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Q60631 (GRB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Growth factor receptor-bound protein 2
Alternative name(s):
Adapter protein GRB2
SH2/SH3 adapter GRB2
Gene names
Name:Grb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway.

Isoform 2 does not bind to phosphorylated epidermal growth factor receptor (EGFR) but inhibits EGF-induced. transactivation of a RAS-responsive element. Isoform 2 acts as a dominant negative protein over GRB2 and by suppressing proliferative signals, may trigger active programmed cell death By similarity.

Subunit structure

Associates (via SH2 domain) with activated EGF receptors (tyrosine phosphorylated). Interacts with PDGFRA (tyrosine phosphorylated); the interaction may be indirect. Also associates to other cellular Tyr-phosphorylated proteins such as SIT1, IRS1, IRS4, SHC and LNK; probably via the concerted action of both its SH2 and SH3 domains. It also seems to interact with RAS in the signaling pathway leading to DNA synthesis. Binds to and translocates the guanine nucleotide exchange factors SOS. Interacts with phosphorylated TOM1L1 and MET. Interacts with the phosphorylated C-terminus of SH2B2. Interacts with phosphorylated SIT1, LAX1, LAT, LAT2 and LIME1 upon TCR and/or BCR activation. Interacts with PTPNS1, REPS2 and the syntrophin SNTA1. Interacts with REPS1 and PIK3C2B via its SH3 domains. Interacts with CBL and CBLB. Interacts with AJUBA. Interacts with SHB, INPP5D/SHIP1, SKAP1 and SKAP2 By similarity. Interacts with CLNK. Forms a complex with MUC1 and SOS1, through interaction of the SH3 domains with SOS1 and the SH2 domain with phosphorylated MUC1. Interacts with PRNP By similarity. Interacts with NISCH and RALGPS1 By similarity. Interacts also with HCST. Interacts with GAPT and PTPRE. Interacts (via SH2 domain) with KIF26A By similarity. Interacts with THEMIS. Interacts (via SH3 2) with GAB2. Interacts with ADAM15. Interacts with PTPRJ and BCR. Interacts with PTPN23. Interacts with FLT4 (tyrosine phosphorylated) By similarity. Part of a complex including TNK2, GRB2 and one receptor tyrosine kinase (RTK) such as AXL, in which GRB2 promotes RTK recruitment by TNK2 By similarity. Interacts with NTRK1 (phosphorylated upon ligand-binding). Interacts with PTK2B/PYK2 (tyrosine phosphorylated) By similarity. Interacts with KDR. Interacts with FLT1 (tyrosine-phosphorylated). Interacts with THEMIS2. Interacts (via SH2 domain) with AXL and KIT (phosphorylated). Interacts with EPHB1 and SHC1; activates the MAPK/ERK cascade to regulate cell migration. Interacts with PTPN11. Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). Interacts with PTK2/FAK1 (tyrosine phosphorylated). Interacts with SCIMP. Interacts with TESPA1. Interacts (via SH3 domains) with GAREM (via proline-rich domain and tyrosine phosphorylated); the interaction occurs upon EGF stimulation. Interacts with ASAP3 (phosphorylated form). Interacts with CD28 By similarity. Interacts with PLCG1, LAT and THEMIS upon TCR activation in thymocytes; the association is weaker in the absence of TESPA1. Interacts with DAB2. Interacts with RAB13; may recruit RAB13 to the leading edge of migrating endothelial cells where it can activate RHOA. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Endosome By similarity. Golgi apparatus Ref.17.

Domain

The SH3 domains mediate interaction with RALGPS1 and SHB By similarity.

Sequence similarities

Belongs to the GRB2/sem-5/DRK family.

Contains 1 SH2 domain.

Contains 2 SH3 domains.

Ontologies

Keywords
   Cellular componentCytoplasm
Endosome
Golgi apparatus
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH2 domain
SH3 domain
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRas protein signal transduction

Traceable author statement PubMed 1322798. Source: MGI

aging

Inferred from electronic annotation. Source: Ensembl

anatomical structure formation involved in morphogenesis

Inferred from mutant phenotype PubMed 11369229. Source: MGI

branching involved in labyrinthine layer morphogenesis

Inferred from mutant phenotype PubMed 11369229. Source: MGI

cell differentiation

Inferred from mutant phenotype PubMed 16908534. Source: MGI

cellular response to ionizing radiation

Inferred from electronic annotation. Source: Ensembl

insulin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin filament polymerization

Inferred from genetic interaction PubMed 17923684. Source: MGI

positive regulation of reactive oxygen species metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of signal transduction

Inferred from direct assay Ref.1. Source: GOC

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

receptor internalization

Inferred from electronic annotation. Source: Ensembl

regulation of MAPK cascade

Inferred from genetic interaction PubMed 15569713. Source: MGI

signal transduction in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentCOP9 signalosome

Inferred from direct assay Ref.33. Source: UniProtKB

Golgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

Grb2-EGFR complex

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from direct assay PubMed 23793062. Source: MGI

cytoplasm

Inferred from direct assay PubMed 15736129. Source: MGI

cytosol

Traceable author statement. Source: Reactome

endosome

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from direct assay PubMed 15983387. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 17923684. Source: MGI

vesicle membrane

Inferred from direct assay PubMed 12147689. Source: MGI

   Molecular_functionSH3 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

SH3/SH2 adaptor activity

Inferred from direct assay Ref.1. Source: MGI

ephrin receptor binding

Inferred from physical interaction Ref.20. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 14722116Ref.28Ref.27Ref.32. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 8438166. Source: MGI

protein phosphatase binding

Inferred from physical interaction PubMed 20398064. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q60631-1)

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.
Isoform 2 (identifier: Q60631-2)

Also known as: GRB3-3;

The sequence of this isoform differs from the canonical sequence as follows:
     60-100: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Growth factor receptor-bound protein 2
PRO_0000088199

Regions

Domain1 – 5858SH3 1
Domain60 – 15293SH2
Domain156 – 21560SH3 2

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue61N6-acetyllysine By similarity
Modified residue501N6-acetyllysine By similarity
Modified residue1091N6-acetyllysine By similarity
Modified residue2111Phosphothreonine By similarity

Natural variations

Alternative sequence60 – 10041Missing in isoform 2.
VSP_001841

Secondary structure

............. 217
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 97F4A4FE4B248DDF

FASTA21725,238
        10         20         30         40         50         60 
MEAIAKYDFK ATADDELSFK RGDILKVLNE ECDQNWYKAE LNGKDGFIPK NYIEMKPHPW 

        70         80         90        100        110        120 
FFGKIPRAKA EEMLSKQRHD GAFLIRESES APGDFSLSVK FGNDVQHFKV LRDGAGKYFL 

       130        140        150        160        170        180 
WVVKFNSLNE LVDYHRSTSV SRNQQIFLRD IEQMPQQPTY VQALFDFDPQ EDGELGFRRG 

       190        200        210 
DFIHVMDNSD PNWWKGACHG QTGMFPRNYV TPVNRNV 

« Hide

Isoform 2 (GRB3-3) [UniParc].

Checksum: 64323FA95FE940C5
Show »

FASTA17620,589

References

« Hide 'large scale' references
[1]"Molecular cloning of the mouse grb2 gene: differential interaction of the Grb2 adaptor protein with epidermal growth factor and nerve growth factor receptors."
Suen K., Bustelo X.R., Pawson T., Barbacid M.
Mol. Cell. Biol. 13:5500-5512(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]Tanaka S.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: BALB/c.
[3]"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).
Strain: C57BL/6 and FVB/N.
Tissue: Brain and Mammary gland.
[4]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 125-136, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[5]"Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase."
Schlaepfer D.D., Hanks S.K., Hunter T., van der Geer P.
Nature 372:786-791(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK2/FAK1.
[6]"Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation."
Bazenet C.E., Gelderloos J.A., Kazlauskas A.
Mol. Cell. Biol. 16:6926-6936(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDGFRA AND PTPN11.
[7]"Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-gamma2 by the M-CSF receptor is necessary for differentiation signaling."
Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.
EMBO J. 16:5880-5893(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSF1R, PHOSPHORYLATION.
[8]"An eps homology (EH) domain protein that binds to the ral-GTPase target, RalBP1."
Yamaguchi A., Urano T., Goi T., Feig L.A.
J. Biol. Chem. 272:31230-31234(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH REPS1.
Tissue: Muscle.
[9]"Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules."
Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.
J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLT1.
[10]"Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2."
Xu X.X., Yi T., Tang B., Lambeth J.D.
Oncogene 16:1561-1569(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2.
[11]"Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor."
Thommes K., Lennartsson J., Carlberg M., Ronnstrand L.
Biochem. J. 341:211-216(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIT.
[12]"Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T- and B-cell antigen receptors."
Nishida K., Yoshida Y., Itoh M., Fukada T., Ohtani T., Shirogane T., Atsumi T., Takahashi-Tezuka M., Ishihara K., Hibi M., Hirano T.
Blood 93:1809-1816(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAB2.
[13]"Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration."
Jones N., Master Z., Jones J., Bouchard D., Gunji Y., Sasaki H., Daly R., Alitalo K., Dumont D.J.
J. Biol. Chem. 274:30896-30905(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TEK/TIE2.
[14]"Ajuba, a novel LIM protein, interacts with Grb2, augments mitogen-activated protein kinase activity in fibroblasts, and promotes meiotic maturation of Xenopus oocytes in a Grb2- and Ras-dependent manner."
Goyal R.K., Lin P., Kanungo J., Payne A.S., Muslin A.J., Longmore G.D.
Mol. Cell. Biol. 19:4379-4389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AJUBA.
[15]"Mouse alpha1-syntrophin binding to Grb2: further evidence of a role for syntrophin in cell signaling."
Oak S.A., Russo K., Petrucci T.C., Jarrett H.W.
Biochemistry 40:11270-11278(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNTA1.
[16]"MIST functions through distinct domains in immunoreceptor signaling in the presence and absence of LAT."
Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.
J. Biol. Chem. 276:36043-36050(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLNK.
[17]"PrPC directly interacts with proteins involved in signaling pathways."
Spielhaupter C., Schaetzl H.M.
J. Biol. Chem. 276:44604-44612(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PRNP.
[18]"Insulin receptor substrate 3 (IRS-3) and IRS-4 impair IRS-1- and IRS-2-mediated signaling."
Tsuruzoe K., Emkey R., Kriauciunas K.M., Ueki K., Kahn C.R.
Mol. Cell. Biol. 21:26-38(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IRS4.
[19]"'Srcasm: a novel Src activating and signaling molecule."
Seykora J.T., Mei L., Dotto G.P., Stein P.L.
J. Biol. Chem. 277:2812-2822(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOM1L1.
[20]"EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis."
Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.
J. Cell Biol. 162:661-671(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHB1 AND SHC1.
[21]"LIME, a novel transmembrane adaptor protein, associates with p56lck and mediates T cell activation."
Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.
J. Exp. Med. 198:1463-1473(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIME1.
[22]"Positive and negative regulation of FcepsilonRI-mediated signaling by the adaptor protein LAB/NTAL."
Zhu M., Liu Y., Koonpaew S., Granillo O., Zhang W.
J. Exp. Med. 200:991-1000(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAT2.
[23]"Negative regulation of mast cell signaling and function by the adaptor LAB/NTAL."
Volna P., Lebduska P., Draberova L., Simova S., Heneberg P., Boubelik M., Bugajev V., Malissen B., Wilson B.S., Horejsi V., Malissen M., Draber P.
J. Exp. Med. 200:1001-1013(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAT2.
[24]"LIME acts as a transmembrane adapter mediating BCR-dependent B-cell activation."
Ahn E., Lee H., Yun Y.
Blood 107:1521-1527(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIME1.
[25]"Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF."
Lamalice L., Houle F., Huot J.
J. Biol. Chem. 281:34009-34020(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDR.
[26]"NKG2D-mediated signaling requires a DAP10-bound Grb2-Vav1 intermediate and phosphatidylinositol-3-kinase in human natural killer cells."
Upshaw J.L., Arneson L.N., Schoon R.A., Dick C.J., Billadeau D.D., Leibson P.J.
Nat. Immunol. 7:524-532(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCST.
[27]"Themis, a T cell-specific protein important for late thymocyte development."
Lesourne R., Uehara S., Lee J., Song K.-D., Li L., Pinkhasov J., Zhang Y., Weng N.-P., Wildt K.F., Wang L., Bosselut R., Love P.E.
Nat. Immunol. 10:840-847(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THEMIS.
[28]"Themis is a member of a new metazoan gene family and is required for the completion of thymocyte positive selection."
Johnson A.L., Aravind L., Shulzhenko N., Morgun A., Choi S.-Y., Crockford T.L., Lambe T., Domaschenz H., Kucharska E.M., Zheng L., Vinuesa C.G., Lenardo M.J., Goodnow C.C., Cornall R.J., Schwartz R.H.
Nat. Immunol. 10:831-839(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THEMIS.
[29]"Gasp, a Grb2-associating protein, is critical for positive selection of thymocytes."
Patrick M.S., Oda H., Hayakawa K., Sato Y., Eshima K., Kirikae T., Iemura S., Shirai M., Abe T., Natsume T., Sasazuki T., Suzuki H.
Proc. Natl. Acad. Sci. U.S.A. 106:16345-16350(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THEMIS.
[30]"Themis2/ICB1 is a signaling scaffold that selectively regulates macrophage Toll-like receptor signaling and cytokine production."
Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S., Lanfrancotti A., Notley C., Hussell T., Cope A.P., Wait R.
PLoS ONE 5:E11465-E11465(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THEMIS2.
[31]"Rab13-dependent trafficking of RhoA is required for directional migration and angiogenesis."
Wu C., Agrawal S., Vasanji A., Drazba J., Sarkaria S., Xie J., Welch C.M., Liu M., Anand-Apte B., Horowitz A.
J. Biol. Chem. 286:23511-23520(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB13.
[32]"SCIMP, a transmembrane adapter protein involved in major histocompatibility complex class II signaling."
Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M., Skopcova T., Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A., Brdicka T.
Mol. Cell. Biol. 31:4550-4562(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCIMP.
[33]"Tespa1 is involved in late thymocyte development through the regulation of TCR-mediated signaling."
Wang D., Zheng M., Lei L., Ji J., Yao Y., Qiu Y., Ma L., Lou J., Ouyang C., Zhang X., He Y., Chi J., Wang L., Kuang Y., Wang J., Cao X., Lu L.
Nat. Immunol. 13:560-568(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAT; PLCG1 AND THEMIS.
Tissue: Thymocyte.
[34]"Solution structure of the Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS: direct refinement against NOEs, J-couplings and 1H and 13C chemical shifts."
Wittekind M., Mapelli C., Lee V., Goldfarb V., Friedrichs M.S., Meyers C.A., Mueller L.
J. Mol. Biol. 267:933-952(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-65.
+Additional computationally mapped references.

Web resources

Wikipedia

Grb2 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07617 mRNA. Translation: AAB40022.1.
D85748 mRNA. Translation: BAA12862.1.
BC052377 mRNA. Translation: AAH52377.1.
BC085254 mRNA. Translation: AAH85254.1.
CCDSCCDS25645.1. [Q60631-1]
PIRA54688.
RefSeqNP_032189.1. NM_008163.3. [Q60631-1]
UniGeneMm.439649.
Mm.490413.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GBQNMR-A1-61[»]
1GBRNMR-A1-59[»]
2GBQNMR-A1-59[»]
3GBQNMR-A1-59[»]
4GBQNMR-A1-59[»]
ProteinModelPortalQ60631.
SMRQ60631. Positions 1-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200046. 28 interactions.
DIPDIP-259N.
IntActQ60631. 64 interactions.
MINTMINT-84889.

Chemistry

BindingDBQ60631.
ChEMBLCHEMBL4830.

PTM databases

PhosphoSiteQ60631.

Proteomic databases

MaxQBQ60631.
PaxDbQ60631.
PRIDEQ60631.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021090; ENSMUSP00000021090; ENSMUSG00000059923. [Q60631-1]
ENSMUST00000106497; ENSMUSP00000102106; ENSMUSG00000059923. [Q60631-1]
ENSMUST00000106499; ENSMUSP00000102108; ENSMUSG00000059923. [Q60631-2]
GeneID14784.
KEGGmmu:14784.
UCSCuc007mij.1. mouse. [Q60631-1]

Organism-specific databases

CTD2885.
MGIMGI:95805. Grb2.

Phylogenomic databases

eggNOGNOG298780.
GeneTreeENSGT00550000074482.
HOGENOMHOG000251625.
HOVERGENHBG005404.
InParanoidQ60631.
KOK04364.
OMAVETKFVQ.
OrthoDBEOG75F4F6.
PhylomeDBQ60631.
TreeFamTF354288.

Gene expression databases

ArrayExpressQ60631.
BgeeQ60631.
CleanExMM_GRB2.
GenevestigatorQ60631.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEPS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGRB2. mouse.
EvolutionaryTraceQ60631.
NextBio286907.
PROQ60631.
SOURCESearch...

Entry information

Entry nameGRB2_MOUSE
AccessionPrimary (citable) accession number: Q60631
Secondary accession number(s): Q61240
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot