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Q14451

- GRB7_HUMAN

UniProt

Q14451 - GRB7_HUMAN

Protein

Growth factor receptor-bound protein 7

Gene

GRB7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Adapter protein that interacts with the cytoplasmic domain of numerous receptor kinases and modulates down-stream signaling. Promotes activation of down-stream protein kinases, including STAT3, AKT1, MAPK1 and/or MAPK3. Promotes activation of HRAS. Plays a role in signal transduction in response to EGF. Plays a role in the regulation of cell proliferation and cell migration. Plays a role in the assembly and stability of RNA stress granules. Binds to the 5'UTR of target mRNA molecules and represses translation of target mRNA species, when not phosphorylated. Phosphorylation impairs RNA binding and promotes stress granule disassembly during recovery after cellular stress By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei239 – 2391Important for lipid binding and for stimulation of cell migration
    Sitei511 – 5111Important for dimerization and for HRAS activation

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. phosphatidylinositol binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein kinase binding Source: UniProtKB
    5. RNA binding Source: UniProtKB-KW
    6. SH3/SH2 adaptor activity Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. epidermal growth factor receptor signaling pathway Source: ProtInc
    3. leukocyte migration Source: Reactome
    4. negative regulation of translation Source: UniProtKB
    5. positive regulation of cell migration Source: UniProtKB
    6. positive regulation of signal transduction Source: GOC
    7. stress granule assembly Source: UniProtKB

    Keywords - Molecular functioni

    Repressor

    Keywords - Ligandi

    Lipid-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_115896. GRB7 events in ERBB2 signaling.
    REACT_12621. Tie2 Signaling.
    REACT_17025. Downstream signal transduction.
    SignaLinkiQ14451.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Growth factor receptor-bound protein 7
    Alternative name(s):
    B47
    Epidermal growth factor receptor GRB-7
    GRB7 adapter protein
    Gene namesi
    Name:GRB7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4567. GRB7.

    Subcellular locationi

    Cytoplasm. Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic granule By similarity. Cell projection
    Note: Predominantly cytoplasmic. Detected in stress granules, where mRNA is stored under stress conditions By similarity.By similarity

    GO - Cellular componenti

    1. cell projection Source: UniProtKB-SubCell
    2. cytoplasmic stress granule Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. focal adhesion Source: UniProtKB
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi188 – 1881Y → F: Abolishes Ras activity increase and ERK1/2 phosphorylation. 1 Publication
    Mutagenesisi239 – 2391R → L: Abolishes phosphoinositide binding. 1 Publication
    Mutagenesisi259 – 2591Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications
    Mutagenesisi260 – 2601Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications
    Mutagenesisi284 – 2841Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications
    Mutagenesisi338 – 3381Y → F: Abolishes Ras activity increase and ERK1/2 phosphorylation. 1 Publication
    Mutagenesisi458 – 4581R → L: Impairs phosphotyrosine binding by SH2 domain.
    Mutagenesisi480 – 4801Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications
    Mutagenesisi492 – 4921Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications
    Mutagenesisi511 – 5111F → R: Abolishes dimerization. Abolishes activation of HRAS. 1 Publication

    Organism-specific databases

    PharmGKBiPA28963.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 532532Growth factor receptor-bound protein 7PRO_0000150344Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei188 – 1881Phosphotyrosine; by FAK12 Publications
    Modified residuei338 – 3381Phosphotyrosine; by FAK12 Publications
    Modified residuei361 – 3611Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on serine and threonine residues in response to heregulin. Phosphorylated on tyrosine residues by TEK/TIE2. Phosphorylated on tyrosine residues in response to NTN1 signaling. Phosphorylation promotes stress granule disassembly during recovery after cellular stress By similarity. Phosphorylated on tyrosine residues by PTK2/FAK1, and possibly also other kinases. Phosphorylation is enhanced by activation of receptor kinases. Tyrosine phosphorylation is essential for activation of down-stream protein kinases.By similarity5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ14451.
    PaxDbiQ14451.
    PRIDEiQ14451.

    PTM databases

    PhosphoSiteiQ14451.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14451.
    BgeeiQ14451.
    CleanExiHS_GRB7.
    GenevestigatoriQ14451.

    Organism-specific databases

    HPAiCAB005226.

    Interactioni

    Subunit structurei

    Homodimer. Interacts (via SH2 domain) with EGFR, ERBB2, ERBB3 (when phosphorylated), ERBB4 (when phosphorylated), EPHB1, INSR, FGFR1, PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Interacts with SHC1. Interacts with RND1. Interacts (when tyrosine phosphorylated) with FHL2 and HAX1 By similarity. Interacts (via SH2 domain) with RET and PTK2/FAK1. Interacts (when not phosphorylated) with ELAVL1. In stressed cells, but not in normal cells, part of a complex that contains at least GRB7, PTK2/FAK1, STAU1, ELAVL1 and TIA1. Interacts (via SH2 domain) with KIT (phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-970191,EBI-970191
    ARP102753EBI-970191,EBI-608057
    CALMP621572EBI-970191,EBI-397403From a different organism.
    Calm3P621619EBI-970191,EBI-397530From a different organism.
    EPHB1P547624EBI-970191,EBI-80252
    ERBB2P046265EBI-970191,EBI-641062
    ERBB3P218607EBI-970191,EBI-720706
    HAX1O001652EBI-970191,EBI-357001
    KITP107214EBI-970191,EBI-1379503
    PDGFRBP096194EBI-970191,EBI-641237
    RND1Q927304EBI-970191,EBI-448618

    Protein-protein interaction databases

    BioGridi109143. 32 interactions.
    DIPiDIP-502N.
    IntActiQ14451. 38 interactions.
    MINTiMINT-1492212.
    STRINGi9606.ENSP00000310771.

    Structurei

    Secondary structure

    1
    532
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi102 – 1087
    Beta strandi113 – 1186
    Helixi124 – 1329
    Beta strandi134 – 1363
    Beta strandi145 – 1484
    Turni150 – 1523
    Beta strandi155 – 1584
    Beta strandi160 – 1623
    Helixi164 – 1685
    Beta strandi173 – 1753
    Beta strandi178 – 1814
    Helixi421 – 4244
    Helixi425 – 4284
    Helixi429 – 4313
    Beta strandi432 – 4365
    Helixi438 – 44710
    Beta strandi454 – 4596
    Beta strandi461 – 4633
    Beta strandi467 – 4737
    Beta strandi476 – 48914
    Beta strandi491 – 4966
    Beta strandi502 – 5043
    Helixi505 – 5128
    Beta strandi513 – 5153
    Beta strandi519 – 5213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MW4NMR-A415-532[»]
    1WGRNMR-A100-186[»]
    2L4KNMR-A415-532[»]
    2QMSX-ray2.10A/B/C/D415-532[»]
    3PQZX-ray2.41A/B/C/D416-532[»]
    ProteinModelPortaliQ14451.
    SMRiQ14451. Positions 98-347, 369-532.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14451.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini100 – 18687Ras-associatingPROSITE-ProRule annotationAdd
    BLAST
    Domaini229 – 338110PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini431 – 52797SH2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The PH domain mediates interaction with membranes containing phosphoinositides.1 Publication

    Sequence similaritiesi

    Belongs to the GRB7/10/14 family.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 Ras-associating domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG307156.
    HOVERGENiHBG000468.
    InParanoidiQ14451.
    OMAiQRNPQGF.
    OrthoDBiEOG7SFHW7.
    PhylomeDBiQ14451.
    TreeFamiTF317511.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR015042. BPS-dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000159. Ras-assoc.
    IPR000980. SH2.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF08947. BPS. 1 hit.
    PF00169. PH. 1 hit.
    PF00788. RA. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    SMARTiSM00233. PH. 1 hit.
    SM00314. RA. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS50200. RA. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: At least 2 isoforms are produced.

    Isoform 1 (identifier: Q14451-1) [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

    MELDLSPPHL SSSPEDLCPA PGTPPGTPRP PDTPLPEEVK RSQPLLIPTT    50
    GRKLREEERR ATSLPSIPNP FPELCSPPSQ SPILGGPSSA RGLLPRDASR 100
    PHVVKVYSED GACRSVEVAA GATARHVCEM LVQRAHALSD ETWGLVECHP 150
    HLALERGLED HESVVEVQAA WPVGGDSRFV FRKNFAKYEL FKSSPHSLFP 200
    EKMVSSCLDA HTGISHEDLI QNFLNAGSFP EIQGFLQLRG SGRKLWKRFF 250
    CFLRRSGLYY STKGTSKDPR HLQYVADVNE SNVYVVTQGR KLYGMPTDFG 300
    FCVKPNKLRN GHKGLRIFCS EDEQSRTCWL AAFRLFKYGV QLYKNYQQAQ 350
    SRHLHPSCLG SPPLRSASDN TLVAMDFSGH AGRVIENPRE ALSVALEEAQ 400
    AWRKKTNHRL SLPMPASGTS LSAAIHRTQL WFHGRISREE SQRLIGQQGL 450
    VDGLFLVRES QRNPQGFVLS LCHLQKVKHY LILPSEEEGR LYFSMDDGQT 500
    RFTDLLQLVE FHQLNRGILP CLLRHCCTRV AL 532
    Length:532
    Mass (Da):59,681
    Last modified:October 17, 2006 - v2
    Checksum:iA6867C20AFD46F74
    GO
    Isoform 2 (identifier: Q14451-2) [UniParc]FASTAAdd to Basket

    Also known as: Grb7V

    The sequence of this isoform differs from the canonical sequence as follows:
         425-447: IHRTQLWFHGRISREESQRLIGQ → CSWSGRVSGTPRALSSLCATCRK
         448-532: Missing.

    Show »
    Length:447
    Mass (Da):49,423
    Checksum:i2406BFDCBEBB1E49
    GO
    Isoform 3 (identifier: Q14451-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGKWRPGQGHTTGSVKPLSCSDAM

    Show »
    Length:555
    Mass (Da):62,064
    Checksum:i90E4D15BCBF428A1
    GO
    Isoform 4 (identifier: Q14451-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         48-81: Missing.

    Show »
    Length:498
    Mass (Da):55,920
    Checksum:iE18D088B19E632C6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181C → W in BAA07827. (PubMed:9125150)Curated
    Sequence conflicti18 – 181C → W in BAA29059. (PubMed:9710451)Curated
    Sequence conflicti18 – 181C → W in BAA29060. (PubMed:9710451)Curated
    Sequence conflicti18 – 181C → W in AAG25938. 1 PublicationCurated
    Sequence conflicti118 – 1181V → A in BAG36998. (PubMed:14702039)Curated
    Sequence conflicti120 – 1201A → T in BAG54211. (PubMed:14702039)Curated
    Sequence conflicti147 – 1471E → G in BAG51372. (PubMed:14702039)Curated
    Sequence conflicti164 – 1641V → L in BAG36998. (PubMed:14702039)Curated
    Sequence conflicti510 – 5101E → D in BAG36998. (PubMed:14702039)Curated
    Isoform 3 (identifier: Q14451-3)
    Sequence conflicti20 – 201C → R in BAG54211. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGKWRPGQGHTTGSVKPLSC SDAM in isoform 3. 1 PublicationVSP_041665
    Alternative sequencei48 – 8134Missing in isoform 4. 1 PublicationVSP_041666Add
    BLAST
    Alternative sequencei425 – 44723IHRTQ…RLIGQ → CSWSGRVSGTPRALSSLCAT CRK in isoform 2. 1 PublicationVSP_035500Add
    BLAST
    Alternative sequencei448 – 53285Missing in isoform 2. 1 PublicationVSP_035501Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D43772 mRNA. Translation: BAA07827.1.
    AB008789 mRNA. Translation: BAA29059.1.
    AB008790 mRNA. Translation: BAA29060.1.
    AF274875 Genomic DNA. Translation: AAG25938.1.
    BT006686 mRNA. Translation: AAP35332.1.
    AK222849 mRNA. Translation: BAD96569.1.
    AK222870 mRNA. Translation: BAD96590.1.
    AK290115 mRNA. Translation: BAF82804.1.
    AK314368 mRNA. Translation: BAG36998.1.
    AK027729 mRNA. Translation: BAG51372.1.
    AK125544 mRNA. Translation: BAG54211.1.
    AC079199 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60600.1.
    CH471152 Genomic DNA. Translation: EAW60601.1.
    BC006535 mRNA. Translation: AAH06535.1.
    D87513 mRNA. Translation: BAA13412.1.
    CCDSiCCDS11345.1. [Q14451-1]
    CCDS56028.1. [Q14451-3]
    PIRiJC5412.
    RefSeqiNP_001025173.1. NM_001030002.2. [Q14451-1]
    NP_001229371.1. NM_001242442.1.
    NP_001229372.1. NM_001242443.1. [Q14451-1]
    NP_005301.2. NM_005310.3. [Q14451-1]
    XP_006721907.1. XM_006721844.1. [Q14451-2]
    UniGeneiHs.86859.

    Genome annotation databases

    EnsembliENST00000309156; ENSP00000310771; ENSG00000141738. [Q14451-1]
    ENST00000394204; ENSP00000377754; ENSG00000141738. [Q14451-2]
    ENST00000394209; ENSP00000377759; ENSG00000141738. [Q14451-1]
    ENST00000394211; ENSP00000377761; ENSG00000141738. [Q14451-1]
    ENST00000445327; ENSP00000403459; ENSG00000141738. [Q14451-3]
    GeneIDi2886.
    KEGGihsa:2886.
    UCSCiuc002hsr.3. human. [Q14451-1]
    uc002hst.3. human. [Q14451-2]
    uc021twu.1. human. [Q14451-3]

    Polymorphism databases

    DMDMi116242503.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D43772 mRNA. Translation: BAA07827.1 .
    AB008789 mRNA. Translation: BAA29059.1 .
    AB008790 mRNA. Translation: BAA29060.1 .
    AF274875 Genomic DNA. Translation: AAG25938.1 .
    BT006686 mRNA. Translation: AAP35332.1 .
    AK222849 mRNA. Translation: BAD96569.1 .
    AK222870 mRNA. Translation: BAD96590.1 .
    AK290115 mRNA. Translation: BAF82804.1 .
    AK314368 mRNA. Translation: BAG36998.1 .
    AK027729 mRNA. Translation: BAG51372.1 .
    AK125544 mRNA. Translation: BAG54211.1 .
    AC079199 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60600.1 .
    CH471152 Genomic DNA. Translation: EAW60601.1 .
    BC006535 mRNA. Translation: AAH06535.1 .
    D87513 mRNA. Translation: BAA13412.1 .
    CCDSi CCDS11345.1. [Q14451-1 ]
    CCDS56028.1. [Q14451-3 ]
    PIRi JC5412.
    RefSeqi NP_001025173.1. NM_001030002.2. [Q14451-1 ]
    NP_001229371.1. NM_001242442.1.
    NP_001229372.1. NM_001242443.1. [Q14451-1 ]
    NP_005301.2. NM_005310.3. [Q14451-1 ]
    XP_006721907.1. XM_006721844.1. [Q14451-2 ]
    UniGenei Hs.86859.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MW4 NMR - A 415-532 [» ]
    1WGR NMR - A 100-186 [» ]
    2L4K NMR - A 415-532 [» ]
    2QMS X-ray 2.10 A/B/C/D 415-532 [» ]
    3PQZ X-ray 2.41 A/B/C/D 416-532 [» ]
    ProteinModelPortali Q14451.
    SMRi Q14451. Positions 98-347, 369-532.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109143. 32 interactions.
    DIPi DIP-502N.
    IntActi Q14451. 38 interactions.
    MINTi MINT-1492212.
    STRINGi 9606.ENSP00000310771.

    Chemistry

    BindingDBi Q14451.
    ChEMBLi CHEMBL1649051.

    PTM databases

    PhosphoSitei Q14451.

    Polymorphism databases

    DMDMi 116242503.

    Proteomic databases

    MaxQBi Q14451.
    PaxDbi Q14451.
    PRIDEi Q14451.

    Protocols and materials databases

    DNASUi 2886.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309156 ; ENSP00000310771 ; ENSG00000141738 . [Q14451-1 ]
    ENST00000394204 ; ENSP00000377754 ; ENSG00000141738 . [Q14451-2 ]
    ENST00000394209 ; ENSP00000377759 ; ENSG00000141738 . [Q14451-1 ]
    ENST00000394211 ; ENSP00000377761 ; ENSG00000141738 . [Q14451-1 ]
    ENST00000445327 ; ENSP00000403459 ; ENSG00000141738 . [Q14451-3 ]
    GeneIDi 2886.
    KEGGi hsa:2886.
    UCSCi uc002hsr.3. human. [Q14451-1 ]
    uc002hst.3. human. [Q14451-2 ]
    uc021twu.1. human. [Q14451-3 ]

    Organism-specific databases

    CTDi 2886.
    GeneCardsi GC17P037894.
    HGNCi HGNC:4567. GRB7.
    HPAi CAB005226.
    MIMi 601522. gene.
    neXtProti NX_Q14451.
    PharmGKBi PA28963.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307156.
    HOVERGENi HBG000468.
    InParanoidi Q14451.
    OMAi QRNPQGF.
    OrthoDBi EOG7SFHW7.
    PhylomeDBi Q14451.
    TreeFami TF317511.

    Enzyme and pathway databases

    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_115896. GRB7 events in ERBB2 signaling.
    REACT_12621. Tie2 Signaling.
    REACT_17025. Downstream signal transduction.
    SignaLinki Q14451.

    Miscellaneous databases

    EvolutionaryTracei Q14451.
    GeneWikii GRB7.
    GenomeRNAii 2886.
    NextBioi 11395.
    PROi Q14451.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14451.
    Bgeei Q14451.
    CleanExi HS_GRB7.
    Genevestigatori Q14451.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR015042. BPS-dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000159. Ras-assoc.
    IPR000980. SH2.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF08947. BPS. 1 hit.
    PF00169. PH. 1 hit.
    PF00788. RA. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    SMARTi SM00233. PH. 1 hit.
    SM00314. RA. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS50200. RA. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of human GRB-7 co-amplified with CAB1 and c-ERBB-2 in primary gastric cancer."
      Kishi T., Sasaki H., Akiyama N., Ishizuka T., Sakamoto H., Aizawa S., Sugimura T., Terada M.
      Biochem. Biophys. Res. Commun. 232:5-9(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Esophageal carcinoma.
    2. "A novel variant of human Grb7 is associated with invasive esophageal carcinoma."
      Tanaka S., Mori M., Akiyoshi T., Tanaka Y., Mafune K., Wands J.R., Sugimachi K.
      J. Clin. Invest. 102:821-827(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    3. "Genomic organization and amplification of the human GRB7 gene."
      Whittock N.V., Eady R.A.J., McGrath J.A.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "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 1; 3 AND 4).
      Tissue: Ovary, Prostate and Thalamus.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 1).
      Tissue: Lung.
    9. "Coexpression of Grb7 with epidermal growth factor receptor or Her2/erbB2 in human advanced esophageal carcinoma."
      Tanaka S., Mori M., Akiyoshi T., Tanaka Y., Mafune K., Wands J.R., Sugimachi K.
      Cancer Res. 57:28-31(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 130-343.
    10. "Analysis of Grb7 recruitment by heregulin-activated erbB receptors reveals a novel target selectivity for erbB3."
      Fiddes R.J., Campbell D.H., Janes P.W., Sivertsen S.P., Sasaki H., Wallasch C., Daly R.J.
      J. Biol. Chem. 273:7717-7724(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERBB3 AND ERBB4, SERINE AND THREONINE PHOSPHORYLATION.
    11. "Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family."
      Vayssiere B., Zalcman G., Mahe Y., Mirey G., Ligensa T., Weidner K.M., Chardin P., Camonis J.
      FEBS Lett. 467:91-96(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RND1.
    12. "Role of Grb7 targeting to focal contacts and its phosphorylation by focal adhesion kinase in regulation of cell migration."
      Han D.C., Shen T.L., Guan J.L.
      J. Biol. Chem. 275:28911-28917(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    13. "Evidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2."
      Kasus-Jacobi A., Bereziat V., Perdereau D., Girard J., Burnol A.F.
      Oncogene 19:2052-2059(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INSR.
    14. "Association of Grb7 with phosphoinositides and its role in the regulation of cell migration."
      Shen T.L., Han D.C., Guan J.L.
      J. Biol. Chem. 277:29069-29077(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2/FAK1, MUTAGENESIS OF ARG-239, DOMAIN.
    15. "EphB1 associates with Grb7 and regulates cell migration."
      Han D.C., Shen T.L., Miao H., Wang B., Guan J.L.
      J. Biol. Chem. 277:45655-45661(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH EPHB1.
    16. "Signal transduction via the stem cell factor receptor/c-Kit."
      Ronnstrand L.
      Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON INTERACTION WITH KIT AND ROLE IN KIT SIGNALING.
    17. "Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."
      Roskoski R. Jr.
      Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN KIT SIGNALING.
    18. "Grb7-SH2 domain dimerisation is affected by a single point mutation."
      Porter C.J., Wilce M.C., Mackay J.P., Leedman P., Wilce J.A.
      Eur. Biophys. J. 34:454-460(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, MUTAGENESIS OF PHE-511.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Tyrosine phosphorylation of growth factor receptor-bound protein-7 by focal adhesion kinase in the regulation of cell migration, proliferation, and tumorigenesis."
      Chu P.Y., Huang L.Y., Hsu C.H., Liang C.C., Guan J.L., Hung T.H., Shen T.L.
      J. Biol. Chem. 284:20215-20226(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-188 AND TYR-338, INTERACTION WITH PTK2/FAK1.
    21. "The cell migration protein Grb7 associates with transcriptional regulator FHL2 in a Grb7 phosphorylation-dependent manner."
      Siamakpour-Reihani S., Argiros H.J., Wilmeth L.J., Haas L.L., Peterson T.A., Johnson D.L., Shuster C.B., Lyons B.A.
      J. Mol. Recognit. 22:9-17(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FHL2, STRUCTURE BY NMR, MUTAGENESIS OF TYR-259; TYR-260; TYR-284; TYR-480 AND TYR-492, SUBCELLULAR LOCATION, TYROSINE PHOSPHORYLATION.
    22. "EGF-induced Grb7 recruits and promotes Ras activity essential for the tumorigenicity of Sk-Br3 breast cancer cells."
      Chu P.Y., Li T.K., Ding S.T., Lai I.R., Shen T.L.
      J. Biol. Chem. 285:29279-29285(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, PHOSPHORYLATION AT TYR-188 AND TYR-338, MUTAGENESIS OF TYR-188 AND TYR-338.
    23. "Grb7 binds to Hax-1 and undergoes an intramolecular domain association that offers a model for Grb7 regulation."
      Siamakpour-Reihani S., Peterson T.A., Bradford A.M., Argiros H.J., Haas L.L., Lor S.N., Haulsee Z.M., Spuches A.M., Johnson D.L., Rohrschneider L.R., Shuster C.B., Lyons B.A.
      J. Mol. Recognit. 24:314-321(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HAX1, MUTAGENESIS OF TYR-259; TYR-260; TYR-284; TYR-480 AND TYR-492, CIRCULAR DICHROISM, TYROSINE PHOSPHORYLATION.
    24. "Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2."
      Ivancic M., Daly R.J., Lyons B.A.
      J. Biomol. NMR 27:205-219(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 415-532 IN COMPLEX WITH ERBB2, INTERACTION WITH ERBB2.
    25. "Solution structure of the RA domain of human GRB7 protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 100-186.
    26. "Grb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferation."
      Porter C.J., Matthews J.M., Mackay J.P., Pursglove S.E., Schmidberger J.W., Leedman P.J., Pero S.C., Krag D.N., Wilce M.C., Wilce J.A.
      BMC Struct. Biol. 7:58-58(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 415-532, INTERACTION WITH THE SYNTHETIC INHIBITOR G7-18NATE, SUBUNIT.

    Entry informationi

    Entry nameiGRB7_HUMAN
    AccessioniPrimary (citable) accession number: Q14451
    Secondary accession number(s): B2RAV1
    , B3KNL0, B3KWP9, B7WP75, J3KQM4, Q53YD3, Q92568, Q96DF9, Q9Y220
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 147 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, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3