NTRK2 and NTRK3 (phosphorylated upon ligand-binding) By similarity. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Grb2Q606315EBI-6880000,EBI-1688

    Protein-protein interaction databases

    BioGridi236497. 6 interactions.
    IntActiQ8C180. 2 interactions.
    MINTiMINT-8013548.
    STRINGi10090.ENSMUSP00000020381.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C180.
    SMRiQ8C180. Positions 11-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 115103IRS-type PTBPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 IRS-type PTB domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG316561.
    GeneTreeiENSGT00510000046707.
    HOGENOMiHOG000290694.
    HOVERGENiHBG062705.
    InParanoidiQ8C180.
    KOiK12461.
    OMAiTRRRDCT.
    OrthoDBiEOG7QG43P.
    PhylomeDBiQ8C180.
    TreeFamiTF324994.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR002404. Insln_rcpt_S1.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF02174. IRS. 1 hit.
    [Graphical view]
    SMARTiSM00310. PTBI. 1 hit.
    [Graphical view]
    PROSITEiPS51064. IRS_PTB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8C180-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSCCSCPDK DTVPDNHRNK FKVINVDDDG NELGSGVMEL TDTELILYTR    50
    KRDSVKWHYL CLRRYGYDSN LFSFESGRRC QTGQGIFAFK CARAEELFNM 100
    LQEIMQNNSI NVVEEPVVER SSHQTELEVP RTPRTPTTPG LGAQNLPNGY 150
    PRYPSFGDAS SHPSSRHPSV GSARLPSVGE ESTHPLLVAE EQVHTYVNTT 200
    GVQEERKNRA SVHVPPEARV SNAESNTPKE EPSNPEDRDP QVLLKPEGVR 250
    FVLGPTPVQK QLMEKEKLEQ LGKDPVSGSG AGNTEWDTGY DSDERRDVPP 300
    VNKLVYENIN GLSIPSASGV RRGRLTSTST SDTQNINNSA QRRPALLNYE 350
    NLPSLPPVWE ARKLSRDEDD NLGPKTPSLN GYHNNLDPMH NYVNTENVTV 400
    PASAHKIDYS KRRDCTPTVF NFDIRRPSLE HRQLNYIQVD LEGGSDSDNP 450
    QTPKTPTTPL PQTPTRRTEL YAVIDIERTA AMSNLQKALP RDDGTSRKTR 500
    HNSTDLPM 508
    Length:508
    Mass (Da):56,794
    Last modified:January 23, 2007 - v3
    Checksum:iDFFE8A818BFF8631
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK028813 mRNA. Translation: BAC26132.1.
    BC043109 mRNA. Translation: AAH43109.1.
    BC055334 mRNA. Translation: AAH55334.1.
    CCDSiCCDS24190.1.
    RefSeqiNP_808466.1. NM_177798.3.
    UniGeneiMm.135965.

    Genome annotation databases

    EnsembliENSMUST00000020381; ENSMUSP00000020381; ENSMUSG00000020170.
    GeneIDi327826.
    KEGGimmu:327826.
    UCSCiuc007hct.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK028813 mRNA. Translation: BAC26132.1 .
    BC043109 mRNA. Translation: AAH43109.1 .
    BC055334 mRNA. Translation: AAH55334.1 .
    CCDSi CCDS24190.1.
    RefSeqi NP_808466.1. NM_177798.3.
    UniGenei Mm.135965.

    3D structure databases

    ProteinModelPortali Q8C180.
    SMRi Q8C180. Positions 11-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 236497. 6 interactions.
    IntActi Q8C180. 2 interactions.
    MINTi MINT-8013548.
    STRINGi 10090.ENSMUSP00000020381.

    PTM databases

    PhosphoSitei Q8C180.

    Proteomic databases

    PRIDEi Q8C180.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020381 ; ENSMUSP00000020381 ; ENSMUSG00000020170 .
    GeneIDi 327826.
    KEGGi mmu:327826.
    UCSCi uc007hct.1. mouse.

    Organism-specific databases

    CTDi 10818.
    MGIi MGI:1100860. Frs2.

    Phylogenomic databases

    eggNOGi NOG316561.
    GeneTreei ENSGT00510000046707.
    HOGENOMi HOG000290694.
    HOVERGENi HBG062705.
    InParanoidi Q8C180.
    KOi K12461.
    OMAi TRRRDCT.
    OrthoDBi EOG7QG43P.
    PhylomeDBi Q8C180.
    TreeFami TF324994.

    Enzyme and pathway databases

    Reactomei REACT_196455. Signaling by FGFR mutants.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198525. Negative regulation of FGFR signaling.
    REACT_223993. PI-3K cascade.
    REACT_226341. PIP3 activates AKT signaling.

    Miscellaneous databases

    NextBioi 397981.
    PROi Q8C180.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8C180.
    CleanExi MM_FRS2.
    Genevestigatori Q8C180.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR002404. Insln_rcpt_S1.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF02174. IRS. 1 hit.
    [Graphical view ]
    SMARTi SM00310. PTBI. 1 hit.
    [Graphical view ]
    PROSITEi PS51064. IRS_PTB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Skin.
    2. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    3. "A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway."
      Kouhara H., Hadari Y.R., Spivak-Kroizman T., Schilling J., Bar-Sagi D., Lax I., Schlessinger J.
      Cell 89:693-702(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 251-260; 305-320; 344-361 AND 468-480, FUNCTION, INTERACTION WITH GRB2, IDENTIFICATION IN A COMPLEX WITH GRB2 AND SOS1, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2; TYR-196; TYR-306; TYR-349 AND TYR-392, PHOSPHORYLATION AT TYR-196; TYR-306; TYR-349 AND TYR-392, TISSUE SPECIFICITY.
    4. "Suc1-associated neurotrophic factor target (SNT) protein is a major FGF-stimulated tyrosine phosphorylated 90-kDa protein which binds to the SH2 domain of GRB2."
      Ong S.-H., Goh K.C., Lim Y.P., Low B.C., Klint P., Claesson-Welsh L., Cao X., Tan Y.H., Guy G.R.
      Biochem. Biophys. Res. Commun. 225:1021-1026(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUC1 AND GRB2, PHOSPHORYLATION AT TYROSINE RESIDUES, SUBCELLULAR LOCATION.
    5. "Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation."
      Hadari Y.R., Kouhara H., Lax I., Schlessinger J.
      Mol. Cell. Biol. 18:3966-3973(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPN11, FUNCTION, PHOSPHORYLATION AT TYR-196; TYR-306; TYR-349; TYR-392 AND TYR-436, MUTAGENESIS OF TYR-436.
    6. "Signaling by fibroblast growth factors (FGF) and fibroblast growth factor receptor 2 (FGFR2)-activating mutations blocks mineralization and induces apoptosis in osteoblasts."
      Mansukhani A., Bellosta P., Sahni M., Basilico C.
      J. Cell Biol. 149:1297-1308(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION IN RESPONSE TO FRFR2 AND FGFR3 ACTIVATION.
    7. "FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors."
      Ong S.-H., Guy G.R., Hadari Y.R., Laks S., Gotoh N., Schlessinger J., Lax I.
      Mol. Cell. Biol. 20:979-989(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFR1 AND NTRK1.
    8. "Docking protein FRS2 links the protein tyrosine kinase RET and its oncogenic forms with the mitogen-activated protein kinase signaling cascade."
      Melillo R.M., Santoro M., Ong S.-H., Billaud M., Fusco A., Hadari Y.R., Schlessinger J., Lax I.
      Mol. Cell. Biol. 21:4177-4187(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RET, PHOSPHORYLATION AT TYROSINE RESIDUES.
    9. "N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling."
      Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.
      Nat. Cell Biol. 3:650-657(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH NCAM1; CDH2; PLCG1; FRS2; SRC; SHC1; GAP43 AND CTTN.
    10. "Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins."
      Ong S.H., Hadari Y.R., Gotoh N., Guy G.R., Schlessinger J., Lax I.
      Proc. Natl. Acad. Sci. U.S.A. 98:6074-6079(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GRB2 AND GAB1, PHOSPHORYLATION AT TYR-196; TYR-306; TYR-349; TYR-392; TYR-436 AND TYR-471.
    11. "The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in endothelial cells."
      Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M., Claesson-Welsh L.
      Mol. Biol. Cell 13:2881-2893(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF SIGNALING VIA RAS AND MAP KINASES, INTERACTION WITH PTPN11, PHOSPHORYLATION.
    12. "FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl."
      Wong A., Lamothe B., Lee A., Schlessinger J., Lax I.
      Proc. Natl. Acad. Sci. U.S.A. 99:6684-6689(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH GRB2 AND CBL, UBIQUITINATION.
    13. "UNC-51-like kinase regulation of fibroblast growth factor receptor substrate 2/3."
      Avery A.W., Figueroa C., Vojtek A.B.
      Cell. Signal. 19:177-184(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY ULK2.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "Regulation of growth factor signaling by FRS2 family docking/scaffold adaptor proteins."
      Gotoh N.
      Cancer Sci. 99:1319-1325(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION; SUBUNIT AND PHOSPHORYLATION.
    16. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    18. "Fibroblast growth factor signalling: from development to cancer."
      Turner N., Grose R.
      Nat. Rev. Cancer 10:116-129(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN FGF SIGNALING.

    Entry informationi

    Entry nameiFRS2_MOUSE
    AccessioniPrimary (citable) accession number: Q8C180
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 101 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3