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Search results 1201 to 1300 out of 1429 for Dab1

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Type Details Score
Genotype
Genotype
Symbol: Dab1/Dab1
Background: involves: C3HeB/FeJ * DC/Le
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Dab1/Dab1
Background: involves: C3HeB/FeJ * DC/LeJ
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Dab1/Dab1
Background: involves: C3HeB/FeJ * C57BL/6J * DC/Le
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Dab1/Dab1<+>
Background: involves: C3HeB/FeJ * C57BL/6J * DC/Le
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Dab1/Dab1
Background: involves: DC/Le
Zygosity: hm
Has Mutant Allele: true
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Publication
12805222 | J:83951
First Author: Hocevar BA
Year: 2003
Journal: EMBO J
Title: Regulation of the Wnt signaling pathway by disabled-2 (Dab2).
Volume: 22
Issue: 12
Pages: 3084-94
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Publication
16984970 | J:188901
First Author: Maurer ME
Year: 2006
Journal: J Cell Sci
Title: The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH.
Volume: 119
Issue: Pt 20
Pages: 4235-46
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Publication
9671493 | -
First Author: Le N
Year: 1998
Journal: Mol Cell Biol
Title: Disabled is a putative adaptor protein that functions during signaling by the sevenless receptor tyrosine kinase.
Volume: 18
Issue: 8
Pages: 4844-54
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Publication
16267015 | -
First Author: Zhoul J
Year: 2005
Journal: Cancer Res
Title: The role of DOC-2/DAB2 in modulating androgen receptor-mediated cell growth via the nongenomic c-Src-mediated pathway in normal prostatic epithelium and cancer.
Volume: 65
Issue: 21
Pages: 9906-13
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Publication
11387212 | -
First Author: Hocevar BA
Year: 2001
Journal: EMBO J
Title: The adaptor molecule Disabled-2 links the transforming growth factor beta receptors to the Smad pathway.
Volume: 20
Issue: 11
Pages: 2789-801
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Publication
7680635 | -
First Author: Gertler FB
Year: 1993
Journal: Genes Dev
Title: Dosage-sensitive modifiers of Drosophila abl tyrosine kinase function: prospero, a regulator of axonal outgrowth, and disabled, a novel tyrosine kinase substrate.
Volume: 7
Issue: 3
Pages: 441-53
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Protein Domain
IPR028761 | Dab
Type: Family
Description: This entry represents the protein disabled (DAB) and related proteins. It includes DAB from Drosophila melanogaster and its mammlian homologues, DAB1 and DAB2 (also known as DOC1 and DOC2). This group of proteins are adapter proteins that play roles in development. In Drosophila melanogaster, DAB acts as an adapter protein for SH2-domain containing proteins in the sevenless (sev) signalling pathway []. Together with Abl, it is involved in embryonic neural development []. In mammals, DAB1 is implicated in neuronal development []. In humans, DAB2 is an adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins []. It is involved in several signalling pathways and plays an important part in cell growth and development [, , ].
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Strain
MGI:2161295 | STOCK Tyrp1<b> +/+ Dab1<scm>
Attribute String: mutant stock
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Publication
19903888 | J:154743
First Author: Xie D
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: DAB2IP coordinates both PI3K-Akt and ASK1 pathways for cell survival and apoptosis.
Volume: 106
Issue: 47
Pages: 19878-83
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Publication
21444365 | -
First Author: Harrison SC
Year: 2012
Journal: Eur Heart J
Title: Association of a sequence variant in DAB2IP with coronary heart disease.
Volume: 33
Issue: 7
Pages: 881-8
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Publication
15310755 | -
First Author: Zhang H
Year: 2004
Journal: J Biol Chem
Title: AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation.
Volume: 279
Issue: 43
Pages: 44955-65
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Publication
18073375 | -
First Author: Duggan D
Year: 2007
Journal: J Natl Cancer Inst
Title: Two genome-wide association studies of aggressive prostate cancer implicate putative prostate tumor suppressor gene DAB2IP.
Volume: 99
Issue: 24
Pages: 1836-44
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Publication
20622881 | -
First Author: Gretarsdottir S
Year: 2010
Journal: Nat Genet
Title: Genome-wide association study identifies a sequence variant within the DAB2IP gene conferring susceptibility to abdominal aortic aneurysm.
Volume: 42
Issue: 8
Pages: 692-7
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Protein Domain
IPR030403 | DAB2IP
Type: Family
Description: DAB-2 interacting protein (Dab2IP) is a GTPase activating protein involved in the regulation of multiple signalling pathways. Dab2IP regulates PI3K-AKT signalling and functions as a tumour suppressor. It modulates the balance between phosphatidylinositol 3-kinase (PI3K) mediated cell survival and ASK1 mediated apoptosis [, ]. Besides its function as a tumour suppressor, Dab2IP is also highly expressed in the brain, where it interacts with Dab1 (Disabled homologue 1), a key mediator of the Reelin pathway that controls several aspects of brain development and function [, , ]. It also functions as an inhibitor in VEGFR2-mediated adaptative angiogenesis [].Dab2IP has been associated with metastatic prostate cancer [], abdominal aortic aneurysms []and coronary heart disease [].
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Publication
17913789 | J:126335
First Author: Hack I
Year: 2007
Journal: Development
Title: Divergent roles of ApoER2 and Vldlr in the migration of cortical neurons.
Volume: 134
Issue: 21
Pages: 3883-91
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Publication
18946489 | J:143787
First Author: Blake SM
Year: 2008
Journal: EMBO J
Title: Thrombospondin-1 binds to ApoER2 and VLDL receptor and functions in postnatal neuronal migration.
Volume: 27
Issue: 22
Pages: 3069-80
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Publication
29691400 | J:264763
First Author: Lanjakornsiripan D
Year: 2018
Journal: Nat Commun
Title: Layer-specific morphological and molecular differences in neocortical astrocytes and their dependence on neuronal layers.
Volume: 9
Issue: 1
Pages: 1623
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Publication
37188781 | J:341134
First Author: Lopera F
Year: 2023
Journal: Nat Med
Title: Resilience to autosomal dominant Alzheimer's disease in a Reelin-COLBOS heterozygous man.
Volume: 29
Issue: 5
Pages: 1243-1252
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Publication
11137154 | J:66167
First Author: Bar I
Year: 2000
Journal: Trends Neurosci
Title: The evolution of cortical development. An hypothesis based on the role of the Reelin signaling pathway.
Volume: 23
Issue: 12
Pages: 633-8
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Publication
10328932 | J:54649
First Author: Lambert de Rouvroit C
Year: 1999
Journal: Exp Neurol
Title: Evolutionarily conserved, alternative splicing of reelin during brain development.
Volume: 156
Issue: 2
Pages: 229-38
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Publication
17548821 | J:248288
First Author: Yasui N
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: Structure of a receptor-binding fragment of reelin and mutational analysis reveal a recognition mechanism similar to endocytic receptors.
Volume: 104
Issue: 24
Pages: 9988-93
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Publication
26503265 | J:239271
First Author: Lawrenson ID
Year: 2017
Journal: Cereb Cortex
Title: Cortical Layer Inversion and Deregulation of Reelin Signaling in the Absence of SOCS6 and SOCS7.
Volume: 27
Issue: 1
Pages: 576-588
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Publication
25128699 | J:217773
 
First Author: Mota SI
Year: 2014
Journal: Exp Neurol
Title: Impaired Src signaling and post-synaptic actin polymerization in Alzheimer's disease mice hippocampus--linking NMDA receptors and the reelin pathway.
Volume: 261
Pages: 698-709
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Publication
26635527 | J:245046
 
First Author: Brai E
Year: 2015
Journal: Front Cell Neurosci
Title: Notch1 Regulates Hippocampal Plasticity Through Interaction with the Reelin Pathway, Glutamatergic Transmission and CREB Signaling.
Volume: 9
Pages: 447
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Publication
19074029 | J:143049
First Author: Park TJ
Year: 2008
Journal: J Neurosci
Title: Crk and Crk-like play essential overlapping roles downstream of disabled-1 in the Reelin pathway.
Volume: 28
Issue: 50
Pages: 13551-62
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Publication
27726110 | J:339400
First Author: Mata A
Year: 2017
Journal: Mol Neurobiol
Title: Reelin Expression in Creutzfeldt-Jakob Disease and Experimental Models of Transmissible Spongiform Encephalopathies.
Volume: 54
Issue: 8
Pages: 6412-6425
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Publication
23209795 | J:225068
First Author: Hellwig S
Year: 2012
Journal: PLoS One
Title: Reelin together with ApoER2 regulates interneuron migration in the olfactory bulb.
Volume: 7
Issue: 11
Pages: e50646
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Publication
28484035 | J:242292
First Author: Jakob B
Year: 2017
Journal: Proc Natl Acad Sci U S A
Title: Intersectin 1 is a component of the Reelin pathway to regulate neuronal migration and synaptic plasticity in the hippocampus.
Volume: 114
Issue: 21
Pages: 5533-5538
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Publication
11835672 | J:74540
First Author: Park C
Year: 2002
Journal: Genesis
Title: The cerebellar deficient folia (cdf) gene acts intrinsically in Purkinje cell migrations.
Volume: 32
Issue: 1
Pages: 32-41
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Publication
25788693 | J:220151
First Author: Kohno T
Year: 2015
Journal: J Neurosci
Title: Importance of Reelin C-terminal region in the development and maintenance of the postnatal cerebral cortex and its regulation by specific proteolysis.
Volume: 35
Issue: 11
Pages: 4776-87
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Publication
14645539 | J:86862
First Author: Arnaud L
Year: 2003
Journal: Mol Cell Biol
Title: Regulation of protein tyrosine kinase signaling by substrate degradation during brain development.
Volume: 23
Issue: 24
Pages: 9293-302
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Publication
14724251 | J:87733
First Author: Jossin Y
Year: 2004
Journal: J Neurosci
Title: The central fragment of Reelin, generated by proteolytic processing in vivo, is critical to its function during cortical plate development.
Volume: 24
Issue: 2
Pages: 514-21
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Publication
23976984 | J:205842
First Author: Sharaf A
Year: 2013
Journal: PLoS One
Title: ApoER2 and VLDLr are required for mediating reelin signalling pathway for normal migration and positioning of mesencephalic dopaminergic neurons.
Volume: 8
Issue: 8
Pages: e71091
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Publication
23326475 | J:195873
First Author: Qiao S
Year: 2013
Journal: PLoS One
Title: Dab2IP GTPase activating protein regulates dendrite development and synapse number in cerebellum.
Volume: 8
Issue: 1
Pages: e53635
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Publication
19033661 | J:144734
First Author: Zhang H
Year: 2008
Journal: J Clin Invest
Title: AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice.
Volume: 118
Issue: 12
Pages: 3904-16
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Protein
F6Y0W2
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: true
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Protein
D6RDE3
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
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Publication
28887403 | J:248393
First Author: Santana J
Year: 2017
Journal: Biochem J
Title: The functions of Reelin in membrane trafficking and cytoskeletal dynamics: implications for neuronal migration, polarization and differentiation.
Volume: 474
Issue: 18
Pages: 3137-3165
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Publication
29049379 | J:249311
First Author: Hass H
Year: 2017
Journal: PLoS One
Title: Mathematical model of early Reelin-induced Src family kinase-mediated signaling.
Volume: 12
Issue: 10
Pages: e0186927
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Publication
12737822 | -
First Author: Stolt PC
Year: 2003
Journal: Structure
Title: Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 PTB domain complexes.
Volume: 11
Issue: 5
Pages: 569-79
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Publication
7798194 | J:39401
First Author: Blaikie P
Year: 1994
Journal: J Biol Chem
Title: A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors.
Volume: 269
Issue: 51
Pages: 32031-4
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Publication
7534213 | -
First Author: Bork P
Year: 1995
Journal: Cell
Title: A phosphotyrosine interaction domain.
Volume: 80
Issue: 5
Pages: 693-4
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Publication
7527937 | -
First Author: Kavanaugh WM
Year: 1994
Journal: Science
Title: An alternative to SH2 domains for binding tyrosine-phosphorylated proteins.
Volume: 266
Issue: 5192
Pages: 1862-5
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Protein Domain
IPR006020 | PTB/PI_dom
Type: Domain
Description: Proteins encoding phosphotyrosine binding (PTB) domains function as adaptors or scaffolds to organise the signaling complexes involved in wide-ranging physiological processes including neural development, immunity, tissue homeostasis and cell growth. Due to structural differences, PTB domains are divided into three groups represented by phosphotyrosine-dependent IRS-like, phosphotyrosine-dependent Shc-like, and phosphotyrosine-independent Dab-like PTBs. The last two PTBs have been named as phosphotyrosine interaction domain (PID or PI domain). PID domain has an average length of about 160 amino acids [].The Shc-like PID specifically binds to the Asn-Pro-Xaa-Tyr(P) motif found in many tyrosine-phosphorylated proteins including growth factor receptors. On the other hand the Dab-like PID domain binds to non-phosphorylated tyrosine residue or even a phenylalanine at the same position []. Most of the ligands for Shc-like PID domains are RTK or cytokine, whereas phosphotyrosine independent Dab-like PID domains seems to mediate other types of signaling pathways, like endocytosis/processing or exocytosis. This domain binds both peptides and headgroups of phosphatidylinositides, utilising two distinct binding motifs to mediate spatial organisation and localisation within cells [, , , ].The 3D structure of PID domain has been solved []. It shares a folding pattern, commonly referred to as the PH-domain "superfold". The core "superfold"consists of seven antiparallel beta strands forming two orthogonal beta sheets. This beta sandwich is capped at the C terminus by an alpha helix. It contains a peptide binding pocket (formed by the beta strand 5 and C-terminal alpha helix) and a highly basic phospholipid binding "crown"(largely composed of residues from loop regions near the N terminus). Both Shcand Dab1 have two additional alpha helices, one of which is located at the Nterminus and the other between beta 1 and beta 2 strands.
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Protein
Q8C142
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: false
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Protein
Q8K2A1
Organism: Mus musculus/domesticus
Length: 304  
Fragment?: false
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Protein
Q9D3A8
Organism: Mus musculus/domesticus
Length: 503  
Fragment?: false
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Protein
O35671
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: false
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Protein
P97318
Organism: Mus musculus/domesticus
Length: 588  
Fragment?: false
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Protein
P98078
Organism: Mus musculus/domesticus
Length: 766  
Fragment?: false
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Protein
Q9DCE6
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: false
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Protein
Q3TRB6
Organism: Mus musculus/domesticus
Length: 271  
Fragment?: false
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Protein
Q3TRE6
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
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Protein
Q0PNF0
Organism: Mus musculus/domesticus
Length: 304  
Fragment?: false
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Protein
D3Z7I6
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: true
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Protein
E0CZ53
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
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Protein
Q3TN55
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
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Protein
F6VRL0
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: true
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Protein
E9QL31
Organism: Mus musculus/domesticus
Length: 745  
Fragment?: false
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Protein
F8WJ71
Organism: Mus musculus/domesticus
Length: 76  
Fragment?: false
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Protein
Q3TMQ2
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
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Protein
B7ZNH1
Organism: Mus musculus/domesticus
Length: 383  
Fragment?: true
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Protein
A2AWA7
Organism: Mus musculus/domesticus
Length: 455  
Fragment?: true
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Protein
E0CXC5
Organism: Mus musculus/domesticus
Length: 299  
Fragment?: false
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Protein
A2AWB0
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: true
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Protein
Q9CUY3
Organism: Mus musculus/domesticus
Length: 59  
Fragment?: true
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Protein
E0CXT5
Organism: Mus musculus/domesticus
Length: 236  
Fragment?: false
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Protein
D3Z549
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: true
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Protein
Q3TRI2
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: false
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Protein
A2AM80
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
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Protein
E0CYH9
Organism: Mus musculus/domesticus
Length: 228  
Fragment?: true
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Protein
A0A0A0MQI4
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: true
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Protein
D3Z1E8
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: true
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Protein
F6TQN9
Organism: Mus musculus/domesticus
Length: 634  
Fragment?: true
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Protein
F2Z465
Organism: Mus musculus/domesticus
Length: 258  
Fragment?: false
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Protein
H7BX82
Organism: Mus musculus/domesticus
Length: 839  
Fragment?: true
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Protein
E9PX84
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: false
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Protein
A0A0R4J104
Organism: Mus musculus/domesticus
Length: 766  
Fragment?: false
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Protein
B2RRQ8
Organism: Mus musculus/domesticus
Length: 555  
Fragment?: false
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Protein
Q3UGH2
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: false
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Protein
Q8K2Y9
Organism: Mus musculus/domesticus
Length: 453  
Fragment?: false
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Protein
Q9QZS3
Organism: Mus musculus/domesticus
Length: 653  
Fragment?: false
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Protein
Q3UBG2
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
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Protein
Q8BUP8
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: false
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Protein
O08919
Organism: Mus musculus/domesticus
Length: 604  
Fragment?: false
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Protein
Q3UUV3
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: false
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Protein
Q80Y77
Organism: Mus musculus/domesticus
Length: 384  
Fragment?: false
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Protein
Q9R021
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: true
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Protein
Q3TXH9
Organism: Mus musculus/domesticus
Length: 768  
Fragment?: true
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Protein
Q8R1Y7
Organism: Mus musculus/domesticus
Length: 292  
Fragment?: true
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Protein
E0CXR5
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: true
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Protein
Q3UH86
Organism: Mus musculus/domesticus
Length: 563  
Fragment?: false
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Protein
Q3ZAX3
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: false
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Protein
Q3T9N0
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
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Protein
A0A1B0GR67
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: true
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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Cambridge CB2 3EH, United Kingdom