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Search results 201 to 300 out of 366 for Cul1

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Type Details Score
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 Coding Gene
MGI:1914729 | Tmem183a
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2442569 | Fbxo48
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:3505735 | Fbxo39
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2448488 | Fbxl16
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1354755 | Fbxo15
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1914072 | Fbxo25
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
12972599 | J:85761
First Author: Lykke-Andersen K
Year: 2003
Journal: Mol Cell Biol
Title: Disruption of the COP9 signalosome Csn2 subunit in mice causes deficient cell proliferation, accumulation of p53 and cyclin E, and early embryonic death.
Volume: 23
Issue: 19
Pages: 6790-7
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Publication
15917222 | J:209489
First Author: Shirogane T
Year: 2005
Journal: J Biol Chem
Title: SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein.
Volume: 280
Issue: 29
Pages: 26863-72
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Publication
21247897 | J:262901
First Author: Huang G
Year: 2011
Journal: J Biol Chem
Title: SCCRO (DCUN1D1) promotes nuclear translocation and assembly of the neddylation E3 complex.
Volume: 286
Issue: 12
Pages: 10297-304
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Publication
10485847 | J:219114
First Author: Freed E
Year: 1999
Journal: Genes Dev
Title: Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle.
Volume: 13
Issue: 17
Pages: 2242-57
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Publication
12481031 | J:85470
First Author: Dias DC
Year: 2002
Journal: Proc Natl Acad Sci U S A
Title: CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex.
Volume: 99
Issue: 26
Pages: 16601-6
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Publication
29070679 | J:253425
First Author: Chen F
Year: 2017
Journal: J Biol Chem
Title: The E3 ubiquitin ligase SCFFBXL14 complex stimulates neuronal differentiation by targeting the Notch signaling factor HES1 for proteolysis.
Volume: 292
Issue: 49
Pages: 20100-20112
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Publication
30653357 | J:288598
First Author: Wan P
Year: 2019
Journal: FASEB J
Title: Cullin1 binds and promotes NLRP3 ubiquitination to repress systematic inflammasome activation.
Volume: 33
Issue: 4
Pages: 5793-5807
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Protein
E0CYT5
Organism: Mus musculus/domesticus
Length: 582  
Fragment?: true
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Protein
Q3TLY0
Organism: Mus musculus/domesticus
Length: 265  
Fragment?: false
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Protein
A0A3Q4EBZ1
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: false
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Protein
F6ZZK0
Organism: Mus musculus/domesticus
Length: 85  
Fragment?: true
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Protein
Q05CY9
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: true
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Protein
D3Z2H3
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
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Protein
Q3UD60
Organism: Mus musculus/domesticus
Length: 433  
Fragment?: true
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Protein
F6UV36
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: true
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Protein
E9PXT5
Organism: Mus musculus/domesticus
Length: 265  
Fragment?: false
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Protein
Q78GU9
Organism: Mus musculus/domesticus
Length: 252  
Fragment?: false
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Publication
8681378 | -
First Author: Kipreos ET
Year: 1996
Journal: Cell
Title: cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family.
Volume: 85
Issue: 6
Pages: 829-39
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Publication
15537541 | -
First Author: Goldenberg SJ
Year: 2004
Journal: Cell
Title: Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases.
Volume: 119
Issue: 4
Pages: 517-28
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Publication
15688063 | -
First Author: Petroski MD
Year: 2005
Journal: Nat Rev Mol Cell Biol
Title: Function and regulation of cullin-RING ubiquitin ligases.
Volume: 6
Issue: 1
Pages: 9-20
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Protein
H7BX52
Organism: Mus musculus/domesticus
Length: 90  
Fragment?: false
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Protein
Q9CSM7
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: false
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Protein Coding Gene
MGI:2442921 | Fbxl21
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1929084 | Fbxo3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2140367 | Fbxl4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1921896 | Spsb1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2141676 | Fbxl14
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1315199 | Spsb2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913599 | Dmac2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:3643620 | Cks1brt
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
A0A0N4SUW1
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: false
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Publication
12183637 | -
First Author: Cope GA
Year: 2002
Journal: Science
Title: Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1.
Volume: 298
Issue: 5593
Pages: 608-11
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Protein Domain
IPR016157 | Cullin_CS
Type: Conserved_site
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact with specific adaptor proteins [, , ].This entry represents a conserved site found in various cullin proteins.
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Protein Domain
IPR016159 | Cullin_repeat-like_dom_sf
Type: Homologous_superfamily
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact with specific adaptor proteins [, , ].This superfamily represents the N-terminal cullin repeat-containing domain; these repeats form a domain with a multi-helical 2-layered alpha/alpha structure, which in turn is folded into a right-handed superhelix. A similar structural domain is found in exocyst complex components such as EXO70 and EXO84.
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Protein Domain
IPR016158 | Cullin_homology
Type: Domain
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact with specific adaptor proteins [, , ].
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Protein Domain
IPR036317 | Cullin_homology_sf
Type: Homologous_superfamily
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact with specific adaptor proteins [, , ].This entry represents the cullin-homology domain superfamily. This domain is composed of three subdomains: a 4-helical bundle domain, an alpha+beta domain, and a winged helix-like domain.
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Protein Domain
IPR001373 | Cullin_N
Type: Domain
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact withspecific adaptor proteins [, , ].This entry represents the N-terminal region of cullin proteins, which consists of several domains, including cullin repeat domain, a 4-helical bundle domain, an alpha+beta domain, and a winged helix-like domain.
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Protein Domain
IPR037740 | CSN5
Type: Family
Description: The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].COP9 signalosome complex subunit 5 (Rri1, CSN5 or JAB1) is a metallo-isopeptidase (MEROPS identifier M67.002) that releases the ubiquitin-like protein Nedd8 from the Cul1 subunit of SCF ubiquitin ligases []. Rri1 binds a zinc ion via the histidines in an HXH motif and an aspartic acid C-terminal to this motif []. This entry includes CSN5 homologues from yeast to human.
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Protein Domain
IPR045093 | Cullin
Type: Family
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact with specific adaptor proteins [, , ].
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Protein
Q3TPM3
Organism: Mus musculus/domesticus
Length: 699  
Fragment?: true
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Protein
Q9D4H8
Organism: Mus musculus/domesticus
Length: 745  
Fragment?: false
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Protein
Q9WTX6
Organism: Mus musculus/domesticus
Length: 776  
Fragment?: false
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Protein
A2A432
Organism: Mus musculus/domesticus
Length: 970  
Fragment?: false
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Protein
Q9D5V5
Organism: Mus musculus/domesticus
Length: 780  
Fragment?: false
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Protein
Q9JLV5
Organism: Mus musculus/domesticus
Length: 768  
Fragment?: false
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Protein
Q3TCH7
Organism: Mus musculus/domesticus
Length: 759  
Fragment?: false
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Protein
Q2M4H5
Organism: Mus musculus/domesticus
Length: 780  
Fragment?: false
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Protein
Q8R1T2
Organism: Mus musculus/domesticus
Length: 594  
Fragment?: false
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Protein
Q6ZQ84
Organism: Mus musculus/domesticus
Length: 792  
Fragment?: true
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Protein
Q571A2
Organism: Mus musculus/domesticus
Length: 748  
Fragment?: true
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Protein
E9Q6Z0
Organism: Mus musculus/domesticus
Length: 651  
Fragment?: false
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Protein
E9PXY1
Organism: Mus musculus/domesticus
Length: 896  
Fragment?: false
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Protein
E9Q4T8
Organism: Mus musculus/domesticus
Length: 702  
Fragment?: false
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Protein
Q3UIA5
Organism: Mus musculus/domesticus
Length: 776  
Fragment?: false
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Protein
G3X914
Organism: Mus musculus/domesticus
Length: 855  
Fragment?: false
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Protein
E9PV12
Organism: Mus musculus/domesticus
Length: 828  
Fragment?: false
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Protein Coding Gene
MGI:1919444 | Fbxl20
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1891471 | Spsb3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1354704 | Fbxl17
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1354698 | Fbxw4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1915681 | Fbxl15
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1354731 | Fbxw5
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1924992 | Fbxo42
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1354744 | Fbxo44
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2443416 | Fbxl13
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2152883 | Fbxl5
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2442933 | Amn1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2685007 | Fbxo27
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1354707 | Fbxo17
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:3039600 | Fbxl19
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1918788 | Fbxo9
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2183445 | Spsb4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q6ZQ38
Organism: Mus musculus/domesticus
Length: 1230  
Fragment?: false
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Protein
Q8R0X2
Organism: Mus musculus/domesticus
Length: 377  
Fragment?: false
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Protein
Q6ZQ73
Organism: Mus musculus/domesticus
Length: 1235  
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
Q3TAW5
Organism: Mus musculus/domesticus
Length: 246  
Fragment?: false
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Protein
Q921D1
Organism: Mus musculus/domesticus
Length: 327  
Fragment?: true
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Protein
D3YWC5
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: true
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Protein
E9PV69
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: false
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Protein
Q3UMI9
Organism: Mus musculus/domesticus
Length: 700  
Fragment?: true
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Protein
Q812A5
Organism: Mus musculus/domesticus
Length: 387  
Fragment?: false
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Protein
Q9JJA2
Organism: Mus musculus/domesticus
Length: 640  
Fragment?: false
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Protein
Q3U5F9
Organism: Mus musculus/domesticus
Length: 640  
Fragment?: false
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Protein
Q3U184
Organism: Mus musculus/domesticus
Length: 578  
Fragment?: true
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Protein
Q8BZQ7
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
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Protein
Q3U430
Organism: Mus musculus/domesticus
Length: 833  
Fragment?: false
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Protein
J3QJX0
Organism: Mus musculus/domesticus
Length: 552  
Fragment?: false
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Protein
Q6P0W7
Organism: Mus musculus/domesticus
Length: 224  
Fragment?: true
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Protein
Q6ZPR8
Organism: Mus musculus/domesticus
Length: 838  
Fragment?: true
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Protein
Q8BYN6
Organism: Mus musculus/domesticus
Length: 340  
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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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