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Q14451 (GRB7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Growth factor receptor-bound protein 7
Alternative name(s):
B47
Epidermal growth factor receptor GRB-7
GRB7 adapter protein
Gene names
Name:GRB7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length532 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein that interacts with the cytoplasmic domain of numerous receptor kinases and modulates down-stream signaling. Promotes activation of down-stream protein kinases, including STAT3, AKT1, MAPK1 and/or MAPK3. Promotes activation of HRAS. Plays a role in signal transduction in response to EGF. Plays a role in the regulation of cell proliferation and cell migration. Plays a role in the assembly and stability of RNA stress granules. Binds to the 5'UTR of target mRNA molecules and represses translation of target mRNA species, when not phosphorylated. Phosphorylation impairs RNA binding and promotes stress granule disassembly during recovery after cellular stress By similarity. Ref.12 Ref.14 Ref.15 Ref.22

Subunit structure

Homodimer. Interacts (via SH2 domain) with EGFR, ERBB2, ERBB3 (when phosphorylated), ERBB4 (when phosphorylated), EPHB1, INSR, FGFR1, PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Interacts with SHC1. Interacts with RND1. Interacts (when tyrosine phosphorylated) with FHL2 and HAX1 By similarity. Interacts (via SH2 domain) with RET and PTK2/FAK1. Interacts (when not phosphorylated) with ELAVL1. In stressed cells, but not in normal cells, part of a complex that contains at least GRB7, PTK2/FAK1, STAU1, ELAVL1 and TIA1. Interacts (via SH2 domain) with KIT (phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) By similarity. Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26

Subcellular location

Cytoplasm. Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic granule By similarity. Cell projection. Note: Predominantly cytoplasmic. Detected in stress granules, where mRNA is stored under stress conditions By similarity. Ref.12 Ref.14 Ref.21

Domain

The PH domain mediates interaction with membranes containing phosphoinositides. Ref.14

Post-translational modification

Phosphorylated on serine and threonine residues in response to heregulin. Phosphorylated on tyrosine residues by TEK/TIE2. Phosphorylated on tyrosine residues in response to NTN1 signaling. Phosphorylation promotes stress granule disassembly during recovery after cellular stress By similarity. Phosphorylated on tyrosine residues by PTK2/FAK1, and possibly also other kinases. Phosphorylation is enhanced by activation of receptor kinases. Tyrosine phosphorylation is essential for activation of down-stream protein kinases. Ref.10 Ref.12 Ref.15 Ref.20 Ref.21 Ref.22 Ref.23

Sequence similarities

Belongs to the GRB7/10/14 family.

Contains 1 PH domain.

Contains 1 Ras-associating domain.

Contains 1 SH2 domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   DomainSH2 domain
   LigandLipid-binding
RNA-binding
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement Ref.2. Source: ProtInc

leukocyte migration

Traceable author statement. Source: Reactome

negative regulation of translation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay Ref.12Ref.14. Source: UniProtKB

positive regulation of signal transduction

Traceable author statement Ref.2. Source: GOC

stress granule assembly

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic stress granule

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay Ref.12Ref.14. Source: UniProtKB

focal adhesion

Inferred from direct assay Ref.12Ref.14. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

SH3/SH2 adaptor activity

Traceable author statement Ref.2. Source: ProtInc

identical protein binding

Inferred from physical interaction Ref.18. Source: IntAct

phosphatidylinositol binding

Inferred from direct assay Ref.14. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10377264Ref.11PubMed 12061724Ref.15Ref.24PubMed 15806159PubMed 16273093Ref.23PubMed 24189400PubMed 24728074PubMed 8940081PubMed 9079677Ref.10. Source: IntAct

protein kinase binding

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: At least 2 isoforms are produced.
Isoform 1 (identifier: Q14451-1)

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: Q14451-2)

Also known as: Grb7V;

The sequence of this isoform differs from the canonical sequence as follows:
     425-447: IHRTQLWFHGRISREESQRLIGQ → CSWSGRVSGTPRALSSLCATCRK
     448-532: Missing.
Isoform 3 (identifier: Q14451-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGKWRPGQGHTTGSVKPLSCSDAM
Isoform 4 (identifier: Q14451-4)

The sequence of this isoform differs from the canonical sequence as follows:
     48-81: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 532532Growth factor receptor-bound protein 7
PRO_0000150344

Regions

Domain100 – 18687Ras-associating
Domain229 – 338110PH
Domain431 – 52797SH2

Sites

Site2391Important for lipid binding and for stimulation of cell migration
Site5111Important for dimerization and for HRAS activation

Amino acid modifications

Modified residue1881Phosphotyrosine; by FAK1 Ref.20 Ref.22
Modified residue3381Phosphotyrosine; by FAK1 Ref.20 Ref.22
Modified residue3611Phosphoserine Ref.19

Natural variations

Alternative sequence11M → MGKWRPGQGHTTGSVKPLSC SDAM in isoform 3.
VSP_041665
Alternative sequence48 – 8134Missing in isoform 4.
VSP_041666
Alternative sequence425 – 44723IHRTQ…RLIGQ → CSWSGRVSGTPRALSSLCAT CRK in isoform 2.
VSP_035500
Alternative sequence448 – 53285Missing in isoform 2.
VSP_035501

Experimental info

Mutagenesis1881Y → F: Abolishes Ras activity increase and ERK1/2 phosphorylation. Ref.22
Mutagenesis2391R → L: Abolishes phosphoinositide binding. Ref.14
Mutagenesis2591Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. Ref.21 Ref.23
Mutagenesis2601Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. Ref.21 Ref.23
Mutagenesis2841Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. Ref.21 Ref.23
Mutagenesis3381Y → F: Abolishes Ras activity increase and ERK1/2 phosphorylation. Ref.22
Mutagenesis4581R → L: Impairs phosphotyrosine binding by SH2 domain.
Mutagenesis4801Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. Ref.21 Ref.23
Mutagenesis4921Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. Ref.21 Ref.23
Mutagenesis5111F → R: Abolishes dimerization. Abolishes activation of HRAS. Ref.18
Sequence conflict181C → W in BAA07827. Ref.1
Sequence conflict181C → W in BAA29059. Ref.2
Sequence conflict181C → W in BAA29060. Ref.2
Sequence conflict181C → W in AAG25938. Ref.3
Sequence conflict1181V → A in BAG36998. Ref.5
Sequence conflict1201A → T in BAG54211. Ref.5
Sequence conflict1471E → G in BAG51372. Ref.5
Sequence conflict1641V → L in BAG36998. Ref.5
Sequence conflict5101E → D in BAG36998. Ref.5
Isoform 3:
Sequence conflict201C → R in BAG54211. Ref.5

Secondary structure

.............................................. 532
Helix Strand Turn

Details...

Sequences

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

Last modified October 17, 2006. Version 2.
Checksum: A6867C20AFD46F74

FASTA53259,681
        10         20         30         40         50         60 
MELDLSPPHL SSSPEDLCPA PGTPPGTPRP PDTPLPEEVK RSQPLLIPTT GRKLREEERR 

        70         80         90        100        110        120 
ATSLPSIPNP FPELCSPPSQ SPILGGPSSA RGLLPRDASR PHVVKVYSED GACRSVEVAA 

       130        140        150        160        170        180 
GATARHVCEM LVQRAHALSD ETWGLVECHP HLALERGLED HESVVEVQAA WPVGGDSRFV 

       190        200        210        220        230        240 
FRKNFAKYEL FKSSPHSLFP EKMVSSCLDA HTGISHEDLI QNFLNAGSFP EIQGFLQLRG 

       250        260        270        280        290        300 
SGRKLWKRFF CFLRRSGLYY STKGTSKDPR HLQYVADVNE SNVYVVTQGR KLYGMPTDFG 

       310        320        330        340        350        360 
FCVKPNKLRN GHKGLRIFCS EDEQSRTCWL AAFRLFKYGV QLYKNYQQAQ SRHLHPSCLG 

       370        380        390        400        410        420 
SPPLRSASDN TLVAMDFSGH AGRVIENPRE ALSVALEEAQ AWRKKTNHRL SLPMPASGTS 

       430        440        450        460        470        480 
LSAAIHRTQL WFHGRISREE SQRLIGQQGL VDGLFLVRES QRNPQGFVLS LCHLQKVKHY 

       490        500        510        520        530 
LILPSEEEGR LYFSMDDGQT RFTDLLQLVE FHQLNRGILP CLLRHCCTRV AL 

« Hide

Isoform 2 (Grb7V) [UniParc].

Checksum: 2406BFDCBEBB1E49
Show »

FASTA44749,423
Isoform 3 [UniParc].

Checksum: 90E4D15BCBF428A1
Show »

FASTA55562,064
Isoform 4 [UniParc].

Checksum: E18D088B19E632C6
Show »

FASTA49855,920

References

« Hide 'large scale' references
[1]"Molecular cloning of human GRB-7 co-amplified with CAB1 and c-ERBB-2 in primary gastric cancer."
Kishi T., Sasaki H., Akiyama N., Ishizuka T., Sakamoto H., Aizawa S., Sugimura T., Terada M.
Biochem. Biophys. Res. Commun. 232:5-9(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Esophageal carcinoma.
[2]"A novel variant of human Grb7 is associated with invasive esophageal carcinoma."
Tanaka S., Mori M., Akiyoshi T., Tanaka Y., Mafune K., Wands J.R., Sugimachi K.
J. Clin. Invest. 102:821-827(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"Genomic organization and amplification of the human GRB7 gene."
Whittock N.V., Eady R.A.J., McGrath J.A.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
Tissue: Ovary, Prostate and Thalamus.
[6]"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].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: Lung.
[9]"Coexpression of Grb7 with epidermal growth factor receptor or Her2/erbB2 in human advanced esophageal carcinoma."
Tanaka S., Mori M., Akiyoshi T., Tanaka Y., Mafune K., Wands J.R., Sugimachi K.
Cancer Res. 57:28-31(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 130-343.
[10]"Analysis of Grb7 recruitment by heregulin-activated erbB receptors reveals a novel target selectivity for erbB3."
Fiddes R.J., Campbell D.H., Janes P.W., Sivertsen S.P., Sasaki H., Wallasch C., Daly R.J.
J. Biol. Chem. 273:7717-7724(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB3 AND ERBB4, SERINE AND THREONINE PHOSPHORYLATION.
[11]"Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family."
Vayssiere B., Zalcman G., Mahe Y., Mirey G., Ligensa T., Weidner K.M., Chardin P., Camonis J.
FEBS Lett. 467:91-96(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RND1.
[12]"Role of Grb7 targeting to focal contacts and its phosphorylation by focal adhesion kinase in regulation of cell migration."
Han D.C., Shen T.L., Guan J.L.
J. Biol. Chem. 275:28911-28917(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[13]"Evidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2."
Kasus-Jacobi A., Bereziat V., Perdereau D., Girard J., Burnol A.F.
Oncogene 19:2052-2059(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INSR.
[14]"Association of Grb7 with phosphoinositides and its role in the regulation of cell migration."
Shen T.L., Han D.C., Guan J.L.
J. Biol. Chem. 277:29069-29077(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2/FAK1, MUTAGENESIS OF ARG-239, DOMAIN.
[15]"EphB1 associates with Grb7 and regulates cell migration."
Han D.C., Shen T.L., Miao H., Wang B., Guan J.L.
J. Biol. Chem. 277:45655-45661(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH EPHB1.
[16]"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.
[17]"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.
[18]"Grb7-SH2 domain dimerisation is affected by a single point mutation."
Porter C.J., Wilce M.C., Mackay J.P., Leedman P., Wilce J.A.
Eur. Biophys. J. 34:454-460(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF PHE-511.
[19]"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 SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Tyrosine phosphorylation of growth factor receptor-bound protein-7 by focal adhesion kinase in the regulation of cell migration, proliferation, and tumorigenesis."
Chu P.Y., Huang L.Y., Hsu C.H., Liang C.C., Guan J.L., Hung T.H., Shen T.L.
J. Biol. Chem. 284:20215-20226(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-188 AND TYR-338, INTERACTION WITH PTK2/FAK1.
[21]"The cell migration protein Grb7 associates with transcriptional regulator FHL2 in a Grb7 phosphorylation-dependent manner."
Siamakpour-Reihani S., Argiros H.J., Wilmeth L.J., Haas L.L., Peterson T.A., Johnson D.L., Shuster C.B., Lyons B.A.
J. Mol. Recognit. 22:9-17(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FHL2, STRUCTURE BY NMR, MUTAGENESIS OF TYR-259; TYR-260; TYR-284; TYR-480 AND TYR-492, SUBCELLULAR LOCATION, TYROSINE PHOSPHORYLATION.
[22]"EGF-induced Grb7 recruits and promotes Ras activity essential for the tumorigenicity of Sk-Br3 breast cancer cells."
Chu P.Y., Li T.K., Ding S.T., Lai I.R., Shen T.L.
J. Biol. Chem. 285:29279-29285(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, PHOSPHORYLATION AT TYR-188 AND TYR-338, MUTAGENESIS OF TYR-188 AND TYR-338.
[23]"Grb7 binds to Hax-1 and undergoes an intramolecular domain association that offers a model for Grb7 regulation."
Siamakpour-Reihani S., Peterson T.A., Bradford A.M., Argiros H.J., Haas L.L., Lor S.N., Haulsee Z.M., Spuches A.M., Johnson D.L., Rohrschneider L.R., Shuster C.B., Lyons B.A.
J. Mol. Recognit. 24:314-321(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HAX1, MUTAGENESIS OF TYR-259; TYR-260; TYR-284; TYR-480 AND TYR-492, CIRCULAR DICHROISM, TYROSINE PHOSPHORYLATION.
[24]"Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2."
Ivancic M., Daly R.J., Lyons B.A.
J. Biomol. NMR 27:205-219(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 415-532 IN COMPLEX WITH ERBB2, INTERACTION WITH ERBB2.
[25]"Solution structure of the RA domain of human GRB7 protein."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 100-186.
[26]"Grb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferation."
Porter C.J., Matthews J.M., Mackay J.P., Pursglove S.E., Schmidberger J.W., Leedman P.J., Pero S.C., Krag D.N., Wilce M.C., Wilce J.A.
BMC Struct. Biol. 7:58-58(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 415-532, INTERACTION WITH THE SYNTHETIC INHIBITOR G7-18NATE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D43772 mRNA. Translation: BAA07827.1.
AB008789 mRNA. Translation: BAA29059.1.
AB008790 mRNA. Translation: BAA29060.1.
AF274875 Genomic DNA. Translation: AAG25938.1.
BT006686 mRNA. Translation: AAP35332.1.
AK222849 mRNA. Translation: BAD96569.1.
AK222870 mRNA. Translation: BAD96590.1.
AK290115 mRNA. Translation: BAF82804.1.
AK314368 mRNA. Translation: BAG36998.1.
AK027729 mRNA. Translation: BAG51372.1.
AK125544 mRNA. Translation: BAG54211.1.
AC079199 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60600.1.
CH471152 Genomic DNA. Translation: EAW60601.1.
BC006535 mRNA. Translation: AAH06535.1.
D87513 mRNA. Translation: BAA13412.1.
CCDSCCDS11345.1. [Q14451-1]
CCDS56028.1. [Q14451-3]
PIRJC5412.
RefSeqNP_001025173.1. NM_001030002.2. [Q14451-1]
NP_001229371.1. NM_001242442.1.
NP_001229372.1. NM_001242443.1. [Q14451-1]
NP_005301.2. NM_005310.3. [Q14451-1]
XP_006721907.1. XM_006721844.1. [Q14451-2]
UniGeneHs.86859.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MW4NMR-A415-532[»]
1WGRNMR-A100-186[»]
2L4KNMR-A415-532[»]
2QMSX-ray2.10A/B/C/D415-532[»]
3PQZX-ray2.41A/B/C/D416-532[»]
ProteinModelPortalQ14451.
SMRQ14451. Positions 98-347, 369-532.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109143. 32 interactions.
DIPDIP-502N.
IntActQ14451. 38 interactions.
MINTMINT-1492212.
STRING9606.ENSP00000310771.

Chemistry

BindingDBQ14451.
ChEMBLCHEMBL1649051.

PTM databases

PhosphoSiteQ14451.

Polymorphism databases

DMDM116242503.

Proteomic databases

MaxQBQ14451.
PaxDbQ14451.
PRIDEQ14451.

Protocols and materials databases

DNASU2886.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309156; ENSP00000310771; ENSG00000141738. [Q14451-1]
ENST00000309185; ENSP00000311752; ENSG00000141738. [Q14451-2]
ENST00000394204; ENSP00000377754; ENSG00000141738. [Q14451-2]
ENST00000394209; ENSP00000377759; ENSG00000141738. [Q14451-1]
ENST00000394211; ENSP00000377761; ENSG00000141738. [Q14451-1]
ENST00000445327; ENSP00000403459; ENSG00000141738. [Q14451-3]
GeneID2886.
KEGGhsa:2886.
UCSCuc002hsr.3. human. [Q14451-1]
uc002hst.3. human. [Q14451-2]
uc021twu.1. human. [Q14451-3]

Organism-specific databases

CTD2886.
GeneCardsGC17P037894.
HGNCHGNC:4567. GRB7.
HPACAB005226.
MIM601522. gene.
neXtProtNX_Q14451.
PharmGKBPA28963.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG307156.
HOVERGENHBG000468.
InParanoidQ14451.
OMAQRNPQGF.
OrthoDBEOG7SFHW7.
PhylomeDBQ14451.
TreeFamTF317511.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
SignaLinkQ14451.

Gene expression databases

ArrayExpressQ14451.
BgeeQ14451.
CleanExHS_GRB7.
GenevestigatorQ14451.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR015042. BPS-dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR000159. Ras-assoc.
IPR000980. SH2.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF08947. BPS. 1 hit.
PF00169. PH. 1 hit.
PF00788. RA. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
SMARTSM00233. PH. 1 hit.
SM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14451.
GeneWikiGRB7.
GenomeRNAi2886.
NextBio11395.
PROQ14451.
SOURCESearch...

Entry information

Entry nameGRB7_HUMAN
AccessionPrimary (citable) accession number: Q14451
Secondary accession number(s): B2RAV1 expand/collapse secondary AC list , B3KNL0, B3KWP9, B7WP75, J3KQM4, Q53YD3, Q92568, Q96DF9, Q9Y220
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 145 of the entry and version 2 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