Q60631 (GRB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Growth factor receptor-bound protein 2

Alternative name(s):
Adapter protein GRB2
SH2/SH3 adapter GRB2

Gene names

Name:

Grb2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	217 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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. 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
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 component	Cytoplasm Endosome Golgi apparatus Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat SH2 domain SH3 domain
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Ras protein signal transduction Traceable author statement PubMed 1322798. Source: MGI aging Inferred from electronic annotation. Source: Compara 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: Compara insulin receptor signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara protein heterooligomerization Inferred from electronic annotation. Source: Compara receptor internalization Inferred from electronic annotation. Source: Compara regulation of MAPK cascade Inferred from genetic interaction PubMed 15569713. Source: MGI signal transduction in response to DNA damage Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell Grb2-EGFR complex Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome endosome Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from direct assay PubMed 17923684. Source: MGI signalosome Inferred from direct assay Ref.32. Source: UniProtKB vesicle membrane Inferred from direct assay PubMed 12147689. Source: MGI
Molecular_function	SH3 domain binding Inferred from sequence or structural similarity. Source: UniProtKB SH3/SH2 adaptor activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Blnk	O54737	4	EBI-1688,EBI-641814
Btk	P35991	4	EBI-1688,EBI-625119
Cblb	B9EKI5	3	EBI-1688,EBI-682463
Cd22	P35329	3	EBI-1688,EBI-300059
Dab2	P98078	4	EBI-1688,EBI-1391846
Errfi1	Q99JZ7	3	EBI-1688,EBI-643375
Gab1	Q9QYY0	5	EBI-1688,EBI-644784
Kif26a	Q52KG5	2	EBI-1688,EBI-2480646
Plcg1	Q62077	2	EBI-1688,EBI-300133
Rapgef1	Q91ZZ2	3	EBI-1688,EBI-644719
Sos1	Q62245	2	EBI-1688,EBI-1693
Sos2	Q02384	4	EBI-1688,EBI-395573
Uck2	Q99PM9	3	EBI-1688,EBI-644712

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 217

217

Growth factor receptor-bound protein 2

PRO_0000088199

Regions

Domain

1 – 58

58

SH3 1

Domain

60 – 152

93

SH2

Domain

156 – 215

60

SH3 2

Amino acid modifications

Modified residue

1

1

N-acetylmethionine By similarity

Modified residue

6

1

N6-acetyllysine By similarity

Modified residue

50

1

N6-acetyllysine By similarity

Modified residue

109

1

N6-acetyllysine By similarity

Modified residue

211

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

60 – 100

41

Missing in isoform 2.

VSP_001841

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

217

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Beta strand

13 – 16

4

Beta strand

24 – 26

3

Beta strand

34 – 41

8

Beta strand

44 – 49

6

Helix

50 – 52

3

Beta strand

53 – 56

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 97F4A4FE4B248DDF	FASTA	217	25,238
	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
	Isoform 2 (GRB3-3) [UniParc]. Checksum: 64323FA95FE940C5	FASTA	176	20,589
	10 20 30 40 50 60 MEAIAKYDFK ATADDELSFK RGDILKVLNE ECDQNWYKAE LNGKDGFIPK NYIEMKPHPF 70 80 90 100 110 120 GNDVQHFKVL RDGAGKYFLW VVKFNSLNEL VDYHRSTSVS RNQQIFLRDI EQMPQQPTYV 130 140 150 160 170 QALFDFDPQE DGELGFRRGD FIHVMDNSDP NWWKGACHGQ TGMFPRNYVT PVNRNV

References

	« Hide 'large scale' referencesShow '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, 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]	"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.
[32]	"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.
[33]	"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.

IPI

IPI00119058.
IPI00230539.

PIR

A54688.

RefSeq

NP_032189.1. NM_008163.3.

UniGene

Mm.439649.
Mm.472452.
Mm.490413.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GBQ	NMR	-	A	1-59	[»]
1GBR	NMR	-	A	1-59	[»]
2GBQ	NMR	-	A	1-59	[»]
3GBQ	NMR	-	A	1-59	[»]
4GBQ	NMR	-	A	1-59	[»]

ProteinModelPortal

Q60631.

SMR

Q60631. Positions 1-217.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-259N.

IntAct

Q60631. 43 interactions.

MINT

MINT-84889.

PTM databases

PhosphoSite

Q60631.

Proteomic databases

PaxDb

Q60631.

PRIDE

Q60631.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000021090; ENSMUSP00000021090; ENSMUSG00000059923.
ENSMUST00000106497; ENSMUSP00000102106; ENSMUSG00000059923.
ENSMUST00000106499; ENSMUSP00000102108; ENSMUSG00000059923.

GeneID

14784.

KEGG

mmu:14784.

Organism-specific databases

CTD

2885.

MGI

MGI:95805. Grb2.

Phylogenomic databases

eggNOG

NOG298780.

GeneTree

ENSGT00550000074482.

HOGENOM

HOG000251625.

HOVERGEN

HBG005404.

InParanoid

Q60631.

KO

K04364.

OMA

VETKFVQ.

OrthoDB

EOG4XSKQS.

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.

Gene expression databases

ArrayExpress

Q60631.

Bgee

Q60631.

CleanEx

MM_GRB2.

Genevestigator

Q60631.

GermOnline

ENSMUSG00000059923. Mus musculus.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR000108. p67phox.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]

PRINTS

PR00499. P67PHOX.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q60631.

ChEMBL

CHEMBL4830.

ChiTaRS

GRB2. mouse.

EvolutionaryTrace

Q60631.

NextBio

286907.

SOURCE

Search...

Entry information

Entry name

GRB2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 145 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program