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Growth factor receptor-bound protein 10 (GRB10 adapter protein) (Maternally expressed gene 1 protein)

 GRB10_MOUSE             Reviewed;         621 AA.
Q60760; O35352; Q3TQ71; Q7TSA4; Q8BSH4; Q8BSS5; Q91WC5;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 2.
10-FEB-2021, entry version 182.
RecName: Full=Growth factor receptor-bound protein 10;
AltName: Full=GRB10 adapter protein;
AltName: Full=Maternally expressed gene 1 protein;
Name=Grb10; Synonyms=Meg1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH EGFR, TISSUE
SPECIFICITY, AND PHOSPHORYLATION.
STRAIN=SWR/J;
PubMed=7731717;
Ooi J., Yajnik V., Immanuel D., Gordon M., Moskow J.J., Buchberg A.,
Margolis B.;
"The cloning of Grb10 reveals a new family of SH2 domain proteins.";
Oncogene 10:1621-1630(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH INSR AND IGF1R,
AND TISSUE SPECIFICITY.
PubMed=9062339; DOI=10.1172/jci119246;
Laviola L., Giorgino F., Chow J.C., Baquero J.A., Hansen H., Ooi J.,
Zhu J., Riedel H., Smith R.J.;
"The adapter protein Grb10 associates preferentially with the insulin
receptor as compared with the IGF-I receptor in mouse fibroblasts.";
J. Clin. Invest. 99:830-837(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic head;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Griffiths C., Sycamore N.;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Eye, and Olfactory epithelium;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IMPRINTING, AND DEVELOPMENTAL STAGE.
PubMed=9448292; DOI=10.1073/pnas.95.3.1102;
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.;
"Identification of the Meg1/Grb10 imprinted gene on mouse proximal
chromosome 11, a candidate for the Silver-Russell syndrome gene.";
Proc. Natl. Acad. Sci. U.S.A. 95:1102-1107(1998).
[7]
INTERACTION WITH FGFR1; INSR; IGF1R; MET AND PDGFRB.
PubMed=10454568; DOI=10.1128/mcb.19.9.6217;
Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A.,
Swamy O.R., Leone M.E., Riedel H.;
"Grb10, a positive, stimulatory signaling adapter in platelet-derived
growth factor BB-, insulin-like growth factor I-, and insulin-mediated
mitogenesis.";
Mol. Cell. Biol. 19:6217-6228(1999).
[8]
IMPRINTING.
PubMed=10861285; DOI=10.1093/hmg/9.11.1587;
Blagitko N., Mergenthaler S., Schulz U., Wollmann H.A., Craigen W.,
Eggermann T., Ropers H.-H., Kalscheuer V.M.;
"Human GRB10 is imprinted and expressed from the paternal and maternal
allele in a highly tissue- and isoform-specific fashion.";
Hum. Mol. Genet. 9:1587-1595(2000).
[9]
INTERACTION WITH GIGYF1 AND GIGYF2.
PubMed=12771153; DOI=10.1074/jbc.m211572200;
Giovannone B., Lee E., Laviola L., Giorgino F., Cleveland K.A., Smith R.J.;
"Two novel proteins that are linked to insulin-like growth factor (IGF-I)
receptors by the Grb10 adapter and modulate IGF-I signaling.";
J. Biol. Chem. 278:31564-31573(2003).
[10]
FUNCTION, AND INTERACTION WITH IGF1R AND NEDD4.
PubMed=12697834; DOI=10.1128/mcb.23.9.3363-3372.2003;
Vecchione A., Marchese A., Henry P., Rotin D., Morrione A.;
"The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and
stability of the insulin-like growth factor I receptor.";
Mol. Cell. Biol. 23:3363-3372(2003).
[11]
FUNCTION, DISRUPTION PHENOTYPE, IMPRINTING, AND DEVELOPMENTAL STAGE.
PubMed=12829789; DOI=10.1073/pnas.1532175100;
Charalambous M., Smith F.M., Bennett W.R., Crew T.E., Mackenzie F.,
Ward A.;
"Disruption of the imprinted Grb10 gene leads to disproportionate
overgrowth by an Igf2-independent mechanism.";
Proc. Natl. Acad. Sci. U.S.A. 100:8292-8297(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[13]
INTERACTION WITH AKT1 AND YWHAE, AND PHOSPHORYLATION.
PubMed=15722337; DOI=10.1074/jbc.m501477200;
Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.;
"Phosphorylation of grb10 regulates its interaction with 14-3-3.";
J. Biol. Chem. 280:16987-16993(2005).
[14]
FUNCTION, AND INTERACTION WITH INSR.
PubMed=15664450; DOI=10.1016/j.mce.2004.11.004;
Mori K., Giovannone B., Smith R.J.;
"Distinct Grb10 domain requirements for effects on glucose uptake and
insulin signaling.";
Mol. Cell. Endocrinol. 230:39-50(2005).
[15]
FUNCTION, AND INTERACTION WITH LRP6.
PubMed=17376403; DOI=10.1016/j.bbrc.2007.03.019;
Tezuka N., Brown A.M., Yanagawa S.;
"GRB10 binds to LRP6, the Wnt co-receptor and inhibits canonical Wnt
signaling pathway.";
Biochem. Biophys. Res. Commun. 356:648-654(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18286479; DOI=10.1002/jcp.21405;
Monami G., Emiliozzi V., Morrione A.;
"Grb10/Nedd4-mediated multiubiquitination of the insulin-like growth factor
receptor regulates receptor internalization.";
J. Cell. Physiol. 216:426-437(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-503, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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. {ECO:0000269|PubMed:12697834, ECO:0000269|PubMed:12829789,
ECO:0000269|PubMed:15664450, ECO:0000269|PubMed:17376403,
ECO:0000269|PubMed:18286479}.
-!- ACTIVITY REGULATION: Phosphorylation by mTORC1 stabilizes and activates
GRB10 constituting a feedback pathway by which mTORC1 inhibits INSR-
dependent signaling. {ECO:0000250}.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- INTERACTION:
Q60760; P15208: Insr; NbExp=6; IntAct=EBI-861810, EBI-6999015;
Q60760; P46935: Nedd4; NbExp=6; IntAct=EBI-861810, EBI-773516;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18286479}.
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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Alpha;
IsoId=Q60760-1; Sequence=Displayed;
Name=2; Synonyms=Delta;
IsoId=Q60760-2; Sequence=VSP_001844;
Name=3;
IsoId=Q60760-3; Sequence=VSP_012379;
-!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:7731717,
ECO:0000269|PubMed:9062339}.
-!- DEVELOPMENTAL STAGE: 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.
{ECO:0000269|PubMed:12829789, ECO:0000269|PubMed:9448292}.
-!- DOMAIN: The PH domain binds relatively non-specifically to several
phosphoinositides, including PI(5)P, PI(4,5)P2, PI(3,4)P2 and
PI(3,4,5)P3, with modest affinities. {ECO:0000250}.
-!- PTM: Phosphorylated on serine residues upon EGF, FGF and PDGF
stimulation. {ECO:0000269|PubMed:15722337, ECO:0000269|PubMed:7731717}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:12829789}.
-!- 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.
-!- MISCELLANEOUS: [Isoform 2]: Predominant isoform in most tissues.
{ECO:0000305}.
-!- SIMILARITY: Belongs to the GRB7/10/14 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH53842.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE37514.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; U18996; AAB53687.1; -; mRNA.
EMBL; AF022072; AAB72103.1; -; mRNA.
EMBL; AK030727; BAC27100.1; -; mRNA.
EMBL; AK032927; BAC28088.1; -; mRNA.
EMBL; AK163841; BAE37514.1; ALT_INIT; mRNA.
EMBL; AL645803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL663087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC016111; AAH16111.1; -; mRNA.
EMBL; BC053842; AAH53842.1; ALT_INIT; mRNA.
CCDS; CCDS24440.1; -. [Q60760-2]
CCDS; CCDS48754.1; -. [Q60760-3]
PIR; I49199; I49199.
RefSeq; NP_001171100.1; NM_001177629.1. [Q60760-3]
RefSeq; NP_034475.2; NM_010345.4. [Q60760-2]
RefSeq; XP_006514592.1; XM_006514529.1.
RefSeq; XP_011241966.1; XM_011243664.1. [Q60760-3]
PDB; 3M7F; X-ray; 2.00 A; A=514-621.
PDBsum; 3M7F; -.
SMR; Q60760; -.
BioGRID; 200045; 5.
DIP; DIP-446N; -.
IntAct; Q60760; 8.
MINT; Q60760; -.
STRING; 10090.ENSMUSP00000091011; -.
iPTMnet; Q60760; -.
PhosphoSitePlus; Q60760; -.
PaxDb; Q60760; -.
PeptideAtlas; Q60760; -.
PRIDE; Q60760; -.
Antibodypedia; 27751; 449 antibodies.
Ensembl; ENSMUST00000093321; ENSMUSP00000091011; ENSMUSG00000020176. [Q60760-2]
Ensembl; ENSMUST00000109654; ENSMUSP00000105281; ENSMUSG00000020176. [Q60760-3]
GeneID; 14783; -.
KEGG; mmu:14783; -.
UCSC; uc007iaz.2; mouse. [Q60760-3]
UCSC; uc007iba.2; mouse. [Q60760-2]
CTD; 2887; -.
MGI; MGI:103232; Grb10.
eggNOG; KOG3751; Eukaryota.
GeneTree; ENSGT00940000155909; -.
HOGENOM; CLU_023207_0_1_1; -.
InParanoid; Q60760; -.
OMA; NGSHTQL; -.
OrthoDB; 497681at2759; -.
PhylomeDB; Q60760; -.
TreeFam; TF317511; -.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-74713; IRS activation.
Reactome; R-MMU-74749; Signal attenuation.
Reactome; R-MMU-74751; Insulin receptor signalling cascade.
Reactome; R-MMU-8853659; RET signaling.
BioGRID-ORCS; 14783; 2 hits in 17 CRISPR screens.
ChiTaRS; Grb10; mouse.
PRO; PR:Q60760; -.
Proteomes; UP000000589; Chromosome 11.
RNAct; Q60760; protein.
Bgee; ENSMUSG00000020176; Expressed in urinary bladder and 319 other tissues.
ExpressionAtlas; Q60760; baseline and differential.
Genevisible; Q60760; MM.
GO; GO:0005829; C:cytosol; TAS:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0005158; F:insulin receptor binding; IPI:BHF-UCL.
GO; GO:0001784; F:phosphotyrosine residue binding; TAS:BHF-UCL.
GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:MGI.
GO; GO:0030159; F:signaling receptor complex adaptor activity; IPI:BHF-UCL.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:MGI.
GO; GO:0010467; P:gene expression; IMP:MGI.
GO; GO:0008286; P:insulin receptor signaling pathway; ISO:MGI.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IPI:MGI.
GO; GO:0046325; P:negative regulation of glucose import; IMP:BHF-UCL.
GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; ISO:MGI.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0042326; P:negative regulation of phosphorylation; IDA:BHF-UCL.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0032868; P:response to insulin; ISO:MGI.
GO; GO:0007165; P:signal transduction; TAS:MGI.
GO; GO:1904738; P:vascular associated smooth muscle cell migration; IMP:MGI.
CDD; cd01259; PH_APBB1IP; 1.
CDD; cd10415; SH2_Grb10; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR015042; BPS-dom.
InterPro; IPR039664; GRB/APBB1IP.
InterPro; IPR035036; Grb10.
InterPro; IPR035037; Grb10_SH2.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR039665; PH_APBB1IP.
InterPro; IPR001849; PH_domain.
InterPro; IPR000159; RA_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR11243; PTHR11243; 1.
PANTHER; PTHR11243:SF4; PTHR11243:SF4; 1.
Pfam; PF08947; BPS; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00788; RA; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00233; PH; 1.
SMART; SM00314; RA; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50200; RA; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cytoplasm; Phosphoprotein;
Reference proteome; SH2 domain.
CHAIN 1..621
/note="Growth factor receptor-bound protein 10"
/id="PRO_0000150347"
DOMAIN 194..278
/note="Ras-associating"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
DOMAIN 318..427
/note="PH"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
DOMAIN 520..601
/note="SH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
MOD_RES 50
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q13322"
MOD_RES 96
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:15345747"
MOD_RES 455
/note="Phosphoserine; by MTOR and PKB/AKT1"
/evidence="ECO:0000250|UniProtKB:Q13322"
MOD_RES 458
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079"
MOD_RES 503
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
VAR_SEQ 117..196
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_012379"
VAR_SEQ 117..141
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9062339"
/id="VSP_001844"
CONFLICT 491..492
/note="KR -> NG (in Ref. 1; AAB53687)"
/evidence="ECO:0000305"
CONFLICT 555
/note="A -> T (in Ref. 3; BAC28088)"
/evidence="ECO:0000305"
HELIX 515..517
/evidence="ECO:0000244|PDB:3M7F"
HELIX 527..536
/evidence="ECO:0000244|PDB:3M7F"
STRAND 543..548
/evidence="ECO:0000244|PDB:3M7F"
STRAND 556..562
/evidence="ECO:0000244|PDB:3M7F"
STRAND 565..576
/evidence="ECO:0000244|PDB:3M7F"
STRAND 579..585
/evidence="ECO:0000244|PDB:3M7F"
STRAND 588..593
/evidence="ECO:0000244|PDB:3M7F"
HELIX 594..601
/evidence="ECO:0000244|PDB:3M7F"
STRAND 608..610
/evidence="ECO:0000244|PDB:3M7F"
SEQUENCE 621 AA; 70585 MW; 6FC737E8F35468BB CRC64;
MNNDINSSVE SLNSACNMQS DTDTAPLLED GQHASNQGAA SSSRGQPQAS PRQKMQRSQP
VHILRRLQEE DQQLRTASLP AIPNPFPELT GAAPGSPPSV APSSLPPPPS QPPAKHCGRC
EKWIPGENTR GNGKRKIWRW QFPPGFQLSK LTRPGLWTKT TARFSKKQPK NQCPTDTVNP
VARMPTSQME KLRLRKDVKV FSEDGTSKVV EILTDMTARD LCQLLVYKSH CVDDNSWTLV
EHHPQLGLER CLEDHEIVVQ VESTMPSESK FLFRKNYAKY EFFKNPVNFF PDQMVNWCQQ
SNGGQAQLLQ NFLNTSSCPE IQGFLQVKEV GRKSWKKLYV CLRRSGLYYS TKGTSKEPRH
LQLLADLEES SIFYLIAGKK QYNAPNEHGM CIKPNKAKTE MKELRLLCAE DEQIRTCWMT
AFRLLKYGML LYQNYRIPQR KGLPPPFNAP MRSVSENSLV AMDFSGQIGR VIDNPAEAQS
AALEEGHAWR KRSTRMNILS SQSPLHPSTL NAVIHRTQHW FHGRISREES HRIIKQQGLV
DGLFLLRDSQ SNPKAFVLTL CHHQKIKNFQ ILPCEDDGQT FFTLDDGNTK FSDLIQLVDF
YQLNKGVLPC KLKHHCIRVA L


Related products :

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GRB2 GRB10 Gene growth factor receptor-bound protein 10
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Pathways :
WP2292: Chemokine signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP1616: ABC transporters
WP1892: Protein folding
WP931: G Protein Signaling Pathways
WP1685: Peptidoglycan biosynthesis
WP1692: Protein export
WP2199: Seed Development
WP1644: DNA replication
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP813: G Protein Signaling Pathways
WP1657: Glycerolipid metabolism
WP1939: Unfolded Protein Response
WP731: Sterol regulatory element binding protein related
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1700: Selenoamino acid metabolism
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP1663: Homologous recombination
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1673: Naphthalene and anthracene degradation
WP35: G Protein Signaling Pathways
WP1531: Vitamin D synthesis
WP2324: AGE/RAGE pathway
WP525: Mitochondrial Unfolded-Protein Response
WP1235: Signaling of Hepatocyte Growth Factor Receptor

Related Genes :
[Gigyf2 Kiaa0642 Perq2 Tnrc15] GRB10-interacting GYF protein 2 (PERQ amino acid-rich with GYF domain-containing protein 2) (Trinucleotide repeat-containing gene 15 protein)
[GRB2 ASH] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[FGFR1 BFGFR CEK FGFBR FLG FLT2 HBGFR] Fibroblast growth factor receptor 1 (FGFR-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (BFGFR) (bFGF-R-1) (Fms-like tyrosine kinase 2) (FLT-2) (N-sam) (Proto-oncogene c-Fgr) (CD antigen CD331)
[EGFR ERBB ERBB1 HER1] Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1)
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[Fgfr1 Flg] Fibroblast growth factor receptor 1 (FGFR-1) (bFGF-R-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (MFR) (Proto-oncogene c-Fgr) (CD antigen CD331)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[Igf1r] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Igf1r] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[Met] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[GRB7] Growth factor receptor-bound protein 7 (B47) (Epidermal growth factor receptor GRB-7) (GRB7 adapter protein)
[Fgfr1 Flg] Fibroblast growth factor receptor 1 (FGFR-1) (bFGF-R-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (MFR) (Proto-oncogene c-Fgr) (CD antigen CD331)
[Grb2] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (SH2/SH3 adapter GRB2)
[Grb7] Growth factor receptor-bound protein 7 (Epidermal growth factor receptor GRB-7) (GRB7 adapter protein)
[Grb2 Ash] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain] (Fragment)
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Met] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)

Bibliography :
[33187293] Recombinant Chromosome 7 Driven by Maternal Chromosome 7 Pericentric Inversion in a Girl with Features of Silver-Russell Syndrome.
[31794259] Role of Grb10 in mTORC1-dependent regulation of insulin signaling and action in human skeletal muscle cells.
[31179345] Distinct Effects of Carrageenan and High-Fat Consumption on the Mechanisms of Insulin Resistance in Nonobese and Obese Models of Type 2 Diabetes.
[31100449] Contribution of GRB10 to the prenatal phenotype in Silver-Russell syndrome? Lessons from 7p12 copy number variations.
[31033440] HRI coordinates translation necessary for protein homeostasis and mitochondrial function in erythropoiesis.
[30932322] Detailed analysis of paternal knockout Grb10 mice suggests effects on stability of social behavior, rather than social dominance.
[30859219] Developmental Dieldrin Exposure Alters DNA Methylation at Genes Related to Dopaminergic Neuron Development and Parkinson's Disease in Mouse Midbrain.
[30630414] Probe-based association analysis identifies several deletions associated with average daily gain in beef cattle.
[30379590] Proproliferative function of adaptor protein GRB10 in prostate carcinoma.
[30251157] Effects of superovulation, in vitro fertilization, and oocyte in vitro maturation on imprinted gene Grb10 in mouse blastocysts.