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Q60760

- GRB10_MOUSE

UniProt

Q60760 - GRB10_MOUSE

Protein

Growth factor receptor-bound protein 10

Gene

Grb10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      Previous versions | rss
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    Functioni

    Adapter protein which modulates coupling of a number of cell surface receptor kinases with specific signaling pathways. Binds to, and suppress signals from, activated receptors tyrosine kinases, including the insulin (INSR) and insulin-like growth factor (IGF1R) receptors. The inhibitory effect can be achieved by 2 mechanisms: interference with the signaling pathway and increased receptor degradation. Delays and reduces AKT1 phosphorylation in response to insulin stimulation. Blocks association between INSR and IRS1 and IRS2 and prevents insulin-stimulated IRS1 and IRS2 tyrosine phosphorylation. Recruits NEDD4 to IGF1R, leading to IGF1R ubiquitination, increased internalization and degradation by both the proteasomal and lysosomal pathways. A similar role in the mediation of ubiquitination has also been suggested with INSR. Negatively regulates Wnt signaling by interacting with LRP6 intracellular portion and interfering with the binding of AXIN1 to LRP6. Positive regulator of the KDR/VEGFR-2 signaling pathway. May inhibit NEDD4-mediated degradation of KDR/VEGFR-2.5 Publications

    Enzyme regulationi

    Phosphorylation by mTORC1 stabilizes and activates GRB10 constituting a feedback pathway by which mTORC1 inhibits INSR-dependent signaling.By similarity

    GO - Molecular functioni

    1. insulin receptor binding Source: BHF-UCL
    2. phosphotyrosine binding Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. SH3/SH2 adaptor activity Source: BHF-UCL

    GO - Biological processi

    1. insulin-like growth factor receptor signaling pathway Source: MGI
    2. insulin receptor signaling pathway Source: Ensembl
    3. negative regulation of glucose import Source: BHF-UCL
    4. negative regulation of glycogen biosynthetic process Source: BHF-UCL
    5. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
    6. negative regulation of phosphorylation Source: BHF-UCL
    7. negative regulation of Wnt signaling pathway Source: UniProtKB
    8. positive regulation of phosphorylation Source: Ensembl
    9. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
    10. signal transduction Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_188578. Signaling by SCF-KIT.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Growth factor receptor-bound protein 10
    Alternative name(s):
    GRB10 adapter protein
    Maternally expressed gene 1 protein
    Gene namesi
    Name:Grb10
    Synonyms:Meg1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:103232. Grb10.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: When complexed with NEDD4 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R before the sorting of the receptor to the lysosomal compartment.

    GO - Cellular componenti

    1. cytosol Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Disruption of the maternal allele results in overgrowth of both the embryo and placenta such that mutant mice are at birth about 30% larger than normal. This effect occurs during embryogenesis and results in addition in disproportionate overgrowth of the liver with relative sparing of the brain. The major part of the growth phenotype seems to be IGF2-independent.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 621621Growth factor receptor-bound protein 10PRO_0000150347Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501PhosphoserineBy similarity
    Modified residuei96 – 961Phosphoserine; alternate1 Publication
    Modified residuei96 – 961Phosphoserine; by MTOR, MAPK1 and MAPK3; alternateBy similarity
    Modified residuei455 – 4551Phosphoserine; by MTOR and PKB/AKT1By similarity
    Modified residuei458 – 4581Phosphoserine1 Publication
    Modified residuei503 – 5031Phosphoserine; by MTOR, MAPK1 and MAPK3By similarity

    Post-translational modificationi

    Phosphorylated on serine residues upon EGF, FGF and PDGF stimulation.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ60760.
    PaxDbiQ60760.
    PRIDEiQ60760.

    PTM databases

    PhosphoSiteiQ60760.

    Expressioni

    Tissue specificityi

    Widely expressed.2 Publications

    Developmental stagei

    At 13.5 dpc, expressed in most embryonic tissues and in placenta. At 14.5 dpc, expressed at high levels in a variety of muscle tissues, including that of the face and trunk, the intercostal muscles, the diaphragm and cardiac muscle, the tongue and limbs (at protein level). In the brain, most abundant expression in the subependymal layers, in the meninges and in the choroid plexus (both epithelium and mesenchyme) (at protein level). High levels in the liver, bronchioles and the cartilage of the atlas, ribs and long bones (at protein level). In the kidney, expression limited to the developing tubules and mesenchyme (at protein level). Also detected in the adrenal gland and pancreatic bud (at protein level). At 12.5 dpc, paternal allele expression detected in the cartilage of the limbs, ribs and face and in the meninges. At 14.5 dpc, paternal allele expressed in the cartilage of the axis, ribs, head, and long bones, in the heart, lungs, gut, umbilicus and tongue, as well as in the meninges of the fourth ventricle. Not detected in the skeletal muscle. In most tissues, paternal expression is lower than maternal.2 Publications

    Gene expression databases

    ArrayExpressiQ60760.
    BgeeiQ60760.
    CleanExiMM_GRB10.
    GenevestigatoriQ60760.

    Interactioni

    Subunit structurei

    Interacts with ligand-activated tyrosine kinase receptors, including FGFR1, INSR, IGF1R, MET and PDGFRB in a phosphotyrosine-dependent manner through the SH2 domain. Poorly binds to the EGFR. Directly interacts with MAP3K14/NIK and is recruited to the EGFR-ERBB2 complex By similarity. Interacts with GIGYF1/PERQ1 and GIGYF2/TNRC15. When unphosphorylated, interacts with AKT1 and when phosphorylated with YWHAE/14-3-3 epsilon. Interacts with NEDD4. Interacts with LRP6, thus interfering with the binding of AXIN1 to LRP6. Binds to activated NRAS By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    InsrP152086EBI-861810,EBI-6999015
    Nedd4P469356EBI-861810,EBI-773516

    Protein-protein interaction databases

    BioGridi200045. 6 interactions.
    DIPiDIP-446N.
    IntActiQ60760. 8 interactions.
    MINTiMINT-102080.

    Structurei

    Secondary structure

    1
    621
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi515 – 5173
    Helixi527 – 53610
    Beta strandi543 – 5486
    Beta strandi556 – 5627
    Beta strandi565 – 57612
    Beta strandi579 – 5857
    Beta strandi588 – 5936
    Helixi594 – 6018
    Beta strandi608 – 6103

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3M7FX-ray2.00A514-621[»]
    ProteinModelPortaliQ60760.
    SMRiQ60760. Positions 195-437, 456-620.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini194 – 27885Ras-associatingPROSITE-ProRule annotationAdd
    BLAST
    Domaini318 – 427110PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini520 – 60182SH2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The PH domain binds relatively non-specifically to several phosphoinositides, including PI5P, PI(4,5)P2, PI(3,4)P2 and PI(3,4,5)P3, with modest affinities.By similarity

    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.
    GeneTreeiENSGT00550000074537.
    HOVERGENiHBG000468.
    InParanoidiQ60760.
    OMAiESTMGSE.
    OrthoDBiEOG7SFHW7.
    PhylomeDBiQ60760.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q60760-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    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

    MNNDINSSVE SLNSACNMQS DTDTAPLLED GQHASNQGAA SSSRGQPQAS    50
    PRQKMQRSQP VHILRRLQEE DQQLRTASLP AIPNPFPELT GAAPGSPPSV 100
    APSSLPPPPS QPPAKHCGRC EKWIPGENTR GNGKRKIWRW QFPPGFQLSK 150
    LTRPGLWTKT TARFSKKQPK NQCPTDTVNP VARMPTSQME KLRLRKDVKV 200
    FSEDGTSKVV EILTDMTARD LCQLLVYKSH CVDDNSWTLV EHHPQLGLER 250
    CLEDHEIVVQ VESTMPSESK FLFRKNYAKY EFFKNPVNFF PDQMVNWCQQ 300
    SNGGQAQLLQ NFLNTSSCPE IQGFLQVKEV GRKSWKKLYV CLRRSGLYYS 350
    TKGTSKEPRH LQLLADLEES SIFYLIAGKK QYNAPNEHGM CIKPNKAKTE 400
    MKELRLLCAE DEQIRTCWMT AFRLLKYGML LYQNYRIPQR KGLPPPFNAP 450
    MRSVSENSLV AMDFSGQIGR VIDNPAEAQS AALEEGHAWR KRSTRMNILS 500
    SQSPLHPSTL NAVIHRTQHW FHGRISREES HRIIKQQGLV DGLFLLRDSQ 550
    SNPKAFVLTL CHHQKIKNFQ ILPCEDDGQT FFTLDDGNTK FSDLIQLVDF 600
    YQLNKGVLPC KLKHHCIRVA L 621
    Length:621
    Mass (Da):70,585
    Last modified:January 4, 2005 - v2
    Checksum:i6FC737E8F35468BB
    GO
    Isoform 2 (identifier: Q60760-2) [UniParc]FASTAAdd to Basket

    Also known as: Delta

    The sequence of this isoform differs from the canonical sequence as follows:
         117-141: Missing.

    Note: Predominant isoform in most tissues.

    Show »
    Length:596
    Mass (Da):67,543
    Checksum:iEB13CA896DF41533
    GO
    Isoform 3 (identifier: Q60760-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         117-196: Missing.

    Show »
    Length:541
    Mass (Da):61,218
    Checksum:iA8FA9ED57C85F674
    GO

    Sequence cautioni

    The sequence AAH53842.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE37514.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti491 – 4922KR → NG in AAB53687. (PubMed:7731717)Curated
    Sequence conflicti555 – 5551A → T in BAC28088. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei117 – 19680Missing in isoform 3. 1 PublicationVSP_012379Add
    BLAST
    Alternative sequencei117 – 14125Missing in isoform 2. 3 PublicationsVSP_001844Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18996 mRNA. Translation: AAB53687.1.
    AF022072 mRNA. Translation: AAB72103.1.
    AK030727 mRNA. Translation: BAC27100.1.
    AK032927 mRNA. Translation: BAC28088.1.
    AK163841 mRNA. Translation: BAE37514.1. Different initiation.
    AL645803, AL663087 Genomic DNA. Translation: CAI23990.1.
    AL645803, AL663087 Genomic DNA. Translation: CAI23991.1.
    AL663087, AL645803 Genomic DNA. Translation: CAI25685.1.
    AL663087, AL645803 Genomic DNA. Translation: CAI25687.1.
    BC016111 mRNA. Translation: AAH16111.1.
    BC053842 mRNA. Translation: AAH53842.1. Different initiation.
    CCDSiCCDS24440.1. [Q60760-2]
    CCDS48754.1. [Q60760-3]
    PIRiI49199.
    RefSeqiNP_001171100.1. NM_001177629.1. [Q60760-3]
    NP_034475.2. NM_010345.4. [Q60760-2]
    XP_006514592.1. XM_006514529.1. [Q60760-1]
    UniGeneiMm.273117.
    Mm.491389.

    Genome annotation databases

    EnsembliENSMUST00000093321; ENSMUSP00000091011; ENSMUSG00000020176. [Q60760-2]
    ENSMUST00000109654; ENSMUSP00000105281; ENSMUSG00000020176. [Q60760-3]
    GeneIDi14783.
    KEGGimmu:14783.
    UCSCiuc007iaz.2. mouse. [Q60760-3]
    uc007iba.2. mouse. [Q60760-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18996 mRNA. Translation: AAB53687.1 .
    AF022072 mRNA. Translation: AAB72103.1 .
    AK030727 mRNA. Translation: BAC27100.1 .
    AK032927 mRNA. Translation: BAC28088.1 .
    AK163841 mRNA. Translation: BAE37514.1 . Different initiation.
    AL645803 , AL663087 Genomic DNA. Translation: CAI23990.1 .
    AL645803 , AL663087 Genomic DNA. Translation: CAI23991.1 .
    AL663087 , AL645803 Genomic DNA. Translation: CAI25685.1 .
    AL663087 , AL645803 Genomic DNA. Translation: CAI25687.1 .
    BC016111 mRNA. Translation: AAH16111.1 .
    BC053842 mRNA. Translation: AAH53842.1 . Different initiation.
    CCDSi CCDS24440.1. [Q60760-2 ]
    CCDS48754.1. [Q60760-3 ]
    PIRi I49199.
    RefSeqi NP_001171100.1. NM_001177629.1. [Q60760-3 ]
    NP_034475.2. NM_010345.4. [Q60760-2 ]
    XP_006514592.1. XM_006514529.1. [Q60760-1 ]
    UniGenei Mm.273117.
    Mm.491389.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3M7F X-ray 2.00 A 514-621 [» ]
    ProteinModelPortali Q60760.
    SMRi Q60760. Positions 195-437, 456-620.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200045. 6 interactions.
    DIPi DIP-446N.
    IntActi Q60760. 8 interactions.
    MINTi MINT-102080.

    PTM databases

    PhosphoSitei Q60760.

    Proteomic databases

    MaxQBi Q60760.
    PaxDbi Q60760.
    PRIDEi Q60760.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000093321 ; ENSMUSP00000091011 ; ENSMUSG00000020176 . [Q60760-2 ]
    ENSMUST00000109654 ; ENSMUSP00000105281 ; ENSMUSG00000020176 . [Q60760-3 ]
    GeneIDi 14783.
    KEGGi mmu:14783.
    UCSCi uc007iaz.2. mouse. [Q60760-3 ]
    uc007iba.2. mouse. [Q60760-2 ]

    Organism-specific databases

    CTDi 2887.
    MGIi MGI:103232. Grb10.

    Phylogenomic databases

    eggNOGi NOG307156.
    GeneTreei ENSGT00550000074537.
    HOVERGENi HBG000468.
    InParanoidi Q60760.
    OMAi ESTMGSE.
    OrthoDBi EOG7SFHW7.
    PhylomeDBi Q60760.
    TreeFami TF317511.

    Enzyme and pathway databases

    Reactomei REACT_188578. Signaling by SCF-KIT.

    Miscellaneous databases

    ChiTaRSi GRB10. mouse.
    NextBioi 286903.
    PROi Q60760.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60760.
    Bgeei Q60760.
    CleanExi MM_GRB10.
    Genevestigatori Q60760.

    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. "The cloning of Grb10 reveals a new family of SH2 domain proteins."
      Ooi J., Yajnik V., Immanuel D., Gordon M., Moskow J.J., Buchberg A., Margolis B.
      Oncogene 10:1621-1630(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH EGFR, TISSUE SPECIFICITY, PHOSPHORYLATION.
      Strain: Swiss.
    2. "The adapter protein Grb10 associates preferentially with the insulin receptor as compared with the IGF-I receptor in mouse fibroblasts."
      Laviola L., Giorgino F., Chow J.C., Baquero J.A., Hansen H., Ooi J., Zhu J., Riedel H., Smith R.J.
      J. Clin. Invest. 99:830-837(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH INSR AND IGF1R, TISSUE SPECIFICITY.
    3. "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] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Embryo and Embryonic head.
    4. Griffiths C., Sycamore N.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      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] (ISOFORMS 2 AND 3).
      Tissue: Eye and Olfactory epithelium.
    6. "Identification of the Meg1/Grb10 imprinted gene on mouse proximal chromosome 11, a candidate for the Silver-Russell syndrome gene."
      Miyoshi N., Kuroiwa Y., Kohda T., Shitara H., Yonekawa H., Kawabe T., Hasegawa H., Barton S.C., Surani M.A., Kaneko-Ishino T., Ishino F.
      Proc. Natl. Acad. Sci. U.S.A. 95:1102-1107(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IMPRINTING, DEVELOPMENTAL STAGE.
    7. "Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis."
      Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A., Swamy O.R., Leone M.E., Riedel H.
      Mol. Cell. Biol. 19:6217-6228(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFR1; INSR; IGF1R; MET AND PDGFRB.
    8. "Human GRB10 is imprinted and expressed from the paternal and maternal allele in a highly tissue- and isoform-specific fashion."
      Blagitko N., Mergenthaler S., Schulz U., Wollmann H.A., Craigen W., Eggermann T., Ropers H.-H., Kalscheuer V.M.
      Hum. Mol. Genet. 9:1587-1595(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IMPRINTING.
    9. "Two novel proteins that are linked to insulin-like growth factor (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signaling."
      Giovannone B., Lee E., Laviola L., Giorgino F., Cleveland K.A., Smith R.J.
      J. Biol. Chem. 278:31564-31573(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GIGYF1 AND GIGYF2.
    10. "The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor."
      Vecchione A., Marchese A., Henry P., Rotin D., Morrione A.
      Mol. Cell. Biol. 23:3363-3372(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IGF1R AND NEDD4.
    11. "Disruption of the imprinted Grb10 gene leads to disproportionate overgrowth by an Igf2-independent mechanism."
      Charalambous M., Smith F.M., Bennett W.R., Crew T.E., Mackenzie F., Ward A.
      Proc. Natl. Acad. Sci. U.S.A. 100:8292-8297(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, IMPRINTING, DEVELOPMENTAL STAGE.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    13. "Phosphorylation of grb10 regulates its interaction with 14-3-3."
      Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.
      J. Biol. Chem. 280:16987-16993(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKT1 AND YWHAE, PHOSPHORYLATION.
    14. "Distinct Grb10 domain requirements for effects on glucose uptake and insulin signaling."
      Mori K., Giovannone B., Smith R.J.
      Mol. Cell. Endocrinol. 230:39-50(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH INSR.
    15. "GRB10 binds to LRP6, the Wnt co-receptor and inhibits canonical Wnt signaling pathway."
      Tezuka N., Brown A.M., Yanagawa S.
      Biochem. Biophys. Res. Commun. 356:648-654(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LRP6.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    17. "Grb10/Nedd4-mediated multiubiquitination of the insulin-like growth factor receptor regulates receptor internalization."
      Monami G., Emiliozzi V., Morrione A.
      J. Cell. Physiol. 216:426-437(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiGRB10_MOUSE
    AccessioniPrimary (citable) accession number: Q60760
    Secondary accession number(s): O35352
    , Q3TQ71, Q7TSA4, Q8BSH4, Q8BSS5, Q91WC5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The GRB10 locus is imprinted. The maternal allele is expressed in most tissues, except the brain where it is expressed from the paternal allele. Expression from the maternal allele in fetal and adult brain was however described in PubMed:10861285.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3