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Search results 101 to 162 out of 162 for Arl2

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Type Details Score
Publication
18588884 | -
First Author: Veltel S
Year: 2008
Journal: FEBS Lett
Title: Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-GAP complex.
Volume: 582
Issue: 17
Pages: 2501-7
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Protein
D3YVP4
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: true
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Protein Domain
IPR044994 | TBCE
Type: Family
Description: Tubulin proteostasis is regulated by a group of molecular chaperones termed tubulin cofactors (TBC). This entry represents TBCE (tubulin-specific chaperone E), which is an alpha-tubulin binding protein that, together with Arl2 and cofactors D (TBCD), A (TBCA or p14), B (TBCB) and C (TBCC), participate in tubulin biogenesis []. TBCE contains an N-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain, a leucine-rich repeat protein-protein interaction domain followed by leucine-rich repeat (LRR) domains, and a C-terminal ubiquitin-like (Ubl) domain [].Mutations in TBCE gene cause the Kenny-Caffey/Sanjad-Sakati syndrome, characterised by hypoparathyroidism, mental retardation and facial dysmorphism [].
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Protein
B1ATU0
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: true
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Protein
F6UI15
Organism: Mus musculus/domesticus
Length: 72  
Fragment?: true
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Publication
24616099 | -
First Author: Ivanova AA
Year: 2014
Journal: J Biol Chem
Title: Characterization of recombinant ELMOD (cell engulfment and motility domain) proteins as GTPase-activating proteins (GAPs) for ARF family GTPases.
Volume: 289
Issue: 16
Pages: 11111-21
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Protein Domain
IPR033162 | TBCD
Type: Family
Description: The tubulin heterodimer consists of one alpha- and one beta-tubulin polypeptide. In humans, five tubulin-specific chaperones termed TBCA/B/C/D/E are essential for bring the alpha- and beta-tubulin subunits together into a tightly associated heterodimer. Following the generation of quasi-native beta- and alpha-tubulin polypeptides (via multiple rounds of ATP-dependent interaction with the cytosolic chaperonin), TBCA and TBCB bind to and stabilise newly synthesised beta- and alpha-tubulin, respectively. The exchange of beta-tubulin between TBCA and TBCD, and of alpha-tubulin between TBCB and TBCE, resulting in the formation of TBCD/beta and TBCE/alpha. These two complexes then interact with each other and form a supercomplex (TBCE/alpha/TBCD/beta). Interaction of the supercomplex with TBCC causes the disassembly of the supercomplex and the release of E-site GDP-bound alpha/beta tubulin heterodimer, which becomes polymerization competent following spontaneous exchange with GTP [].This entry represents tubulin-folding cofactor D (TBCD) and its homologues. Its ability to interact with beta tubulin is regulated via its interaction with ARL2 (ADP ribosylation factor-like protein 2), a small monomeric G protein. ARL2 inhibits the beta-tubulin GTPase activating protein (GAP) activity of TBCD, and its interaction with native tubulin dimers [, ].
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Publication
9819391 | J:51174
First Author: Brown MT
Year: 1998
Journal: Mol Cell Biol
Title: ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src.
Volume: 18
Issue: 12
Pages: 7038-51
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Publication
10980193 | J:65970
First Author: Lin CY
Year: 2000
Journal: J Biol Chem
Title: ARL4, an ARF-like protein that is developmentally regulated and localized to nuclei and nucleoli.
Volume: 275
Issue: 48
Pages: 37815-23
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Publication
31628468 | J:293683
First Author: Li W
Year: 2019
Journal: Hum Mol Genet
Title: Elmod3 knockout leads to progressive hearing loss and abnormalities in cochlear hair cell stereocilia.
Volume: 28
Issue: 24
Pages: 4103-4112
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Publication
30446707 | J:268484
First Author: Wright ZC
Year: 2018
Journal: Sci Rep
Title: ADP-Ribosylation Factor-Like 2 (ARL2) regulates cilia stability and development of outer segments in rod photoreceptor neurons.
Volume: 8
Issue: 1
Pages: 16967
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Publication
23014990 | -
First Author: East MP
Year: 2012
Journal: J Biol Chem
Title: ELMO domains, evolutionary and functional characterization of a novel GTPase-activating protein (GAP) domain for Arf protein family GTPases.
Volume: 287
Issue: 47
Pages: 39538-53
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Publication
18376416 | J:169883
First Author: Veltel S
Year: 2008
Journal: Nat Struct Mol Biol
Title: The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3.
Volume: 15
Issue: 4
Pages: 373-80
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Publication
22558334 | J:187273
First Author: Johnson KR
Year: 2012
Journal: PLoS One
Title: Mutations of the mouse ELMO domain containing 1 gene (Elmod1) link small GTPase signaling to actin cytoskeleton dynamics in hair cell stereocilia.
Volume: 7
Issue: 4
Pages: e36074
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Publication
19966137 | -
First Author: Pulkkinen V
Year: 2010
Journal: FASEB J
Title: ELMOD2, a candidate gene for idiopathic pulmonary fibrosis, regulates antiviral responses.
Volume: 24
Issue: 4
Pages: 1167-77
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Publication
16773575 | -
First Author: Hodgson U
Year: 2006
Journal: Am J Hum Genet
Title: ELMOD2 is a candidate gene for familial idiopathic pulmonary fibrosis.
Volume: 79
Issue: 1
Pages: 149-54
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Publication
21613931 | -
First Author: Lawson WE
Year: 2011
Journal: Am J Med Sci
Title: Genetics in pulmonary fibrosis--familial cases provide clues to the pathogenesis of idiopathic pulmonary fibrosis.
Volume: 341
Issue: 6
Pages: 439-43
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Protein Domain
IPR030731 | ELMOD3
Type: Family
Description: ELMOD3 (ELMO domain-containing protein 3) is an GTPase-activating protein that acts on Arl2 GTPase. A mutation in the ELMOD3 gene is associated with hearing impairment in humans [].There are six ELMO domain containing proteins identified in humans. They can be classified into two subgroups, ELMOs and ELMODs, according to protein size and domain architecture []. ELMOs are approximately twice as large as ELMODs and contain multiple domains. The function of the ELMO domain is not clear. ELMOs and ELMODs seem to have distinct cellular and biochemical functions. ELMOs interact with DOCKs and enhance the GEF activity of DOCKs, while ELMODs may play a general role in integrating signalling pathways controlled by Arls and other GTPases [, ].
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Protein Domain
IPR030724 | ELMOD2
Type: Family
Description: ELMOD2 is an GTPase-activating protein that acts on Arl2 and Arf GTPases [, ]. It has been implicated in idiopathic pulmonary fibrosis (IPF) [, ]. It has also being shown to regulate antiviral responses [].There are six ELMO domain containing proteins identified in humans. They can be classified into two subgroups, ELMOs and ELMODs, according to protein size and domain architecture []. ELMOs are approximately twice as large as ELMODs and contain multiple domains. The function of the ELMO domain is not clear. ELMOs and ELMODs seem to have distinct cellular and biochemical functions. ELMOs interact with DOCKs and enhance the GEF activity of DOCKs, while ELMODs may play a general role in integrating signalling pathways controlled by Arls and other GTPases [, ].
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Protein Domain
IPR030722 | ELMOD1
Type: Family
Description: ELMOD1 is an ELMO domain containing protein that activates Arl2 GTPase []and possibly other GTPases of the Arf family []. Mutations in the mouse ELMOD1 gene cause cochlear hair cell dysfunction and hearing loss []. There are six ELMO domain containing proteins identified in humans. They can be classified into two subgroups, ELMOs and ELMODs, according to protein size and domain architecture []. ELMOs are approximately twice as large as ELMODs and contain multiple domains. The function of the ELMO domain is not clear. ELMOs and ELMODs seem to have distinct cellular and biochemical functions. ELMOs interact with DOCKs and enhance the GEF activity of DOCKs, while ELMODs may play a general role in integrating signalling pathways controlled by Arls and other GTPases [, ].
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Protein
Q3V1U8
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
Q8BGF6
Organism: Mus musculus/domesticus
Length: 293  
Fragment?: false
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Protein
Q91YP6
Organism: Mus musculus/domesticus
Length: 381  
Fragment?: false
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Protein
Q3TPW1
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
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Protein
Q8BHN8
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
B7ZN22
Organism: Mus musculus/domesticus
Length: 269  
Fragment?: false
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Protein
B7ZN20
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: true
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Protein
A0A0U1RPA9
Organism: Mus musculus/domesticus
Length: 213  
Fragment?: true
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Protein
E9Q0K9
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
Q0P556
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: true
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Protein
A0A1B0GRZ8
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: true
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Protein
Q8BHP4
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: false
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Protein
Q8CHC0
Organism: Mus musculus/domesticus
Length: 352  
Fragment?: true
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Protein
Q8R199
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: true
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Publication
12225668 | -
First Author: Kirik V
Year: 2002
Journal: Curr Biol
Title: Functional analysis of the tubulin-folding cofactor C in Arabidopsis thaliana.
Volume: 12
Issue: 17
Pages: 1519-23
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Publication
25908846 | -
First Author: Serna M
Year: 2015
Journal: J Cell Sci
Title: The structure of the complex between α-tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism.
Volume: 128
Issue: 9
Pages: 1824-34
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Publication
12389028 | -
First Author: Parvari R
Year: 2002
Journal: Nat Genet
Title: Mutation of TBCE causes hypoparathyroidism-retardation-dysmorphism and autosomal recessive Kenny-Caffey syndrome.
Volume: 32
Issue: 3
Pages: 448-52
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Protein Domain
IPR006816 | ELMO_dom
Type: Domain
Description: This entry represents the ELMO (EnguLfment and Cell MOtility) domain, which is found in a number of eukaryotic proteins involved in the cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility, including CED-12, ELMO-1 and ELMO-2. ELMO-1 and ELMO-2 are components of signalling pathways that regulate phagocytosis and cell migration and are mammalian orthologues of the Caenorhabditis elegans gene, ced-12 that is required for the engulfment of dying cells and cell migration. ELMO-1/2 act in association with DOCK1 and CRK. ELMO-1/2 interact with the SH3-domain of DOCK1 via an SH3-binding site to enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1. ELMO-1/2 could be part of a complex with DOCK1 and Rac1 that could be required to activate Rac Rho small GTPases. Regulatory GTPases in the Ras superfamily employ a cycle of alternating GTP binding and hydrolysis, controlled by guanine nucleotide exchange factors and GTPase-activating proteins (GAPs), as essential features of their actions in cells. Within the Ras superfamily, the Arf family is composed of 30 members, including 22 Arf-like (Arl) proteins. The ELMO domain has been proposed to be a GAP domain for ARL2 and other members of the Arf family [].
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Protein
Q8BYA0
Organism: Mus musculus/domesticus
Length: 1196  
Fragment?: false
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Protein
Q9WUL7
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: false
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Protein
Q543P7
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: false
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Protein
A0A494BAJ6
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
E0CZ81
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
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Protein
A0A1Y7VIX9
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
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Publication
23973072 | -
 
First Author: Tian G
Year: 2013
Journal: Methods Cell Biol
Title: Tubulin-specific chaperones: components of a molecular machine that assembles the α/β heterodimer.
Volume: 115
Pages: 155-71
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Protein
Q8C5W3
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: false
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Protein
O55057
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
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Protein
Q8CIV8
Organism: Mus musculus/domesticus
Length: 524  
Fragment?: false
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Protein
Q8VCN9
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: false
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Protein
Q05D34
Organism: Mus musculus/domesticus
Length: 590  
Fragment?: false
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Protein
Q3TZG4
Organism: Mus musculus/domesticus
Length: 506  
Fragment?: false
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Protein
Q3URU9
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
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Protein
F6YXR3
Organism: Mus musculus/domesticus
Length: 290  
Fragment?: true
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Protein
Q3TDQ8
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
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Protein
A0A0R4J0M1
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: false
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Protein
Q8BHL5
Organism: Mus musculus/domesticus
Length: 732  
Fragment?: false
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Protein
Q8BYZ7
Organism: Mus musculus/domesticus
Length: 720  
Fragment?: false
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Protein
Q8BPU7
Organism: Mus musculus/domesticus
Length: 727  
Fragment?: false
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Protein
Q640P7
Organism: Mus musculus/domesticus
Length: 552  
Fragment?: false
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Protein
Q571D6
Organism: Mus musculus/domesticus
Length: 741  
Fragment?: true
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Protein
A0A1D5RMK9
Organism: Mus musculus/domesticus
Length: 703  
Fragment?: false
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Protein
Q9EPK2
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: false
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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