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Search results 201 to 300 out of 439 for Cop1

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Type Details Score
Protein Coding Gene
MGP_129S1SvImJ_G0032380 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0032359 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0032295 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0032371 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0032084 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1923625 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0032863 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0031412 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0032050 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0032205 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0032160 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0032286 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0032197 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0032881 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0031132 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0031530 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0013093 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0030973 | -
Type: protein_coding_gene
Organism: Mus spretus
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Allele
Det1<+> | MGI:3525351
   
Name: DET1 partner of COP1 E3 ubiquitin ligase; wild type
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Publication
24838976 | -
First Author: Xu D
Year: 2014
Journal: Plant Cell
Title: The RING-Finger E3 Ubiquitin Ligase COP1 SUPPRESSOR1 Negatively Regulates COP1 Abundance in Maintaining COP1 Homeostasis in Dark-Grown Arabidopsis Seedlings.
Volume: 26
Issue: 5
Pages: 1981-1991
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Publication
28735869 | -
First Author: Kim SH
Year: 2017
Journal: Biochem Biophys Res Commun
Title: DHU1 negatively regulates UV-B signaling via its direct interaction with COP1 and RUP1.
Volume: 491
Issue: 2
Pages: 285-290
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Allele
Det1<Gt(OST61773)Lex> | MGI:4168218
 
Name: DET1 partner of COP1 E3 ubiquitin ligase; gene trap OST61773, Lexicon Genetics
Allele Type: Gene trapped
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Allele
Det1<em16Gpt> | MGI:7297947
Name: DET1 partner of COP1 E3 ubiquitin ligase; endonuclease-mediated mutation 16, GemPharmatech Co., Ltd
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Allele
Det1<Gt(OST149285)Lex> | MGI:4205931
 
Name: DET1 partner of COP1 E3 ubiquitin ligase; gene trap OST149285, Lexicon Genetics
Allele Type: Gene trapped
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Allele
Det1<tm1.1Vmd> | MGI:6258678
Name: DET1 partner of COP1 E3 ubiquitin ligase; targeted mutation 1.1, Vishva M Dixit
Allele Type: Targeted
Attribute String: Epitope tag
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Allele
Det1<em1(IMPC)Bay> | MGI:7547399
Name: DET1 partner of COP1 E3 ubiquitin ligase; endonuclease-mediated mutation 1, Baylor College of Medicine
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Allele
Det1<Gt(OST259573)Lex> | MGI:4254560
 
Name: DET1 partner of COP1 E3 ubiquitin ligase; gene trap OST259573, Lexicon Genetics
Allele Type: Gene trapped
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Allele
Det1<tm2.1Vmd> | MGI:6258682
Name: DET1 partner of COP1 E3 ubiquitin ligase; targeted mutation 2.1, Vishva M Dixit
Allele Type: Targeted
Attribute String: Conditional ready
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Allele
Det1<Gt(D054C12)Wrst> | MGI:3889288
 
Name: DET1 partner of COP1 E3 ubiquitin ligase; gene trap D054C12, German Gene Trap Consortium
Allele Type: Gene trapped
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Interaction Experiment
Yoshida A (2013)
Description: COP1 targets C/EBP for degradation and induces acute myeloid leukemia via Trib1.
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Interaction Experiment
Kung JE (2019)
Description: The pseudokinase TRIB1 toggles an intramolecular switch to regulate COP1 nuclear export.
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Pathway
R-MMU-349425 | Autodegradation of the E3 ubiquitin ligase COP1
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Allele
Cop1<em1Smoc> | MGI:7289098
Name: COP1, E3 ubiquitin ligase; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Interaction Experiment
Yu J (2012)
Description: Modulation of fatty acid synthase degradation by concerted action of p38 MAP kinase, E3 ligase COP1 and SH2-tyrosine phosphatase Shp2.
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Interaction Experiment
Wang X (2021)
Description: Invivo CRISPR screens identify the E3 ligase Cop1 as a modulator of macrophage infiltration and cancer immunotherapy target.
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Publication
15861129 | -
First Author: Yoneda-Kato N
Year: 2005
Journal: EMBO J
Title: Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via COP9 signalosome subunit 3.
Volume: 24
Issue: 9
Pages: 1739-49
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Publication
23884858 | -
First Author: Yoshida A
Year: 2013
Journal: Blood
Title: COP1 targets C/EBPα for degradation and induces acute myeloid leukemia via Trib1.
Volume: 122
Issue: 10
Pages: 1750-60
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Publication
30692133 | -
 
First Author: Kung JE
Year: 2019
Journal: EMBO J
Title: The pseudokinase TRIB1 toggles an intramolecular switch to regulate COP1 nuclear export.
Volume: 38
Issue: 4
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Strain
MGI:6354696 | C57BL/6J-Cop1<em1Smoc>/Smoc
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
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Allele
Cop1<tm3.1Vmd> | MGI:6258676
Name: COP1, E3 ubiquitin ligase; targeted mutation 3.1, Vishva M Dixit
Allele Type: Targeted
Attribute String: Epitope tag
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Allele
Det1<Gt(505G1)Cmhd> | MGI:4954429
 
Name: DET1 partner of COP1 E3 ubiquitin ligase; gene trap 505G1, Centre for Modeling Human Disease
Allele Type: Gene trapped
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Allele
Det1<tm1(KOMP)Mbp> | MGI:4456586
Name: DET1 partner of COP1 E3 ubiquitin ligase; targeted mutation 1, Mouse Biology Program, UC Davis
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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HT Experiment
E-GEOD-18636 | Transcriptomic profiling of Cop1-deficient embryos
Series Id: GSE18636
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: ArrayExpress
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Publication
18930926 | -
First Author: Mallappa C
Year: 2008
Journal: J Biol Chem
Title: GBF1, a transcription factor of blue light signaling in Arabidopsis, is degraded in the dark by a proteasome-mediated pathway independent of COP1 and SPA1.
Volume: 283
Issue: 51
Pages: 35772-82
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Publication
25546391 | J:245546
First Author: Hoffmeister M
Year: 2014
Journal: PLoS One
Title: The ubiquitin E3 ligase NOSIP modulates protein phosphatase 2A activity in craniofacial development.
Volume: 9
Issue: 12
Pages: e116150
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Publication
15548660 | -
First Author: Dreyer J
Year: 2004
Journal: J Neurosci
Title: Nitric oxide synthase (NOS)-interacting protein interacts with neuronal NOS and regulates its distribution and activity.
Volume: 24
Issue: 46
Pages: 10454-65
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Publication
16135813 | -
First Author: Schleicher M
Year: 2005
Journal: Mol Cell Biol
Title: Cell cycle-regulated inactivation of endothelial NO synthase through NOSIP-dependent targeting to the cytoskeleton.
Volume: 25
Issue: 18
Pages: 8251-8
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Protein Domain
IPR016818 | NOSIP
Type: Family
Description: This entry includes animal NOSIP (nitric oxide synthase-interacting protein) and plant CSU1. They are ubiquitin E3 ligases [, ]. Human NOSIP negatively regulates nitric oxide production by inducing NOS1 and NOS3 translocation to actin cytoskeleton and inhibiting their enzymatic activity [, , ].Arabidopsis CSU1 plays a important role in maintaining COP1 homeostasis by targeting COP1 for ubiquitination and degradation in dark-grown seedlings [].
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HT Experiment
GSE111564 | Gene Expression in COP1-ETV1-ETV5-cJun deficient mouse brain
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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Publication
11149895 | -
First Author: Dedio J
Year: 2001
Journal: FASEB J
Title: NOSIP, a novel modulator of endothelial nitric oxide synthase activity.
Volume: 15
Issue: 1
Pages: 79-89
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Publication
25193399 | -
First Author: Kim SH
Year: 2014
Journal: Plant Mol Biol
Title: DWD HYPERSENSITIVE TO UV-B 1 is negatively involved in UV-B mediated cellular responses in Arabidopsis.
Volume: 86
Issue: 6
Pages: 571-83
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Protein Domain
IPR046377 | DHU1
Type: Family
Description: This is a plant family of proteins which includes DWD HYPERSENSITIVE TO UV-B 1 protein (DHU1) from Arabidopsis. DHU1 may act as a substrate receptor of a CUL4-RING E3 ubiquitin-protein ligase (CRL4) complex involved in the negative regulation of cellular responses to ultraviolet-B (UV-B) illumination, likely in coordination with RUP1 [, ]. It interacts with COP1 and probably prevents the formation of active UVR8-COP1 complex, thus avoiding UVR8-COP1-mediated positive regulation of UV-B responses [].
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Publication
15308756 | -
First Author: Laubinger S
Year: 2004
Journal: Plant Cell
Title: The SPA quartet: a family of WD-repeat proteins with a central role in suppression of photomorphogenesis in arabidopsis.
Volume: 16
Issue: 9
Pages: 2293-306
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Publication
27444995 | -
First Author: Chen S
Year: 2016
Journal: BMC Plant Biol
Title: The functional divergence between SPA1 and SPA2 in Arabidopsis photomorphogenesis maps primarily to the respective N-terminal kinase-like domain.
Volume: 16
Issue: 1
Pages: 165
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Publication
28433946 | -
 
First Author: Hoecker U
Year: 2017
Journal: Curr Opin Plant Biol
Title: The activities of the E3 ubiquitin ligase COP1/SPA, a key repressor in light signaling.
Volume: 37
Pages: 63-69
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Publication
12887588 | -
First Author: Laubinger S
Year: 2003
Journal: Plant J
Title: The SPA1-like proteins SPA3 and SPA4 repress photomorphogenesis in the light.
Volume: 35
Issue: 3
Pages: 373-85
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Publication
32994167 | -
 
First Author: Lee S
Year: 2020
Journal: Development
Title: SPAs promote thermomorphogenesis by regulating the phyB-PIF4 module in Arabidopsis.
Volume: 147
Issue: 19
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Protein Domain
IPR044630 | SPA1/2/3/4
Type: Family
Description: In Arabidopsis, SPA1/2/3/4 play a central role in suppression of photomorphogenesis. SPA1 and SPA2 predominate in dark-grown seedlings, whereas SPA3 and SPA4 prevalently regulate the elongation growth in adult plants []. SPAs contain a kinase-like domain, a coiled-coil domain and the WD-repeats. SPAs and COP1 (a ring finger E3 ubiquitin ligase) can form homo- and heterodimers via their respective coiled-coil domains, and the COP1/SPA complex forms a tetramer of two COP1 and two SPA proteins []. The SPA proteins can self-associate or interact with each other, forming a heterogeneous group of SPA-COP1 complexes []. Besides recognizing substrates, both COP1 and SPA bind DDB1 in the CUL4 complex through their C-terminal WD-repeat domains. They serve as DDB1-CUL4-associated factors (DCAFs) similar to other substrate adaptors in CUL4-based E3 ligases. SPA1 interacts with photoreceptor cry2 via its kinase-like domain, with cry1 via its WD-repeat domain and with phytochromes possibly via both []. SPAs have also been shown to regulate the phyB-PIF4 module at high ambient temperature [].
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Publication
30405104 | J:267547
First Author: Cui CP
Year: 2018
Journal: Nat Commun
Title: Dynamic ubiquitylation of Sox2 regulates proteostasis and governs neural progenitor cell differentiation.
Volume: 9
Issue: 1
Pages: 4648
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Publication
32572256 | J:297704
First Author: Gretarsson KH
Year: 2020
Journal: Nat Struct Mol Biol
Title: Dppa2 and Dppa4 counteract de novo methylation to establish a permissive epigenome for development.
Volume: 27
Issue: 8
Pages: 706-716
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Publication
16531484 | -
First Author: Chatterjee M
Year: 2006
Journal: Plant Physiol
Title: Cryptochrome 1 from Brassica napus is up-regulated by blue light and controls hypocotyl/stem growth and anthocyanin accumulation.
Volume: 141
Issue: 1
Pages: 61-74
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Publication
32169020 | -
 
First Author: Wang Q
Year: 2020
Journal: Annu Rev Plant Biol
Title: Mechanisms of Cryptochrome-Mediated Photoresponses in Plants.
Volume: 71
Pages: 103-129
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Publication
17002522 | -
First Author: Li QH
Year: 2007
Journal: Photochem Photobiol
Title: Cryptochrome signaling in plants.
Volume: 83
Issue: 1
Pages: 94-101
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Publication
15751956 | -
First Author: Partch CL
Year: 2005
Journal: Biochemistry
Title: Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor.
Volume: 44
Issue: 10
Pages: 3795-805
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Protein Domain
IPR020978 | Cryptochrome_C
Type: Domain
Description: Cryptochromes are blue/ultraviolet-A light sensing photoreceptors involved in regulating various growth and developmental responses in plants []. Cryptochromes are inactive monomers in the dark but change its conformation to homooligomers upon photon absoption []. This entry represents the C-terminal end of Cryptochrome proteins from plants, which is typically between 113 and 125 amino acids in length. The domain is found in association with and .In Arabidopsis, a conformational change in the C-terminal domain is required for activity []. The domain is know to interact with the protein COP1 [].
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Publication
11927603 | -
First Author: Shorter J
Year: 2002
Journal: J Cell Biol
Title: Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115.
Volume: 157
Issue: 1
Pages: 45-62
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Publication
23515163 | J:196449
First Author: Satoh T
Year: 2013
Journal: Nature
Title: Critical role of Trib1 in differentiation of tissue-resident M2-like macrophages.
Volume: 495
Issue: 7442
Pages: 524-8
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Publication
35851102 | J:339952
First Author: Jiang Y
Year: 2022
Journal: Commun Biol
Title: Cytoplasmic sequestration of p53 by lncRNA-CIRPILalleviates myocardial ischemia/reperfusion injury.
Volume: 5
Issue: 1
Pages: 716
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Publication
32730594 | J:303716
First Author: Yoshino S
Year: 2021
Journal: Blood
Title: Trib1 promotes acute myeloid leukemia progression by modulating the transcriptional programs of Hoxa9.
Volume: 137
Issue: 1
Pages: 75-88
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Publication
10491391 | J:57877
First Author: Rahman A
Year: 1999
Journal: J Cell Biol
Title: Defective kinesin heavy chain behavior in mouse kinesin light chain mutants.
Volume: 146
Issue: 6
Pages: 1277-88
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Publication
11809732 | J:74649
First Author: Maron R
Year: 2002
Journal: Int Immunol
Title: Oral tolerance to copolymer 1 in myelin basic protein (MBP) TCR transgenic mice: cross-reactivity with MBP-specific TCR and differential induction of anti-inflammatory cytokines.
Volume: 14
Issue: 2
Pages: 131-8
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Publication
15492238 | J:93649
First Author: Dornan D
Year: 2004
Journal: Cancer Res
Title: COP1, the negative regulator of p53, is overexpressed in breast and ovarian adenocarcinomas.
Volume: 64
Issue: 20
Pages: 7226-30
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Publication
12077354 | -
First Author: Whyte JR
Year: 2002
Journal: J Cell Sci
Title: Vesicle tethering complexes in membrane traffic.
Volume: 115
Issue: Pt 13
Pages: 2627-37
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Protein Domain
IPR006955 | Uso1_p115_C
Type: Domain
Description: This domain identifies a group of proteins, which are described as: General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein. This myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerisation, and a short C-terminal acidic region []. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the Golgi stack. This domain is found in the acidic C-terminal region, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another [].
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Protein Domain
IPR006953 | Vesicle_Uso1_P115_head
Type: Domain
Description: This domain identifies a group of proteins, which are described as: General vesicular transport factor, Transcytosis associated protein (TAP) or Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerisation, and a short C-terminal acidic region []. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the Golgi stack. This domain is found in the head region. The head region is highly conserved, but its function is unknown. It does not seem to be essential for vesicle tethering []. The N-terminal part of the head region contains context-detected Armadillo/beta-catenin-like repeats.
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Protein
Q9D6T0
Organism: Mus musculus/domesticus
Length: 301  
Fragment?: false
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Protein
A0A1B0GT07
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: true
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Protein
A0A1B0GS52
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: false
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Protein
A0A1B0GS48
Organism: Mus musculus/domesticus
Length: 167  
Fragment?: true
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Protein
A0A1B0GSR8
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: true
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Protein Domain
IPR016460 | COPB1
Type: Family
Description: Proteins synthesised on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. This traffic is bidirectional, to ensure that proteins required to form vesicles are recycled. Vesicles have specific coat proteins (such as clathrin or coatomer) that are important for cargo selection and direction of transfer []. While clathrin mediates endocytic protein transport, and transport from ER to Golgi, coatomers primarily mediate intra-Golgi transport, as well as the reverse Golgi to ER transport of dilysine-tagged proteins []. For example, the coatomer COP1 (coat protein complex 1) is responsible for reverse transport of recycled proteins from Golgi and pre-Golgi compartments back to the ER, while COPII buds vesicles from the ER to the Golgi []. Coatomers reversibly associate with Golgi (non-clathrin-coated) vesicles to mediate protein transport and for budding from Golgi membranes []. Activated small guanine triphosphatases (GTPases) attract coat proteins to specific membrane export sites, thereby linking coatomers to export cargos. As coat proteins polymerise, vesicles are formed and budded from membrane-bound organelles. Coatomer complexes also influence Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. In mammals, coatomer complexes can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunits. This group represents the coatomer beta subunit.
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Protein Domain
IPR016453 | COPB2
Type: Family
Description: Proteins synthesised on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. This traffic is bidirectional, to ensure that proteins required to form vesicles are recycled. Vesicles have specific coat proteins (suchas clathrin or coatomer) that are important for cargo selection and direction of transfer []. While clathrin mediates endocytic protein transport, and transport from ER to Golgi, coatomers primarily mediate intra-Golgi transport, as well as the reverse Golgi to ER transport of dilysine-tagged proteins []. For example, the coatomer COP1 (coat protein complex 1) is responsible for reverse transport of recycled proteins from Golgi and pre-Golgi compartments back to the ER, while COPII buds vesicles from the ER to the Golgi []. Coatomers reversibly associate with Golgi (non-clathrin-coated) vesicles to mediate protein transport and for budding from Golgi membranes []. Activated small guanine triphosphatases (GTPases) attract coat proteins to specific membrane export sites, thereby linking coatomers to export cargos. As coat proteins polymerise, vesicles are formed and budded from membrane-bound organelles. Coatomer complexes also influence Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. In mammals, coatomer complexes can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunits. This group represents the coatomer beta' subunit.
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Protein Domain
IPR017106 | Coatomer_gsu
Type: Family
Description: Proteins synthesised on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. This traffic is bidirectional, to ensure that proteins required to form vesicles are recycled. Vesicles have specific coat proteins (such as clathrin or coatomer) that are important for cargo selection and direction of transfer []. While clathrin mediates endocytic protein transport, and transport from ER to Golgi, coatomers primarily mediate intra-Golgi transport, as well as the reverse Golgi to ER transport of dilysine-tagged proteins []. For example, the coatomer COP1 (coat protein complex 1) is responsible for reverse transport of recycled proteins from Golgi and pre-Golgi compartmentsback to the ER, while COPII buds vesicles from the ER to the Golgi []. Coatomers reversibly associate with Golgi (non-clathrin-coated) vesicles to mediate protein transport and for budding from Golgi membranes []. Activated small guanine triphosphatases (GTPases) attract coat proteins to specific membrane export sites, thereby linking coatomers to export cargos. As coat proteins polymerise, vesicles are formed and budded from membrane-bound organelles. Coatomer complexes also influence Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. In mammals, coatomer complexes can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunits. This group represents the coatomer gamma subunit.
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Protein Coding Gene
MGI:98834 | Trp53
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:107202 | Atm
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q62388
Organism: Mus musculus/domesticus
Length: 3066  
Fragment?: false
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Protein
P02340
Organism: Mus musculus/domesticus
Length: 390  
Fragment?: false
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Protein
Q8R393
Organism: Mus musculus/domesticus
Length: 580  
Fragment?: true
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Publication
10469566 | -
First Author: Shima DT
Year: 1999
Journal: Curr Biol
Title: Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes.
Volume: 9
Issue: 15
Pages: 821-4
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Publication
12893528 | -
First Author: Duden R
Year: 2003
Journal: Mol Membr Biol
Title: ER-to-Golgi transport: COP I and COP II function (Review).
Volume: 20
Issue: 3
Pages: 197-207
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Publication
9151686 | J:20036
First Author: Simpson F
Year: 1997
Journal: J Cell Biol
Title: Characterization of the adaptor-related protein complex, AP-3.
Volume: 137
Issue: 4
Pages: 835-45
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Protein
Q8BTF3
Organism: Mus musculus/domesticus
Length: 470  
Fragment?: false
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Protein
Q99JW9
Organism: Mus musculus/domesticus
Length: 300  
Fragment?: true
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Publication
8647451 | -
First Author: Chow VT
Year: 1996
Journal: Gene
Title: HEP-COP, a novel human gene whose product is highly homologous to the alpha-subunit of the yeast coatomer protein complex.
Volume: 169
Issue: 2
Pages: 223-7
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Publication
9261053 | -
First Author: Cosson P
Year: 1997
Journal: Curr Opin Cell Biol
Title: Coatomer (COPI)-coated vesicles: role in intracellular transport and protein sorting.
Volume: 9
Issue: 4
Pages: 484-7
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Publication
27048656 | -
First Author: Vece TJ
Year: 2016
Journal: J Clin Immunol
Title: Copa Syndrome: a Novel Autosomal Dominant Immune Dysregulatory Disease.
Volume: 36
Issue: 4
Pages: 377-387
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Publication
33582567 | -
 
First Author: Astroski JW
Year: 2021
Journal: Neurobiol Aging
Title: Mutations in the COPI coatomer subunit α-COP induce release of Aβ-42 and amyloid precursor protein intracellular domain and increase tau oligomerization and release.
Volume: 101
Pages: 57-69
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Publication
31712447 | -
First Author: Travis SM
Year: 2019
Journal: Proc Natl Acad Sci U S A
Title: Roles of singleton tryptophan motifs in COPI coat stability and vesicle tethering.
Volume: 116
Issue: 48
Pages: 24031-24040
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Publication
26160949 | -
First Author: Dodonova SO
Year: 2015
Journal: Science
Title: VESICULAR TRANSPORT. A structure of the COPI coat and the role of coat proteins in membrane vesicle assembly.
Volume: 349
Issue: 6244
Pages: 195-8
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Protein Domain
IPR006692 | Coatomer_WD-assoc_reg
Type: Domain
Description: Proteins synthesised on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. This traffic is bidirectional, to ensure that proteins required to form vesicles are recycled. Vesicles have specific coat proteins (such as clathrin or coatomer) that are important for cargo selection and direction of transfer []. While clathrin mediates endocytic protein transport, and transport from ER to Golgi, coatomers primarily mediate intra-Golgi transport, as well as the reverse Golgi to ER transport of dilysine-tagged proteins []. For example, the coatomer COP1 (coat protein complex 1) is responsible for reverse transport of recycled proteins from Golgi and pre-Golgi compartments back to the ER, while COPII buds vesicles from the ER to the Golgi []. Coatomers reversibly associate with Golgi (non-clathrin-coated) vesicles to mediate protein transport and for budding from Golgi membranes []. Activated small guanine triphosphatases (GTPases) attract coat proteins to specific membrane export sites, thereby linking coatomers to export cargos. As coat proteins polymerise, vesicles are formed and budded from membrane-bound organelles. Coatomer complexes also influence Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. In mammals, coatomer complexes can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunits. This entry represents the WD-associated region found in coatomer subunits alpha, beta and beta' subunits. The alpha-subunit (RET1P) of the coatomer complex in Saccharomyces cerevisiae (Baker's yeast), participates in membrane transport between the endoplasmic reticulum and Golgi apparatus. The protein contains six WD-40 repeat motifs in its N-terminal region [].
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