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Protein

Growth factor receptor-bound protein 7

Gene

GRB7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 similarity4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei239Important for lipid binding and for stimulation of cell migration1
Sitei511Important for dimerization and for HRAS activation1

GO - Molecular functioni

  • phosphatidylinositol binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • RNA binding Source: UniProtKB-KW
  • SH3/SH2 adaptor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Ligandi

Lipid-binding, RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141738-MONOMER.
ReactomeiR-HSA-1306955. GRB7 events in ERBB2 signaling.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-186763. Downstream signal transduction.
R-HSA-210993. Tie2 Signaling.
R-HSA-8853659. RET signaling.
SignaLinkiQ14451.
SIGNORiQ14451.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:4567. GRB7.

Subcellular locationi

GO - Cellular componenti

  • cell projection Source: UniProtKB-SubCell
  • cytoplasmic stress granule Source: UniProtKB
  • cytosol Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi188Y → F: Abolishes Ras activity increase and ERK1/2 phosphorylation. 1 Publication1
Mutagenesisi239R → L: Abolishes phosphoinositide binding. 1 Publication1
Mutagenesisi259Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications1
Mutagenesisi260Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications1
Mutagenesisi284Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications1
Mutagenesisi338Y → F: Abolishes Ras activity increase and ERK1/2 phosphorylation. 1 Publication1
Mutagenesisi458R → L: Impairs phosphotyrosine binding by SH2 domain. 1
Mutagenesisi480Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications1
Mutagenesisi492Y → F: Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1. 2 Publications1
Mutagenesisi511F → R: Abolishes dimerization. Abolishes activation of HRAS. 1 Publication1

Organism-specific databases

DisGeNETi2886.
OpenTargetsiENSG00000141738.
PharmGKBiPA28963.

Chemistry databases

ChEMBLiCHEMBL1649051.

Polymorphism and mutation databases

BioMutaiGRB7.
DMDMi116242503.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001503441 – 532Growth factor receptor-bound protein 7Add BLAST532

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei188Phosphotyrosine; by FAK12 Publications1
Modified residuei338Phosphotyrosine; by FAK12 Publications1
Modified residuei361PhosphoserineCombined sources1

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 similarity4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ14451.
MaxQBiQ14451.
PaxDbiQ14451.
PeptideAtlasiQ14451.
PRIDEiQ14451.

PTM databases

iPTMnetiQ14451.
PhosphoSitePlusiQ14451.

Expressioni

Gene expression databases

BgeeiENSG00000141738.
CleanExiHS_GRB7.
ExpressionAtlasiQ14451. baseline and differential.
GenevisibleiQ14451. HS.

Organism-specific databases

HPAiCAB005226.
CAB073538.
HPA057084.

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
KCTD6Q8NC693EBI-970191,EBI-2511344
KITP107214EBI-970191,EBI-1379503
LAX1Q8IWV13EBI-970191,EBI-10232942
OLIG1Q8TAK63EBI-970191,EBI-3867416
PDGFRBP096194EBI-970191,EBI-641237
PTK2Q053973EBI-970191,EBI-702142
RND1Q927304EBI-970191,EBI-448618
TRIM36Q9NQ863EBI-970191,EBI-2341518

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
  • SH3/SH2 adaptor activity Source: ProtInc

Protein-protein interaction databases

BioGridi109143. 37 interactors.
DIPiDIP-502N.
IntActiQ14451. 48 interactors.
MINTiMINT-1492212.
STRINGi9606.ENSP00000403459.

Chemistry databases

BindingDBiQ14451.

Structurei

Secondary structure

1532
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi102 – 108Combined sources7
Beta strandi113 – 118Combined sources6
Helixi124 – 132Combined sources9
Beta strandi134 – 136Combined sources3
Beta strandi145 – 148Combined sources4
Turni150 – 152Combined sources3
Beta strandi155 – 158Combined sources4
Beta strandi160 – 162Combined sources3
Helixi164 – 168Combined sources5
Beta strandi173 – 175Combined sources3
Beta strandi178 – 181Combined sources4
Helixi421 – 424Combined sources4
Helixi425 – 428Combined sources4
Helixi429 – 431Combined sources3
Beta strandi432 – 436Combined sources5
Helixi438 – 447Combined sources10
Beta strandi454 – 459Combined sources6
Beta strandi461 – 463Combined sources3
Beta strandi466 – 473Combined sources8
Beta strandi476 – 487Combined sources12
Beta strandi490 – 496Combined sources7
Beta strandi502 – 504Combined sources3
Helixi505 – 512Combined sources8
Beta strandi513 – 515Combined sources3
Beta strandi519 – 521Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4WWQX-ray1.80A/B415-532[»]
4X6SX-ray2.55A/B423-529[»]
5D0JX-ray2.60A/B/C/D415-532[»]
5EELX-ray2.47A/B/C/D/E/F415-532[»]
5EEQX-ray1.60A/B415-532[»]
ProteinModelPortaliQ14451.
SMRiQ14451.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14451.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini100 – 186Ras-associatingPROSITE-ProRule annotationAdd BLAST87
Domaini229 – 338PHPROSITE-ProRule annotationAdd BLAST110
Domaini431 – 527SH2PROSITE-ProRule annotationAdd BLAST97

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

eggNOGiKOG3751. Eukaryota.
ENOG410XXC8. LUCA.
GeneTreeiENSGT00550000074537.
HOVERGENiHBG000468.
InParanoidiQ14451.
OMAiVQAAWPI.
OrthoDBiEOG091G135G.
PhylomeDBiQ14451.
TreeFamiTF317511.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR015042. BPS-dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000159. RA_dom.
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]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF54236. 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti18C → W in BAA07827 (PubMed:9125150).Curated1
Sequence conflicti18C → W in BAA29059 (PubMed:9710451).Curated1
Sequence conflicti18C → W in BAA29060 (PubMed:9710451).Curated1
Sequence conflicti18C → W in AAG25938 (Ref. 3) Curated1
Sequence conflicti118V → A in BAG36998 (PubMed:14702039).Curated1
Sequence conflicti120A → T in BAG54211 (PubMed:14702039).Curated1
Sequence conflicti147E → G in BAG51372 (PubMed:14702039).Curated1
Sequence conflicti164V → L in BAG36998 (PubMed:14702039).Curated1
Sequence conflicti510E → D in BAG36998 (PubMed:14702039).Curated1
Isoform 3 (identifier: Q14451-3)
Sequence conflicti20C → R in BAG54211 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0416651M → MGKWRPGQGHTTGSVKPLSC SDAM in isoform 3. 1 Publication1
Alternative sequenceiVSP_04166648 – 81Missing in isoform 4. 1 PublicationAdd BLAST34
Alternative sequenceiVSP_035500425 – 447IHRTQ…RLIGQ → CSWSGRVSGTPRALSSLCAT CRK in isoform 2. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_035501448 – 532Missing in isoform 2. 1 PublicationAdd BLAST85

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS82116.1. [Q14451-2]
PIRiJC5412.
RefSeqiNP_001025173.1. NM_001030002.2. [Q14451-1]
NP_001229371.1. NM_001242442.1.
NP_001229372.1. NM_001242443.1. [Q14451-1]
NP_001317136.1. NM_001330207.1.
NP_005301.2. NM_005310.3. [Q14451-1]
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.4. human. [Q14451-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS82116.1. [Q14451-2]
PIRiJC5412.
RefSeqiNP_001025173.1. NM_001030002.2. [Q14451-1]
NP_001229371.1. NM_001242442.1.
NP_001229372.1. NM_001242443.1. [Q14451-1]
NP_001317136.1. NM_001330207.1.
NP_005301.2. NM_005310.3. [Q14451-1]
UniGeneiHs.86859.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4WWQX-ray1.80A/B415-532[»]
4X6SX-ray2.55A/B423-529[»]
5D0JX-ray2.60A/B/C/D415-532[»]
5EELX-ray2.47A/B/C/D/E/F415-532[»]
5EEQX-ray1.60A/B415-532[»]
ProteinModelPortaliQ14451.
SMRiQ14451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109143. 37 interactors.
DIPiDIP-502N.
IntActiQ14451. 48 interactors.
MINTiMINT-1492212.
STRINGi9606.ENSP00000403459.

Chemistry databases

BindingDBiQ14451.
ChEMBLiCHEMBL1649051.

PTM databases

iPTMnetiQ14451.
PhosphoSitePlusiQ14451.

Polymorphism and mutation databases

BioMutaiGRB7.
DMDMi116242503.

Proteomic databases

EPDiQ14451.
MaxQBiQ14451.
PaxDbiQ14451.
PeptideAtlasiQ14451.
PRIDEiQ14451.

Protocols and materials databases

DNASUi2886.
Structural Biology KnowledgebaseSearch...

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.4. human. [Q14451-1]

Organism-specific databases

CTDi2886.
DisGeNETi2886.
GeneCardsiGRB7.
HGNCiHGNC:4567. GRB7.
HPAiCAB005226.
CAB073538.
HPA057084.
MIMi601522. gene.
neXtProtiNX_Q14451.
OpenTargetsiENSG00000141738.
PharmGKBiPA28963.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3751. Eukaryota.
ENOG410XXC8. LUCA.
GeneTreeiENSGT00550000074537.
HOVERGENiHBG000468.
InParanoidiQ14451.
OMAiVQAAWPI.
OrthoDBiEOG091G135G.
PhylomeDBiQ14451.
TreeFamiTF317511.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141738-MONOMER.
ReactomeiR-HSA-1306955. GRB7 events in ERBB2 signaling.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-186763. Downstream signal transduction.
R-HSA-210993. Tie2 Signaling.
R-HSA-8853659. RET signaling.
SignaLinkiQ14451.
SIGNORiQ14451.

Miscellaneous databases

EvolutionaryTraceiQ14451.
GeneWikiiGRB7.
GenomeRNAii2886.
PROiQ14451.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000141738.
CleanExiHS_GRB7.
ExpressionAtlasiQ14451. baseline and differential.
GenevisibleiQ14451. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR015042. BPS-dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000159. RA_dom.
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]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 169 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.