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Search results 101 to 140 out of 140 for Arf5

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Type Details Score
Publication
12058076 | -
First Author: Liu Y
Year: 2002
Journal: Mol Biol Cell
Title: The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly.
Volume: 13
Issue: 6
Pages: 2147-56
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Publication
11062263 | -
First Author: Jackson TR
Year: 2000
Journal: J Cell Biol
Title: ACAPs are arf6 GTPase-activating proteins that function in the cell periphery.
Volume: 151
Issue: 3
Pages: 627-38
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Protein Domain
IPR033742 | IQSEC_PH
Type: Domain
Description: The IQSEC (IQ motif and SEC7 domain-containing protein), also called BRAG (Brefeldin A-resistant Arf-gunanine nucleotide exchange factor) family are a subset of Arf GEFs that have been shown to activate Arf6, which acts in the endocytic pathway to control the trafficking of a subset of cargo proteins including integrins. IQSEC family also have key roles in the function and organization of distinct excitatory and inhibitory synapses in the retina [, ]. The family consists of 3 members: IQSEC1 (also called BRAG2/GEP100), IQSEC2 (also called BRAG1), and IQSEC3 (also called SynArfGEF, BRAG3, or KIAA1110). IQSEC1 interacts with clathrin and modulates cell adhesion by regulating integrin surface expression and in addition to Arf6, it also activates the class II Arfs, Arf4 and Arf5 []. Mutations in IQSEC2 cause non-syndromic X-linked intellectual disability as well as reduced activation of Arf substrates (Arf1, Arf6) []. IQSEC3 regulates Arf6 at inhibitory synapses and associates with the dystrophin-associated glycoprotein complex and S-SCAM [].These IQSEC family members contain a IQ domain that may bind calmodulin, a PH domain that is thought to mediate membrane localization, and a SEC7 domain that can promote GEF activity on ARF []. The PH domain of BRAG2 has been shown to potentiate nucleotide exchange by binding to polyanionic membranes without marked phosphoinositides preference [].
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Publication
11950392 | -
First Author: Takatsu H
Year: 2002
Journal: Biochem J
Title: GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors.
Volume: 365
Issue: Pt 2
Pages: 369-78
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Publication
16461286 | -
First Author: Dunphy JL
Year: 2006
Journal: Curr Biol
Title: The Arf6 GEF GEP100/BRAG2 regulates cell adhesion by controlling endocytosis of beta1 integrins.
Volume: 16
Issue: 3
Pages: 315-20
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Publication
22815487 | -
First Author: Moravec R
Year: 2012
Journal: J Biol Chem
Title: BRAG2/GEP100/IQSec1 interacts with clathrin and regulates α5β1 integrin endocytosis through activation of ADP ribosylation factor 5 (Arf5).
Volume: 287
Issue: 37
Pages: 31138-47
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Publication
17850229 | -
First Author: Casanova JE
Year: 2007
Journal: Traffic
Title: Regulation of Arf activation: the Sec7 family of guanine nucleotide exchange factors.
Volume: 8
Issue: 11
Pages: 1476-85
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Publication
15979507 | -
First Author: Donaldson JG
Year: 2005
Journal: Biochim Biophys Acta
Title: Multiple activities for Arf1 at the Golgi complex.
Volume: 1744
Issue: 3
Pages: 364-73
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Publication
15728366 | -
First Author: Deretic D
Year: 2005
Journal: Proc Natl Acad Sci U S A
Title: Rhodopsin C terminus, the site of mutations causing retinal disease, regulates trafficking by binding to ADP-ribosylation factor 4 (ARF4).
Volume: 102
Issue: 9
Pages: 3301-6
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Publication
16030262 | -
First Author: Volpicelli-Daley LA
Year: 2005
Journal: Mol Biol Cell
Title: Isoform-selective effects of the depletion of ADP-ribosylation factors 1-5 on membrane traffic.
Volume: 16
Issue: 10
Pages: 4495-508
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Publication
12446727 | -
First Author: Kim SW
Year: 2003
Journal: J Biol Chem
Title: ADP-ribosylation factor 4 small GTPase mediates epidermal growth factor receptor-dependent phospholipase D2 activation.
Volume: 278
Issue: 4
Pages: 2661-8
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Protein Domain
IPR045872 | Arf1-5-like
Type: Family
Description: Arf GTPases are involved in the formation of coated carrier vesicles by recruiting coat proteins. This entry includes Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned []. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins []. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor []. Arf4 has also been shown to recognise the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialised post-Golgi rhodopsin transport carriers (RTCs) []. There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs) [].
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Protein
Q3TES0
Organism: Mus musculus/domesticus
Length: 1195  
Fragment?: false
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Protein
Q8R0S2
Organism: Mus musculus/domesticus
Length: 961  
Fragment?: false
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Protein
A4GZ26
Organism: Mus musculus/domesticus
Length: 1479  
Fragment?: false
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Protein
E9PUA3
Organism: Mus musculus/domesticus
Length: 1099  
Fragment?: false
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Protein
A0A1D5RM83
Organism: Mus musculus/domesticus
Length: 1051  
Fragment?: false
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Protein
Q3UHJ6
Organism: Mus musculus/domesticus
Length: 766  
Fragment?: false
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Protein
A0A5F8MPT9
Organism: Mus musculus/domesticus
Length: 788  
Fragment?: true
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Protein
Q5DU25
Organism: Mus musculus/domesticus
Length: 1478  
Fragment?: false
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Protein
D3Z6V7
Organism: Mus musculus/domesticus
Length: 949  
Fragment?: false
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Protein
D3Z5I6
Organism: Mus musculus/domesticus
Length: 1154  
Fragment?: false
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Protein
E9QAD8
Organism: Mus musculus/domesticus
Length: 1488  
Fragment?: false
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Protein
P61750
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
P84084
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
Q8BSL7
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
P61205
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
P84078
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
Q9DD04
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
Q3U344
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
Q14BR4
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
Q9QWY8
Organism: Mus musculus/domesticus
Length: 1147  
Fragment?: false
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Protein
Q3UJA5
Organism: Mus musculus/domesticus
Length: 1087  
Fragment?: false
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Protein
E9QN63
Organism: Mus musculus/domesticus
Length: 1147  
Fragment?: false
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Protein
H3BKD4
Organism: Mus musculus/domesticus
Length: 1075  
Fragment?: false
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Protein
E9QMI7
Organism: Mus musculus/domesticus
Length: 1090  
Fragment?: false
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Protein
H3BL41
Organism: Mus musculus/domesticus
Length: 1124  
Fragment?: false
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Protein
H3BKE6
Organism: Mus musculus/domesticus
Length: 1087  
Fragment?: false
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Protein
E9QMJ1
Organism: Mus musculus/domesticus
Length: 1112  
Fragment?: false
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Protein
H3BJY2
Organism: Mus musculus/domesticus
Length: 1144  
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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