COPG2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0030126 COPI vesicle coat	IBA GO_REF:0000033	ACCEPT	Summary: COPG2/gamma2-COP is a core structural component of the COPI vesicle coat. The protein is part of the gamma/zeta adaptor subcomplex within the heptameric coatomer. Studies show gamma2-COP forms COPI-like complexes that can substitute for gamma1-COP [PMID:11056392, PMID:14729954]. Reason: This is the core cellular component for COPG2. The protein is an integral part of the COPI vesicle coat, confirmed by multiple experimental studies. PMID:14729954 showed that gamma2/zeta1 coatomer is preferentially incorporated into COPI vesicles, with a population identified that "almost exclusively contains gamma2/zeta1 coatomer." Supporting Evidence: PMID:11056392 gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region. [...] gamma2-COP can form a complex with beta-COP in vivo. PMID:14729954 A population of COPI vesicles was characterized that almost exclusively contains gamma2/zeta1 coatomer. file:human/COPG2/COPG2-deep-research-falcon.md COPG2 encodes gamma2-COP, a paralog of gamma1-COP involved in COPI/coatomer biology and Golgi-associated membrane trafficking
GO:0072384 organelle transport along microtubule	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: COPI vesicles are transported along microtubules between compartments. However, COPG2 functions as a structural coat component rather than directly mediating microtubule-based transport, which is carried out by motor proteins. Reason: While COPI vesicles do travel along microtubules (as documented in Reactome pathway R-HSA-6809003), COPG2 is part of the vesicle coat structure, not a motor protein. The annotation reflects an indirect role as a component of transported vesicles. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md gamma2-COP (within coatomer) shuttles between the cytosol and Golgi/ERGIC membranes
GO:0000139 Golgi membrane	IBA GO_REF:0000033	ACCEPT	Summary: COPG2/gamma2-COP localizes to Golgi membranes where it functions as part of the COPI coat complex. Immunofluorescence confirms colocalization with other COP subunits at the cis-Golgi [PMID:11056392], although localization summaries indicate gamma2-COP is enriched at the trans-Golgi relative to gamma1-COP. Reason: Golgi membrane localization is well-documented for COPG2. The protein is recruited to Golgi membranes by ARF1-GTP as part of the coatomer complex for vesicle formation. Supporting Evidence: PMID:11056392 Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region. file:human/COPG2/COPG2-deep-research-falcon.md gamma1-COP is enriched at the cis-Golgi, whereas gamma2-COP (COPG2) is enriched at the trans-Golgi
GO:0005783 endoplasmic reticulum	IBA GO_REF:0000033	ACCEPT	Summary: COPI vesicles deliver cargo to the ER during retrograde transport, and the coat is released upon uncoating at the ER. COPG2 transiently associates with ER membranes during this process. Reason: COPI-mediated retrograde transport terminates at the ER. The Reactome pathways document ER membrane localization during vesicle tethering and uncoating (R-HSA-6811423 and R-HSA-6811427). Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md COPI-coated vesicles mediate retrograde transport from the Golgi back to the endoplasmic reticulum (ER)
GO:0005793 endoplasmic reticulum-Golgi intermediate compartment	IBA GO_REF:0000033	ACCEPT	Summary: The ERGIC is a key site of COPI function. COPI is recruited to ERGIC membranes and mediates retrograde transport from ERGIC back to the ER. Reason: The ERGIC is a documented site of COPI activity. GBF1 (ARF-GEF) activates ARF1 at ER-Golgi intermediates, enabling COPI recruitment. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md COPI-coated intermediates form at the ER-Golgi intermediate compartment (ERGIC) file:human/COPG2/COPG2-deep-research-falcon.md ARF1 activation by ARF-GEFs such as GBF1 and subsequent recruitment of the COPI coatomer to membranes at the cis-Golgi/ERGIC
GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport	IBA GO_REF:0000033	MODIFY	Summary: This annotation is problematic. COPI is primarily involved in RETROGRADE transport (Golgi-to-ER), not anterograde (ER-to-Golgi) transport. ER-to-Golgi anterograde transport is mediated by COPII, not COPI. Reason: COPI's primary function is retrograde transport from Golgi to ER, not anterograde transport. While COPI may have some role in ERGIC maturation during anterograde traffic, this is not its core function. The annotation should be for retrograde transport. Proposed replacements: retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md COPI-coated vesicles mediate retrograde transport from the Golgi back to the endoplasmic reticulum (ER) as well as intra-Golgi transport
GO:0006891 intra-Golgi vesicle-mediated transport	IBA GO_REF:0000033	ACCEPT	Summary: COPI is involved in retrograde transport within the Golgi stack, moving material from trans to cis cisternae as part of cisternal maturation. This is a core function supported by both IBA and IDA evidence [PMID:11056392]. Reason: Intra-Golgi retrograde transport is a well-documented function of COPI. PMID:14729954 discusses COPI's role in retrograde transport within the Golgi apparatus to maintain the identity of Golgi cisternae. Supporting Evidence: PMID:14729954 COPI vesicles are held to mediate [...] retrograde transport within the Golgi apparatus to maintain the identity of Golgi cisternae during maturation of this organelle system
GO:0009306 protein secretion	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: COPI function is essential for maintaining secretory pathway homeostasis, but its direct role is in retrograde transport, not anterograde secretion. Reason: COPI's retrograde transport is required for recycling ER-resident proteins and maintaining the secretory pathway, but this is an indirect effect. COPI does not directly mediate anterograde secretion - that is COPII's role. Notably, COPG2 knockdown in hepatocytes did not impair HDL uptake (unlike essential COPI subunits) and actually increased apoA-I secretion by 33%, indicating COPG2 is dispensable for and may even oppose certain secretory outputs. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md COPI coat function contributes to Golgi structural maintenance and dynamics file:human/COPG2/COPG2-deep-research-falcon.md COPG2 knockdown did not alter HDL uptake [...] COPG2 knockdown increased apoA-I secretion by 33%
GO:0000139 Golgi membrane	IEA GO_REF:0000120	ACCEPT	Summary: Electronic annotation supporting Golgi membrane localization, consistent with IBA and experimental evidence. Reason: Consistent with IBA annotation and immunofluorescence data from PMID:11056392. Supporting Evidence: PMID:11056392 Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region.
GO:0005198 structural molecule activity	IEA GO_REF:0000002	ACCEPT	Summary: COPG2 functions as a structural component of the COPI coatomer complex. This is the primary molecular function of the protein. Reason: COPG2's primary molecular function is structural - it is an essential subunit of the COPI coat that contributes to coat assembly, membrane curvature, and vesicle formation. The deep research confirms it is "not an enzyme or transporter" but "a structural component." Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md The gamma2-COP protein is a structural component of the COPI coat complex and is not an enzyme or transporter. Its primary function is to help form the lattice of the COPI coat on budding vesicles file:human/COPG2/COPG2-deep-research-falcon.md COPG2 should be annotated as a COPI/coatomer-related gamma-COP paralog whose roles are context dependent
GO:0005794 Golgi apparatus	IEA GO_REF:0000117	ACCEPT	Summary: General Golgi apparatus localization, consistent with more specific Golgi membrane annotations. Reason: Correct but less specific than Golgi membrane annotations. Consistent with experimental and IBA evidence. Supporting Evidence: PMID:11056392 Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region.
GO:0005829 cytosol	IEA GO_REF:0000044	ACCEPT	Summary: COPG2 is cytoplasmic when not membrane-associated. The coatomer cycles between cytosol and Golgi/ERGIC membranes. Reason: UniProt confirms cytoplasmic localization. The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md Like all coatomer subunits, gamma2-COP resides in the cytosol when not active, and upon ARF1 activation it localizes to the cytosolic face of the Golgi and ERGIC membranes file:human/COPG2/COPG2-deep-research-falcon.md coat assembly begins with Arf1 binding to Golgi membranes, with GBF1 as the Arf1 GEF, and that Arf1 activation exposes an N-terminal amphipathic helix to anchor in the membrane, recruiting coatomer as an intact unit
GO:0006886 intracellular protein transport	IEA GO_REF:0000002	ACCEPT	Summary: COPG2 is involved in intracellular protein transport as part of the COPI coat. This is a broad but accurate annotation. Reason: COPI mediates intracellular protein transport, specifically retrograde transport from Golgi to ER. This general annotation is correct. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md COPI-coated vesicles retrieve escaped ER proteins and recycling membrane proteins from the Golgi, maintaining protein localization and organelle homeostasis
GO:0015031 protein transport	IEA GO_REF:0000043	ACCEPT	Summary: Very broad annotation for protein transport, derived from UniProt keyword mapping. Reason: Correct but very general. COPG2 is involved in protein transport via COPI-mediated vesicle trafficking. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md COPI-coated vesicles mediate retrograde transport from the Golgi back to the endoplasmic reticulum
GO:0016192 vesicle-mediated transport	IEA GO_REF:0000120	ACCEPT	Summary: COPG2 functions in vesicle-mediated transport as a component of the COPI vesicle coat. Reason: Correct and well-supported. COPI mediates vesicle-mediated transport between Golgi and ER compartments. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md COPI-coated vesicles mediate retrograde transport from the Golgi back to the endoplasmic reticulum (ER) as well as intra-Golgi transport
GO:0030117 membrane coat	IEA GO_REF:0000002	ACCEPT	Summary: COPG2 is part of a membrane coat - specifically the COPI vesicle coat. This is the parent term of COPI vesicle coat. Reason: Correct as a more general cellular component annotation. COPG2 is part of the COPI membrane coat. Supporting Evidence: PMID:14729954 Coatomer is a stable protein complex composed of seven subunits
GO:0030126 COPI vesicle coat	IEA GO_REF:0000002	ACCEPT	Summary: Electronic annotation from InterPro mapping confirming COPI vesicle coat component. Reason: Correct and consistent with IBA annotation. Core localization for COPG2. Supporting Evidence: PMID:14729954 A population of COPI vesicles was characterized that almost exclusively contains gamma2/zeta1 coatomer
GO:0030133 transport vesicle	IEA GO_REF:0000117	ACCEPT	Summary: General transport vesicle localization. COPG2 is found on COPI-coated transport vesicles. Reason: Correct but general. COPI vesicles are transport vesicles that carry cargo between Golgi and ER. Supporting Evidence: PMID:14729954 the gamma2/zeta1 isotype is preferentially incorporated into COPI vesicles
GO:0030663 COPI-coated vesicle membrane	IEA GO_REF:0000044	ACCEPT	Summary: COPG2 localizes to COPI-coated vesicle membrane as a peripheral membrane protein on the cytoplasmic face. Reason: Correct and specific localization. UniProt confirms COPI-coated vesicle membrane localization as peripheral membrane protein on cytoplasmic side. Supporting Evidence: PMID:14729954 A population of COPI vesicles was characterized that almost exclusively contains gamma2/zeta1 coatomer
GO:0031410 cytoplasmic vesicle	IEA GO_REF:0000043	ACCEPT	Summary: General cytoplasmic vesicle localization. COPI vesicles are cytoplasmic vesicles. Reason: Correct but general. COPI-coated vesicles are cytoplasmic vesicles. Supporting Evidence: PMID:14729954 the gamma2/zeta1 isotype is preferentially incorporated into COPI vesicles
GO:0098588 bounding membrane of organelle	IEA GO_REF:0000117	ACCEPT	Summary: Very broad annotation for organelle membrane localization. Reason: Correct but very general. COPG2 associates with Golgi and ER membranes, which are organelle membranes. Supporting Evidence: PMID:11056392 gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region
GO:0030137 COPI-coated vesicle	IEA GO_REF:0000120	ACCEPT	Summary: COPG2 is a component of COPI-coated vesicles. Reason: Well-supported by experimental evidence showing gamma2-COP incorporation into COPI vesicles. Supporting Evidence: PMID:14729954 A population of COPI vesicles was characterized that almost exclusively contains gamma2/zeta1 coatomer
GO:0030426 growth cone	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Growth cone localization transferred from mouse ortholog. COPI vesicle trafficking may be important for axon growth and guidance. Reason: This annotation is transferred from mouse and may reflect specialized neuronal function. Interestingly, studies show COPG1 (not COPG2) is specifically required for neurite outgrowth, suggesting COPG2 may not have a specialized role in growth cones. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md Copg2 knockout did not hinder neurite outgrowth or neuron formation file:human/COPG2/COPG2-deep-research-falcon.md gamma1-COP depletion disrupts neurite extension, while gamma2-COP removal does not measurably affect neurite outgrowth in the same paradigm
GO:0000139 Golgi membrane	NAS PMID:33378371 A genetic screen in Drosophila reveals an unexpected role fo...	ACCEPT	Summary: Golgi membrane localization from ComplexPortal annotation. Reason: Consistent with IBA and IEA annotations. Well-supported localization. Supporting Evidence: PMID:11056392 Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region.
GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum	NAS PMID:33378371 A genetic screen in Drosophila reveals an unexpected role fo...	ACCEPT	Summary: Core biological process for COPG2 - retrograde transport from Golgi to ER. Reason: This is the primary biological process function of COPI and COPG2. The complex mediates retrograde transport of cargo bearing dilysine retrieval signals and KDEL receptor-bound cargo. Supporting Evidence: PMID:14729954 COPI vesicles are held to mediate retrograde transport, between the Golgi and the ER
GO:0030126 COPI vesicle coat	NAS PMID:33378371 A genetic screen in Drosophila reveals an unexpected role fo...	ACCEPT	Summary: COPI vesicle coat component annotation from ComplexPortal. Reason: Core cellular component for COPG2. Consistent with IBA and IEA annotations. Supporting Evidence: PMID:14729954 gamma2/zeta1 coatomer [...] almost exclusively contains gamma2/zeta1 coatomer
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-6811423	ACCEPT	Summary: ER membrane localization during retrograde vesicle tethering at the ER. Reason: COPI vesicles are tethered at the ER membrane during retrograde transport. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md COPI-coated vesicles mediate retrograde transport from the Golgi back to the endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-6811427	ACCEPT	Summary: ER membrane localization during COPI vesicle uncoating at the ER. Reason: COPI uncoating occurs at the ER membrane where COPG2 is released from the vesicle. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md the coat assembles to form a vesicle and then disassembles after budding, returning coatomer subunits (including gamma2-COP) to the cytoplasm
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-6809006	ACCEPT	Summary: Golgi membrane localization during vesicle tethering. Reason: COPI vesicles are tethered at Golgi membranes. Consistent with core localization. Supporting Evidence: PMID:11056392 gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-6809010	ACCEPT	Summary: Golgi membrane localization during COPI vesicle uncoating. Reason: COPI uncoating also occurs at Golgi membranes during intra-Golgi transport. Supporting Evidence: PMID:14729954 COPI vesicles are held to mediate [...] retrograde transport within the Golgi apparatus
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-6809011	ACCEPT	Summary: Golgi membrane localization during SNARE binding on tethered vesicle. Reason: Part of the COPI vesicle fusion process at Golgi membranes. Supporting Evidence: PMID:11056392 gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region
GO:0030133 transport vesicle	TAS Reactome:R-HSA-6807877	ACCEPT	Summary: Transport vesicle localization during ARFGAPs stimulate ARF GTPase activity. Reason: COPG2 is present on transport vesicles during the ARF GTPase cycle. Supporting Evidence: PMID:14729954 the gamma2/zeta1 isotype is preferentially incorporated into COPI vesicles
GO:0030133 transport vesicle	TAS Reactome:R-HSA-6809003	ACCEPT	Summary: Transport vesicle localization during ERGIC-to-Golgi vesicle binding to dynein. Reason: COPI vesicles bind dynein:dynactin for transport along microtubules. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md COPI-coated intermediates form at the ER-Golgi intermediate compartment (ERGIC)
GO:0030133 transport vesicle	TAS Reactome:R-HSA-6809006	ACCEPT	Summary: Transport vesicle localization during vesicle tethering. Reason: COPI vesicles are tethered through interactions with golgins and COG complex. Supporting Evidence: PMID:14729954 the gamma2/zeta1 isotype is preferentially incorporated into COPI vesicles
GO:0030133 transport vesicle	TAS Reactome:R-HSA-6811418	ACCEPT	Summary: Transport vesicle localization during ARFGAPs stimulate ARF GTPase activity at Golgi. Reason: Part of the COPI vesicle biogenesis cycle at the Golgi. Supporting Evidence: PMID:14729954 coat recruitment for the formation of coat protein I (COPI) vesicles involves binding to donor Golgi membranes of the small GTPase ADP-ribosylation factor 1
GO:0030133 transport vesicle	TAS Reactome:R-HSA-6811423	ACCEPT	Summary: Transport vesicle localization during retrograde vesicle tethering at ER. Reason: COPI vesicles are tethered at the ER by the NRZ complex. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md COPI-coated vesicles mediate retrograde transport from the Golgi back to the endoplasmic reticulum
GO:0030133 transport vesicle	TAS Reactome:R-HSA-6811426	ACCEPT	Summary: Transport vesicle localization during retrograde COPI vesicle binding to kinesin. Reason: Retrograde COPI vesicles bind kinesin and microtubules for transport to ER. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md COPI-coated vesicles mediate retrograde transport from the Golgi back to the endoplasmic reticulum
GO:0005829 cytosol	TAS Reactome:R-HSA-6807872	ACCEPT	Summary: Cytosol localization during active ARF recruits coatomer step. Reason: Coatomer is recruited from the cytosol to membranes by ARF1-GTP. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md gamma2-COP resides in the cytosol when not active, and upon ARF1 activation it localizes to the cytosolic face of the Golgi and ERGIC membranes
GO:0005829 cytosol	TAS Reactome:R-HSA-6807875	ACCEPT	Summary: Cytosol localization during ARFGAP, cargo, v-SNAREs and p24 proteins bind nascent COPI complex. Reason: Cytosolic coatomer is recruited and additional factors bind during coat assembly. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md the coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi
GO:0005829 cytosol	TAS Reactome:R-HSA-6807877	ACCEPT	Summary: Cytosol localization during ARFGAPs stimulate ARF GTPase activity. Reason: ARF GTPase cycle occurs at the cytosolic face of membranes. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md the crystal structure of the gamma-COP appendage revealed a platform subdomain that provides a protein-protein interaction site [...] in mammals gamma-COP similarly binds ARFGAP2
GO:0005829 cytosol	TAS Reactome:R-HSA-6809010	ACCEPT	Summary: Cytosol localization during COPI vesicle uncoating. Reason: Upon uncoating, COPG2 is released back to the cytosol. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md the coat assembles to form a vesicle and then disassembles after budding, returning coatomer subunits (including gamma2-COP) to the cytoplasm
GO:0005829 cytosol	TAS Reactome:R-HSA-6811412	ACCEPT	Summary: Cytosol localization during active ARF recruits coatomer to the Golgi. Reason: Coatomer is recruited from cytosol to Golgi membranes. Supporting Evidence: PMID:14729954 coat recruitment for the formation of coat protein I (COPI) vesicles involves binding to donor Golgi membranes of the small GTPase ADP-ribosylation factor 1 and subsequent attachment of the cytoplasmic heptameric complex coatomer
GO:0005829 cytosol	TAS Reactome:R-HSA-6811417	ACCEPT	Summary: Cytosol localization during cargo and adaptor binding at Golgi. Reason: Cytosolic face of Golgi where coat assembly occurs. Supporting Evidence: PMID:14729954 subsequent attachment of the cytoplasmic heptameric complex coatomer
GO:0005829 cytosol	TAS Reactome:R-HSA-6811418	ACCEPT	Summary: Cytosol localization during ARFGAPs stimulate ARF GTPase activity at Golgi membrane. Reason: ARF GTPase activity regulation occurs at cytosolic face. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md gamma-COP similarly binds ARFGAP2 [...] ARFGAP proteins trigger ARF1 GTP hydrolysis
GO:0005829 cytosol	TAS Reactome:R-HSA-6811427	ACCEPT	Summary: Cytosol localization during COPI vesicle uncoating at the ER. Reason: Upon uncoating at ER, coatomer is released to cytosol. Supporting Evidence: file:human/COPG2/COPG2-deep-research-openai.md the coat assembles to form a vesicle and then disassembles after budding, returning coatomer subunits (including gamma2-COP) to the cytoplasm
GO:0030126 COPI vesicle coat	IDA PMID:14729954 Novel isotypic gamma/zeta subunits reveal three coatomer com...	ACCEPT	Summary: Direct experimental evidence showing COPG2 incorporation into COPI vesicle coat. PMID:14729954 identified gamma2/zeta1 coatomer as one of three coatomer isoforms and showed this isoform is preferentially incorporated into COPI vesicles. Reason: High-quality direct experimental evidence from PMID:14729954. The study used immunoprecipitation and Western blotting to demonstrate gamma2-COP incorporation into coatomer and identified a population of COPI vesicles that "almost exclusively contains gamma2/zeta1 coatomer." Supporting Evidence: PMID:14729954 A population of COPI vesicles was characterized that almost exclusively contains gamma2/zeta1 coatomer.
GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum	TAS PMID:11030615 The debate about transport in the Golgi--two sides of the sa...	ACCEPT	Summary: COPI mediates retrograde transport from Golgi to ER. This is a core function of the COPI complex. Reason: Well-established core function of COPI. Multiple studies confirm this role. Supporting Evidence: PMID:14729954 COPI vesicles are held to mediate retrograde transport, between the Golgi and the ER
GO:0006891 intra-Golgi vesicle-mediated transport	IDA PMID:11056392 Identification and characterization of novel isoforms of COP...	ACCEPT	Summary: Direct experimental evidence for COPG2 function in intra-Golgi transport. PMID:11056392 showed that gamma2-COP-containing complexes can interact with p23 (TMED10) and function in COPI-mediated vesicle transport. Reason: Core biological process supported by direct experimental evidence. The study demonstrated that gamma2-COP forms functional COPI-like complexes that interact with p24 family proteins involved in intra-Golgi transport. Supporting Evidence: PMID:11056392 The gamma1-COP-containing and gamma2-COP-containing complexes can similarly interact with the cytoplasmic domain of p23.
GO:0030126 COPI vesicle coat	IDA PMID:11056392 Identification and characterization of novel isoforms of COP...	ACCEPT	Summary: Direct experimental evidence showing gamma2-COP incorporation into COPI complex. PMID:11056392 demonstrated that gamma2-COP can form a complex with beta-COP in vivo. Reason: Key paper establishing gamma2-COP as a bona fide COPI component. The study used immunofluorescence, yeast two-hybrid, and co-immunoprecipitation to demonstrate COPI complex formation. Supporting Evidence: PMID:11056392 Like gamma1-COP, gamma2-COP can form a complex with beta-COP in vivo.

Gene Description

Existing Annotations Review

Core Functions

References

Deep Research

Falcon

OpenAI

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