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Search results 401 to 500 out of 562 for Rhog

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0.028s

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Type Details Score
Publication
15710388 | J:96146
First Author: Nishikimi A
Year: 2005
Journal: FEBS Lett
Title: Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange factor expressed predominantly in lymphocytes.
Volume: 579
Issue: 5
Pages: 1039-46
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Publication
19004829 | -
First Author: Sanders MA
Year: 2009
Journal: J Biol Chem
Title: DOCK5 and DOCK1 regulate Caco-2 intestinal epithelial cell spreading and migration on collagen IV.
Volume: 284
Issue: 1
Pages: 27-35
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Publication
12637522 | J:83589
First Author: Rossman KL
Year: 2003
Journal: J Biol Chem
Title: Multifunctional roles for the PH domain of Dbs in regulating Rho GTPase activation.
Volume: 278
Issue: 20
Pages: 18393-400
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Publication
23536706 | -
First Author: Ueda S
Year: 2013
Journal: Mol Biol Cell
Title: Rac GEF Dock4 interacts with cortactin to regulate dendritic spine formation.
Volume: 24
Issue: 10
Pages: 1602-13
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Protein Domain
IPR026796 | DOCK9
Type: Family
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents DOCK9 (also known as Zizimin). DOCK9 and DOCK11 activate Cdc42 [, ].
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Protein Domain
IPR026799 | DOCK_2
Type: Family
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents DOCK2 (dedicator of cytokinesis 2). DOCK2 is involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. It activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. It may also participate in IL2 transcriptional activation via the activation of RAC2 [].
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Protein Domain
IPR026800 | DOCK3
Type: Family
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents DOCK3. DOCK3 is linked to Alzheimer disease due to its interaction with presenilin proteins and ability to stimulate Tau/MAPT phosphorylation [].
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Protein Domain
IPR030717 | DOCK5
Type: Family
Description: This entry includes DOCK5, which, along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on collagen IV [].DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) [].
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Protein Domain
IPR037014 | DOCK4
Type: Family
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents DOCK4. DOCK4 plays a critical role in mediating TGF-beta's prometastatic effects in lungcancer [].
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Protein Domain
IPR035732 | VAV2_SH3_2
Type: Domain
Description: VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42 []. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others [, , , , ]. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins [, , ].This entry represents the second SH3 domain of VAV2.
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Protein Domain
IPR035733 | VAV2_SH3_1
Type: Domain
Description: VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42 []. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others [, , , , ]. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins [, , ].This entry represents the first SH3 domain of VAV2.
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Protein Domain
IPR035767 | DOCK3_SH3
Type: Domain
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents the SH3 domain found in DOCK3, which has been linked to Alzheimer's disease due to its interaction with presenilin proteins and ability to stimulate Tau/MAPT phosphorylation [].
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Protein Domain
IPR035769 | DOCK4_SH3
Type: Domain
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents the SH3 domain found in DOCK4. DOCK4 regulates dendritic spine formation and has been linked to autism, dyslexia, and schizophrenia []. It also plays a critical role in mediating TGF-beta's prometastatic effects in lung cancer [].
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Protein Domain
IPR035534 | DBS_PH
Type: Domain
Description: This entry represents the PH domain of guanine nucleotide exchange factor DBS. The DBS PH domain participates in binding to both the Cdc42 and RhoA GTPases []. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner [].DBS, also called MCF2L or OST, functions as a Rho GTPase guanine nucleotide exchange factor (RhoGEF), facilitating the exchange of GDP and GTP. It was originally isolated from a cDNA screen for sequences that cause malignant growth. It plays roles in regulating clathrin-mediated endocytosis and cell migration through its activation of Rac1 and Cdc42 [, ]. Depending on cell type, DBS can also activate RhoA and RhoG [, ]. DBS contains a Sec14-like domain [], spectrin-like repeats, a RhoGEF or Dbl homology (DH) domain, a Pleckstrin homology (PH) domain [], and an SH3 domain.
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Protein Domain
IPR021816 | DOCK_C/D_N
Type: Domain
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents the N-terminal domain of the DOCK-C subfamily (DOCK 6, 7, 8) and DOCK-D subfamily (DOCK 9, 10, 11).
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Publication
17000758 | J:118143
First Author: Kostenko EV
Year: 2006
Journal: Mol Cell Biol
Title: Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs.
Volume: 26
Issue: 23
Pages: 8964-75
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Protein
A0A1B0GS53
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: true
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Protein
Q3TMS1
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
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Publication
22204307 | -
 
First Author: Krause-Gruszczynska M
Year: 2011
Journal: Cell Commun Signal
Title: The signaling pathway of Campylobacter jejuni-induced Cdc42 activation: Role of fibronectin, integrin beta1, tyrosine kinases and guanine exchange factor Vav2.
Volume: 9
Pages: 32
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Publication
20298788 | -
First Author: Moon MS
Year: 2010
Journal: Mol Cell Neurosci
Title: Balanced Vav2 GEF activity regulates neurite outgrowth and branching in vitro and in vivo.
Volume: 44
Issue: 2
Pages: 118-28
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Publication
20140013 | -
First Author: Thalappilly S
Year: 2010
Journal: Oncogene
Title: VAV2 regulates epidermal growth factor receptor endocytosis and degradation.
Volume: 29
Issue: 17
Pages: 2528-39
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Publication
19451809 | -
First Author: Holthusen K
Year: 2009
Journal: Am J Ther
Title: Guanine exchange factor Vav2: a novel potential target for the development of drugs effective in the prevention of papillomavirus infection and disease.
Volume: 16
Issue: 6
Pages: 496-507
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Publication
18434624 | -
First Author: Arora PD
Year: 2008
Journal: Am J Physiol Cell Physiol
Title: Collagen phagocytosis is regulated by the guanine nucleotide exchange factor Vav2.
Volume: 295
Issue: 1
Pages: C130-7
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Publication
19796679 | -
First Author: Miyamoto Y
Year: 2010
Journal: Cell Signal
Title: Cellular signaling of Dock family proteins in neural function.
Volume: 22
Issue: 2
Pages: 175-82
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Publication
19803396 | -
First Author: Katoh H
Year: 2009
Journal: Seikagaku
Title: [Regulation of cell morphology and motility by Dock family proteins].
Volume: 81
Issue: 8
Pages: 711-6
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Protein Coding Gene
MGI:98923 | Vav1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:106211 | Cdc42
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:96610 | Itgb1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P60766
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: false
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Protein
P09055
Organism: Mus musculus/domesticus
Length: 798  
Fragment?: false
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Protein
P27870
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein Domain
IPR037808 | C2_Dock-C
Type: Domain
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents the C2 domain found in the Dock-C members. In addition to the C2 domain (also known as DHR-1 domain) and the DHR-2 domain, Dock-C members contain a functionally uncharacterised domain upstream of the C2 domain. DHR-2 has the catalytic activity for Rac and/or Cdc42, but is structurally unrelated to the DH domain. The C2/DHR-1 domains of Dock1 (also known as Dock180) and Dock4 have been shown to bind phosphatidylinositol-3, 4, 5-triphosphate (PtdIns(3,4,5)P3) [, , ].
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Protein Domain
IPR037809 | C2_Dock-D
Type: Domain
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents the C2 domain of the Dock-D members. In addition to the C2 domain (also known as the DHR-1 domain) and the DHR-2, Dock-D members contain a functionally uncharacterised domain and a PH domain upstream of the C2 domain. DHR-2 has the catalytic activity for Rac and/or Cdc42, but is structurally unrelated to the DH domain. The C2/DHR-1 domains of Dock1 (also known as Dock180) and Dock4 have been shown to bind phosphatidylinositol-3, 4, 5-triphosphate (PtdIns(3,4,5)P3). The PH domain broadly binds to phospholipids and is thought to be involved in targeting the plasma membrane [, , ].
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Protein Domain
IPR037811 | C2_Dock-B
Type: Domain
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents the C2 domain of the Dock-B members. Most of these members have been shown to be GEFs specific for Rac, although Dock4 has also been shown to interact indirectly with the Ras family GTPase Rap1, probably through Rap regulatory proteins. In addition to the C2 domain (also known as DHR-1 domain) and the DHR-2 domain, Dock-B members contain a SH3 domain upstream of the C2 domain and a proline-rich region downstream. DHR-2 has the catalytic activity for Rac and/or Cdc42, but is structurally unrelated to the DH domain. The C2/DHR-1 domains of Dock1 (also known as Dock180) and Dock4 have been shown to bind phosphatidylinositol-3, 4, 5-triphosphate (PtdIns(3,4,5)P3)[, , ].
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Publication
9115846 | -
First Author: Romero F
Year: 1996
Journal: Cell Signal
Title: Structure and function of vav.
Volume: 8
Issue: 8
Pages: 545-53
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Protein
A0A1L1ST98
Organism: Mus musculus/domesticus
Length: 577  
Fragment?: true
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Publication
12432077 | -
First Author: Côté JF
Year: 2002
Journal: J Cell Sci
Title: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity.
Volume: 115
Issue: Pt 24
Pages: 4901-13
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Protein Coding Gene
MGI:97583 | Pik3r1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P26450
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: false
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Protein
Q6A088
Organism: Mus musculus/domesticus
Length: 333  
Fragment?: true
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Publication
20167601 | -
First Author: Premkumar L
Year: 2010
Journal: J Biol Chem
Title: Structural basis of membrane targeting by the Dock180 family of Rho family guanine exchange factors (Rho-GEFs).
Volume: 285
Issue: 17
Pages: 13211-22
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Protein
A0A2I3BRF7
Organism: Mus musculus/domesticus
Length: 132  
Fragment?: true
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Protein
Q8C6J6
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: false
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Publication
8643598 | -
First Author: Debant A
Year: 1996
Journal: Proc Natl Acad Sci U S A
Title: The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains.
Volume: 93
Issue: 11
Pages: 5466-71
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Publication
17391702 | -
First Author: Chhatriwala MK
Year: 2007
Journal: J Mol Biol
Title: The DH and PH domains of Trio coordinately engage Rho GTPases for their efficient activation.
Volume: 368
Issue: 5
Pages: 1307-20
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Publication
9139723 | -
First Author: Alam MR
Year: 1997
Journal: J Biol Chem
Title: Kalirin, a cytosolic protein with spectrin-like and GDP/GTP exchange factor-like domains that interacts with peptidylglycine alpha-amidating monooxygenase, an integral membrane peptide-processing enzyme.
Volume: 272
Issue: 19
Pages: 12667-75
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Publication
11606631 | -
First Author: Penzes P
Year: 2001
Journal: J Neurosci
Title: Distinct roles for the two Rho GDP/GTP exchange factor domains of kalirin in regulation of neurite growth and neuronal morphology.
Volume: 21
Issue: 21
Pages: 8426-34
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Publication
18057561 | -
First Author: Youn H
Year: 2007
Journal: J Alzheimers Dis
Title: Under-expression of Kalirin-7 Increases iNOS activity in cultured cells and correlates to elevated iNOS activity in Alzheimer's disease hippocampus.
Volume: 12
Issue: 3
Pages: 271-81
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Publication
22548195 | -
 
First Author: Mandela P
Year: 2012
Journal: Neural Plast
Title: Kalirin, a key player in synapse formation, is implicated in human diseases.
Volume: 2012
Pages: 728161
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Publication
15215162 | -
First Author: Zheng M
Year: 2004
Journal: Am J Pathol
Title: TRIO amplification and abundant mRNA expression is associated with invasive tumor growth and rapid tumor cell proliferation in urinary bladder cancer.
Volume: 165
Issue: 1
Pages: 63-9
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Publication
30407917 | -
     
First Author: Dufurrena Q
Year: 2018
Journal: J Mol Endocrinol
Title: Kalirin/Trio Rho GDP/GTP exchange factors regulate proinsulin and insulin secretion.
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Publication
17881726 | -
First Author: Ferraro F
Year: 2007
Journal: Mol Biol Cell
Title: Kalirin/Trio Rho guanine nucleotide exchange factors regulate a novel step in secretory granule maturation.
Volume: 18
Issue: 12
Pages: 4813-25
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Publication
12832783 | -
First Author: Skowronek K
Year: 2003
Journal: Acta Crystallogr D Biol Crystallogr
Title: Crystallization and initial crystal characterization of the N-terminal DH/PH domain of Trio.
Volume: 59
Issue: Pt 7
Pages: 1273-5
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Protein Domain
IPR028570 | Kalirin/TRIO
Type: Family
Description: This entry includes a group of RhoGEFs, including Kalirin and TRIO from mammals. Kalirin and TRIO are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and TRIO share the same complex multidomain structure and display several splice variants. They are implicated in secretory granule (SG) maturation and exocytosis [, ]. The longest Kalirin and TRIO proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and TRIO are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner [, ].Triple functional domain protein (TRIO) contains a protein kinase domain and two guanine nucleotide exchange factor (GEF) domains []. These functional domains suggest that it may play a role in signalling pathways controlling cell proliferation []. TRIO may form a complex with LAR transmembrane protein tyrosine phosphatase (PT-Pase), which localises to the ends of focal adhesions and plays an important part in coordinating cell-matrix and cytoskeletal rearrangements necessary for cell migration []. Its expression is associated with invasive tumor growth and rapid tumor cell proliferation in urinary bladder cancer [].Kalirin () promotes the exchange of GDP by GTP and stimulates the activity of specific Rho GTPases []. There are several Kalirin isoforms in humans and mice. Each Kalirin isoform is composed of a unique collection of domains and may have different functions []. In rat, isoforms 1 and 7 are necessary for neuronal development and axonal outgrowth, while isoform 6 is required for dendritic spine formation []. In humans, the major isoform of Kalirin in the adult brain is Kalirin-7, which plays a critical role in spine formation/synaptic plasticity. Kalirin-7 has been linked to neuropsychiatric and neurological diseases such as Alzheimer's, Huntingtin's, ischemic stroke, schizophrenia, depression, and cocaine addiction [, , ].
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Protein
F6VMI1
Organism: Mus musculus/domesticus
Length: 552  
Fragment?: true
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Protein
Q3UYH1
Organism: Mus musculus/domesticus
Length: 279  
Fragment?: true
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Protein
A0A087WQA1
Organism: Mus musculus/domesticus
Length: 546  
Fragment?: true
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Protein
Q3US86
Organism: Mus musculus/domesticus
Length: 557  
Fragment?: true
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Protein
F6YXW9
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: true
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Protein
A0A0U1RNY4
Organism: Mus musculus/domesticus
Length: 811  
Fragment?: true
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Protein
A0A1L1STJ1
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: true
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Protein
Q8BLX9
Organism: Mus musculus/domesticus
Length: 373  
Fragment?: true
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Publication
16107646 | J:100324
First Author: Bulfone A
Year: 2005
Journal: J Neurosci
Title: Telencephalic embryonic subtractive sequences: a unique collection of neurodevelopmental genes.
Volume: 25
Issue: 33
Pages: 7586-600
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•
•
Protein
Q8VDR9
Organism: Mus musculus/domesticus
Length: 2080  
Fragment?: false
•
•
•
•
•
Protein
Q8R1A4
Organism: Mus musculus/domesticus
Length: 2130  
Fragment?: false
•
•
•
•
•
Protein
A0A1L1SQR4
Organism: Mus musculus/domesticus
Length: 2111  
Fragment?: false
•
•
•
•
•
Protein
Q6ZPS1
Organism: Mus musculus/domesticus
Length: 1909  
Fragment?: true
•
•
•
•
•
Protein
A0A0U1RNK7
Organism: Mus musculus/domesticus
Length: 2098  
Fragment?: false
•
•
•
•
•
Protein
A2A9M5
Organism: Mus musculus/domesticus
Length: 2128  
Fragment?: false
•
•
•
•
•
Protein
E9PX48
Organism: Mus musculus/domesticus
Length: 2100  
Fragment?: false
•
•
•
•
•
Protein
A2A9M4
Organism: Mus musculus/domesticus
Length: 2130  
Fragment?: false
•
•
•
•
•
Protein
Q8BIK4
Organism: Mus musculus/domesticus
Length: 2055  
Fragment?: false
•
•
•
•
•
Protein
F8VPN7
Organism: Mus musculus/domesticus
Length: 2113  
Fragment?: false
•
•
•
•
•
Protein
B2RY79
Organism: Mus musculus/domesticus
Length: 2058  
Fragment?: false
•
•
•
•
•
Protein
A0A1D5RMM1
Organism: Mus musculus/domesticus
Length: 2088  
Fragment?: false
•
•
•
•
•
Protein
A0A1D5RLE0
Organism: Mus musculus/domesticus
Length: 2042  
Fragment?: false
•
•
•
•
•
Protein
E9QMR2
Organism: Mus musculus/domesticus
Length: 2058  
Fragment?: false
•
•
•
•
•
Protein
A0A0U1RP53
Organism: Mus musculus/domesticus
Length: 102  
Fragment?: true
•
•
•
•
•
Protein
A0A5F8MPL9
Organism: Mus musculus/domesticus
Length: 2055  
Fragment?: false
•
•
•
•
•
Protein
B2RXS7
Organism: Mus musculus/domesticus
Length: 2088  
Fragment?: false
•
•
•
•
•
Protein
A0A0U1RPH6
Organism: Mus musculus/domesticus
Length: 46  
Fragment?: true
•
•
•
•
•
Protein
A0A2I3BRK3
Organism: Mus musculus/domesticus
Length: 178  
Fragment?: true
•
•
•
•
•
Protein
Q8BMP2
Organism: Mus musculus/domesticus
Length: 1134  
Fragment?: false
•
•
•
•
•
Protein
B2RY08
Organism: Mus musculus/domesticus
Length: 2042  
Fragment?: false
•
•
•
•
•
Publication
9285789 | -
First Author: Colomer V
Year: 1997
Journal: Hum Mol Genet
Title: Huntingtin-associated protein 1 (HAP1) binds to a Trio-like polypeptide, with a rac1 guanine nucleotide exchange factor domain.
Volume: 6
Issue: 9
Pages: 1519-25
•
•
•
•
•
Publication
12172552 | -
First Author: Meller N
Year: 2002
Journal: Nat Cell Biol
Title: Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins.
Volume: 4
Issue: 9
Pages: 639-47
•
•
•
•
•
Protein
Q6PF84
Organism: Mus musculus/domesticus
Length: 738  
Fragment?: false
•
•
•
•
•
Publication
15886116 | -
First Author: Tybulewicz VL
Year: 2005
Journal: Curr Opin Immunol
Title: Vav-family proteins in T-cell signalling.
Volume: 17
Issue: 3
Pages: 267-74
•
•
•
•
•
Protein
Q8BZN6
Organism: Mus musculus/domesticus
Length: 2150  
Fragment?: false
•
•
•
•
•
Protein
A2AF47
Organism: Mus musculus/domesticus
Length: 2073  
Fragment?: false
•
•
•
•
•
Protein
Q8C147
Organism: Mus musculus/domesticus
Length: 2100  
Fragment?: false
•
•
•
•
•
Protein
A0A2X0U2I4
Organism: Mus musculus/domesticus
Length: 2008  
Fragment?: false
•
•
•
•
•
Protein
Q3UHH9
Organism: Mus musculus/domesticus
Length: 1601  
Fragment?: true
•
•
•
•
•
Protein
B9EJ70
Organism: Mus musculus/domesticus
Length: 2100  
Fragment?: false
•
•
•
•
•
Protein
Q7TN11
Organism: Mus musculus/domesticus
Length: 1920  
Fragment?: true
•
•
•
•
•
Protein
A0A087WQ86
Organism: Mus musculus/domesticus
Length: 2175  
Fragment?: false
•
•
•
•
•
Protein
E9QM99
Organism: Mus musculus/domesticus
Length: 2187  
Fragment?: false
•
•
•
•
•
Protein
A0A087WRP5
Organism: Mus musculus/domesticus
Length: 2151  
Fragment?: false
•
•
•
•
•
Protein
B2RWY0
Organism: Mus musculus/domesticus
Length: 2150  
Fragment?: false
•
•
•
•
•
Protein
Q6A0A3
Organism: Mus musculus/domesticus
Length: 1567  
Fragment?: true
•
•
•
•
•




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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom