[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Oesophageal carcinoma; DOI=10.1006/bbrc.1997.6218; PubMed=9125150 [NCBI, ExPASy, EBI, Israel, Japan] Kishi T., Sasaki H., Akiyama N., Ishizuka T., Sakamoto H., Aizawa S., Sugimura T., Terada M.; "Molecular cloning of human GRB-7 co-amplified with CAB1 and c-ERBB-2 in primary gastric cancer."; Biochem. Biophys. Res. Commun. 232:5-9(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=9710451 [NCBI, ExPASy, EBI, Israel, Japan] Tanaka S., Mori M., Akiyoshi T., Tanaka Y., Mafune K., Wands J.R., Sugimachi K.; "A novel variant of human Grb7 is associated with invasive esophageal carcinoma."; J. Clin. Invest. 102:821-827(1998).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Whittock N.V., Eady R.A.J., McGrath J.A.; "Genomic organization and amplification of the human GRB7 gene."; Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 130-343. PubMed=8988034 [NCBI, ExPASy, EBI, Israel, Japan] Tanaka S., Mori M., Akiyoshi T., Tanaka Y., Mafune K., Wands J.R., Sugimachi K.; "Coexpression of Grb7 with epidermal growth factor receptor or Her2/erbB2 in human advanced esophageal carcinoma."; Cancer Res. 57:28-31(1997).
[6]	INTERACTION WITH RND1. DOI=10.1016/S0014-5793(99)01530-6; PubMed=10664463 [NCBI, ExPASy, EBI, Israel, Japan] Vayssiere B., Zalcman G., Mahe Y., Mirey G., Ligensa T., Weidner K.M., Chardin P., Camonis J.; "Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family."; FEBS Lett. 467:91-96(2000).
[7]	STRUCTURE BY NMR OF 100-186. RIKEN structural genomics initiative (RSGI); "Solution structure of the RA domain of human GRB7 protein."; Submitted (NOV-2004) to the PDB data bank.

Comments

FUNCTION: Interacts with the cytoplasmic domain of the epidermal growth factor receptor which is then inhibited. The interaction is mediated by the SH2 domain. Also binds to ERBB2.
SUBUNIT: Interacts with RND1.
INTERACTION:
P62157:CALM (xeno); NbExp=1; IntAct=EBI-1257061, EBI-397403;
P62161:Calm1 (xeno); NbExp=1; IntAct=EBI-1257061, EBI-397530;
ALTERNATIVE PRODUCTS: 1 named isoform [FASTA] produced by alternative splicing. At least 2 isoforms are produced.

Name 1

Isoform ID Q14451-1

This is the isoform sequence displayed in this entry.
PTM: Phosphorylated on tyrosine residues.
SIMILARITY: Belongs to the GRB7/10/14 family.
SIMILARITY: Contains 1 PH domain.
SIMILARITY: Contains 1 Ras-associating domain.
SIMILARITY: Contains 1 SH2 domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D43772; BAA07827.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB008789; BAA29059.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF274875; AAG25938.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006535; AAH06535.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D87513; BAA13412.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC5412; JC5412.

RefSeq

NP_001025173.1; -.
NP_005301.2; -.

UniGene

Hs.86859

3D structure databases

PDB

1MW4; NMR; -; A=415-532.	[ExPASy / RCSB / EBI]
1WGR; NMR; -; A=100-186.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1MW4; -.
1WGR; -.

ModBase

Q14451.

Protein-protein interaction databases

DIP

DIP:502N; -.

IntAct

Q14451; -.

PTM databases

PhosphoSite

Q14451; -.

Organism-specific databases

HIX0013788; -.

HGNC:4567; GRB7.

CAB005226; -.

601522; gene. [NCBI / EBI]

PharmGKB

PA28963; -.

GeneCards

Q14451.

Gene expression databases

ArrayExpress

Q14451; -.

CleanEx

HS_GRB7; -.

GermOnline

ENSG00000141738; Homo sapiens.

Ontologies

GO:0005070;	Molecular function: SH3/SH2 adaptor activity (traceable author statement from ProtInc).
GO:0007173;	Biological process: epidermal growth factor receptor signaling pathway (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR015042; BPS.
IPR001849; PH.
IPR011993; PH_type.
IPR000159; Ras-assoc.
IPR000980; SH2.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.29.30; PH_type; 1.
G3DSA:3.30.505.10; SH2; 1.

Pfam

PF08947; BPS; 1.
PF00169; PH; 1.
PF00788; RA; 1.
PF00017; SH2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00401; SH2DOMAIN.

ProDom

PD000093; SH2; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00233; PH; 1.
SM00314; RA; 1.
SM00252; SH2; 1.
SMART graphical view of domain structure.

PROSITE

PS50003; PH_DOMAIN; 1.
PS50200; RA; 1.
PS50001; SH2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q14451.

Genome annotation databases

Ensembl

ENSG00000141738; Homo sapiens. [Contig view]

GeneID

2886; -.

KEGG

hsa:2886; -.

Phylogenomic databases

HOGENOM

Q14451; -.

HOVERGEN

Q14451; -.

Other

GRB7; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Phosphoprotein; SH2 domain.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 532`	`532`	`Growth factor receptor-bound protein 7.`	`PRO_0000150344`
`DOMAIN`	`100 186`	`87`	`Ras-associating.`
`DOMAIN`	`229 338`	`110`	`PH.`
`DOMAIN`	`431 527`	`97`	`SH2.`
`MOD_RES`	`297 297`		`Phosphothreonine (By similarity).`
`MOD_RES`	`366 366`		`Phosphoserine (By similarity).`
`CONFLICT`	`18 18`		`C -> W (in Ref. 1, 2 and 3).`
`STRAND`	`102 108`	`7`
`STRAND`	`113 118`	`6`
`HELIX`	`124 132`	`9`
`STRAND`	`134 136`	`3`
`STRAND`	`145 148`	`4`
`TURN`	`150 152`	`3`
`STRAND`	`155 158`	`4`
`STRAND`	`160 162`	`3`
`HELIX`	`164 168`	`5`
`STRAND`	`173 175`	`3`
`STRAND`	`178 181`	`4`
`STRAND`	`427 429`	`3`
`STRAND`	`432 434`	`3`
`HELIX`	`438 444`	`7`
`HELIX`	`445 447`	`3`
`STRAND`	`456 459`	`4`
`STRAND`	`461 463`	`3`
`STRAND`	`467 472`	`6`
`STRAND`	`477 483`	`7`
`HELIX`	`505 511`	`7`
`STRAND`	`513 515`	`3`

Sequence information

Length: 532 AA [This is the length of the unprocessed precursor]

Molecular weight: 59681 Da [This is the MW of the unprocessed precursor]

CRC64: A6867C20AFD46F74 [This is a checksum on the sequence]

        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

Q14451 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools