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O43597

- SPY2_HUMAN

UniProt

O43597 - SPY2_HUMAN

Protein

Protein sprouty homolog 2

Gene

SPRY2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein kinase binding Source: BHF-UCL
    3. protein serine/threonine kinase activator activity Source: UniProtKB
    4. protein serine/threonine kinase inhibitor activity Source: BHF-UCL

    GO - Biological processi

    1. branching morphogenesis of an epithelial tube Source: Ensembl
    2. cell fate commitment Source: Ensembl
    3. epidermal growth factor receptor signaling pathway Source: Reactome
    4. fibroblast growth factor receptor signaling pathway Source: Reactome
    5. inner ear morphogenesis Source: Ensembl
    6. lung growth Source: Ensembl
    7. lung morphogenesis Source: Ensembl
    8. negative regulation of apoptotic process Source: UniProtKB
    9. negative regulation of cell proliferation Source: Ensembl
    10. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
    11. negative regulation of ERK1 and ERK2 cascade Source: Ensembl
    12. negative regulation of fibroblast growth factor receptor signaling pathway Source: Ensembl
    13. negative regulation of MAP kinase activity Source: Ensembl
    14. negative regulation of neurotrophin TRK receptor signaling pathway Source: Ensembl
    15. negative regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
    16. negative regulation of Ras GTPase activity Source: Ensembl
    17. negative regulation of Ras protein signal transduction Source: Ensembl
    18. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    19. positive regulation of gene expression Source: UniProtKB
    20. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
    21. positive regulation of protein kinase B signaling Source: UniProtKB
    22. positive regulation of protein serine/threonine kinase activity Source: GOC
    23. sensory perception of sound Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Enzyme and pathway databases

    ReactomeiREACT_111080. Spry regulation of FGF signaling.
    REACT_12484. EGFR downregulation.
    SignaLinkiO43597.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein sprouty homolog 2
    Short name:
    Spry-2
    Gene namesi
    Name:SPRY2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:11270. SPRY2.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cell projectionruffle membrane 1 Publication
    Note: Associated with microtubules in unstimulated cells but is translocated to the membrane ruffles in cells stimulated ith EGF (epidermal growth factor).

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. microtubule Source: UniProtKB-KW
    3. plasma membrane Source: Reactome
    4. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36099.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 315315Protein sprouty homolog 2PRO_0000076901Add
    BLAST

    Proteomic databases

    PaxDbiO43597.
    PRIDEiO43597.

    PTM databases

    PhosphoSiteiO43597.

    Expressioni

    Inductioni

    By FGF signaling.

    Gene expression databases

    BgeeiO43597.
    CleanExiHS_SPRY2.
    GenevestigatoriO43597.

    Organism-specific databases

    HPAiCAB037205.

    Interactioni

    Subunit structurei

    Interacts with RAF1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CBLP2268117EBI-742487,EBI-518228
    GRB2P629933EBI-742487,EBI-401755
    SH3KBP1Q96B972EBI-742487,EBI-346595

    Protein-protein interaction databases

    BioGridi115547. 52 interactions.
    IntActiO43597. 28 interactions.
    MINTiMINT-2999467.
    STRINGi9606.ENSP00000366306.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BUMX-ray2.00A49-61[»]
    3OB1X-ray2.20A49-60[»]
    ProteinModelPortaliO43597.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43597.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini177 – 291115SPRPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi125 – 1317Poly-Ser
    Compositional biasi178 – 301124Cys-richAdd
    BLAST

    Domaini

    The Cys-rich domain is responsible for the localization of the protein to the membrane ruffles.1 Publication

    Sequence similaritiesi

    Belongs to the sprouty family.Curated
    Contains 1 SPR (sprouty) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG83905.
    HOVERGENiHBG003544.
    InParanoidiO43597.
    KOiK17383.
    OMAiPHGEPDL.
    OrthoDBiEOG7G4QDV.
    PhylomeDBiO43597.
    TreeFamiTF325070.

    Family and domain databases

    InterProiIPR007875. Sprouty.
    [Graphical view]
    PfamiPF05210. Sprouty. 1 hit.
    [Graphical view]
    PROSITEiPS51227. SPR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O43597-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEARAQSGNG SQPLLQTPRD GGRQRGEPDP RDALTQQVHV LSLDQIRAIR    50
    NTNEYTEGPT VVPRPGLKPA PRPSTQHKHE RLHGLPEHRQ PPRLQHSQVH 100
    SSARAPLSRS ISTVSSGSRS STRTSTSSSS SEQRLLGSSF SSGPVADGII 150
    RVQPKSELKP GELKPLSKED LGLHAYRCED CGKCKCKECT YPRPLPSDWI 200
    CDKQCLCSAQ NVIDYGTCVC CVKGLFYHCS NDDEDNCADN PCSCSQSHCC 250
    TRWSAMGVMS LFLPCLWCYL PAKGCLKLCQ GCYDRVNRPG CRCKNSNTVC 300
    CKVPTVPPRN FEKPT 315
    Length:315
    Mass (Da):34,688
    Last modified:June 1, 1998 - v1
    Checksum:i8CC6256929D91A7E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481A → V in BAG36546. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061P → S.
    Corresponds to variant rs504122 [ dbSNP | Ensembl ].
    VAR_024647

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039843 mRNA. Translation: AAC04258.1.
    AL713749 mRNA. Translation: CAD28524.1.
    AK313810 mRNA. Translation: BAG36546.1.
    AL354668 Genomic DNA. Translation: CAI14911.1.
    BC015745 mRNA. Translation: AAH15745.1.
    CCDSiCCDS9463.1.
    RefSeqiNP_005833.1. NM_005842.2.
    XP_005266274.1. XM_005266217.1.
    XP_006719815.1. XM_006719752.1.
    XP_006719816.1. XM_006719753.1.
    UniGeneiHs.18676.

    Genome annotation databases

    EnsembliENST00000377102; ENSP00000366306; ENSG00000136158.
    ENST00000377104; ENSP00000366308; ENSG00000136158.
    ENST00000540649; ENSP00000439027; ENSG00000136158.
    GeneIDi10253.
    KEGGihsa:10253.
    UCSCiuc001vli.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039843 mRNA. Translation: AAC04258.1 .
    AL713749 mRNA. Translation: CAD28524.1 .
    AK313810 mRNA. Translation: BAG36546.1 .
    AL354668 Genomic DNA. Translation: CAI14911.1 .
    BC015745 mRNA. Translation: AAH15745.1 .
    CCDSi CCDS9463.1.
    RefSeqi NP_005833.1. NM_005842.2.
    XP_005266274.1. XM_005266217.1.
    XP_006719815.1. XM_006719752.1.
    XP_006719816.1. XM_006719753.1.
    UniGenei Hs.18676.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BUM X-ray 2.00 A 49-61 [» ]
    3OB1 X-ray 2.20 A 49-60 [» ]
    ProteinModelPortali O43597.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115547. 52 interactions.
    IntActi O43597. 28 interactions.
    MINTi MINT-2999467.
    STRINGi 9606.ENSP00000366306.

    PTM databases

    PhosphoSitei O43597.

    Proteomic databases

    PaxDbi O43597.
    PRIDEi O43597.

    Protocols and materials databases

    DNASUi 10253.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377102 ; ENSP00000366306 ; ENSG00000136158 .
    ENST00000377104 ; ENSP00000366308 ; ENSG00000136158 .
    ENST00000540649 ; ENSP00000439027 ; ENSG00000136158 .
    GeneIDi 10253.
    KEGGi hsa:10253.
    UCSCi uc001vli.3. human.

    Organism-specific databases

    CTDi 10253.
    GeneCardsi GC13M080910.
    HGNCi HGNC:11270. SPRY2.
    HPAi CAB037205.
    MIMi 602466. gene.
    neXtProti NX_O43597.
    PharmGKBi PA36099.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG83905.
    HOVERGENi HBG003544.
    InParanoidi O43597.
    KOi K17383.
    OMAi PHGEPDL.
    OrthoDBi EOG7G4QDV.
    PhylomeDBi O43597.
    TreeFami TF325070.

    Enzyme and pathway databases

    Reactomei REACT_111080. Spry regulation of FGF signaling.
    REACT_12484. EGFR downregulation.
    SignaLinki O43597.

    Miscellaneous databases

    EvolutionaryTracei O43597.
    GeneWikii SPRY2.
    GenomeRNAii 10253.
    NextBioi 35467891.
    PROi O43597.
    SOURCEi Search...

    Gene expression databases

    Bgeei O43597.
    CleanExi HS_SPRY2.
    Genevestigatori O43597.

    Family and domain databases

    InterProi IPR007875. Sprouty.
    [Graphical view ]
    Pfami PF05210. Sprouty. 1 hit.
    [Graphical view ]
    PROSITEi PS51227. SPR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sprouty encodes a novel antagonist of FGF signaling that patterns apical branching of the Drosophila airways."
      Hacohen N., Kramer S., Sutherland D., Hiromi Y., Krasnow M.A.
      Cell 92:253-263(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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: Substantia nigra.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Skin.
    6. "Sprouty proteins are targeted to membrane ruffles upon growth factor receptor tyrosine kinase activation. Identification of a novel translocation domain."
      Lim J., Wong E.S.M., Ong S.H., Yusoff P., Low B.C., Guy G.R.
      J. Biol. Chem. 275:32837-32845(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
    7. "Mammalian Sprouty4 suppresses Ras-independent ERK activation by binding to Raf1."
      Sasaki A., Taketomi T., Kato R., Saeki K., Nonami A., Sasaki M., Kuriyama M., Saito N., Shibuya M., Yoshimura A.
      Nat. Cell Biol. 5:427-432(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAF1.
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.

    Entry informationi

    Entry nameiSPY2_HUMAN
    AccessioniPrimary (citable) accession number: O43597
    Secondary accession number(s): B2R9J9, Q5T6Z7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 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 13
      Human chromosome 13: 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