BioPAX pathway converted from "Golgi Associated Vesicle Biogenesis" in the Reactome database.Golgi Associated Vesicle BiogenesisGolgi Associated Vesicle BiogenesisProteins that have been synthesized, processed and sorted eventually reach the final steps of the secretory pathway. This pathway is responsible not only for proteins that are secreted from the cell but also enzymes and other resident proteins in the lumen of the ER, Golgi, and lysosomes as well as integral proteins transported in the vesicle membranes.Authored: Gillespie, ME, 2009-08-27Reviewed: Simpson, Jeremy C, 2009-08-27Edited: Gillespie, ME, 2009-08-14Formation Of Bloc-1 ComplexFormation Of Bloc-1 ComplexThe ubiquitously expressed protein complexes, named biogenesis of lysosome-related organelles complex or BLOC are required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.Authored: Gillespie, ME, 2009-08-27Reviewed: Simpson, Jeremy C, 2009-08-27Edited: Gillespie, ME, 2009-09-09Reactome DB_ID: 4298131lysosomal lumenGO0043202UniProt:Q8NBS9 TXNDC5TXNDC5TLP46UNQ364/PRO700TXNDC5FUNCTION Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast (By similarity).SIMILARITY Belongs to the protein disulfide isomerase family.Reactomehttp://www.reactome.orgHomo sapiensNCBI Taxonomy9606UniProtQ8NBS9Chain Coordinates33EQUAL432EQUALReactome DB_ID: 2644691cytosolGO0005829UniProt:P54920 NAPANAPANAPASNAPAFUNCTION Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus (Probable). Together with GNA12 promotes CDH5 localization to plasma membrane (PubMed:15980433).SUBUNIT Interacts with PRKCABP, and disrupts the interaction between GRIA2 and PRKCABP, leading to the internalization of GRIA2 (By similarity). Found in a complex with VAMP8 (By similarity). Component of a SNARE-like complex that contains at least ZW10, USE1L, RINT1, STX18 and NAPA/SNAP-alpha (PubMed:15029241). Interacts with VTI1A (By similarity). Interacts with STX12 (By similarity). Interacts with GNA12 (via N-terminus); the interaction promotes CDH5 localization to plasma membrane (PubMed:15980433).SIMILARITY Belongs to the SNAP family.UniProtP549201EQUAL295EQUALReactome DB_ID: 4298211lysosomal membraneGO0005765UniProt:P78537 BLOC1S1BLOC1S1RT14GCN5L1BLOC1S1BLOS1FUNCTION Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension (PubMed:17182842). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (PubMed:25898167).FUNCTION May negatively regulate aerobic respiration through mitochondrial protein lysine-acetylation. May counteract the action of the deacetylase SIRT3 by acetylating and regulating proteins of the mitochondrial respiratory chain including ATP5F1A and NDUFA9.SUBUNIT Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8 (PubMed:15102850, PubMed:22203680). The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos (By similarity). Component of the BLOC-one-related complex (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN (PubMed:25898167). Interacts with ATP5F1A and NDUFA9; involved in their acetylation on lysine residues (PubMed:22309213). Interacts with KXD1 (By similarity).SIMILARITY Belongs to the BLOC1S1 family.UniProtP785371EQUAL153EQUALReactome DB_ID: 4298171UniProt:Q9NUP1 BLOC1S4BLOC1S4BLOC1S4CNOFUNCTION Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking.SUBUNIT Interacts with BLOC1S5 and BLOC1S6 (By similarity). Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos.SIMILARITY Belongs to the BLOC1S4 family.UniProtQ9NUP11EQUAL217EQUALReactome DB_ID: 4298201UniProt:Q6QNY0 BLOC1S3BLOC1S3BLOS3BLOC1S3FUNCTION Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking.SUBUNIT Interacts with BLOC1S4, BLOC1S5 and BLOC1S6 (By similarity). Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. Interacts directly with BLOC1S2.SIMILARITY Belongs to the BLOC1S3 family.UniProtQ6QNY01EQUAL202EQUALReactome DB_ID: 4298191UniProt:Q96EV8 DTNBP1DTNBP1My031DTNBP1BLOC1S8FUNCTION Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Associates with the BLOC-2 complex to facilitate the transport of TYRP1 independent of AP-3 function. Plays a role in synaptic vesicle trafficking and in neurotransmitter release. Plays a role in the regulation of cell surface exposure of DRD2. May play a role in actin cytoskeleton reorganization and neurite outgrowth. May modulate MAPK8 phosphorylation. Appears to promote neuronal transmission and viability through regulating the expression of SNAP25 and SYN1, modulating PI3-kinase-Akt signaling and influencing glutamatergic release. Regulates the expression of SYN1 through binding to its promoter. Modulates prefrontal cortical activity via the dopamine/D2 pathway.SUBUNIT Interacts (via its coiled coil domain) with KXD1. Interacts with CMYA5, PI4K2 and RNF151 (By similarity). Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of at least BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts directly in the complex with BLOC1S5, BLOC1S6 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. This BLOC-1 complex also associates with the BLOC-2 complex in endosomes. Binds to DTNA and DTNB but may not be a physiological binding partner (PubMed:16980328). Interacts (isoform 1 and isoform 2 only) with the DNA-dependent protein kinase complex DNA-PK; the interaction phosphorylates DTNBP1 in vitro. Interacts directly in this complex with XRCC5 and XRCC6. Interacts with AP3M1, AP3B2 and TRIM32. Interacts with XPO1; the interaction exports DTNBP1 out of the nucleus.TISSUE SPECIFICITY Detected in brain, in neurons and in neuropil. Isoform 1 is expressed in the cerebral cortex, and hippocampal frontal (HF). Specific expression in the posterior half of the superior temporal gyrus (pSTG). Higher expression of isoform 2 and 3 in the HF than in the pSTG while isoform 1 shows no difference in expression in these areas. In the HF, detected in dentate gyrus (DG) and in pyramidal cells of hippocampus CA2 and CA3 (at protein level). Expressed in all principal neuronal populations of the HF, namely pyramidal neurons in the subiculum and CA1-3, granule cells in the dense cell layer of the DG (DGg), and polymorph cells in the hilus of the DG (DGh). Maximal levels in CA2, CA3, and DGh. Isoform 2 not expressed in the cerebral cortex.PTM Ubiquitinated by TRIM32. Ubiquitination leads to DTNBP1 degradation.PTM Isoforms 1 and 2 highly phosphorylated by PRKDC in vitro. Isoform 3 only weakly phosphorylated by PRKDC in vitro.DISEASE Defects in DTNBP1 are associated with susceptibility to schizophrenia, a mental disorder characterized by a breakdown of thought processes and by poor emotional responsiveness. Genetic mutations lead to alterations in the glutamatergic transmission in the brain and modified Akt signaling (PubMed:15345706). Protein levels and expression are reduced in nerve terminals of the hippocampus and there is an increased release of glutamate in schizophrenic patients (PubMed:15124027). Levels of isoform 1 are reduced in the pSTG, but not in HF, by about 48% in 92% of schizophrenic patients. In the HF, there is an average of 33% reduction in synaptic expression of isoform 2 in 67% of cases, and of isoform 3, an average reduction of 35% in 80% of cases. In the dorsolateral prefrontal cortex (DLPFC), significant reductions in levels of isoform 3 are observed about 71% of schizophrenic patients showed an average reduction of this isoform of about 60% (PubMed:19617633).SIMILARITY Belongs to the dysbindin family.UniProtQ96EV81EQUAL351EQUALReactome DB_ID: 4298161UniProt:Q9UL45 BLOC1S6BLOC1S6PABLOC1S6PLDNFUNCTION Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. May play a role in intracellular vesicle trafficking, particularly in the vesicle-docking and fusion process.SUBUNIT Interacts with BLOC1S4 and DTNBP1/BLOC1S7 (By similarity). Homodimer. Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. Interacts with BLOC1S5, F-actin, SNAP25 isoform 1 and isoform 2, SNAP47 and STX12.TISSUE SPECIFICITY Widely expressed.PTM Phosphorylated.SIMILARITY Belongs to the BLOC1S6 family.CAUTION A paper showing involvement in Hermansky-Pudlak syndrome 9 was retracted due to image duplication.UniProtQ9UL451EQUAL172EQUALReactome DB_ID: 4298251BLOC-1 Complex [lysosomal membrane]BLOC-1 ComplexReactome DB_ID: 429813133EQUAL432EQUALReactome DB_ID: 26446911EQUAL295EQUALReactome DB_ID: 42982111EQUAL153EQUALReactome DB_ID: 42981711EQUAL217EQUALReactome DB_ID: 42982011EQUAL202EQUALReactome DB_ID: 42981911EQUAL351EQUALReactome DB_ID: 42981611EQUAL172EQUALReactome Database ID Release 75429825Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=429825ReactomeR-HSA-4298251Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-429825.1Reactome Database ID Release 75429815Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=429815ReactomeR-HSA-4298152Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-429815.217116749Pubmed2006Comparative proteomics of clathrin-coated vesiclesBorner, GHHarbour, MHester, SLilley, KSRobinson, MSJ Cell Biol 175:571-815102850Pubmed2004Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1)Starcevic, MDell'Angelica, ECJ Biol Chem 279:28393-401Recruitment Of Cytoplasmic Proteins To VesiclesRecruitment Of Cytoplasmic Proteins To VesiclesCytosolic proteins are also recruited to the cytoplasmic face of newly formed vesicles.Authored: Gillespie, ME, 2009-08-12Reviewed: Simpson, Jeremy C, 2009-08-27Edited: Gillespie, ME, 2008-09-08 03:19:22Reactome DB_ID: 4342021UniProt:Q5HYK7 SH3D19SH3D19SH3D19FUNCTION May play a role in regulating A disintegrin and metalloproteases (ADAMs) in the signaling of EGFR-ligand shedding. May be involved in suppression of Ras-induced cellular transformation and Ras-mediated activation of ELK1. Plays a role in the regulation of cell morphology and cytoskeletal organization.SUBUNIT Interacts with ADAM12. Isoform 4 and isoform 5 (but not isoform 1 and isoform 2) interact with ADAM9, ADAM10, ADAM15 and ADAM17. Interacts with SH3GL1 SH3 domain. Interacts via SH3 3 and SH3 4 or SH3 4 and SH3 5 domains with SOS2. Probably forms a trimeric complex with SH3GL1 and SOS2. Interacts with SH3YL1 (By similarity).TISSUE SPECIFICITY Widely expressed with highest levels in heart, skeletal muscle, kidney, liver, placenta, small intestine and lung. Expressed at low levels in colon, thymus, spleen and leukocytes.CAUTION It is uncertain whether Met-1 or Met-4 is the initiator.UniProtQ5HYK71EQUAL790EQUALReactome DB_ID: 4343501Ferritin Complex [cytosol]Ferritin ComplexConverted from EntitySet in ReactomeReactome DB_ID: 43435624FTH1:FTL [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityFTH1 [cytosol]FTL [cytosol]UniProtP02794UniProtP02792Reactome Database ID Release 75434350Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=434350ReactomeR-HSA-4343501Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-434350.1Reactome DB_ID: 4298111UniProt:Q14677 CLINT1CLINT1EPN4CLINT1ENTHKIAA0171EPNRFUNCTION Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly.SUBUNIT Binds clathrin heavy chain, GGA2, AP-2 and AP1G1 (PubMed:12213833, PubMed:12429846, PubMed:12538641). Interacts with VTI1B (PubMed:18033301).TISSUE SPECIFICITY Ubiquitously expressed at low to intermediate levels.POLYMORPHISM Genetic variations in CLINT1 may contribute to susceptibility to schizophrenia (SCZD1) and psychotic disorders in some populations.SIMILARITY Belongs to the epsin family.UniProtQ146771EQUAL625EQUALReactome DB_ID: 4342111UniProt:Q14671 PUM1PUM1KIAA0099PUM1PUMH1FUNCTION Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (PubMed:21572425, PubMed:18328718, PubMed:21653694, PubMed:21397187). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:20818387, PubMed:20860814, PubMed:22345517). Following growth factor stimulation, phosphorylated and binds to the 3'-UTR of CDKN1B/p27 mRNA, inducing a local conformational change that exposes miRNA-binding sites, promoting association of miR-221 and miR-222, efficient suppression of CDKN1B/p27 expression, and rapid entry to the cell cycle (PubMed:20818387). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517, PubMed:29474920). Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm (PubMed:26724866). Involved in neuronal functions by regulating ATXN1 mRNA levels: acts by binding to the 3'-UTR of ATXN1 transcripts, leading to their down-regulation independently of the miRNA machinery (PubMed:25768905, PubMed:29474920). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). In testis, acts as a post-transcriptional regulator of spermatogenesis by binding to the 3'-UTR of mRNAs coding for regulators of p53/TP53. Involved in embryonic stem cell renewal by facilitating the exit from the ground state: acts by targeting mRNAs coding for naive pluripotency transcription factors and accelerates their down-regulation at the onset of differentiation (By similarity). Binds specifically to miRNA MIR199A precursor, with PUM2, regulates miRNA MIR199A expression at a postranscriptional level (PubMed:28431233).SUBUNIT Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). In case of viral infection, interacts with DHX58 (PubMed:25340845). Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (PubMed:23125361).TISSUE SPECIFICITY Expressed in brain, heart, kidney, muscle, intestine and stomach. Not expressed in cerebellum, corpus callosum, caudate nucleus, hippocampus, medulla oblongata and putamen. Expressed in all fetal tissues tested.INDUCTION Strongly down-regulated in keratinocytes upon UVB irradiation.DOMAIN The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. RNA-binding occurs on the concave side of the surface (PubMed:21397187). PUM1 is composed of 8 pumilio repeats of 36 residues; each repeat binds a single nucleotide in its RNA target. Residues at positions 12 and 16 of the pumilio repeat bind each RNA base via hydrogen bonding or van der Waals contacts with the Watson-Crick edge, while the amino acid at position 13 makes a stacking interaction. The recognition of RNA by pumilio repeats is base specific: cysteine and glutamine at position 12 and 16, respectively, bind adenine; asparagine and glutamine bind uracil; and serine and glutamate bind guanine (PubMed:21572425. PubMed:18328718, PubMed:21653694).PTM Phosphorylation at Ser-714 promotes RNA-binding activity. Following growth factor stimulation phosphorylated at Ser-714, promoting binding to the 3'-UTR of CDKN1B/p27 mRNA.UniProtQ146711EQUAL1186EQUALConverted from EntitySet in ReactomeReactome DB_ID: 4326731cytoplasmic vesicle membraneGO0030659Vamp [cytoplasmic vesicle membrane]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityReactome DB_ID: 4343511Golgi-associated vesicle interacting proteins [cytosol]Golgi-associated vesicle interacting proteinsReactome DB_ID: 43420211EQUAL790EQUALReactome DB_ID: 4343501Reactome DB_ID: 42981111EQUAL625EQUALReactome DB_ID: 43421111EQUAL1186EQUALReactome Database ID Release 75434351Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=434351ReactomeR-HSA-4343511Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-434351.1Converted from EntitySet in ReactomeReactome DB_ID: 4326731Reactome Database ID Release 75434362Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=434362ReactomeR-HSA-4343622Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-434362.2Vamp And trans-Golgi Network AP-1 Binding Coupled With Cargo CaptureVamp And trans-Golgi Network AP-1 Binding Coupled With Cargo CaptureOnce AP-1 is recruited to the trans-Golgi Network membrane the complex of functional vesicle building proteins is joined by the cargo that will be within that vesicle. As with other types of vesicles the cargo itself is part of the vesicle development. Here the cargo is destined for the Golgi-associated vesicle membrane. It is at this stage that a specific Synaptobrevin (Vamp) molecule also joins the complex. It should be noted that only certain Vamp molecules will be found with specific cargo molecules on the newly forming vesicles. However here we represent this reaction in bulk, without specific Vamp and cargo molecule pairings.Authored: Gillespie, ME, 2009-08-27Reviewed: Simpson, Jeremy C, 2009-08-27Edited: Gillespie, ME, 2008-05-21 20:31:35Reactome DB_ID: 1677171AP-1 Complex [cytosol]AP-1 ComplexConverted from EntitySet in ReactomeReactome DB_ID: 1677161AP-1 mu [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityAP1M1 [cytosol]AP1M2 [cytosol]UniProtQ9BXS5UniProtQ9Y6Q5Reactome DB_ID: 1677051UniProt:Q10567 AP1B1AP1B1ADTB1AP1B1CLAPB2BAM22FUNCTION Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes (PubMed:31630791). The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.SUBUNIT Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3).TISSUE SPECIFICITY Widely expressed.SIMILARITY Belongs to the adaptor complexes large subunit family.UniProtQ105671EQUAL949EQUALConverted from EntitySet in ReactomeReactome DB_ID: 1677131AP-1 sigma [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityAP1S1 [cytosol]AP1S2 [cytosol]AP1S3 [cytosol]UniProtP61966UniProtP56377UniProtQ96PC3Reactome DB_ID: 1677031UniProt:O43747 AP1G1AP1G1CLAPG1AP1G1ADTGFUNCTION Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.SUBUNIT Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). Binds RABEP1 and SYNRG. Interacts (via GAE domain) with AP1AR (via coiled-coil domain). Interacts with CLN3 (via dileucine motif); this interaction facilitates lysosomal targeting (PubMed:15598649).TISSUE SPECIFICITY Widely expressed.SIMILARITY Belongs to the adaptor complexes large subunit family.UniProtO437472EQUAL822EQUALReactome Database ID Release 75167717Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=167717ReactomeR-HSA-1677171Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-167717.1Converted from EntitySet in ReactomeReactome DB_ID: 4326741Golgi membraneGO0000139Golgi-associated Vesicle Destined Cargo [Golgi membrane]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityReactome DB_ID: 1999811Arf1-GTP [Golgi membrane]Arf1-GTPReactome DB_ID: 1999711UniProt:P84077 ARF1ARF1ARF1FUNCTION GTP-binding protein involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD).FUNCTION (Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.SUBUNIT Interacts (when activated) with GGA1, GGA2 and GGA3; the interaction is required for proper subcellular location of GGA1, GGA2 and GGA3 (PubMed:11950392, PubMed:28868155). Interacts with ARHGAP21, ASAP2, HERC1, PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2 (PubMed:10022920, PubMed:17347647, PubMed:23889934, PubMed:8861955). Interacts with ARFGAP1, which hydrolyzes GTP and thus, regulates its function (PubMed:10102276). Interacts with PI4KB in the Golgi complex (PubMed:17555535). Interacts with NCS1/FREQ in the Golgi and at the plasma membrane (PubMed:17555535). Interacts with PLEKHA3 (PubMed:21454700). Interacts with PLEKHA8; the interaction, together with phosphatidylinositol 4-phosphate binding, is required for FAPP2-mediated glucosylceramide transfer activity (PubMed:15107860). Interacts (activated) with PICK1 (via PDZ domain); the interaction blocks Arp2/3 complex inhibition (PubMed:23889934). Interacts with IQSEC1 (PubMed:24058294). Interacts with C9orf72 (By similarity) (PubMed:24058294).PTM Demyristoylated by S.flexneri cysteine protease IpaJ which cleaves the peptide bond between N-myristoylated Gly-2 and Asn-3.SIMILARITY Belongs to the small GTPase superfamily. Arf family.UniProtP840772EQUAL181EQUALReactome DB_ID: 294381GTP [ChEBI:15996]GTPGuanosine 5'-triphosphateChEBI15996Reactome Database ID Release 75199981Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=199981ReactomeR-HSA-1999811Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-199981.1Converted from EntitySet in ReactomeReactome DB_ID: 4326681Vamp [Golgi membrane]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityConverted from EntitySet in ReactomeReactome DB_ID: 4350321Golgi lumenGO0005796Golgi-associated Vesicle Destined Cargo [Golgi lumen]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityReactome DB_ID: 2644701UniProt:P49407 ARRB1ARRB1ARRB1ARR1FUNCTION Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6) (By similarity). Involved in IL8-mediated granule release in neutrophils. Required for atypical chemokine receptor ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3. Negatively regulates the NOTCH signaling pathway by mediating the ubiquitination and degradation of NOTCH1 by ITCH. Participates in the recruitment of the ubiquitin-protein ligase to the receptor (PubMed:23886940).SUBUNIT Monomer. Homodimer. Homooligomer; the self-association is mediated by InsP6-binding. Heterooligomer with ARRB2; the association is mediated by InsP6-binding. Interacts with GPR143. Interacts with ADRB2 (phosphorylated). Interacts with CHRM2 (phosphorylated). Interacts with LHCGR. Interacts with CYTH2 and CASR. Interacts with AP2B1 (dephosphorylated at 'Tyr-737'); phosphorylation of AP2B1 at 'Tyr-737' disrupts the interaction. Interacts (dephosphorylated at Ser-412) with CLTC. Interacts with CCR2 and GRK2. Interacts with CRR5. Interacts with PTAFR (phosphorylated on serine residues). Interacts with CLTC and MAP2K3. Interacts with CREB1. Interacts with TRAF6. Interacts with IGF1R and MDM2. Interacts with C5AR1. Interacts with PDE4D. Interacts with SRC (via the SH3 domain and the protein kinase domain); the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with TACR1. Interacts with RAF1. Interacts with CHUK, IKBKB and MAP3K14. Interacts with DVL1; the interaction is enhanced by phosphorylation of DVL1. Interacts with DVL2; the interaction is enhanced by phosphorylation of DVL2. Interacts with IGF1R. Associates with MAP kinase p38. Part of a MAPK signaling complex consisting of TACR1, ARRB1, SRC, MAPK1 (activated) and MAPK3 (activated). Part of a MAPK signaling complex consisting of F2RL1, ARRB1, RAF1, MAPK1 (activated) and MAPK3 (activated) (By similarity). Interacts with MAP2K4/MKK4. Interacts with HCK and CXCR1 (phosphorylated). Interacts with ACKR3 and ACKR4. Interacts with ARRDC1; the interaction is direct (PubMed:23886940). Interacts with GPR61, GPR62 and GPR135 (PubMed:28827538).DOMAIN The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1 (By similarity). Binding to phosphorylated GPCRs induces a conformationanl change that exposes the motif to the surface.DOMAIN The N-terminus binds InsP6 with low affinity.DOMAIN The C-terminus binds InsP6 with high affinity.PTM Constitutively phosphorylated at Ser-412 in the cytoplasm. At the plasma membrane, is rapidly dephosphorylated, a process that is required for clathrin binding and ADRB2 endocytosis but not for ADRB2 binding and desensitization. Once internalized, is rephosphorylated.PTM The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to occur GPCR-specific. Ubiquitinated by MDM2; the ubiquitination is required for rapid internalization of ADRB2. Deubiquitinated by USP33; the deubiquitination leads to a dissociation of the beta-arrestin-GPCR complex. Stimulation of a class A GPCR, such as ADRB2, induces transient ubiquitination and subsequently promotes association with USP33.SIMILARITY Belongs to the arrestin family.UniProtP494071EQUAL418EQUALReactome DB_ID: 4326691Cargo:AP-1:Arf1-GTP:beta-Arrestin-1:Vamp Complex [Golgi membrane]Cargo:AP-1:Arf1-GTP:beta-Arrestin-1:Vamp ComplexReactome DB_ID: 3508111AP-1 Complex [Golgi membrane]AP-1 ComplexConverted from EntitySet in ReactomeReactome DB_ID: 3508071AP-1 sigma [Golgi membrane]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityAP1S1 [Golgi membrane]AP1S2 [Golgi membrane]AP1S3 [Golgi membrane]Reactome DB_ID: 35080911EQUAL949EQUALReactome DB_ID: 35080812EQUAL822EQUALConverted from EntitySet in ReactomeReactome DB_ID: 3508151AP-1 mu [Golgi membrane]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityAP1M2 [Golgi membrane]AP1M1 [Golgi membrane]Reactome Database ID Release 75350811Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=350811ReactomeR-HSA-3508111Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-350811.1Reactome DB_ID: 35083111EQUAL418EQUALConverted from EntitySet in ReactomeReactome DB_ID: 4326741Reactome DB_ID: 1999811Converted from EntitySet in ReactomeReactome DB_ID: 4326681Converted from EntitySet in ReactomeReactome DB_ID: 4350321Reactome Database ID Release 75432669Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=432669ReactomeR-HSA-4326691Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-432669.1Reactome Database ID Release 75421833Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=421833ReactomeR-HSA-4218331Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-421833.111994746Pubmed2002Regulated transport of the glucose transporter GLUT4.Bryant, NJGovers, RJames, DENat Rev Mol Cell Biol 3:267-7711694590Pubmed2001GGAs: roles of the different domains and comparison with AP-1 and clathrinHirst, JLindsay, MRRobinson, MSMol Biol Cell 12:3573-88trans-Golgi Network Coat Assemblytrans-Golgi Network Coat AssemblyOnce the basic components of the docking complex are assembled with one end of AP-1 bound to cargo molecules, the other end binds to clathrin. Clathrin triskelions polymerize into hexagons and pentagons, forming a cage, which leads to membrane deformation. This polymerization step drives the sculpting of the vesicle. The number of clathrin triskelions required to sculpt a vesicle appears to be variable, but has been estimated to require 36 - 60 triskelions assocaited with 30 - 66 AP-1 complexes. Here a ~380 angstroms vesicle is represented with 48 clathrin triskelions and 52 AP-1 complexes.Authored: Gillespie, ME, 2009-08-27Reviewed: Simpson, Jeremy C, 2009-08-27Edited: Gillespie, ME, 2008-05-21 20:31:35Reactome DB_ID: 1829581UniProt:Q99962 SH3GL2SH3GL2SH3D2ACNSA2SH3GL2FUNCTION Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes.SUBUNIT Monomer; in cytoplasm. Homodimer; when associated with membranes (By similarity). Interacts with OPHN1 (By similarity). Interacts with SYNJ1 (PubMed:10542231). Interacts with DNM1 (By similarity). Interacts with MAP4K3; the interaction appears to regulate MAP4K3-mediated JNK activation (By similarity). Interacts with PDCD6IP (PubMed:17350572). Interacts with ATX2 (PubMed:18602463). Interacts with ADAM9 and ADAM15 cytoplasmic tails (PubMed:10531379). Interacts with BIN2 (PubMed:23285027). Interacts with TMEM108 (By similarity). Interacts with ADGRB2 (PubMed:28891236).TISSUE SPECIFICITY Brain, mostly in frontal cortex. Expressed at high level in fetal cerebellum.DOMAIN An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes. The BAR domain dimer forms a rigid crescent shaped bundle of helices with the pair of second amphipathic helices protruding towards the membrane-binding surface.MISCELLANEOUS HeLa cells expressing the N-BAR domain of SH3GL2 show tubulation of the plasma membrane. The N-BAR domain binds liposomes and induces formation of tubules from liposomes. The N-terminal amphipathic helix is required for liposome binding. The second amphipathic helix enhances liposome tubulation.SIMILARITY Belongs to the endophilin family.UniProtQ999621EQUAL352EQUALReactome DB_ID: 22131801UniProt:P50570 DNM2DNM2DYN2DNM2FUNCTION Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Plays an important role in vesicular trafficking processes, in particular endocytosis. Involved in cytokinesis (PubMed:12498685). Regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (By similarity).SUBUNIT Interacts with MYOF (By similarity). Interacts with CTTN and ACTN1 (By similarity). Interacts with SHANK1, SHANK2, SH3BP4 and NOSTRIN. Interacts with SNX9. Interacts with SNX33 (via SH3 domain). Interacts with MYO1E (via SH3 domain). Interacts with PSTPIP1. Interacts with CTNND2 (PubMed:22022388). May interact with PIK3C3 (By similarity). May be a component of a complex composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3 (By similarity). Interacts with BIN1 (PubMed:17676042).TISSUE SPECIFICITY Ubiquitously expressed.PTM Phosphorylation at Ser-764 by CDK1 is greatly increased upon mitotic entry. It regulates cytokinesis downstream of calcineurin, and does not affect clathrin-mediated endocytosis. Dephosphorylated by calcineurin/PP2 (By similarity). Phosphorylated on tyrosine residues after activation of SRC (By similarity).MISCELLANEOUS Overexpression of CNM- and CMT-related DNM2 mutants in COS7 cells, whatever the mutated domain, led to a reduction in clathrin-mediated receptor endocytosis associated with MAPK ERK-1 and ERK-2 impairment. The membrane trafficking impairment process may represent a common pathophysiological pathway in the autosomal forms of CNM DNM2-CMT neuropathy.SIMILARITY Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.UniProtP505701EQUAL870EQUALReactome DB_ID: 35082748Clathrin Triskelion [cytosol]Clathrin TriskelionReactome DB_ID: 3508243UniProt:Q00610-1 CLTCCLTCCLTCL2CLH17CLTCKIAA0034FUNCTION Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577, PubMed:16968737, PubMed:21297582). The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825). Plays a role in early autophagosome formation (PubMed:20639872).SUBUNIT Clathrin triskelions, composed of 3 heavy chains and 3 light chains, are the basic subunits of the clathrin coat (PubMed:16968737). In the presence of light chains, hub assembly is influenced by both the pH and the concentration of calcium. Interacts with HIP1 (PubMed:11532990). Interacts with DENND1A, DENND1B and DENND1C (By similarity). May interact with OCRL (By similarity). Interacts with ERBB2 (PubMed:16314522). Interacts with FKBP6 (PubMed:18529014). Interacts with CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges; the complex implicates clathrin triskelions; TACC3 and CLTC are proposed to form a composite microtubule interaction surface (PubMed:21297582). Interacts with ATG16L1 (via N-terminus) (PubMed:20639872). Interacts with RFTN1; the interaction occurs in response to pathogens (PubMed:27022195, PubMed:21266579). Interacts with USP2 isoform 4 (PubMed:26756164).DOMAIN The N-terminal seven-bladed beta-propeller is formed by WD40-like repeats, and projects inward from the polyhedral outer clathrin coat. It constitutes a major protein-protein interaction node.SIMILARITY Belongs to the clathrin heavy chain family.UniProtQ00610-12EQUAL1675EQUALReactome DB_ID: 3508283UniProt:P09496-1 CLTACLTACLTAFUNCTION Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577, PubMed:21297582).SUBUNIT Clathrin coats are formed from molecules containing 3 heavy chains and 3 light chains. Interacts with CALY; the interaction stimulates clathrin self-assembly and clathrin-mediated endocytosis. Interacts with CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges; the complex implicates clathrin triskelions.SIMILARITY Belongs to the clathrin light chain family.UniProtP09496-11EQUAL248EQUALReactome Database ID Release 75350827Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=350827ReactomeR-HSA-3508271Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-350827.1Reactome DB_ID: 43266952Reactome DB_ID: 20134052Arf1-GDP [cytosol]Arf1-GDPReactome DB_ID: 20082612EQUAL181EQUALReactome DB_ID: 294201GDP [ChEBI:17552]GDPGuanosine 5'-diphosphateGuanosine diphosphateChEBI17552Reactome Database ID Release 75201340Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=201340ReactomeR-HSA-2013401Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-201340.1Reactome DB_ID: 3508251Cargo:AP-1:Beta-arrestin:Vamp:Clathrin Triskelion:Dynamin:Endophilin Complex [Golgi membrane]Cargo:AP-1:Beta-arrestin:Vamp:Clathrin Triskelion:Dynamin:Endophilin ComplexReactome DB_ID: 35118911EQUAL352EQUALReactome DB_ID: 43267752Cargo:AP-1:beta-Arrestin-1:Vamp Complex [Golgi membrane]Cargo:AP-1:beta-Arrestin-1:Vamp ComplexReactome DB_ID: 3508111Reactome DB_ID: 35083111EQUAL418EQUALConverted from EntitySet in ReactomeReactome DB_ID: 4326741Converted from EntitySet in ReactomeReactome DB_ID: 4326681Converted from EntitySet in ReactomeReactome DB_ID: 4350321Reactome Database ID Release 75432677Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=432677ReactomeR-HSA-4326771Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-432677.1Reactome DB_ID: 298084211EQUAL870EQUALReactome DB_ID: 35082748Reactome Database ID Release 75350825Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=350825ReactomeR-HSA-3508251Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-350825.1Reactome DB_ID: 2937252hydrogenphosphate [ChEBI:43474]hydrogenphosphate[PO3(OH)](2-)HYDROGENPHOSPHATE IONhydrogen phosphate[P(OH)O3](2-)HPO4(2-)phosphateINORGANIC PHOSPHATE GROUPChEBI43474Reactome Database ID Release 75421831Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=421831ReactomeR-HSA-4218311Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-421831.110394364Pubmed1999Functional organization of clathrin in coats: combining electron cryomicroscopy and X-ray crystallographyMusacchio, ASmith, CJRoseman, AMHarrison, SCKirchhausen, TomasPearse, BMMol Cell 3:761-7017095010Pubmed2007Cryo-electron tomography of clathrin-coated vesicles: structural implications for coat assemblyCheng, YBoll, WKirchhausen, THarrison, SCWalz, TJ Mol Biol 365:892-9trans-Golgi Network Derived Vesicle Uncoatingtrans-Golgi Network Derived Vesicle UncoatingThe heat shock protein Hsc70 and auxilin, a J-domain containing protein, are responsible for clathrin disassembly through an ATP-dependent reaction. This uncoating step may be a point in the pathway subject to regulation. This final step releases the vesicle from the clathrin cage. The vesicle still contatins a specific Vamp molecule, part of the targeting and fusion mechanism that delivers the vesicle to its ultimate destination. This vesicle also contains its cargo, membrane proteins embeded in the Golgi-associated vesicle membrane.Authored: Gillespie, ME, 2009-08-27Reviewed: Simpson, Jeremy C, 2009-08-27Edited: Gillespie, ME, 2008-05-21 20:31:41Reactome DB_ID: 3511751HSC70:Auxillin Complex [cytosol]HSC70:Auxillin ComplexReactome DB_ID: 2644721UniProt:O75061 DNAJC6DNAJC6DNAJC6KIAA0473FUNCTION Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Plays a role in clathrin-mediated endocytosis in neurons (By similarity).SUBUNIT Interacts with HSPA8/HSC70. Interacts with CLTC. Interacts with AP2A2 (By similarity).TISSUE SPECIFICITY Expressed in various brain regions, including cerebellum, corpus callosum, cortex, striatum, brainstem, pons, putamen, spinal cord and substantia nigra. Very low expression in non-neural tissues such as leukocytes, liver, adipose tissue, skeletal muscle and bone marrow.UniProtO750611EQUAL913EQUALReactome DB_ID: 2644761UniProt:P11142 HSPA8HSPA8HSPA8HSPA10HSC70HSP73FUNCTION Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). Interacts with VGF-derived peptide TLQP-21 (PubMed:28934328).SUBUNIT Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with DNAJC7. Interacts with DNAJB12 (via J domain) (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661). Interacts with DNAJB14 (via J domain) (PubMed:23018488, PubMed:24732912, PubMed:27916661). Interacts (via C-terminus) with the E3 ligase CHIP forming a 210 kDa complex of one CHIP and two HSPA8 molecules. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with TRIM5. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with METTL21A. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1. Interacts with PRKN. Interacts with FOXP3. Interacts with DNAJC9 (via J domain) (PubMed:17182002). Interacts with MLLT11 (PubMed:24880125). Interacts with RNF207 (PubMed:25281747). Interacts with DNAJC21 (PubMed:27346687). Interacts with DNAJB2 (PubMed:15936278). Interacts with TTC1 (via TPR repeats) (PubMed:15708368). Interacts with SGTA (via TPR repeats) (By similarity). Interacts with HSF1 (via transactivation domain) (PubMed:9499401). Interacts with HOPX, HSP40 and HSP90 (PubMed:27708256). Interacts with STUB1 (PubMed:27708256). Interacts with BAG2 (PubMed:24318877). Interacts with BAG3 (PubMed:27474739, PubMed:24318877). Interacts with DNAJC12 (PubMed:24122553). Interacts with ZMYND10 (PubMed:29601588). Interacts with HSPC138 (PubMed:25760597). Interacts with BCL2L1, GIMAP5 and MCL1; the interaction with BCL2L1 or MCL1 is impaired in the absence of GIMAP5 (By similarity). Interacts with NLPR12 (PubMed:17947705). Interacts with TTC4 (PubMed:18320024).SUBUNIT (Microbial infection) Interacts with SV40 VP1.TISSUE SPECIFICITY Ubiquitous.INDUCTION Constitutively synthesized.DOMAIN The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins.PTM Acetylated.PTM ISGylated.PTM Trimethylation at Lys-561 reduces fibrillar SNCA binding.SIMILARITY Belongs to the heat shock protein 70 family.UniProtP111422EQUAL646EQUALReactome Database ID Release 75351175Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351175ReactomeR-HSA-3511751Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-351175.1Reactome DB_ID: 3511981Cargo:AP-1:Beta-arrestin:Clathrin Triskelion:Vamp Complex [cytoplasmic vesicle membrane]Cargo:AP-1:Beta-arrestin:Clathrin Triskelion:Vamp ComplexConverted from EntitySet in ReactomeReactome DB_ID: 43267252Golgi-associated Vesicle Cargo [cytoplasmic vesicle membrane]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityReactome DB_ID: 35118652AP-1 Complex [cytoplasmic vesicle membrane]AP-1 ComplexConverted from EntitySet in ReactomeReactome DB_ID: 3511921AP-1 mu [cytoplasmic vesicle membrane]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityAP1M2 [cytoplasmic vesicle membrane]AP1M1 [cytoplasmic vesicle membrane]Reactome DB_ID: 35119412EQUAL822EQUALReactome DB_ID: 35118111EQUAL949EQUALConverted from EntitySet in ReactomeReactome DB_ID: 3511801AP-1 sigma [cytoplasmic vesicle membrane]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityAP1S1 [cytoplasmic vesicle membrane]AP1S3 [cytoplasmic vesicle membrane]AP1S2 [cytoplasmic vesicle membrane]Reactome Database ID Release 75351186Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351186ReactomeR-HSA-3511861Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-351186.1Converted from EntitySet in ReactomeReactome DB_ID: 43502952cytoplasmic vesicle lumenGO0060205Golgi-associated Vesicle Cargo [cytoplasmic vesicle lumen]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityReactome DB_ID: 35082748Reactome DB_ID: 351187521EQUAL418EQUALConverted from EntitySet in ReactomeReactome DB_ID: 43267352Reactome Database ID Release 75351198Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351198ReactomeR-HSA-3511981Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-351198.1Reactome DB_ID: 1135921ATP(4-) [ChEBI:30616]ATP(4-)Adenosine 5'-triphosphateatpATPChEBI30616Reactome DB_ID: 3511751Converted from EntitySet in ReactomeReactome DB_ID: 43267252Reactome DB_ID: 16771752Converted from EntitySet in ReactomeReactome DB_ID: 43502952Reactome DB_ID: 293701ADP(3-) [ChEBI:456216]ADP(3-)ADP trianion5'-O-[(phosphonatooxy)phosphinato]adenosineADPChEBI456216Reactome DB_ID: 35082748Reactome DB_ID: 264470521EQUAL418EQUALReactome DB_ID: 293721Converted from EntitySet in ReactomeReactome DB_ID: 43267352Reactome Database ID Release 75421836Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=421836ReactomeR-HSA-4218361Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-421836.18524399Pubmed1995Role of auxilin in uncoating clathrin-coated vesiclesUngewickell, EUngewickell, HHolstein, SELindner, RPrasad, KBarouch, WMartin, BGreene, LEEisenberg, ENature 378:632-516155256Pubmed2005Depletion of GAK/auxilin 2 inhibits receptor-mediated endocytosis and recruitment of both clathrin and clathrin adaptorsLee, DWZhao, XiaodongZhang, FEisenberg, EGreene, LEJ Cell Sci 118:4311-218374173Pubmed1993Alteration of clathrin light chain expression by transfection and gene disruptionActon, SLWong, DHParham, PBrodsky, FMJackson, APMol Biol Cell 4:647-603.6.5.43.6.5.33.6.5.23.6.5.1trans-Golgi Network Vesicle Scissiontrans-Golgi Network Vesicle ScissionDynamin is recruited to the growing vesicle and, under conditions that interfere with its GTPase activity, dynamin forms a collar or ring around the neck of the budding vesicle. It is unclear whether dynamin acts as a mechanochemical transducer to generate fission or as a recruiter to attach other proteins that are directly responsible for the fission step. Lipid-modifying enzymes such as endophilin are also involved in vesicle formation. Endophilin is an acyltransferase that interacts with dynamin and that generates lysophosphatidic acid. The current view is that this reaction produces a negative curvature at the neck of the vesicle.Authored: Gillespie, ME, 2009-08-27Reviewed: Simpson, Jeremy C, 2009-08-27Edited: Gillespie, ME, 2008-05-21 20:31:41Reactome DB_ID: 294381Reactome DB_ID: 3508251Reactome DB_ID: 18295811EQUAL352EQUALReactome DB_ID: 221318011EQUAL870EQUALReactome DB_ID: 3511981Reactome DB_ID: 294201Reactome DB_ID: 293721PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 350825GO0003924GO molecular functionReactome Database ID Release 75351174Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=351174Reactome Database ID Release 75421835Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=421835ReactomeR-HSA-4218351Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-421835.18670264Pubmed1996Dynamin II binds to the trans-Golgi networkMaier, OKnoblich, MWestermann, PBiochem Biophys Res Commun 223:229-3311604418Pubmed2001Generation of high curvature membranes mediated by direct endophilin bilayer interactionsFarsad, KRingstad, NTakei, KFloyd, SRRose, KDe Camilli, PietroJ Cell Biol 155:193-200ACBD3 binds GOLGB1ACBD3 binds GOLGB1Golgi resident protein GCP60 (ACBD3) is a Golgi membrane-associated protein thought to be involved in the maintenance of the Golgi structure by interacting with Golgin subfamily B member 1 (GOLGB1, giantin), which may mediate protein transport between the endoplasmic reticulum and the Golgi (Sohda et al. 2001).Authored: Jassal, Bijay, 2016-05-31Reviewed: D'Eustachio, Peter, 2016-07-15Edited: Jassal, Bijay, 2016-05-31Reactome DB_ID: 68105051GOLGB1 homodimer [Golgi membrane]GOLGB1 homodimerReactome DB_ID: 68100042UniProt:Q14789 GOLGB1GOLGB1GOLGB1FUNCTION May participate in forming intercisternal cross-bridges of the Golgi complex.SUBUNIT Homodimer; disulfide-linked. Interacts with PLK3.MISCELLANEOUS Antigen in chronic rheumatoid arthritis and in the autoimmune disease Sjoegren syndrome.UniProtQ147891EQUAL3259EQUALReactome Database ID Release 756810505Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=6810505ReactomeR-HSA-68105051Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-6810505.1Reactome DB_ID: 88749811UniProt:Q9H3P7 ACBD3ACBD3GOLPH1GCP60GOCAP1ACBD3FUNCTION Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi (PubMed:11590181). Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity). Recruits PI4KB to the Golgi apparatus membrane; enhances the enzyme activity of PI4KB activity via its membrane recruitment thereby increasing the local concentration of the substrate in the vicinity of the kinase (PubMed:27009356).FUNCTION (Microbial infection) Plays an essential role in Aichi virus RNA replication by recruiting PI4KB at the viral replication sites.SUBUNIT Homodimer (PubMed:23572552). Interacts with the C-terminal cytoplasmic domain of giantin/GOLGB1 (PubMed:11590181). Interacts with PBR and PKA regulatory subunit RI-alpha. Does not interact with PKA regulatory subunit RI-beta nor PKA regulatory subunit RII-alpha (By similarity). Interacts (via Q domain) with PI4KB (via N-terminus) (PubMed:23572552, PubMed:27009356, PubMed:27989622, PubMed:22124328, PubMed:22258260). Interacts (via Q domain) with TBC1D22A AND TBC1D22B; interactions with PI4KB and with TBC1D22A and TBC1D22B are mutually exclusive (PubMed:23572552, PubMed:27009356, PubMed:27989622, PubMed:22124328). Interacts with C10ORF76 and RAB11B (PubMed:23572552).SUBUNIT (Microbial infection) Interacts (via GOLD domain) with 3A proteins from various picornaviruses, including poliovirus, enterovirus A71, enterovirus D68, hepatitis A virus, human parechovirus 1, poliovirus, Human rhinovirus-14 (Hrv-14), coysackievirus B2, coysackievirus B3, coysackievirus B5, Aichi virus and human klassevirus (PubMed:23572552, PubMed:22258260, PubMed:31381608). Interacts (via GOLD domain) with Aichi virus protein 3A; this interaction allows the formation of a 3A/ACBD3/PI4KB complex in order to synthesize PI4P at the viral RNA replication sites (PubMed:23572552, PubMed:22124328, PubMed:27989622, PubMed:30755512) (Probable). Interacts with Aichi virus protein 2B (PubMed:22124328). Interacts with Aichi virus protein 2C (PubMed:22124328).TISSUE SPECIFICITY Ubiquitous, with highest expression in testis and ovary.DOMAIN The central Gln-rich region (Q domain) is involved in binding to PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552). The C-terminal GOLD domain is essential for giantin binding. The GOLD domain is also involved in homodimerization (PubMed:23572552).DOMAIN (Microbial infection) The GOLD domain is involved in binding to the picornaviral protein 3A.UniProtQ9H3P72EQUAL528EQUALReactome DB_ID: 88749751ACBD3:GOLGB1 dimer [Golgi membrane]ACBD3:GOLGB1 dimerReactome DB_ID: 68105051Reactome DB_ID: 887498112EQUAL528EQUALReactome Database ID Release 758874975Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=8874975ReactomeR-HSA-88749751Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-8874975.1Reactome Database ID Release 758874979Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=8874979ReactomeR-HSA-88749791Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-8874979.111590181Pubmed2001Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantinSohda, MMisumi, YYamamoto, AYano, ANakamura, NIkehara, YJ. Biol. Chem. 276:45298-306Reactome Database ID Release 75432722Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=432722ReactomeR-HSA-4327223Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-432722.3