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P62993 (GRB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Protein Ash
SH2/SH3 adapter GRB2
Gene names
Name:GRB2
Synonyms:ASH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.1 Ref.3 Ref.54

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. Ref.1 Ref.3 Ref.54

Subunit structure

Associates with activated Tyr-phosphorylated EGF receptor/EGFR and PDGF receptors via its SH2 domain. 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 NISCH, PTPNS1, REPS2 and the syntrophin SNTA1. Interacts with REPS1 and PIK3C2B via its SH3 domains By similarity. Interacts with HCV NS5A via its SH3 domains. Interacts with CBL and CBLB. Interacts with AJUBA and CLNK By similarity. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) By similarity. Interacts with SHB, INPP5D/SHIP1, SKAP1 and SKAP2. Forms a complex with MUC1 and SOS1, through interaction of the SH3 domains with SOS1 and the SH2 domain with phosphorylated MUC1. Interacts with PTPN11. Interacts with PRNP and THEMIS By similarity. Interacts with FLT1 (tyrosine phosphorylated) and KDR. Interacts with PDGFRA (tyrosine phosphorylated); the interaction may be indirect By similarity. Interacts with RALGPS1 and with HCST. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts with GAPT and PTPRE. Interacts (via SH2 domain) with KIF26A. Interacts (via SH3 2) with GAB2. Interacts with ADAM15. Interacts with THEMIS2. Interacts (via SH2 domain) with AXL and KIT (phosphorylated). Interacts with PTPRJ and BCR. Interacts with FLT4 (tyrosine phosphorylated). Interacts with EPHB1 and SHC1; activates the MAPK/ERK cascade to regulate cell migration. Interacts with PTPN23. Part of a complex including TNK2, GRB2 and one receptor tyrosine kinase (RTK) such as AXL, in which GRB2 promotes RTK recruitment by TNK2. Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Interacts with ERBB4. Interacts with NTRK1 (phosphorylated upon ligand-binding). Interacts with PTK2/FAK1 (tyrosine phosphorylated). Interacts with PTK2B/PYK2 (tyrosine phosphorylated). Isoform 1 interacts with SCIMP. Interacts with PLCG1, LAT and THEMIS upon TCR activation in thymocytes By similarity. Interacts with TESPA1 and DAB2. Interacts (via SH3 domains) with GAREM isoform 1 (via proline-rich domain and tyrosine phosphorylated); the interaction occurs upon EGF stimulation. Interacts with RAB13; may recruit RAB13 to the leading edge of migrating endothelial cells where it can activate RHOA. Interacts with ASAP3 (phosphorylated form). 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 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.46 Ref.49 Ref.50 Ref.51 Ref.53 Ref.54 Ref.55 Ref.56 Ref.59 Ref.60 Ref.62 Ref.63 Ref.64

Subcellular location

Nucleus. Cytoplasm. Endosome. Golgi apparatus By similarity Ref.60.

Domain

The SH3 domains mediate interaction with RALGPS1 and SHB.

Sequence similarities

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

Contains 1 SH2 domain.

Contains 2 SH3 domains.

Ontologies

Keywords
   Biological processHost-virus interaction
   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_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

Ras protein signal transduction

Traceable author statement PubMed 8253073. Source: UniProtKB

T cell costimulation

Traceable author statement. Source: Reactome

aging

Inferred from electronic annotation. Source: Ensembl

anatomical structure formation involved in morphogenesis

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

branching involved in labyrinthine layer morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell-cell signaling

Traceable author statement PubMed 8253073. Source: UniProtKB

cellular response to ionizing radiation

Inferred from mutant phenotype PubMed 20160708. Source: BHF-UCL

epidermal growth factor receptor signaling pathway

Traceable author statement Ref.1. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Inferred from physical interaction Ref.11. Source: UniProtKB

leukocyte migration

Traceable author statement. Source: Reactome

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

positive regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

positive regulation of reactive oxygen species metabolic process

Inferred from mutant phenotype PubMed 20160708. Source: BHF-UCL

positive regulation of signal transduction

Traceable author statement PubMed 8253073. Source: GOC

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

receptor internalization

Inferred from mutant phenotype PubMed 14985334. Source: BHF-UCL

regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

signal transduction in response to DNA damage

Inferred from mutant phenotype PubMed 20160708. Source: BHF-UCL

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCOP9 signalosome

Inferred from direct assay Ref.64. Source: UniProtKB

Golgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

Grb2-EGFR complex

Inferred from direct assay PubMed 20086093. Source: BHF-UCL

cytoplasm

Inferred from direct assay Ref.60. Source: UniProtKB

cytosol

Traceable author statement PubMed 14722116. Source: HGNC

endosome

Inferred from direct assay Ref.60. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

nucleus

Inferred from direct assay Ref.60. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

vesicle membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionSH3 domain binding

Inferred from direct assay Ref.56. Source: UniProtKB

SH3/SH2 adaptor activity

Traceable author statement PubMed 8253073. Source: UniProtKB

ephrin receptor binding

Inferred from physical interaction Ref.41. Source: UniProtKB

epidermal growth factor receptor binding

Inferred from physical interaction PubMed 12577067. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 12577067PubMed 22536782PubMed 22726438. Source: IntAct

insulin receptor substrate binding

Inferred from physical interaction Ref.11. Source: UniProtKB

neurotrophin TRKA receptor binding

Inferred from physical interaction Ref.43. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 20086093. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself5EBI-401755,EBI-401755
O929722EBI-401755,EBI-710506From a different organism.
P266623EBI-401755,EBI-9099462From a different organism.
P279583EBI-401755,EBI-706378From a different organism.
ABL2P426842EBI-401755,EBI-1102694
ADAM15Q134443EBI-401755,EBI-77818
AGERQ151092EBI-401755,EBI-1646426
ANK2Q014842EBI-401755,EBI-941975
ARHGEF5Q127744EBI-401755,EBI-602199
ASAP1Q9ULH17EBI-401755,EBI-346622
ASAP2O431503EBI-401755,EBI-310968
AXLP305303EBI-401755,EBI-2850927
BCRP112748EBI-401755,EBI-712838
BLNKQ8WV284EBI-401755,EBI-2623522
BRD4O608852EBI-401755,EBI-723869
CBLP226816EBI-401755,EBI-518228
CBLBQ131915EBI-401755,EBI-744027
CD2APQ9Y5K63EBI-401755,EBI-298152
DAB2P980822EBI-401755,EBI-1171238
Dab2P980784EBI-401755,EBI-1391846From a different organism.
DARSP148682EBI-401755,EBI-358730
DLGAP1O144903EBI-401755,EBI-1753207
DLGAP2Q9P1A62EBI-401755,EBI-1753397
DLGAP4Q9Y2H02EBI-401755,EBI-722139
DNM1Q051933EBI-401755,EBI-713135
DNM2P505704EBI-401755,EBI-346547
DOCK1Q141852EBI-401755,EBI-446740
EGFRP0053328EBI-401755,EBI-297353
EPHB1P547622EBI-401755,EBI-80252
ERBB2P046263EBI-401755,EBI-641062
ERRFI1Q9UJM38EBI-401755,EBI-2941912
FANCAO153602EBI-401755,EBI-81570
FGFR2P218025EBI-401755,EBI-1028658
FLNAP213332EBI-401755,EBI-350432
FLNBO753692EBI-401755,EBI-352089
FLNCQ143152EBI-401755,EBI-489954
GAB1Q134805EBI-401755,EBI-517684
GAB2Q9UQC214EBI-401755,EBI-975200
GAREMQ9H7063EBI-401755,EBI-3440103
Irs1P355705EBI-401755,EBI-520230From a different organism.
KHDRBS1Q076668EBI-401755,EBI-1364
KITP107214EBI-401755,EBI-1379503
KRT8P057873EBI-401755,EBI-297852
LATO4356112EBI-401755,EBI-1222766
LCP2Q130947EBI-401755,EBI-346946
LEPRP483573EBI-401755,EBI-518596
MAP2K5Q131632EBI-401755,EBI-307294
MAP4K1Q929188EBI-401755,EBI-881
MAP4K3Q8IVH82EBI-401755,EBI-1758170
MAP4K5Q9Y4K44EBI-401755,EBI-1279
MED28Q9H2043EBI-401755,EBI-514199
MYH9P355793EBI-401755,EBI-350338
NELFBQ8WX922EBI-401755,EBI-347721
PAK2Q131772EBI-401755,EBI-1045887
PIK3C2BO007502EBI-401755,EBI-641107
PIK3R1P279863EBI-401755,EBI-79464
PIK3R2O004594EBI-401755,EBI-346930
PLCG1P191742EBI-401755,EBI-79387
PLD2O149394EBI-401755,EBI-1053996
PPP3CAQ082093EBI-401755,EBI-352922
PRKAB1Q9Y4782EBI-401755,EBI-719769
Ptk2P341523EBI-401755,EBI-77070From a different organism.
PTPN1P180312EBI-401755,EBI-968788
PTPN11Q061246EBI-401755,EBI-297779
Ptpn11P352357EBI-401755,EBI-397236From a different organism.
PTPN22Q9Y2R22EBI-401755,EBI-1211241
PTPN23Q9H3S76EBI-401755,EBI-724478
PTPRAP184338EBI-401755,EBI-2609645
PTPRTO145222EBI-401755,EBI-728180
REPS2Q8NFH8-28EBI-401755,EBI-8029141
SF3B4Q154272EBI-401755,EBI-348469
SHANK2Q9UPX82EBI-401755,EBI-1570571
SHANK3Q9BYB02EBI-401755,EBI-1752330
SHC1P2935322EBI-401755,EBI-78835
SHC1P29353-13EBI-401755,EBI-8160716
SOS1Q0788922EBI-401755,EBI-297487
Sos1Q6224511EBI-401755,EBI-1693From a different organism.
SOS2Q078908EBI-401755,EBI-298181
SPRY2O435973EBI-401755,EBI-742487
STAMBPO956303EBI-401755,EBI-396676
SYNJ2O150562EBI-401755,EBI-310513
TNPO1Q929732EBI-401755,EBI-286693
TOM1L1O756742EBI-401755,EBI-712991
TPX2Q9ULW02EBI-401755,EBI-1037322
UGP2Q168512EBI-401755,EBI-743729
VAV1P154982EBI-401755,EBI-625518
VAV3Q9UKW45EBI-401755,EBI-297568
WASLO004013EBI-401755,EBI-957615
WIPF1O435163EBI-401755,EBI-346356
WIPF2Q8TF743EBI-401755,EBI-2850112

Alternative products

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

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P62993-1)

Also known as: Ash-L;

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: P62993-2)

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_0000088198

Regions

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

Amino acid modifications

Modified residue11N-acetylmethionine Ref.58 Ref.65
Modified residue61N6-acetyllysine Ref.58
Modified residue501N6-acetyllysine Ref.58
Modified residue1091N6-acetyllysine Ref.58
Modified residue2111Phosphothreonine Ref.52

Natural variations

Alternative sequence60 – 10041Missing in isoform 2.
VSP_001839

Experimental info

Mutagenesis491P → L: Ineffective in DNA synthesis. Abolishes interaction with SHB; when associated with L-206. Ref.1 Ref.24
Mutagenesis2031G → R: Ineffective in DNA synthesis. Ref.1
Mutagenesis2061P → L: Abolishes interaction with SHB; when associated with L-49. Ref.24

Secondary structure

.................................................... 217
Helix Strand Turn

Details...

Sequences

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

Last modified August 31, 2004. Version 1.
Checksum: 83A4B0BA1B248DC4

FASTA21725,206
        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 IEQVPQQPTY VQALFDFDPQ EDGELGFRRG 

       190        200        210 
DFIHVMDNSD PNWWKGACHG QTGMFPRNYV TPVNRNV 

« Hide

Isoform 2 (GRB3-3) [UniParc] [UniParc].

Checksum: 70622BED0FE940DE
Show »

FASTA17620,557

References

« Hide 'large scale' references
[1]"The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling."
Lowenstein E.J., Daly R.J., Batzer A.G., Li W., Margolis B., Lammers R., Ullrich A., Skolnik E.Y., Bar-Sagi D., Schlessinger J.
Cell 70:431-442(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF PRO-49 AND GLY-203.
Tissue: Brain.
[2]"Cloning of ASH, a ubiquitous protein composed of one Src homology region (SH) 2 and two SH3 domains, from human and rat cDNA libraries."
Matuoka K., Yamakawa A., Shibata M., Takenawa T.
Proc. Natl. Acad. Sci. U.S.A. 89:9015-9019(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal lung.
[3]"Cloning of a Grb2 isoform with apoptotic properties."
Fath I., Schweighoffer F., Rey I., Multon M.-C., Boiziau J., Duchesne M., Tocque B.
Science 264:971-974(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
Tissue: Placenta.
[4]"The gene structure of the human growth factor bound protein GRB2."
Bochmann H., Gehrisch S., Jaross W.
Genomics 56:203-207(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Epidermis.
[5]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lymph.
[9]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 11-20; 27-38; 77-109; 118-136; 143-149 AND 179-195, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]"Mutation of Tyr697, a GRB2-binding site, and Tyr721, a PI 3-kinase binding site, abrogates signal transduction by the murine CSF-1 receptor expressed in Rat-2 fibroblasts."
van der Geer P., Hunter T.
EMBO J. 12:5161-5172(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSF1R.
[11]"Insulin stimulates association of insulin receptor substrate-1 with the protein abundant Src homology/growth factor receptor-bound protein 2."
Tobe K., Matuoka K., Tamemoto H., Ueki K., Kaburagi Y., Asai S., Noguchi T., Matsuda M., Tanaka S., Hattori S., Fukui Y., Akanuma Y., Yazaki Y., Takenawa T., Kadowaki T.
J. Biol. Chem. 268:11167-11171(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IRS1.
[12]"The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signalling."
Skolnik E.Y., Lee C.-H., Batzer A.G., Vicentini L.M., Zhou M., Daly R.J., Myers M.J. Jr., Backer J.M., Ullrich A., White M.F., Schlessinger J.
EMBO J. 12:1929-1936(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IRS1 AND SHC.
[13]"Association of the DF3/MUC1 breast cancer antigen with Grb2 and the Sos/Ras exchange protein."
Pandey P., Kharbanda S., Kufe D.
Cancer Res. 55:4000-4003(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH MUC1 AND SOS1, INTERACTION WITH MUC1 AND SOS1.
[14]"Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2."
Kavanaugh W.M., Pot D.A., Chin S.M., Deuter-Reinhard M., Jefferson A.B., Norris F.A., Masiarz F.R., Cousens L.S., Majerus P.W., Williams L.T.
Curr. Biol. 6:438-445(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INPP5D.
[15]"Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells."
Stein E., Cerretti D.P., Daniel T.O.
J. Biol. Chem. 271:23588-23593(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHB1.
[16]"Purification and molecular cloning of SH2- and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl."
Odai H., Sasaki K., Iwamatsu A., Nakamoto T., Ueno H., Yamagata T., Mitani K., Yazaki Y., Hirai H.
Blood 89:2745-2756(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INPP5D.
[17]"Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src."
Schlaepfer D.D., Hunter T.
J. Biol. Chem. 272:13189-13195(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK2/FAK1.
[18]"A family of proteins that inhibit signalling through tyrosine kinase receptors."
Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J., Ullrich A.
Nature 386:181-186(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPNS1.
[19]"Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site."
Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R., Ullrich A., Bartram C.R., Janssen J.W.
Oncogene 14:2619-2631(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXL.
[20]"Cloning and characterization of APS, an adaptor molecule containing PH and SH2 domains that is tyrosine phosphorylated upon B-cell receptor stimulation."
Yokouchi M., Suzuki R., Masuhara M., Komiya S., Inoue A., Yoshimura A.
Oncogene 15:7-15(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH2B2.
[21]"LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation."
Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.
Cell 92:83-92(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAT.
[22]"Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral."
Ikeda M., Ishida O., Hinoi T., Kishida S., Kikuchi A.
J. Biol. Chem. 273:814-821(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH REPS2.
[23]"Characterization of insulin receptor substrate 4 in human embryonic kidney 293 cells."
Fantin V.R., Sparling J.D., Slot J.W., Keller S.R., Lienhard G.E., Lavan B.E.
J. Biol. Chem. 273:10726-10732(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IRS4.
[24]"Stimulation through the T cell receptor leads to interactions between SHB and several signaling proteins."
Welsh M., Songyang Z., Frantz J.D., Trueb T., Reedquist K.A., Karlsson T., Miyazaki M., Cantley L.C., Band H., Shoelson S.E.
Oncogene 16:891-901(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHB, MUTAGENESIS OF PRO-49 AND PRO-206.
[25]"Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck."
Braverman L.E., Quilliam L.A.
J. Biol. Chem. 274:5542-5549(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EGFR.
[26]"Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation."
Elly C., Witte S., Zhang Z., Rosnet O., Lipkowitz S., Altman A., Liu Y.-C.
Oncogene 18:1147-1156(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBLB.
[27]"cbl-b inhibits epidermal growth factor receptor signaling."
Ettenberg S.A., Keane M.M., Nau M.M., Frankel M., Wang L.-M., Pierce J.H., Lipkowitz S.
Oncogene 18:1855-1866(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBL AND CBLB.
[28]"NS5A, a nonstructural protein of hepatitis C virus, binds growth factor receptor-bound protein 2 adaptor protein in a Src homology 3 domain/ligand-dependent manner and perturbs mitogenic signaling."
Tan S.-L., Nakao H., He Y., Vijaysri S., Neddermann P., Jacobs B.L., Mayer B.J., Katze M.G.
Proc. Natl. Acad. Sci. U.S.A. 96:5533-5538(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV NS5A.
[29]"Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral."
Rebhun J.F., Chen H., Quilliam L.A.
J. Biol. Chem. 275:13406-13410(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RALGPS1.
[30]"Ligand discrimination in signaling through an ErbB4 receptor homodimer."
Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C., Carraway K.L. III
J. Biol. Chem. 275:19803-19807(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB4.
[31]"Interaction of linker for activation of T cells with multiple adapter proteins in platelets activated by the glycoprotein VI-selective ligand, convulxin."
Asazuma N., Wilde J.I., Berlanga O., Leduc M., Leo A., Schweighoffer E., Tybulewicz V., Bon C., Liu S.K., McGlade C.J., Schraven B., Watson S.P.
J. Biol. Chem. 275:33427-33434(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP2.
[32]"Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control."
Gil-Henn H., Volohonsky G., Toledano-Katchalski H., Gandre S., Elson A.
Oncogene 19:4375-4384(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPRE.
[33]"Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein)."
Pfrepper K.-I., Marie-Cardine A., Simeoni L., Kuramitsu Y., Leo A., Spicka J., Hilgert I., Scherer J., Schraven B.
Eur. J. Immunol. 31:1825-1836(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIT1.
[34]"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK."
Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M., Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.
J. Biol. Chem. 276:42389-42400(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
[35]"Recruitment of the class II phosphoinositide 3-kinase C2beta to the epidermal growth factor receptor: role of Grb2."
Wheeler M., Domin J.
Mol. Cell. Biol. 21:6660-6667(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND EGFR, INTERACTION WITH PIK3C2B.
[36]"Insulin receptor substrate 4 associates with the protein IRAS."
Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.
J. Biol. Chem. 277:19439-19447(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NISCH.
[37]"SKAP55 recruits to lipid rafts and positively mediates the MAPK pathway upon T cell receptor activation."
Wu L., Yu Z., Shen S.-H.
J. Biol. Chem. 277:40420-40427(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP1.
[38]"Molecular cloning of a novel gene encoding a membrane-associated adaptor protein (LAX) in lymphocyte signaling."
Zhu M., Janssen E., Leung K., Zhang W.
J. Biol. Chem. 277:46151-46158(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAX1.
[39]"Non-T cell activation linker (NTAL): a transmembrane adaptor protein involved in immunoreceptor signaling."
Brdicka T., Imrich M., Angelisova P., Brdickova N., Horvath O., Spicka J., Hilgert I., Luskova P., Draber P., Novak P., Engels N., Wienands J., Simeoni L., Oesterreicher J., Aguado E., Malissen M., Schraven B., Horejsi V.
J. Exp. Med. 196:1617-1626(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAT2.
[40]"Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1."
Palka H.L., Park M., Tonks N.K.
J. Biol. Chem. 278:5728-5735(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPRJ.
[41]"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.
[42]"LAB: a new membrane-associated adaptor molecule in B cell activation."
Janssen E., Zhu M., Zhang W., Koonpaew S., Zhang W.
Nat. Immunol. 4:117-123(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAT2.
[43]"TrkA alternative splicing: a regulated tumor-promoting switch in human neuroblastoma."
Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A., Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A., Mackay A.R.
Cancer Cell 6:347-360(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NTRK1.
[44]"Activation of vascular endothelial growth factor receptor-3 and its downstream signaling promote cell survival under oxidative stress."
Wang J.F., Zhang X., Groopman J.E.
J. Biol. Chem. 279:27088-27097(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLT4.
[45]"Signal transduction via the stem cell factor receptor/c-Kit."
Ronnstrand L.
Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON INTERACTION WITH KIT AND ROLE IN KIT SIGNALING.
[46]"The c-Fes tyrosine kinase cooperates with the breakpoint cluster region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-dependent manner."
Laurent C.E., Smithgall T.E.
Exp. Cell Res. 299:188-198(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCR.
[47]"Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."
Roskoski R. Jr.
Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[48]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[49]"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.
[50]"Identification of a new transmembrane adaptor protein that constitutively binds Grb2 in B cells."
Liu Y., Zhang W.
J. Leukoc. Biol. 84:842-851(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAPT.
[51]"Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma."
Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M., Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C., Edwards D.R.
Mol. Cancer Res. 6:383-394(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAM15.
[52]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[53]"An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis."
Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F., Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.
Curr. Biol. 19:1788-1798(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EGFR.
[54]"Cytoplasmic ACK1 interaction with multiple receptor tyrosine kinases is mediated by Grb2: an analysis of ACK1 effects on Axl signaling."
Pao-Chun L., Chan P.M., Chan W., Manser E.
J. Biol. Chem. 284:34954-34963(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXL; LTK; PDGFRL AND TNK2, FUNCTION.
[55]"KIF26A is an unconventional kinesin and regulates GDNF-Ret signaling in enteric neuronal development."
Zhou R., Niwa S., Homma N., Takei Y., Hirokawa N.
Cell 139:802-813(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIF26A.
[56]"GAREM, a novel adaptor protein for growth factor receptor-bound protein 2, contributes to cellular transformation through the activation of extracellular signal-regulated kinase signaling."
Tashiro K., Tsunematsu T., Okubo H., Ohta T., Sano E., Yamauchi E., Taniguchi H., Konishi H.
J. Biol. Chem. 284:20206-20214(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAREM.
[57]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[58]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-6; LYS-50 AND LYS-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[59]"Recruitment of Pyk2 to SHPS-1 signaling complex is required for IGF-I-dependent mitogenic signaling in vascular smooth muscle cells."
Shen X., Xi G., Radhakrishnan Y., Clemmons D.R.
Cell. Mol. Life Sci. 67:3893-3903(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK2B/PYK2.
[60]"Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL."
Tanase C.A.
PLoS ONE 5:E14339-E14339(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPN23, SUBCELLULAR LOCATION.
[61]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[62]"ACAP4 protein cooperates with Grb2 protein to orchestrate epidermal growth factor-stimulated integrin beta1 recycling in cell migration."
Yu X., Wang F., Liu H., Adams G., Aikhionbare F., Liu D., Cao X., Fan L., Hu G., Chen Y., Frost A., Partridge E., Ding X., Yao X.
J. Biol. Chem. 286:43735-43747(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASAP3.
[63]"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.
[64]"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 TESPA1.
Tissue: Thymocyte.
[65]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[66]"Nuclear magnetic resonance solution structure of the growth factor receptor-bound protein 2 Src homology 2 domain."
Thornton K.H., Mueller W.T., McConnell P., Zhu G., Saltiel A.R., Thanabal V.
Biochemistry 35:11852-11864(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 58-164.
[67]"The three-dimensional solution structure of the Src homology domain-2 of the growth factor receptor-bound protein-2."
Senior M.M., Frederick A.F., Black S., Murgolo N.J., Perkins L.M., Wilson O., Snow M.E., Wang Y.-S.
J. Biomol. NMR 11:153-164(1998)
Cited for: STRUCTURE BY NMR OF 52-163.
[68]"Solution structure and ligand-binding site of the carboxy-terminal SH3 domain of GRB2."
Kohda D., Terasawa H., Ichikawa S., Ogura K., Hatanaka H., Mandiyan V., Ullrich A., Schlessinger J., Inagaki F.
Structure 2:1029-1040(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 157-215.
[69]"Crystal structure of the mammalian Grb2 adaptor."
Maignan S., Guilloteau J.-P., Fromage N., Arnoux B., Becquart J., Ducruix A.
Science 268:291-293(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
[70]"Structural basis for the high affinity of amino-aromatic SH2 phosphopeptide ligands."
Rahuel J., Garcia-Echeverria C., Furet P., Strauss A., Caravatti G., Fretz H., Schoepfer J., Gay B.
J. Mol. Biol. 279:1013-1022(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 56-153.
[71]"Structural and conformational requirements for high-affinity binding to the SH2 domain of Grb2(1)."
Ettmayer P., France D., Gounarides J., Jarosinski M., Martin M.-S., Rondeau J.-M., Sabio M., Topiol S., Weidmann B., Zurini M., Bair K.W.
J. Med. Chem. 42:971-980(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 47-163.
[72]"Structure-based design, synthesis, and X-ray crystallography of a high- affinity antagonist of the Grb2-SH2 domain containing an asparagine mimetic."
Furet P., Garcia-Echeverria C., Gay B., Schoepfer J., Zeller M., Rahuel J.
J. Med. Chem. 42:2358-2363(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 57-152.
[73]"Dimer formation through domain swapping in the crystal structure of the Grb2-SH2-Ac-pYVNV complex."
Schiering N., Casale E., Caccia P., Giordano P., Battistini C.
Biochemistry 39:13376-13382(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 52-160 IN COMPLEX WITH MET.
[74]"Crystal structures of the SH2 domain of Grb2: highlight on the binding of a new high-affinity inhibitor."
Nioche P., Liu W.-Q., Broutin I., Charbonnier F., Latreille M.-T., Vidal M., Roques B., Garbay C., Ducruix A.
J. Mol. Biol. 315:1167-1177(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 56-151 IN COMPLEX WITH THE TYROSINE PHOSPHORYLATED PEPTIDE TYR-VAL-ASN-VAL-GLN-ASN AND IN COMPLEX WITH A PEPTIDE INHIBITOR.
[75]"Distinct binding modes of two epitopes in Gab2 that interact with the SH3C domain of Grb2."
Harkiolaki M., Tsirka T., Lewitzky M., Simister P.C., Joshi D., Bird L.E., Jones E.Y., O'Reilly N., Feller S.M.
Structure 17:809-822(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 158-211 IN COMPLEX WITH GAB2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96995 mRNA. Translation: AAA58448.1.
X62852 mRNA. Translation: CAA44664.1.
L29511 mRNA. Translation: AAC37549.1.
AF063618 expand/collapse EMBL AC list , AF063614, AF063615, AF063616, AF063617 Genomic DNA. Translation: AAC72075.1.
AF498925 mRNA. Translation: AAM21073.1.
CR541942 mRNA. Translation: CAG46740.1.
AC011933 Genomic DNA. No translation available.
BC000631 mRNA. Translation: AAH00631.1.
PIRA43321.
RefSeqNP_002077.1. NM_002086.4.
NP_987102.1. NM_203506.2.
UniGeneHs.444356.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZENMR-A1-56[»]
1BM2X-ray2.10A49-163[»]
1BMBX-ray1.80A49-168[»]
1CJ1X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L57-152[»]
1FHSNMR-A53-163[»]
1FYRX-ray2.40A/B/C/D50-161[»]
1GCQX-ray1.68A/B159-217[»]
1GFCNMR-A159-215[»]
1GFDNMR-A159-215[»]
1GHUNMR-A60-158[»]
1GRIX-ray3.10A/B1-217[»]
1IO6NMR-A159-215[»]
1JYQX-ray2.00A/B60-151[»]
1JYRX-ray1.55A60-151[»]
1JYUX-ray2.75A60-151[»]
1QG1NMR-E58-159[»]
1TZEX-ray2.10E55-152[»]
1X0NNMR-A58-159[»]
1ZFPX-ray1.80E56-153[»]
2AOAX-ray1.99A/B55-153[»]
2AOBX-ray1.80A/B/C/D55-153[»]
2H46X-ray1.90E53-162[»]
2H5KX-ray3.25A/B53-162[»]
2HUWX-ray1.90A/B53-162[»]
2VVKX-ray1.60A161-214[»]
2VWFX-ray1.58A159-214[»]
2W0ZX-ray1.70A159-214[»]
3C7IX-ray1.70A53-162[»]
3IMDX-ray2.00A/B53-163[»]
3IMJX-ray2.02A/B53-163[»]
3IN7X-ray2.00A/C53-163[»]
3IN8X-ray1.70A53-163[»]
3KFJX-ray2.02A53-163[»]
3MXCX-ray2.00A55-152[»]
3MXYX-ray2.30A55-152[»]
3N7YX-ray2.02A/B/C55-152[»]
3N84X-ray2.00A/B/C/D/E/F53-163[»]
3N8MX-ray2.00A53-163[»]
3OV1X-ray1.60A53-163[»]
3OVEX-ray1.82A53-163[»]
3S8LX-ray1.71A53-163[»]
3S8NX-ray1.71A53-163[»]
3S8OX-ray1.85A53-163[»]
3WA4X-ray1.35A60-152[»]
DisProtDP00210.
ProteinModelPortalP62993.
SMRP62993. Positions 1-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109142. 456 interactions.
DIPDIP-29229N.
IntActP62993. 694 interactions.
MINTMINT-91952.
STRING9606.ENSP00000339007.

Chemistry

BindingDBP62993.
ChEMBLCHEMBL3663.
DrugBankDB00061. Pegademase bovine.

PTM databases

PhosphoSiteP62993.

Polymorphism databases

DMDM51702266.

2D gel databases

OGPP62993.
SWISS-2DPAGEP62993.

Proteomic databases

PaxDbP62993.
PRIDEP62993.

Protocols and materials databases

DNASU2885.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316615; ENSP00000317360; ENSG00000177885. [P62993-2]
ENST00000316804; ENSP00000339007; ENSG00000177885. [P62993-1]
ENST00000392562; ENSP00000376345; ENSG00000177885. [P62993-1]
ENST00000392563; ENSP00000376346; ENSG00000177885. [P62993-2]
ENST00000392564; ENSP00000376347; ENSG00000177885. [P62993-1]
GeneID2885.
KEGGhsa:2885.
UCSCuc002jnx.4. human.
uc002jny.4. human. [P62993-2]

Organism-specific databases

CTD2885.
GeneCardsGC17M073313.
HGNCHGNC:4566. GRB2.
HPACAB002589.
MIM108355. gene.
neXtProtNX_P62993.
PharmGKBPA28962.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298780.
HOGENOMHOG000251625.
HOVERGENHBG005404.
InParanoidP62993.
KOK04364.
OMAVETKFVQ.
OrthoDBEOG75F4F6.
PhylomeDBP62993.
TreeFamTF354288.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP62993.

Gene expression databases

ArrayExpressP62993.
BgeeP62993.
CleanExHS_GRB2.
GenevestigatorP62993.

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. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEPS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGRB2. human.
EvolutionaryTraceP62993.
GeneWikiGRB2.
GenomeRNAi2885.
NextBio11389.
PROP62993.
SOURCESearch...

Entry information

Entry nameGRB2_HUMAN
AccessionPrimary (citable) accession number: P62993
Secondary accession number(s): P29354 expand/collapse secondary AC list , Q14450, Q63057, Q63059
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM