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Search results 301 to 400 out of 423 for Cop1

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Type Details Score
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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Protein Domain
IPR016391 | Coatomer_asu
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 Coatomer subunit alpha. Structural studies show the homo-oligomerization of this protein plays a key role in the stability of the coat complex [, ]. In humans, defects in its expression are related to primary immunodeficiencies that lead to immune dysregulation, arthritis and interstitial lung disease []. This protein has also been related to Alzheimer's disease [].
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Protein Domain
IPR006822 | Coatomer_esu
Type: Family
Description: This entry represents the epsilon subunit of the coatomer complex, which is involved in the regulation of intracellular protein trafficking between the endoplasmic reticulum and the Golgi complex [].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.
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Protein Domain
IPR010714 | Coatomer_asu_C
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 C terminus (approximately 500 residues) of the eukaryotic coatomer alpha subunit [, ]. This domain is found along with the domain.
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Protein Domain
IPR029446 | COPB1_appendage_platform_dom
Type: Domain
Description: This entry represents a domain found in the C-terminal of the coatamer beta subunit proteins (Beta-coat proteins). It is a platform domain on the appendage that carries a highly conserved tryptophan [, ].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.
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Protein Domain
IPR027059 | Coatomer_dsu
Type: Family
Description: This entry represents the delta subunit of the coatomer complex, which is involved in the regulation of intracellular protein trafficking between the endoplasmic reticulum and the Golgi complex [].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.
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Protein Domain
IPR013040 | Coatomer_gsu_app_Ig-like_dom
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 a β-sandwich structural motif found in the appendage domain of the gamma subunit of coatomer complexes. This subdomain has an immunoglobulin-like β-sandwich fold containing 7 strands in 2 β-sheets in a Greek key topology []. The appendage domain of the gamma coatomer subunit has a similar overall fold to the appendage domain of clathrin adaptors, and can also share the same motif-based cargo recognition and accessory factor recruitment mechanisms.
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Protein Domain
IPR037067 | Coatomer_gsu_app_sf
Type: Homologous_superfamily
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 a β-sandwich structural motif found in the appendage domain superfamily of the gamma subunit of coatomer complexes. This subdomain has an immunoglobulin-like β-sandwich fold containing 7 strands in 2 β-sheets in a Greek key topology []. The appendage domain of the gamma coatomer subunit has a similar overall fold to the appendage domain of clathrin adaptors, and can also share the same motif-based cargo recognition and accessory factor recruitment mechanisms.
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Protein Domain
IPR011710 | Coatomer_bsu_C
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 C-terminal domain of the beta subunit from coatomer proteins (Beta-coat proteins). The C-terminal domain probably adapts the function of the N-terminal domain. Coatomer protein complex I (COPI)-coated vesicles are involved in transport between the endoplasmic reticulum and the Golgi but also participate in transport from early to late endosomes within the endocytic pathway [].
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Publication
11208122 | -
First Author: Barlowe C
Year: 2000
Journal: Traffic
Title: Traffic COPs of the early secretory pathway.
Volume: 1
Issue: 5
Pages: 371-7
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Publication
11409905 | -
First Author: Takatsu H
Year: 2001
Journal: Biochem Biophys Res Commun
Title: Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three-hybrid system.
Volume: 284
Issue: 4
Pages: 1083-9
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Protein
Q9Z1Z0
Organism: Mus musculus/domesticus
Length: 959  
Fragment?: false
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Protein
Q8CIE6
Organism: Mus musculus/domesticus
Length: 1224  
Fragment?: false
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Protein
Q9JIF7
Organism: Mus musculus/domesticus
Length: 953  
Fragment?: false
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Protein
Q63ZW9
Organism: Mus musculus/domesticus
Length: 1131  
Fragment?: true
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Protein
F8WHL2
Organism: Mus musculus/domesticus
Length: 1233  
Fragment?: false
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Protein
Q8BTF0
Organism: Mus musculus/domesticus
Length: 1224  
Fragment?: false
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Publication
14690497 | -
First Author: Watson PJ
Year: 2004
Journal: Traffic
Title: Gamma-COP appendage domain - structure and function.
Volume: 5
Issue: 2
Pages: 79-88
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Publication
17041781 | -
First Author: Béthune J
Year: 2006
Journal: J Membr Biol
Title: COPI-mediated transport.
Volume: 211
Issue: 2
Pages: 65-79
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Protein Coding Gene
MGI:1917497 | Psmd1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:104880 | Psmb6
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1916327 | Psmd11
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1347014 | Psmb3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98858 | Psmd3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:105047 | Psmc5
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1914247 | Psmd12
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1347006 | Psma6
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:104883 | Psma3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:106054 | Psmc1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:104885 | Psma2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913663 | Psmd6
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1914339 | Psmc6
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1194513 | Psmb5
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1096584 | Psmd2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:104884 | Psmb1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:107637 | Psmb7
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913284 | Psmd14
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1098754 | Psmc3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1347070 | Psma7
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1929289 | Adrm1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1098257 | Psmb4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1347009 | Psma5
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1347045 | Psmb2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:109555 | Psmc2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1346093 | Psmc4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1888669 | Psmd8
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1347005 | Psma1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1345192 | Psmd13
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1351511 | Psmd7
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1347060 | Psma4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q9JKV1
Organism: Mus musculus/domesticus
Length: 407  
Fragment?: false
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Protein
Q9R1P1
Organism: Mus musculus/domesticus
Length: 205  
Fragment?: false
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Protein
P99026
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Protein
Q60692
Organism: Mus musculus/domesticus
Length: 238  
Fragment?: false
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Protein
P70195
Organism: Mus musculus/domesticus
Length: 277  
Fragment?: false
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Protein
P46471
Organism: Mus musculus/domesticus
Length: 433  
Fragment?: false
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Protein
Q9R1P0
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: false
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Protein
Q9WVJ2
Organism: Mus musculus/domesticus
Length: 376  
Fragment?: false
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Protein
Q8BG32
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
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Protein
Q9Z2U0
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
P54775
Organism: Mus musculus/domesticus
Length: 418  
Fragment?: false
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Protein
P14685
Organism: Mus musculus/domesticus
Length: 530  
Fragment?: false
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Protein
Q9Z2U1
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: false
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Protein
Q9R1P3
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
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Protein
Q99JI4
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
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Protein
O70435
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: false
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Protein
P62334
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
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Protein
Q9D8W5
Organism: Mus musculus/domesticus
Length: 456  
Fragment?: false
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Protein
Q9QUM9
Organism: Mus musculus/domesticus
Length: 246  
Fragment?: false
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Protein
O09061
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: false
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Protein
O88685
Organism: Mus musculus/domesticus
Length: 442  
Fragment?: false
•
•
•
•
•
Protein
Q9CX56
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: false
•
•
•
•
•
Protein
O35593
Organism: Mus musculus/domesticus
Length: 310  
Fragment?: false
•
•
•
•
•
Protein
Q8VDM4
Organism: Mus musculus/domesticus
Length: 908  
Fragment?: false
•
•
•
•
•
Protein
P26516
Organism: Mus musculus/domesticus
Length: 321  
Fragment?: false
•
•
•
•
•
Protein
O55234
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
•
•
•
•
•
Protein
P62196
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false
•
•
•
•
•
Protein
Q3TXS7
Organism: Mus musculus/domesticus
Length: 953  
Fragment?: false
•
•
•
•
•
Protein
P62192
Organism: Mus musculus/domesticus
Length: 440  
Fragment?: false
•
•
•
•
•
Protein
Q9R1P4
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: false
•
•
•
•
•
Protein
P49722
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: false
•
•
•
•
•
Protein
O89079
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: false
•
•
•
•
•
Protein
F6YFR7
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: true
•
•
•
•
•
Protein
Q3TDU1
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: true
•
•
•
•
•
Protein
Q9D1J2
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: false
•
•
•
•
•
Protein
D3Z315
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: true
•
•
•
•
•
Protein
F6XIG5
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
•
•
•
•
•
Protein
E9Q6I5
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: false
•
•
•
•
•
Protein
O55029
Organism: Mus musculus/domesticus
Length: 905  
Fragment?: false
•
•
•
•
•
Publication
14527408 | -
First Author: Hoffman GR
Year: 2003
Journal: Mol Cell
Title: Conserved structural motifs in intracellular trafficking pathways: structure of the gammaCOP appendage domain.
Volume: 12
Issue: 3
Pages: 615-25
•
•
•
•
•
Publication
15261670 | -
First Author: McMahon HT
Year: 2004
Journal: Curr Opin Cell Biol
Title: COP and clathrin-coated vesicle budding: different pathways, common approaches.
Volume: 16
Issue: 4
Pages: 379-91
•
•
•
•
•
Protein
Q8C0G7
Organism: Mus musculus/domesticus
Length: 273  
Fragment?: false
•
•
•
•
•




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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