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Search results 201 to 226 out of 226 for Cand2

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Type Details Score
Publication
22206669 | -
First Author: Jin G
Year: 2012
Journal: Biochem Biophys Res Commun
Title: Two G-protein-coupled-receptor candidates, Cand2 and Cand7, are involved in Arabidopsis root growth mediated by the bacterial quorum-sensing signals N-acyl-homoserine lactones.
Volume: 417
Issue: 3
Pages: 991-5
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Protein
Q6ZQ73
Organism: Mus musculus/domesticus
Length: 1235  
Fragment?: false
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Allele
Cand2<em1Smoc> | MGI:7288629
Name: cullin associated and neddylation dissociated 2 (putative); endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Conditional ready, No functional change
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Protein
Q99MU1
Organism: Mus musculus/domesticus
Length: 369  
Fragment?: false
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Protein
D3Z018
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: true
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Protein
A0A0N4SUW2
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Protein
A0A0N4SVI2
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
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Protein
A0A0N4SVH0
Organism: Mus musculus/domesticus
Length: 222  
Fragment?: true
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Protein
A0A0N4SW75
Organism: Mus musculus/domesticus
Length: 222  
Fragment?: false
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Protein
A0A0N4SW46
Organism: Mus musculus/domesticus
Length: 230  
Fragment?: true
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Publication
29702752 | -
First Author: Wei J
Year: 2018
Journal: J Pineal Res
Title: Phytomelatonin receptor PMTR1-mediated signaling regulates stomatal closure in Arabidopsis thaliana.
Volume: 65
Issue: 2
Pages: e12500
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Protein Domain
IPR018781 | TPRA1/CAND2/CAND8
Type: Family
Description: This family of membrane proteins are conserved from plants to humans, including CAND2 and CAND8 from Arabidopsis. CAND2 and CAND8 are predicted G-protein coupled receptors []. CAND2 plays a role in plants and microbes interactions []and acts as a phytomelatonin receptor that regulates stomatal closure through the Galpha subunit-mediated H2O2 production and Ca2 flux dynamics [].
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Publication
18671868 | -
First Author: Gookin TE
Year: 2008
Journal: Genome Biol
Title: Whole proteome identification of plant candidate G-protein coupled receptors in Arabidopsis, rice, and poplar: computational prediction and in-vivo protein coupling.
Volume: 9
Issue: 7
Pages: R120
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Publication
31426861 | J:284276
First Author: Koskimäki J
Year: 2019
Journal: Acta Neuropathol Commun
Title: Transcriptome clarifies mechanisms of lesion genesis versus progression in models of Ccm3 cerebral cavernous malformations.
Volume: 7
Issue: 1
Pages: 132
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Publication
12504026 | -
First Author: Zheng J
Year: 2002
Journal: Mol Cell
Title: CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex.
Volume: 10
Issue: 6
Pages: 1519-26
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Publication
12504025 | -
First Author: Liu J
Year: 2002
Journal: Mol Cell
Title: NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases.
Volume: 10
Issue: 6
Pages: 1511-8
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Publication
12609982 | -
First Author: Min KW
Year: 2003
Journal: J Biol Chem
Title: TIP120A associates with cullins and modulates ubiquitin ligase activity.
Volume: 278
Issue: 18
Pages: 15905-10
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Publication
16449638 | -
First Author: Lo SC
Year: 2006
Journal: Mol Cell Biol
Title: CAND1-mediated substrate adaptor recycling is required for efficient repression of Nrf2 by Keap1.
Volume: 26
Issue: 4
Pages: 1235-44
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Publication
23453757 | -
First Author: Pierce NW
Year: 2013
Journal: Cell
Title: Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins.
Volume: 153
Issue: 1
Pages: 206-15
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Protein Domain
IPR039852 | CAND1/CAND2
Type: Family
Description: This entry includes cullin-associated NEDD8-dissociated proteins 1 (CAND1 also known as TIP120A) and 2 (CAND2); these proteins have a C-terminal TATA-binding protein interacting (TIP20) domain. CAND1 is required for the assembly of the SCF E3 ubiquitin ligase complex. The SCF ubiquitin E3 ligase consists of SKP1, CUL1 and F-box protein, and it regulates ubiquitin-dependent proteolysis. CAND1 binds to CUL1, preventing it from associating with the other components that form the ligase. Neddylation of CUL1 (or the presence of SKP1 and ATP) dissociates it from CAND1, allowing the ligase complex to form [, , ]. CAND1 also interacts with CUL3, a component of the Cul3-dependent E3 ubiquitin ligase complex []. CAND1 has been proposed to be an F-box protein exchange factor, and as substrates of the ligase complex are degraded by the proteasome and depleted, the ligase complex enters an intermediate, deneddylated state when CAND1 can bind, promoting dissociation of the substrate-recognition subunit and recruitment of a new substrate-recognition subunit []. CAND2 is uncharacterized but is assumed to have similar roles to CAND1.
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Protein
Q9CSM7
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: false
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Protein
Q6ZQ38
Organism: Mus musculus/domesticus
Length: 1230  
Fragment?: false
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Protein
Q3UM57
Organism: Mus musculus/domesticus
Length: 1235  
Fragment?: false
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Protein
Q3TD19
Organism: Mus musculus/domesticus
Length: 487  
Fragment?: true
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Protein
D3YWC5
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: true
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Protein
Q3UMI9
Organism: Mus musculus/domesticus
Length: 700  
Fragment?: true
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