Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8WU20

- FRS2_HUMAN

UniProt

Q8WU20 - FRS2_HUMAN

Protein

Fibroblast growth factor receptor substrate 2

Gene

FRS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 4 (14 Oct 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 NTRK1.2 Publications

    GO - Molecular functioni

    1. fibroblast growth factor receptor binding Source: MGI
    2. neurotrophin TRKA receptor binding Source: UniProtKB
    3. phosphatase activator activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. transmembrane receptor protein tyrosine kinase adaptor activity Source: UniProtKB

    GO - Biological processi

    1. activation of MAPK activity Source: Ensembl
    2. activation of MAPKK activity Source: Reactome
    3. anterior/posterior axis specification, embryo Source: Ensembl
    4. epidermal growth factor receptor signaling pathway Source: Reactome
    5. Fc-epsilon receptor signaling pathway Source: Reactome
    6. fibroblast growth factor receptor signaling pathway Source: UniProtKB
    7. forebrain development Source: Ensembl
    8. gastrulation with mouth forming second Source: Ensembl
    9. G-protein coupled receptor signaling pathway Source: UniProtKB
    10. innate immune response Source: Reactome
    11. insulin receptor signaling pathway Source: Reactome
    12. neuroblast proliferation Source: Ensembl
    13. neurotrophin TRK receptor signaling pathway Source: Reactome
    14. optic placode formation involved in camera-type eye formation Source: Ensembl
    15. organ induction Source: Ensembl
    16. phosphatidylinositol-mediated signaling Source: Reactome
    17. prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Source: Ensembl
    18. regulation of epithelial cell proliferation Source: Ensembl
    19. transmembrane receptor protein tyrosine phosphatase signaling pathway Source: UniProtKB
    20. ventricular septum development Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_111184. Negative regulation of FGFR signaling.
    REACT_12076. Frs2-mediated activation.
    REACT_121398. Signaling by FGFR mutants.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_21247. FRS2-mediated cascade.
    REACT_21270. PI-3K cascade.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_976. PI3K Cascade.
    SignaLinkiQ8WU20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibroblast growth factor receptor substrate 2
    Short name:
    FGFR substrate 2
    Alternative name(s):
    FGFR-signaling adaptor SNT
    Suc1-associated neurotrophic factor target 1
    Short name:
    SNT-1
    Gene namesi
    Name:FRS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:16971. FRS2.

    Subcellular locationi

    Endomembrane system
    Note: Cytoplasmic, membrane-bound.

    GO - Cellular componenti

    1. endosome Source: Reactome
    2. integral component of plasma membrane Source: UniProtKB
    3. membrane Source: ProtInc
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134850063.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 508507Fibroblast growth factor receptor substrate 2PRO_0000087344Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine2 Publications
    Modified residuei196 – 1961Phosphotyrosine; by FGFR1By similarity
    Modified residuei211 – 2111PhosphoserineBy similarity
    Modified residuei221 – 2211Phosphoserine1 Publication
    Modified residuei306 – 3061Phosphotyrosine; by FGFR1By similarity
    Modified residuei349 – 3491Phosphotyrosine; by FGFR1By similarity
    Modified residuei392 – 3921Phosphotyrosine; by FGFR1By similarity
    Modified residuei436 – 4361Phosphotyrosine; by FGFR1By similarity
    Modified residuei471 – 4711Phosphotyrosine; by FGFR1By similarity

    Post-translational modificationi

    Phosphorylated by ULK2 in vitro By similarity. Phosphorylated on tyrosine residues upon stimulation by NGF or FGF2. 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.By similarity6 Publications
    Ubiquitinated when tyrosine phosphorylated and in a complex with GRB2. The unphosphorylated form is not subject to ubiquitination By similarity.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8WU20.
    PaxDbiQ8WU20.
    PRIDEiQ8WU20.

    PTM databases

    PhosphoSiteiQ8WU20.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis.1 Publication

    Gene expression databases

    ArrayExpressiQ8WU20.
    BgeeiQ8WU20.
    CleanExiHS_FRS2.
    GenevestigatoriQ8WU20.

    Organism-specific databases

    HPAiCAB010347.
    HPA038323.

    Interactioni

    Subunit structurei

    Part of a complex containing FRS2, GRB2, GAB1, PIK3R1 and SOS1. Part of a complex containing GRB2 and CBL. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Binds RET By similarity. Binds ALK, FGFR1, CKS2, 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 similarity7 Publications

    Protein-protein interaction databases

    BioGridi116031. 17 interactions.
    IntActiQ8WU20. 4 interactions.
    MINTiMINT-8019836.
    STRINGi9606.ENSP00000299293.

    Structurei

    Secondary structure

    1
    508
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni15 – 184
    Beta strandi20 – 267
    Beta strandi32 – 343
    Beta strandi36 – 405
    Beta strandi45 – 495
    Turni50 – 523
    Beta strandi53 – 575
    Turni59 – 613
    Beta strandi62 – 676
    Beta strandi69 – 768
    Beta strandi84 – 907
    Helixi94 – 10714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XR0NMR-B11-136[»]
    2MFQNMR-A11-122[»]
    ProteinModelPortaliQ8WU20.
    SMRiQ8WU20. Positions 11-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8WU20.

    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.
    HOGENOMiHOG000290694.
    HOVERGENiHBG062705.
    InParanoidiQ8WU20.
    KOiK12461.
    OMAiTRRRDCT.
    PhylomeDBiQ8WU20.
    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.

    Q8WU20-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSCCSCPDK DTVPDNHRNK FKVINVDDDG NELGSGIMEL TDTELILYTR    50
    KRDSVKWHYL CLRRYGYDSN LFSFESGRRC QTGQGIFAFK CARAEELFNM 100
    LQEIMQNNSI NVVEEPVVER NNHQTELEVP RTPRTPTTPG FAAQNLPNGY 150
    PRYPSFGDAS SHPSSRHPSV GSARLPSVGE ESTHPLLVAE EQVHTYVNTT 200
    GVQEERKNRT SVHVPLEARV SNAESSTPKE EPSSIEDRDP QILLEPEGVK 250
    FVLGPTPVQK QLMEKEKLEQ LGRDQVSGSG ANNTEWDTGY DSDERRDAPS 300
    VNKLVYENIN GLSIPSASGV RRGRLTSTST SDTQNINNSA QRRTALLNYE 350
    NLPSLPPVWE ARKLSRDEDD NLGPKTPSLN GYHNNLDPMH NYVNTENVTV 400
    PASAHKIEYS RRRDCTPTVF NFDIRRPSLE HRQLNYIQVD LEGGSDSDNP 450
    QTPKTPTTPL PQTPTRRTEL YAVIDIERTA AMSNLQKALP RDDGTSRKTR 500
    HNSTDLPM 508
    Length:508
    Mass (Da):57,029
    Last modified:October 14, 2008 - v4
    Checksum:i833714EE12097C75
    GO

    Sequence cautioni

    The sequence AAH21562.1 differs from that shown. Reason: Erroneous termination at position 509. Translated as stop.
    The sequence BAG35381.1 differs from that shown. Reason: Erroneous termination at position 509. Translated as stop.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti303 – 3031K → N.
    Corresponds to variant rs12580717 [ dbSNP | Ensembl ].
    VAR_046966
    Natural varianti449 – 4491N → D.
    Corresponds to variant rs35232109 [ dbSNP | Ensembl ].
    VAR_046967

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036717 mRNA. Translation: AAB92554.1.
    AK312477 mRNA. Translation: BAG35381.1. Sequence problems.
    EU332842 Genomic DNA. Translation: ABY87531.1.
    AC018921 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97225.1.
    BC021562 mRNA. Translation: AAH21562.1. Sequence problems.
    CCDSiCCDS41809.1.
    RefSeqiNP_001036020.1. NM_001042555.2.
    NP_001265280.1. NM_001278351.1.
    NP_001265282.1. NM_001278353.1.
    NP_001265283.1. NM_001278354.1.
    NP_001265284.1. NM_001278355.1.
    NP_001265285.1. NM_001278356.1.
    NP_001265286.1. NM_001278357.1.
    NP_006645.3. NM_006654.4.
    UniGeneiHs.593446.

    Genome annotation databases

    EnsembliENST00000397997; ENSP00000381083; ENSG00000166225.
    ENST00000549921; ENSP00000450048; ENSG00000166225.
    ENST00000550389; ENSP00000447241; ENSG00000166225.
    GeneIDi10818.
    KEGGihsa:10818.
    UCSCiuc001suy.3. human.

    Polymorphism databases

    DMDMi209572769.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036717 mRNA. Translation: AAB92554.1 .
    AK312477 mRNA. Translation: BAG35381.1 . Sequence problems.
    EU332842 Genomic DNA. Translation: ABY87531.1 .
    AC018921 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97225.1 .
    BC021562 mRNA. Translation: AAH21562.1 . Sequence problems.
    CCDSi CCDS41809.1.
    RefSeqi NP_001036020.1. NM_001042555.2.
    NP_001265280.1. NM_001278351.1.
    NP_001265282.1. NM_001278353.1.
    NP_001265283.1. NM_001278354.1.
    NP_001265284.1. NM_001278355.1.
    NP_001265285.1. NM_001278356.1.
    NP_001265286.1. NM_001278357.1.
    NP_006645.3. NM_006654.4.
    UniGenei Hs.593446.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XR0 NMR - B 11-136 [» ]
    2MFQ NMR - A 11-122 [» ]
    ProteinModelPortali Q8WU20.
    SMRi Q8WU20. Positions 11-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116031. 17 interactions.
    IntActi Q8WU20. 4 interactions.
    MINTi MINT-8019836.
    STRINGi 9606.ENSP00000299293.

    PTM databases

    PhosphoSitei Q8WU20.

    Polymorphism databases

    DMDMi 209572769.

    Proteomic databases

    MaxQBi Q8WU20.
    PaxDbi Q8WU20.
    PRIDEi Q8WU20.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397997 ; ENSP00000381083 ; ENSG00000166225 .
    ENST00000549921 ; ENSP00000450048 ; ENSG00000166225 .
    ENST00000550389 ; ENSP00000447241 ; ENSG00000166225 .
    GeneIDi 10818.
    KEGGi hsa:10818.
    UCSCi uc001suy.3. human.

    Organism-specific databases

    CTDi 10818.
    GeneCardsi GC12P069864.
    HGNCi HGNC:16971. FRS2.
    HPAi CAB010347.
    HPA038323.
    MIMi 607743. gene.
    neXtProti NX_Q8WU20.
    PharmGKBi PA134850063.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG316561.
    HOGENOMi HOG000290694.
    HOVERGENi HBG062705.
    InParanoidi Q8WU20.
    KOi K12461.
    OMAi TRRRDCT.
    PhylomeDBi Q8WU20.
    TreeFami TF324994.

    Enzyme and pathway databases

    Reactomei REACT_111184. Negative regulation of FGFR signaling.
    REACT_12076. Frs2-mediated activation.
    REACT_121398. Signaling by FGFR mutants.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_21247. FRS2-mediated cascade.
    REACT_21270. PI-3K cascade.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_976. PI3K Cascade.
    SignaLinki Q8WU20.

    Miscellaneous databases

    ChiTaRSi FRS2. human.
    EvolutionaryTracei Q8WU20.
    GeneWikii FRS2.
    GenomeRNAii 10818.
    NextBioi 41095.
    PROi Q8WU20.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WU20.
    Bgeei Q8WU20.
    CleanExi HS_FRS2.
    Genevestigatori Q8WU20.

    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. "Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins."
      Xu H., Lee K.W., Goldfarb M.P.
      J. Biol. Chem. 273:17987-17990(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FGFR1, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT TYROSINE RESIDUES.
      Tissue: Placenta.
    2. "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].
      Tissue: Hippocampus.
    3. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Uterus.
    7. "The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation."
      Meakin S.O., MacDonald J.I.S., Gryz E.A., Kubu C.J., Verdi J.M.
      J. Biol. Chem. 274:9861-9870(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CKS2; GRB2; PTPN11; SRC; NTRK1; NTRK2 AND NTRK3, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT TYROSINE RESIDUES, TISSUE SPECIFICITY.
    8. "EGFR and FGFR signaling through FRS2 is subject to negative feedback control by ERK1/2."
      Wu Y., Chen Z., Ullrich A.
      Biol. Chem. 384:1215-1226(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MAPK1/ERK2 AND MAPK3/ERK1, INTERACTION WITH MAPK1/ERK2 AND MAPK3/ERK1, FUNCTION.
    9. Cited for: INTERACTION WITH NTRK1.
    10. "ALK activation induces Shc and FRS2 recruitment: Signaling and phenotypic outcomes in PC12 cells differentiation."
      Degoutin J., Vigny M., Gouzi J.Y.
      FEBS Lett. 581:727-734(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALK, PHOSPHORYLATION.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Nedd4-1 binds and ubiquitylates activated FGFR1 to control its endocytosis and function."
      Persaud A., Alberts P., Hayes M., Guettler S., Clarke I., Sicheri F., Dirks P., Ciruna B., Rotin D.
      EMBO J. 30:3259-3273(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF AKT1; PLCG1; MAPK1/ERK2, MAPK3/ERK1 AND MAP KINASE SIGNALING, INTERACTION WITH FGFR1, PHOSPHORYLATION.
    13. "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.
    14. "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.
    15. "Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors."
      Dhalluin C., Yan K.S., Plotnikova O., Lee K.W., Zeng L., Kuti M., Mujtaba S., Goldfarb M.P., Zhou M.-M.
      Mol. Cell 6:921-929(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 11-136 IN COMPLEX WITH FGFR1.

    Entry informationi

    Entry nameiFRS2_HUMAN
    AccessioniPrimary (citable) accession number: Q8WU20
    Secondary accession number(s): B0LPF2
    , B2R684, O43558, Q7LDQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 115 of the entry and version 4 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, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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