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Q14451

- GRB7_HUMAN

UniProt

Q14451 - GRB7_HUMAN

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Protein

Growth factor receptor-bound protein 7

Gene

GRB7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei239 – 2391Important for lipid binding and for stimulation of cell migration
Sitei511 – 5111Important for dimerization and for HRAS activation

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. phosphatidylinositol binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. RNA binding Source: UniProtKB-KW
  5. SH3/SH2 adaptor activity Source: ProtInc

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. epidermal growth factor receptor signaling pathway Source: ProtInc
  3. leukocyte migration Source: Reactome
  4. negative regulation of translation Source: UniProtKB
  5. positive regulation of cell migration Source: UniProtKB
  6. positive regulation of signal transduction Source: GOC
  7. stress granule assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Ligandi

Lipid-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_115896. GRB7 events in ERBB2 signaling.
REACT_12621. Tie2 Signaling.
REACT_17025. Downstream signal transduction.
SignaLinkiQ14451.

Names & Taxonomyi

Protein namesi
Recommended name:
Growth factor receptor-bound protein 7
Alternative name(s):
B47
Epidermal growth factor receptor GRB-7
GRB7 adapter protein
Gene namesi
Name:GRB7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:4567. GRB7.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. cytoplasmic stress granule Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi188 – 1881Y → F: Abolishes Ras activity increase and ERK1/2 phosphorylation. 1 Publication
Mutagenesisi239 – 2391R → L: Abolishes phosphoinositide binding. 1 Publication
Mutagenesisi259 – 2591Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications
Mutagenesisi260 – 2601Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications
Mutagenesisi284 – 2841Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications
Mutagenesisi338 – 3381Y → F: Abolishes Ras activity increase and ERK1/2 phosphorylation. 1 Publication
Mutagenesisi458 – 4581R → L: Impairs phosphotyrosine binding by SH2 domain.
Mutagenesisi480 – 4801Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications
Mutagenesisi492 – 4921Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications
Mutagenesisi511 – 5111F → R: Abolishes dimerization. Abolishes activation of HRAS. 1 Publication

Organism-specific databases

PharmGKBiPA28963.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 532532Growth factor receptor-bound protein 7PRO_0000150344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881Phosphotyrosine; by FAK12 Publications
Modified residuei338 – 3381Phosphotyrosine; by FAK12 Publications
Modified residuei361 – 3611Phosphoserine1 Publication

Post-translational modificationi

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.By similarity5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14451.
PaxDbiQ14451.
PRIDEiQ14451.

PTM databases

PhosphoSiteiQ14451.

Expressioni

Gene expression databases

BgeeiQ14451.
CleanExiHS_GRB7.
ExpressionAtlasiQ14451. baseline and differential.
GenevestigatoriQ14451.

Organism-specific databases

HPAiCAB005226.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-970191,EBI-970191
ARP102753EBI-970191,EBI-608057
CALMP621572EBI-970191,EBI-397403From a different organism.
Calm3P621619EBI-970191,EBI-397530From a different organism.
EPHB1P547624EBI-970191,EBI-80252
ERBB2P046265EBI-970191,EBI-641062
ERBB3P218607EBI-970191,EBI-720706
HAX1O001652EBI-970191,EBI-357001
KITP107214EBI-970191,EBI-1379503
PDGFRBP096194EBI-970191,EBI-641237
RND1Q927304EBI-970191,EBI-448618

Protein-protein interaction databases

BioGridi109143. 32 interactions.
DIPiDIP-502N.
IntActiQ14451. 38 interactions.
MINTiMINT-1492212.
STRINGi9606.ENSP00000310771.

Structurei

Secondary structure

1
532
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi102 – 1087
Beta strandi113 – 1186
Helixi124 – 1329
Beta strandi134 – 1363
Beta strandi145 – 1484
Turni150 – 1523
Beta strandi155 – 1584
Beta strandi160 – 1623
Helixi164 – 1685
Beta strandi173 – 1753
Beta strandi178 – 1814
Helixi421 – 4244
Helixi425 – 4284
Helixi429 – 4313
Beta strandi432 – 4365
Helixi438 – 44710
Beta strandi454 – 4596
Beta strandi461 – 4633
Beta strandi467 – 4737
Beta strandi476 – 48914
Beta strandi491 – 4966
Beta strandi502 – 5043
Helixi505 – 5128
Beta strandi513 – 5153
Beta strandi519 – 5213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ14451.
SMRiQ14451. Positions 98-347, 369-532.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14451.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini100 – 18687Ras-associatingPROSITE-ProRule annotationAdd
BLAST
Domaini229 – 338110PHPROSITE-ProRule annotationAdd
BLAST
Domaini431 – 52797SH2PROSITE-ProRule annotationAdd
BLAST

Domaini

The PH domain mediates interaction with membranes containing phosphoinositides.1 Publication

Sequence similaritiesi

Belongs to the GRB7/10/14 family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 Ras-associating domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG307156.
GeneTreeiENSGT00550000074537.
HOVERGENiHBG000468.
InParanoidiQ14451.
OMAiQRNPQGF.
OrthoDBiEOG7SFHW7.
PhylomeDBiQ14451.
TreeFamiTF317511.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR015042. BPS-dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000159. Ras-assoc.
IPR000980. SH2.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF08947. BPS. 1 hit.
PF00169. PH. 1 hit.
PF00788. RA. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00233. PH. 1 hit.
SM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: At least 2 isoforms are produced.

Isoform 1 (identifier: Q14451-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MELDLSPPHL SSSPEDLCPA PGTPPGTPRP PDTPLPEEVK RSQPLLIPTT
60 70 80 90 100
GRKLREEERR ATSLPSIPNP FPELCSPPSQ SPILGGPSSA RGLLPRDASR
110 120 130 140 150
PHVVKVYSED GACRSVEVAA GATARHVCEM LVQRAHALSD ETWGLVECHP
160 170 180 190 200
HLALERGLED HESVVEVQAA WPVGGDSRFV FRKNFAKYEL FKSSPHSLFP
210 220 230 240 250
EKMVSSCLDA HTGISHEDLI QNFLNAGSFP EIQGFLQLRG SGRKLWKRFF
260 270 280 290 300
CFLRRSGLYY STKGTSKDPR HLQYVADVNE SNVYVVTQGR KLYGMPTDFG
310 320 330 340 350
FCVKPNKLRN GHKGLRIFCS EDEQSRTCWL AAFRLFKYGV QLYKNYQQAQ
360 370 380 390 400
SRHLHPSCLG SPPLRSASDN TLVAMDFSGH AGRVIENPRE ALSVALEEAQ
410 420 430 440 450
AWRKKTNHRL SLPMPASGTS LSAAIHRTQL WFHGRISREE SQRLIGQQGL
460 470 480 490 500
VDGLFLVRES QRNPQGFVLS LCHLQKVKHY LILPSEEEGR LYFSMDDGQT
510 520 530
RFTDLLQLVE FHQLNRGILP CLLRHCCTRV AL
Length:532
Mass (Da):59,681
Last modified:October 17, 2006 - v2
Checksum:iA6867C20AFD46F74
GO
Isoform 2 (identifier: Q14451-2) [UniParc]FASTAAdd to Basket

Also known as: Grb7V

The sequence of this isoform differs from the canonical sequence as follows:
     425-447: IHRTQLWFHGRISREESQRLIGQ → CSWSGRVSGTPRALSSLCATCRK
     448-532: Missing.

Show »
Length:447
Mass (Da):49,423
Checksum:i2406BFDCBEBB1E49
GO
Isoform 3 (identifier: Q14451-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGKWRPGQGHTTGSVKPLSCSDAM

Show »
Length:555
Mass (Da):62,064
Checksum:i90E4D15BCBF428A1
GO
Isoform 4 (identifier: Q14451-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:498
Mass (Da):55,920
Checksum:iE18D088B19E632C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181C → W in BAA07827. (PubMed:9125150)Curated
Sequence conflicti18 – 181C → W in BAA29059. (PubMed:9710451)Curated
Sequence conflicti18 – 181C → W in BAA29060. (PubMed:9710451)Curated
Sequence conflicti18 – 181C → W in AAG25938. 1 PublicationCurated
Sequence conflicti118 – 1181V → A in BAG36998. (PubMed:14702039)Curated
Sequence conflicti120 – 1201A → T in BAG54211. (PubMed:14702039)Curated
Sequence conflicti147 – 1471E → G in BAG51372. (PubMed:14702039)Curated
Sequence conflicti164 – 1641V → L in BAG36998. (PubMed:14702039)Curated
Sequence conflicti510 – 5101E → D in BAG36998. (PubMed:14702039)Curated
Isoform 3 (identifier: Q14451-3)
Sequence conflicti20 – 201C → R in BAG54211. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGKWRPGQGHTTGSVKPLSC SDAM in isoform 3. 1 PublicationVSP_041665
Alternative sequencei48 – 8134Missing in isoform 4. 1 PublicationVSP_041666Add
BLAST
Alternative sequencei425 – 44723IHRTQ…RLIGQ → CSWSGRVSGTPRALSSLCAT CRK in isoform 2. 1 PublicationVSP_035500Add
BLAST
Alternative sequencei448 – 53285Missing in isoform 2. 1 PublicationVSP_035501Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11345.1. [Q14451-1]
CCDS56028.1. [Q14451-3]
PIRiJC5412.
RefSeqiNP_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]
UniGeneiHs.86859.

Genome annotation databases

EnsembliENST00000309156; ENSP00000310771; ENSG00000141738. [Q14451-1]
ENST00000394204; ENSP00000377754; ENSG00000141738. [Q14451-2]
ENST00000394209; ENSP00000377759; ENSG00000141738. [Q14451-1]
ENST00000394211; ENSP00000377761; ENSG00000141738. [Q14451-1]
ENST00000445327; ENSP00000403459; ENSG00000141738. [Q14451-3]
GeneIDi2886.
KEGGihsa:2886.
UCSCiuc002hsr.3. human. [Q14451-1]
uc002hst.3. human. [Q14451-2]
uc021twu.1. human. [Q14451-3]

Polymorphism databases

DMDMi116242503.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11345.1. [Q14451-1 ]
CCDS56028.1. [Q14451-3 ]
PIRi JC5412.
RefSeqi NP_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 ]
UniGenei Hs.86859.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MW4 NMR - A 415-532 [» ]
1WGR NMR - A 100-186 [» ]
2L4K NMR - A 415-532 [» ]
2QMS X-ray 2.10 A/B/C/D 415-532 [» ]
3PQZ X-ray 2.41 A/B/C/D 416-532 [» ]
ProteinModelPortali Q14451.
SMRi Q14451. Positions 98-347, 369-532.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109143. 32 interactions.
DIPi DIP-502N.
IntActi Q14451. 38 interactions.
MINTi MINT-1492212.
STRINGi 9606.ENSP00000310771.

Chemistry

BindingDBi Q14451.
ChEMBLi CHEMBL1649051.

PTM databases

PhosphoSitei Q14451.

Polymorphism databases

DMDMi 116242503.

Proteomic databases

MaxQBi Q14451.
PaxDbi Q14451.
PRIDEi Q14451.

Protocols and materials databases

DNASUi 2886.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309156 ; ENSP00000310771 ; ENSG00000141738 . [Q14451-1 ]
ENST00000394204 ; ENSP00000377754 ; ENSG00000141738 . [Q14451-2 ]
ENST00000394209 ; ENSP00000377759 ; ENSG00000141738 . [Q14451-1 ]
ENST00000394211 ; ENSP00000377761 ; ENSG00000141738 . [Q14451-1 ]
ENST00000445327 ; ENSP00000403459 ; ENSG00000141738 . [Q14451-3 ]
GeneIDi 2886.
KEGGi hsa:2886.
UCSCi uc002hsr.3. human. [Q14451-1 ]
uc002hst.3. human. [Q14451-2 ]
uc021twu.1. human. [Q14451-3 ]

Organism-specific databases

CTDi 2886.
GeneCardsi GC17P037894.
HGNCi HGNC:4567. GRB7.
HPAi CAB005226.
MIMi 601522. gene.
neXtProti NX_Q14451.
PharmGKBi PA28963.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG307156.
GeneTreei ENSGT00550000074537.
HOVERGENi HBG000468.
InParanoidi Q14451.
OMAi QRNPQGF.
OrthoDBi EOG7SFHW7.
PhylomeDBi Q14451.
TreeFami TF317511.

Enzyme and pathway databases

Reactomei REACT_111040. Signaling by SCF-KIT.
REACT_115896. GRB7 events in ERBB2 signaling.
REACT_12621. Tie2 Signaling.
REACT_17025. Downstream signal transduction.
SignaLinki Q14451.

Miscellaneous databases

EvolutionaryTracei Q14451.
GeneWikii GRB7.
GenomeRNAii 2886.
NextBioi 11395.
PROi Q14451.
SOURCEi Search...

Gene expression databases

Bgeei Q14451.
CleanExi HS_GRB7.
ExpressionAtlasi Q14451. baseline and differential.
Genevestigatori Q14451.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR015042. BPS-dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000159. Ras-assoc.
IPR000980. SH2.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF08947. BPS. 1 hit.
PF00169. PH. 1 hit.
PF00788. RA. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
SMARTi SM00233. PH. 1 hit.
SM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiGRB7_HUMAN
AccessioniPrimary (citable) accession number: Q14451
Secondary accession number(s): B2RAV1
, B3KNL0, B3KWP9, B7WP75, J3KQM4, Q53YD3, Q92568, Q96DF9, Q9Y220
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3