ELOC

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0006511 ubiquitin-dependent protein catabolic process	IBA GO_REF:0000033	ACCEPT	Summary: Accepted as a pathway-level consequence. ELOC-containing CRL2/CRL5 complexes target substrates for ubiquitination and downstream proteasomal degradation. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md A central and well-established role of ELOC is within the VHL–ELOB/ELOC–CUL2–RBX1 E3 ubiquitin ligase
GO:0070449 elongin complex	IBA GO_REF:0000033	ACCEPT	Summary: Correct. ELOC is Elongin C, the SKP1-like subunit of the Elongin BC module and Elongin complex. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md ELOC (Elongin C) forms a heterodimer with ELOB (Elongin B), commonly referred to as the Elongin BC module.
GO:0030674 protein-macromolecule adaptor activity	IBA GO_REF:0000033	ACCEPT	Summary: Correct and informative. ELOC acts as a protein-macromolecule adaptor within Elongin BC, bridging BC-box/VHL-box/SOCS-box substrate receptors to Cul2/Cul5 CRL scaffolds. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md The literature retrieved here consistently uses ELOC as the human gene encoding Elongin C (also called TCEB1) and describes it as the Elongin B/C adaptor subunit that binds BC-box/VHL-box/SOCS-box motifs and bridges substrate receptors to CUL2 or CUL5 in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
GO:0000151 ubiquitin ligase complex	IEA GO_REF:0000117	MARK AS OVER ANNOTATED	Summary: Correct but broad. ELOC is better captured as an adaptor subunit in specific Cul2/Cul5 ubiquitin ligase complexes rather than by the generic ubiquitin ligase complex term alone. Reason: More specific Cul2-RING, Cul5-RING, and Elongin complex annotations capture the supported complex membership.
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: Supported. ELOC has nuclear functions in Elongin/CRL assemblies and has experimentally observed nuclear/nucleolar localization. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005737 cytoplasm	IEA GO_REF:0000117	MARK AS OVER ANNOTATED	Summary: Correct but less precise than the available cytosol and nuclear/nucleoplasm localization annotations. Reason: Use cytosol and nucleus/nucleoplasm annotations where available rather than generic cytoplasm.
GO:0006511 ubiquitin-dependent protein catabolic process	IEA GO_REF:0000002	ACCEPT	Summary: Accepted as a pathway-level consequence. ELOC-containing CRL2/CRL5 complexes target substrates for ubiquitination and downstream proteasomal degradation. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md A central and well-established role of ELOC is within the VHL–ELOB/ELOC–CUL2–RBX1 E3 ubiquitin ligase
GO:0005515 protein binding	IPI PMID:10205047 Structure of the VHL-ElonginC-ElonginB complex: implications...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:12004076 Structure of an HIF-1alpha -pVHL complex: hydroxyproline rec...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:12050673 Structural basis for the recognition of hydroxyproline in HI...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:12149480 Mammalian mediator subunit mMED8 is an Elongin BC-interactin...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:15601820 VHL-box and SOCS-box domains determine binding specificity f...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:16643902 The E3 ubiquitin ligase HOIL-1 induces the polyubiquitinatio...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:17183367 COMMD1 promotes the ubiquitination of NF-kappaB subunits thr...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:19159283 Array MAPPIT: high-throughput interactome analysis in mammal...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:19322197 Termination of NF-kappaB activity through a gammaherpesvirus...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:19327355 Requirement for microtubule integrity in the SOCS1-mediated ...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:20211142 An atlas of combinatorial transcriptional regulation in mous...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:21516116 Next-generation sequencing to generate interactome datasets.	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:21822215 The tumour antigen PRAME is a subunit of a Cul2 ubiquitin li...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:21988832 Toward an understanding of the protein interaction network o...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:22190034 Global landscape of HIV-human protein complexes.	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:23460923 PRAME is a golgi-targeted protein that associates with the E...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:23563313 CCDC22 deficiency in humans blunts activation of proinflamma...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:32353859 A SARS-CoV-2 protein interaction map reveals targets for dru...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:33060197 Comparative host-coronavirus protein interaction networks re...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:33827988 ORF10-Cullin-2-ZYG11B complex is not required for SARS-CoV-2...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:36217030 A comprehensive SARS-CoV-2-human protein-protein interactome...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0016567 protein ubiquitination	IEA GO_REF:0000041	ACCEPT	Summary: Accepted. ELOC is not the catalytic ubiquitin-transfer subunit, but it is required as an Elongin BC adaptor component of CRL2/CRL5 ligases that mediate substrate ubiquitination. Reason: Keep the process annotation because ELOC is a direct required module in CRL ubiquitination complexes. Do not add GO:1990756 for ELOC itself, because substrate recognition is supplied by SOCS-box, VHL-box, or related substrate receptor proteins rather than by ELOC. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md ELOC’s primary biochemical function in these contexts is protein–protein interaction and complex assembly, not ubiquitin transfer catalysis per se.
GO:0031466 Cul5-RING ubiquitin ligase complex	IEA GO_REF:0000107	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0070449 elongin complex	IEA GO_REF:0000107	ACCEPT	Summary: Correct. ELOC is Elongin C, the SKP1-like subunit of the Elongin BC module and Elongin complex. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md ELOC (Elongin C) forms a heterodimer with ELOB (Elongin B), commonly referred to as the Elongin BC module.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:40963025 Covariation MS uncovers a protein that controls cysteine cat...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0000122 negative regulation of transcription by RNA polymerase II	NAS PMID:28591624 Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligas...	KEEP AS NON CORE	Summary: Kept as non-core. Negative transcriptional regulation can arise in specific Elongin-associated contexts, but it is not the central ELOC molecular function. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md The literature retrieved here consistently uses ELOC as the human gene encoding Elongin C (also called TCEB1) and describes it as the Elongin B/C adaptor subunit that binds BC-box/VHL-box/SOCS-box motifs and bridges substrate receptors to CUL2 or CUL5 in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process	NAS PMID:31273098 A glycine-specific N-degron pathway mediates the quality con...	KEEP AS NON CORE	Summary: Supported as a non-core consequence of ELOC-containing CRL activity. ELOC is an adaptor/regulatory subunit rather than the proteasome or catalytic ubiquitin-transfer component. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md A central and well-established role of ELOC is within the VHL–ELOB/ELOC–CUL2–RBX1 E3 ubiquitin ligase
GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway	NAS PMID:15601820 VHL-box and SOCS-box domains determine binding specificity f...	KEEP AS NON CORE	Summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL2 uses CUL2 as scaffold and RBX1 as the RING component, and uniquely uses ELOB/ELOC as adaptor proteins for substrate receptors like VHL.
GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway	NAS PMID:21822215 The tumour antigen PRAME is a subunit of a Cul2 ubiquitin li...	KEEP AS NON CORE	Summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL2 uses CUL2 as scaffold and RBX1 as the RING component, and uniquely uses ELOB/ELOC as adaptor proteins for substrate receptors like VHL.
GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway	NAS PMID:22649776 The Role of Elongin BC-Containing Ubiquitin Ligases.	KEEP AS NON CORE	Summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL2 uses CUL2 as scaffold and RBX1 as the RING component, and uniquely uses ELOB/ELOC as adaptor proteins for substrate receptors like VHL.
GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway	NAS PMID:29779948 The Eukaryotic Proteome Is Shaped by E3 Ubiquitin Ligases Ta...	KEEP AS NON CORE	Summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL2 uses CUL2 as scaffold and RBX1 as the RING component, and uniquely uses ELOB/ELOC as adaptor proteins for substrate receptors like VHL.
GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway	NAS PMID:33398168 Molecular basis for arginine C-terminal degron recognition b...	KEEP AS NON CORE	Summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL2 uses CUL2 as scaffold and RBX1 as the RING component, and uniquely uses ELOB/ELOC as adaptor proteins for substrate receptors like VHL.
GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway	NAS PMID:34743205 CRL2-KLHDC3 E3 ubiquitin ligase complex suppresses ferroptos...	KEEP AS NON CORE	Summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL2 uses CUL2 as scaffold and RBX1 as the RING component, and uniquely uses ELOB/ELOC as adaptor proteins for substrate receptors like VHL.
GO:1990116 ribosome-associated ubiquitin-dependent protein catabolic process	NAS PMID:33909987 Convergence of mammalian RQC and C-end rule proteolytic path...	KEEP AS NON CORE	Summary: Supported as a non-core specialized CRL pathway context. ELOC contributes through Elongin BC adaptor function in substrate-specific ligase assemblies. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md The literature retrieved here consistently uses ELOC as the human gene encoding Elongin C (also called TCEB1) and describes it as the Elongin B/C adaptor subunit that binds BC-box/VHL-box/SOCS-box motifs and bridges substrate receptors to CUL2 or CUL5 in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
GO:2000104 negative regulation of DNA-templated DNA replication	NAS PMID:22649776 The Role of Elongin BC-Containing Ubiquitin Ligases.	KEEP AS NON CORE	Summary: Kept as non-core. Negative regulation of DNA-templated DNA replication is likely a downstream substrate-specific consequence of ELOC-containing ligase activity rather than ELOC's primary molecular role. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md ELOC’s primary biochemical function in these contexts is protein–protein interaction and complex assembly, not ubiquitin transfer catalysis per se.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:39039081 Molecular insights into degron recognition by CRL5(ASB7) ubi...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:40440427 ASB7 is a negative regulator of H3K9me3 homeostasis.	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0031462 Cul2-RING ubiquitin ligase complex	IDA PMID:37844242 Molecular basis for C-degron recognition by CRL2(APPBP2) ubi...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul2-RING ligase assemblies such as CRL2-VHL. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL2 uses CUL2 as scaffold and RBX1 as the RING component, and uniquely uses ELOB/ELOC as adaptor proteins for substrate receptors like VHL.
GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway	IDA PMID:37844242 Molecular basis for C-degron recognition by CRL2(APPBP2) ubi...	KEEP AS NON CORE	Summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL2 uses CUL2 as scaffold and RBX1 as the RING component, and uniquely uses ELOB/ELOC as adaptor proteins for substrate receptors like VHL.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:35512830 Rab40c regulates focal adhesions and PP6 activity by control...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:37816714 Structure-based design of a phosphotyrosine-masked covalent ...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:34857742 Discovery of an exosite on the SOCS2-SH2 domain that enhance...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:21980433 The SOCS2 ubiquitin ligase complex regulates growth hormone ...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:25505247 Biophysical studies on interactions and assembly of full-siz...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:38418882 The CRL5-SPSB3 ubiquitin ligase targets nuclear cGAS for deg...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:31387940 BIK ubiquitination by the E3 ligase Cul5-ASB11 determines ce...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:32513959 Structure and dynamics of the ASB9 CUL-RING E3 Ligase.	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:23837592 Multimeric complexes among ankyrin-repeat and SOCS-box prote...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:33268465 The Mechanism of NEDD8 Activation of CUL5 Ubiquitin E3 Ligas...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0140958 target-directed miRNA degradation	IMP PMID:33184237 The ZSWIM8 ubiquitin ligase mediates target-directed microRN...	KEEP AS NON CORE	Summary: Kept as non-core. Target-directed miRNA degradation is a specialized pathway context for an ELOC-containing CRL assembly rather than the general function of ELOC itself. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md The literature retrieved here consistently uses ELOC as the human gene encoding Elongin C (also called TCEB1) and describes it as the Elongin B/C adaptor subunit that binds BC-box/VHL-box/SOCS-box motifs and bridges substrate receptors to CUL2 or CUL5 in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
GO:0005515 protein binding	IPI PMID:22510880 Nuclear receptor binding protein 1 regulates intestinal prog...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0001222 transcription corepressor binding	IPI PMID:7660122 Inhibition of transcription elongation by the VHL tumor supp...	KEEP AS NON CORE	Summary: Kept as non-core. ELOC can participate in transcriptional regulatory complexes, but its primary role is the Elongin BC adaptor/regulatory module. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md The literature retrieved here consistently uses ELOC as the human gene encoding Elongin C (also called TCEB1) and describes it as the Elongin B/C adaptor subunit that binds BC-box/VHL-box/SOCS-box motifs and bridges substrate receptors to CUL2 or CUL5 in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
GO:0006367 transcription initiation at RNA polymerase II promoter	IDA PMID:7660122 Inhibition of transcription elongation by the VHL tumor supp...	REMOVE	Summary: Remove. The cited PMID:7660122 paper concerns VHL inhibition of Elongin-dependent RNA polymerase II transcription elongation, not transcription initiation. Reason: Evidence-term mismatch: PMID:7660122 supports transcription elongation biology, not GO:0006367 transcription initiation at RNA polymerase II promoter.
GO:0070449 elongin complex	IDA PMID:7660122 Inhibition of transcription elongation by the VHL tumor supp...	ACCEPT	Summary: Correct. ELOC is Elongin C, the SKP1-like subunit of the Elongin BC module and Elongin complex. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md ELOC (Elongin C) forms a heterodimer with ELOB (Elongin B), commonly referred to as the Elongin BC module.
GO:0016567 protein ubiquitination	IDA PMID:30166453 CRL4(AMBRA1) targets Elongin C for ubiquitination and degrad...	ACCEPT	Summary: Accepted. ELOC is not the catalytic ubiquitin-transfer subunit, but it is required as an Elongin BC adaptor component of CRL2/CRL5 ligases that mediate substrate ubiquitination. Reason: Keep the process annotation because ELOC is a direct required module in CRL ubiquitination complexes. Do not add GO:1990756 for ELOC itself, because substrate recognition is supplied by SOCS-box, VHL-box, or related substrate receptor proteins rather than by ELOC. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md ELOC’s primary biochemical function in these contexts is protein–protein interaction and complex assembly, not ubiquitin transfer catalysis per se.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:30166453 CRL4(AMBRA1) targets Elongin C for ubiquitination and degrad...	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors.
GO:0005515 protein binding	IPI PMID:21119685 Notch-induced Asb2 expression promotes protein ubiquitinatio...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0031462 Cul2-RING ubiquitin ligase complex	ISS GO_REF:0000024	ACCEPT	Summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul2-RING ligase assemblies such as CRL2-VHL. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md CRL2 uses CUL2 as scaffold and RBX1 as the RING component, and uniquely uses ELOB/ELOC as adaptor proteins for substrate receptors like VHL.
GO:0005515 protein binding	IPI PMID:21199876 Regulation of inducible nitric-oxide synthase by the SPRY do...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005829 cytosol	TAS Reactome:R-HSA-1234159	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-1234163	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-1234173	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-1234175	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-1234177	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-1234183	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-180540	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-180555	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-180603	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-8952039	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-8952044	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-8952625	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-8952626	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-8955241	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-8955289	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-8956040	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-8956099	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-8956103	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-8956106	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-9705738	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-9755303	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-9833107	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-9833155	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-9954721	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005829 cytosol	TAS Reactome:R-HSA-9954723	ACCEPT	Summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-112379	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-112385	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-112392	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-112395	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-112396	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-112435	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-112436	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-113411	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-113412	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-113413	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-113414	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-113429	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-1234169	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-1234172	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-1234175	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-6797606	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-6797616	ACCEPT	Summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin.
GO:0005515 protein binding	IPI PMID:15590694 Suppressors of cytokine signaling 4 and 5 regulate epidermal...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0005515 protein binding	IPI PMID:10851083 Tracheal development and the von Hippel-Lindau tumor suppres...	REMOVE	Summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership. Reason: Replace generic binding with specific adaptor and CRL complex annotations.
GO:0006357 regulation of transcription by RNA polymerase II	TAS PMID:7660129 Elongin (SIII): a multisubunit regulator of elongation by RN...	KEEP AS NON CORE	Summary: Kept as non-core. Regulation of RNA polymerase II transcription is a supported broader context, but ELOC is best captured by Elongin BC adaptor and CRL complex roles. Supporting Evidence: file:human/ELOC/ELOC-deep-research-falcon.md The literature retrieved here consistently uses ELOC as the human gene encoding Elongin C (also called TCEB1) and describes it as the Elongin B/C adaptor subunit that binds BC-box/VHL-box/SOCS-box motifs and bridges substrate receptors to CUL2 or CUL5 in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.

Core Functions

ELOC is the SKP1-like adaptor subunit of Elongin BC that enables substrate-receptor coupling and assembly of Elongin, CRL2, and CRL5 complexes rather than acting as a ubiquitin-transfer enzyme itself.

Molecular Function:

protein-macromolecule adaptor activity

Directly Involved In:

protein ubiquitination ubiquitin-dependent protein catabolic process

Cellular Locations:

nucleoplasm cytosol

In Complex:

elongin complex

Supporting Evidence:

file:human/ELOC/ELOC-deep-research-falcon.md
The literature retrieved here consistently uses **ELOC** as the human gene encoding **Elongin C** (also called **TCEB1**) and describes it as the **Elongin B/C adaptor subunit** that binds **BC-box/VHL-box/SOCS-box** motifs and bridges substrate receptors to **CUL2** or **CUL5** in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
file:human/ELOC/ELOC-deep-research-falcon.md
**ELOC (Elongin C)** forms a heterodimer with **ELOB (Elongin B)**, commonly referred to as the **Elongin BC** module.
file:human/ELOC/ELOC-deep-research-falcon.md
ELOC’s primary biochemical function in these contexts is **protein–protein interaction and complex assembly**, not ubiquitin transfer catalysis per se.

References

GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000024

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000041

Gene Ontology annotation based on UniPathway vocabulary mapping

GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000107

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

GO_REF:0000117

Electronic Gene Ontology annotations created by ARBA machine learning models

PMID:10205047

Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function.

PMID:10851083

Tracheal development and the von Hippel-Lindau tumor suppressor homolog in Drosophila.

PMID:12004076

Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling.

PMID:12050673

Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL.

PMID:12149480

Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase.

PMID:15590694

Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling.

PMID:15601820

VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases.

PMID:16189514

Towards a proteome-scale map of the human protein-protein interaction network.

PMID:16643902

The E3 ubiquitin ligase HOIL-1 induces the polyubiquitination and degradation of SOCS6 associated proteins.

PMID:17183367

COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase.

PMID:19159283

Array MAPPIT: high-throughput interactome analysis in mammalian cells.

PMID:19322197

Termination of NF-kappaB activity through a gammaherpesvirus protein that assembles an EC5S ubiquitin-ligase.

PMID:19327355

Requirement for microtubule integrity in the SOCS1-mediated intracellular dynamics of HIV-1 Gag.

PMID:20211142

An atlas of combinatorial transcriptional regulation in mouse and man.

PMID:21119685

Notch-induced Asb2 expression promotes protein ubiquitination by forming non-canonical E3 ligase complexes.

PMID:21145461

Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics.

PMID:21199876

Regulation of inducible nitric-oxide synthase by the SPRY domain- and SOCS box-containing proteins.

PMID:21516116

Next-generation sequencing to generate interactome datasets.

PMID:21822215

The tumour antigen PRAME is a subunit of a Cul2 ubiquitin ligase and associates with active NFY promoters.

PMID:21980433

The SOCS2 ubiquitin ligase complex regulates growth hormone receptor levels.

PMID:21988832

Toward an understanding of the protein interaction network of the human liver.

PMID:22190034

Global landscape of HIV-human protein complexes.

PMID:22510880

Nuclear receptor binding protein 1 regulates intestinal progenitor cell homeostasis and tumour formation.

PMID:22649776

The Role of Elongin BC-Containing Ubiquitin Ligases.

PMID:23460923

PRAME is a golgi-targeted protein that associates with the Elongin BC complex and is upregulated by interferon-gamma and bacterial PAMPs.

PMID:23563313

CCDC22 deficiency in humans blunts activation of proinflammatory NF-κB signaling.

PMID:23837592

Multimeric complexes among ankyrin-repeat and SOCS-box protein 9 (ASB9), ElonginBC, and Cullin 5: insights into the structure and assembly of ECS-type Cullin-RING E3 ubiquitin ligases.

PMID:25416956

A proteome-scale map of the human interactome network.

PMID:25505247

Biophysical studies on interactions and assembly of full-size E3 ubiquitin ligase: suppressor of cytokine signaling 2 (SOCS2)-elongin BC-cullin 5-ring box protein 2 (RBX2).

PMID:28514442

Architecture of the human interactome defines protein communities and disease networks.

PMID:28591624

Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex.

PMID:29779948

The Eukaryotic Proteome Is Shaped by E3 Ubiquitin Ligases Targeting C-Terminal Degrons.

PMID:30166453

CRL4(AMBRA1) targets Elongin C for ubiquitination and degradation to modulate CRL5 signaling.

PMID:31273098

A glycine-specific N-degron pathway mediates the quality control of protein N-myristoylation.

PMID:31387940

BIK ubiquitination by the E3 ligase Cul5-ASB11 determines cell fate during cellular stress.

PMID:31515488

Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.

PMID:31980649

Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).

PMID:32296183

A reference map of the human binary protein interactome.

PMID:32353859

A SARS-CoV-2 protein interaction map reveals targets for drug repurposing.

PMID:32513959

Structure and dynamics of the ASB9 CUL-RING E3 Ligase.

PMID:33060197

Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms.

PMID:33184237

The ZSWIM8 ubiquitin ligase mediates target-directed microRNA degradation.

PMID:33268465

The Mechanism of NEDD8 Activation of CUL5 Ubiquitin E3 Ligases.

PMID:33398168

Molecular basis for arginine C-terminal degron recognition by Cul2(FEM1) E3 ligase.

PMID:33827988

ORF10-Cullin-2-ZYG11B complex is not required for SARS-CoV-2 infection.

PMID:33909987

Convergence of mammalian RQC and C-end rule proteolytic pathways via alanine tailing.

PMID:33961781

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

PMID:34743205

CRL2-KLHDC3 E3 ubiquitin ligase complex suppresses ferroptosis through promoting p14(ARF) degradation.

PMID:34857742

Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands.

PMID:35512830

Rab40c regulates focal adhesions and PP6 activity by controlling ANKRD28 ubiquitylation.

PMID:36217030

A comprehensive SARS-CoV-2-human protein-protein interactome reveals COVID-19 pathobiology and potential host therapeutic targets.

PMID:37816714

Structure-based design of a phosphotyrosine-masked covalent ligand targeting the E3 ligase SOCS2.

PMID:37844242

Molecular basis for C-degron recognition by CRL2(APPBP2) ubiquitin ligase.

PMID:38418882

The CRL5-SPSB3 ubiquitin ligase targets nuclear cGAS for degradation.

PMID:39039081

Molecular insights into degron recognition by CRL5(ASB7) ubiquitin ligase.

PMID:40205054

Multimodal cell maps as a foundation for structural and functional genomics.

PMID:40440427

ASB7 is a negative regulator of H3K9me3 homeostasis.

PMID:40963025

Covariation MS uncovers a protein that controls cysteine catabolism.

PMID:7660122

Inhibition of transcription elongation by the VHL tumor suppressor protein.

PMID:7660129

Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II.

Reactome:R-HSA-112379

Recruitment of elongation factors to form elongation complex

Reactome:R-HSA-112385

Addition of nucleotides leads to transcript elongation

Reactome:R-HSA-112392

Resumption of elongation after recovery from pausing

Reactome:R-HSA-112395

Abortive termination of elongation after arrest

Reactome:R-HSA-112396

Separation of elongating transcript from template

Reactome:R-HSA-112435

Formation of Elongin BC complex

Reactome:R-HSA-112436

Formation of Elongin complex

Reactome:R-HSA-113411

2-4 nt.backtracking of Pol II complex on the template leading to elongation pausing

Reactome:R-HSA-113412

Pol II elongation complex moves on the template as transcript elongates

Reactome:R-HSA-113413

TFIIS-mediated recovery of elongation from arrest

Reactome:R-HSA-113414

7-14 nt. Backtracking of Pol II complex on the template leading to elongation arrest

Reactome:R-HSA-113429

Elongating transcript encounters a lesion in the template

Reactome:R-HSA-1234159

Proteasome proteolyzes ub-HIF-alpha

Reactome:R-HSA-1234163

Cytosolic VBC complex ubiquitinylates hydroxyprolyl-HIF-alpha

Reactome:R-HSA-1234169

Nuclear VHL:EloB,C:CUL2:RBX1 binds hydroxyprolyl-HIF-alpha

Reactome:R-HSA-1234172

Nuclear VBC complex ubiquitinylates HIF-alpha

Reactome:R-HSA-1234173

Cytosolic PHD2,3 hydroxylates proline residues on HIF3A

Reactome:R-HSA-1234175

ub-hydroxyPro-HIF-alpha:VHL:EloB,C:CUL2:RBX1 translocates from the nucleus to the cytosol

Reactome:R-HSA-1234177

Cytosolic PHD2,3 hydroxylates proline residues on HIF1A

Reactome:R-HSA-1234183

Cytosolic VHL:EloB,C:CUL2:RBX1 binds hydroxyprolyl-HIF-alpha

Reactome:R-HSA-180540

Multi-ubiquitination of APOBEC3G

Reactome:R-HSA-180555

Association of APOBEC3G:Vif with the Cul5-SCF complex

Reactome:R-HSA-180603

Proteosome-mediated degradation of APOBEC3G

Reactome:R-HSA-6797606

CDK12 phosphorylates RNA Pol II CTD at DNA repair genes

Reactome:R-HSA-6797616

CCNK:CDK12 binds RNA Pol II at DNA repair genes

Reactome:R-HSA-8952039

NEDD8:AcM-UBE2F binds CRL5 E3 ubiquitin ligase complex

Reactome:R-HSA-8952044

AcM-UBE2F transfers NEDD8 to CRL5 E3 ubiquitin ligase complex

Reactome:R-HSA-8952625

NEDD8:AcM-UBE2M binds CRL2 E3 ubiquitin ligase complex

Reactome:R-HSA-8952626

AcM-UBE2M transfers NEDD8 to CRL2 E3 ubiquitin ligase complex

Reactome:R-HSA-8955241

CAND1 binds cytosolic CRL E3 ubiquitin ligases

Reactome:R-HSA-8955289

COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes

Reactome:R-HSA-8956040

COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes

Reactome:R-HSA-8956099

VHL:EloB,C:NEDD8-CUL2:RBX1 complex binds UBXN7

Reactome:R-HSA-8956103

VHL:EloB,C:NEDD8-CUL2:RBX1 complex binds hydroxyprolyl-HIF-alpha

Reactome:R-HSA-8956106

VHL:EloB,C:NEDD8-CUL2:RBX1 complex ubiquitinylates HIF-alpha

Reactome:R-HSA-9705738

SOCS1,3 ubiquitinates CSF3R in SOCS1,3:p-4Y-CSF3R:CSF3 dimer:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2:CUL5:ELOB:ELOC:RNF7

Reactome:R-HSA-9755303

26S proteasome degrades HIFalpha

Reactome:R-HSA-9833107

Association of NS1 (1C) with Cul5 and SCF

Reactome:R-HSA-9833155

Ubiquitination of STAT2

Reactome:R-HSA-9954721

NEDD8-K699-CUL2:ELOB:ELOC:RBX1:KLHDC10 K48 polyubiquitinates alanine-tailed nascent peptide

Reactome:R-HSA-9954723

NEDD8-K699-CUL2:ELOB:ELOC:RBX1:KLHDC10 binds alanine-tailed nascent peptide

file:human/ELOC/ELOC-deep-research-falcon.md

Falcon deep research report for human ELOC

Suggested Experiments

Experiment: Rescue ELOC-depleted cells with interface mutants and compare VHL-HIF turnover, SOCS-box CRL5 substrate degradation, and RNA polymerase II elongation readouts.

Hypothesis: ELOC interface residues differentially support CRL2-VHL, CRL5-SOCS, and Elongin transcription elongation assemblies.

Experiment: Reconstitute ELOBC-containing CRL2 and CRL5 complexes with wild-type and mutant ELOC and measure complex formation, substrate receptor recruitment, and ubiquitination kinetics.

Hypothesis: ELOC promotes ubiquitin-dependent substrate degradation through adaptor-mediated complex assembly rather than catalytic ubiquitin transfer.

Deep Research

Falcon

(ELOC-deep-research-falcon.md)

this with annotations you find in gene/protein databases, but these can be outdated or inaccurate. Falcon Edison Scientific Literature 44 citations 2026-05-11T14:25:20.283197

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Research report: Human ELOC (TCEB1) / Elongin-C (UniProt Q15369)—functional annotation and recent research

0) Target verification (gene/protein identity)

The literature retrieved here consistently uses ELOC as the human gene encoding Elongin C (also called TCEB1) and describes it as the Elongin B/C adaptor subunit that binds BC-box/VHL-box/SOCS-box motifs and bridges substrate receptors to CUL2 or CUL5 in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role. (kim2025identificationofnovel pages 4-6, fischer2023decipheringthemolecular pages 54-57, fischer2023decipheringthemolecular pages 65-67)

1) Key concepts and definitions (current understanding)

1.1 Elongin BC is an adaptor module; ELOC provides the BC-box binding surface

ELOC (Elongin C) forms a heterodimer with ELOB (Elongin B), commonly referred to as the Elongin BC module. This module is reused as an adaptor in multiple pathways and complexes, notably:
- transcription-related Elongin (ABC) complexes, and
- CRL2 and CRL5 ubiquitin ligases, where Elongin BC bridges substrate receptors to a cullin scaffold. (fischer2023decipheringthemolecular pages 54-57, fischer2023decipheringthemolecular pages 57-59)

At the interaction-motif level, many substrate receptors carry a BC-box (often within a larger VHL-box or SOCS-box), which binds Elongin BC; for VHL-box proteins, an additional CUL2-box mediates selective binding to CUL2, while for SOCS-box proteins a CUL5-box mediates binding to CUL5. (fischer2023decipheringthemolecular pages 54-57, fischer2023decipheringthemolecular pages 57-59)

1.2 Canonical CRL architectures relevant to ELOC

Cullin-RING ligases are modular E3 ubiquitin ligases. For the ELOC-relevant CRLs:
- CRL2 uses CUL2 as scaffold and RBX1 as the RING component, and uniquely uses ELOB/ELOC as adaptor proteins for substrate receptors like VHL. (fischer2023decipheringthemolecular pages 54-57)
- CRL5 uses CUL5 and RBX2/SAG, and commonly uses SOCS-box substrate receptors that recruit ELOB/ELOC as adaptors. (fischer2023decipheringthemolecular pages 57-59)

1.3 ELOC is not the catalytic enzyme; it is a structural adaptor controlling assembly and specificity

ELOC’s primary biochemical function in these contexts is protein–protein interaction and complex assembly, not ubiquitin transfer catalysis per se. Its functional impact is therefore mainly through:
- enabling assembly of active E3 complexes,
- selecting cullin scaffold (CUL2 vs CUL5) via receptor motifs, and
- controlling kinetics/geometry of ubiquitination indirectly through complex stability and dynamics. (lin2024diversityofstructure pages 3-5, wang2024cand1inhibitscullin2ring pages 6-8)

2) Molecular functions, complexes, and pathways

2.1 CRL2^VHL: oxygen sensing via HIFα degradation

A central and well-established role of ELOC is within the VHL–ELOB/ELOC–CUL2–RBX1 E3 ubiquitin ligase (often termed CRL2^VHL), which targets HIF-α subunits for ubiquitination after proline hydroxylation by PHD enzymes. (fischer2023decipheringthemolecular pages 54-57, andreou2022elonginc(eloctceb1)associated pages 4-7)

Structural/mechanistic evidence for the ELOC–pVHL interface. A recurrent disease hotspot variant ELOC p.Tyr79Cys lies in a conserved region important for pVHL interaction; Tyr79 mediates a key contact (hydrogen bond) with pVHL (shown structurally). (andreou2022elonginc(eloctceb1)associated pages 2-4, andreou2022elonginc(eloctceb1)associated media cca6df01)

Functional consequence in tumors. In ELOC-mutated RCC described as “VHL-competent,” the Tyr79Cys variant shows reduced co-precipitation with other complex components and correlates with accumulation of HIF-1α and HIF-2α, consistent with impaired CRL2^VHL-mediated degradation. (andreou2022elonginc(eloctceb1)associated pages 4-7)

Network-level impact. HIF activation drives broad transcriptional programs; one synthesis in the retrieved literature states HIF directly regulates >800 target genes, illustrating the magnitude of downstream consequences when the ELOC/VHL axis is disrupted. (fischer2023decipheringthemolecular pages 54-57)

ELOC also functions as the adaptor (via ELOB/ELOC) that allows SOCS-box proteins to assemble CRL5 complexes with CUL5 and RBX2. In this framework, SOCS-box proteins use a BC-box to bind ELOB/ELOC and a CUL5-box (LPΦP-like motif) to bind CUL5. (fischer2023decipheringthemolecular pages 57-59)

In the disease-genetics study on ELOC-associated VHL-like disease, ELOC is explicitly linked to SOCS-mediated complexes and their substrates, including signaling proteins such as JAK2, reinforcing the connection to cytokine/JAK/STAT pathway control via CRL5 assemblies. (andreou2022elonginc(eloctceb1)associated pages 4-7)

2.3 Cross-regulation of CRL signaling: ELOC as a regulated subunit

ELOC is not only a shared component of CRL5-type ligases; it can itself be polyubiquitinated and degraded. A proteomics-driven EMBO Journal study reported that CRL4^AMBRA1 targets ELOC for ubiquitination and degradation, disrupting CRL5 assembly and attenuating CRL5 activity; this cross-regulation was tied to IL-6/STAT3 signaling and HIV-1 infectivity (via CRL5^Vif). (chen2018crl4ambra1targetselongin pages 1-2)

2.4 Host–pathogen interactions and subcellular trafficking (localization-linked function)

In human HuH-7 cells, endogenous Elongin C shows nuclear/nucleolar-like speckles with 1:1 overlap with nucleolin. During infection with La Crosse virus (LACV), the viral protein NSs triggers a marked redistribution of Elongin C away from these nucleolar speckles without decreasing ELOC protein abundance on immunoblots, consistent with relocalization rather than degradation. (schoen2020elonginccontributes pages 7-8)

Mechanistically, inhibiting CRM1/exportin-1 with leptomycin B partially traps Elongin C back in nucleoli during infection, supporting an export- or retention-based relocalization mechanism. (schoen2020elonginccontributes pages 8-11)

3) Recent developments (prioritizing 2023–2024)

3.1 2024: CAND1 as a conditional inhibitor of CRL2^VHL—implications for ELOC-containing ligase dynamics

A 2024 Nature Structural & Molecular Biology study provided quantitative kinetic and cellular evidence that CAND1 binds unneddylated CUL2 and prevents stable assembly of CUL2 with the VHL•ELOB•ELOC (VBC) substrate-receptor module, functioning as an inhibitor of CRL2 (contrasting with the exchange-factor role of CAND1 in CRL1). (wang2024cand1inhibitscullin2ring pages 3-4)

Key quantitative findings relevant to CRL2^VHL (hence ELOC-containing CRL2):
- CRL2^VHL assembly is biphasic with reported parameters kon,fast = 1.1×10^6 M−1 s−1, kon,slow = 0.015 s−1, and koff = 5.7×10−4 s−1 (t1/2 ≈ 20 min). (wang2024cand1inhibitscullin2ring pages 6-8)
- Adding CAND1 can accelerate VBC dissociation from CUL2 dramatically (maximum observed rate ~0.15 s−1; KM ~60 nM), effectively increasing the dissociation rate from 5.7×10−4 s−1 to ~0.15 s−1 in the in vitro assay context. (wang2024cand1inhibitscullin2ring pages 6-8)
- In cells, CAND1 knockout accelerated PROTAC-induced degradation (e.g., ARV-771-induced BRD2 degradation showed 34% reduction in t1/2 and 42% lower plateau versus WT), demonstrating that CRL2^VHL regulatory dynamics can strongly affect induced proximity pharmacology. (wang2024cand1inhibitscullin2ring pages 3-4)

These data support an emerging view that ELOC-containing CRL2 activity is shaped not only by receptor affinity, but also by assembly/disassembly control and neddylation state, with consequences for both endogenous substrates and drug-induced neo-substrates. (wang2024cand1inhibitscullin2ring pages 9-11, wang2024cand1inhibitscullin2ring pages 6-8)

3.2 2024: ELOC-mutated RCC as a molecularly defined entity in the WHO 2022 classification—diagnostic integration of NGS

A 2024 Virchows Archiv review emphasizes that the 2022 WHO classification incorporated “molecularly defined” renal tumor entities, explicitly including ELOC-mutated RCC, underscoring the clinical shift toward NGS-based classification. (zhang2024genomicalterationsand pages 1-3)

The review also notes that ELOC (formerly TCEB1) is located on chromosome 8, encodes elongin C as a crucial component of the VHL complex, and that ELOC mutations often occur in the VHL-binding site, consistent with disruption of the VHL–HIF axis. (zhang2024genomicalterationsand pages 5-6)

3.3 2024: Clinical and epidemiologic framing of ELOC lesions in renal cancer and therapeutic inference from VHL syndrome (HIF-2α inhibitors)

A 2024 Nature Reviews Nephrology synthesis reports that:
- ELOC is deleted in ~40% of ccRCC (consistent with chromosome 8 loss), and inactivating ELOC mutations occur in ~3% of ccRCC; ELOC and VHL mutations are mutually exclusive. (coffey2024metabolicalterationsin pages 4-6)
- Because loss of ELOC collapses the pVHL-associated E3 ligase complex and stabilizes HIF, the authors suggest that HIF2α inhibitors used in VHL syndrome could be therapeutic for ELOC-mutated RCC. (coffey2024metabolicalterationsin pages 4-6)

The same review summarizes clinical performance of HIF2α inhibition in VHL-associated disease and sporadic ccRCC:
- In VHL syndrome-associated ccRCC, belzutifan reduced tumor growth in 49% of patients and stabilized disease in another 49% for 2 years, and received FDA approval in 2021 for VHL syndrome-associated ccRCC. (coffey2024metabolicalterationsin pages 4-6)
- In sporadic/metastatic ccRCC, a PT2977 analog (PT2385) produced complete, partial, and stable responses in 2%, 12%, and 52% of patients, respectively, with 34% resistance in that context (versus ~2% resistance in VHL-associated ccRCC reported in the synthesis). (coffey2024metabolicalterationsin pages 4-6)

4) Current applications and real-world implementations

4.1 Molecular pathology: ELOC-mutated RCC diagnosis and classification

ELOC-mutated RCC is now treated as a molecularly defined renal tumor entity in contemporary diagnostic frameworks (WHO 2022). This creates direct real-world applications:
- Using NGS to identify defining ELOC variants (e.g., p.Y79C) when morphology overlaps with other RCC types. (zhang2024genomicalterationsand pages 3-5, zhang2024genomicalterationsand pages 1-3)
- Incorporating ELOC/TCEB1 findings into differential diagnosis, consistent with the broader move toward genotype-informed renal tumor classification. (zhang2024genomicalterationsand pages 5-6, zhang2024genomicalterationsand pages 1-3)

4.2 Precision therapeutics: HIF-2α inhibitors as mechanism-based therapy for ELOC pathway disruption

Because ELOC loss impairs CRL2^VHL and stabilizes HIF, the current expert synthesis supports therapeutic inference that HIF2α inhibitors (e.g., belzutifan) used in VHL syndrome may be relevant for ELOC-mutant RCC, even though the clinical evidence base is largely derived from VHL pathway contexts. (coffey2024metabolicalterationsin pages 4-6)

4.3 Targeted protein degradation (TPD/PROTACs): engineering VHL-recruiting degraders and accounting for CRL2 regulation

CRL2^VHL is a widely used E3 ligase system for targeted protein degradation. The 2024 mechanistic findings on CAND1-mediated inhibition demonstrate that cellular CRL2^VHL availability and dynamics can materially affect degradation kinetics and depth for VHL-recruiting PROTACs, suggesting that ELOC-containing complex regulation is a practical consideration in degrader design and interpretation. (wang2024cand1inhibitscullin2ring pages 3-4, wang2024cand1inhibitscullin2ring pages 9-11)

5) Subcellular localization (evidence-based summary)

Nucleus/nucleolus-associated localization: In HuH-7 cells, endogenous Elongin C shows nucleolar-like speckles colocalizing 1:1 with nucleolin, indicating a prominent nuclear/nucleolar pool under baseline conditions. (schoen2020elonginccontributes pages 7-8)
Dynamic relocalization under viral stress: LACV infection redistributes Elongin C away from nucleolar speckles; the relocalization can be partially reversed by leptomycin B, supporting CRM1/exportin involvement. (schoen2020elonginccontributes pages 8-11)

Note: These data are context-specific (cell type, infection), but they provide direct experimental support for at least one physiological localization state and its perturbability. (schoen2020elonginccontributes pages 7-8, schoen2020elonginccontributes pages 11-12)

6) Expert opinion and analysis (authoritative synthesis)

6.1 Why ELOC is “central” in CRL2/CRL5 biology

Across reviews and mechanistic studies, ELOC emerges as a reused adaptor subunit—analogous in concept to other adaptor proteins (e.g., SKP1)—that enables modular recruitment of many distinct substrate receptors to a limited set of cullin scaffolds. This reuse explains why:
- ELOC mutations can phenocopy defects in specific receptors (e.g., VHL) by collapsing the assembly interface. (coffey2024metabolicalterationsin pages 4-6)
- ELOC dynamics can affect drug-induced ubiquitination (PROTACs) by altering assembly/disassembly kinetics and the effective concentration of ligase-competent CRL2^VHL. (wang2024cand1inhibitscullin2ring pages 3-4, wang2024cand1inhibitscullin2ring pages 9-11)

6.2 Interpreting ELOC-mutant tumors mechanistically

The disease genetics and renal-cancer literature converge on a mechanistic model: ELOC mutations at the VHL-binding interface (e.g., Y79C) impair CRL2^VHL assembly/function, stabilizing HIF and driving a “pseudohypoxic” transcriptional/metabolic state typical of VHL pathway disruption. This supports both diagnostic classification and therapeutic inference (HIF-2α targeting). (andreou2022elonginc(eloctceb1)associated pages 2-4, coffey2024metabolicalterationsin pages 4-6, zhang2024genomicalterationsand pages 5-6)

Summary table of ELOC functions and evidence

The table below consolidates ELOC’s major functional contexts, key interfaces, and quantitative evidence.

Functional context/complex	Core role of ELOC	Key binding interfaces/motifs/residues	Representative recent sources (date, URL)	Key quantitative/statistical data
Elongin ABC transcription elongation factor	ELOC (Elongin C/TCEB1) forms the Elongin BC heterodimer with ELOB and stabilizes/assembles Elongin A-containing complexes involved in transcription elongation; it also serves as the BC-box-binding subunit used by BC-box proteins in transcription-linked complexes. (kim2025identificationofnovel pages 4-6, fischer2023decipheringthemolecular pages 51-54, bi2026dysregulationofthe pages 4-5)	BC-box recognition surface on ELOC; hydrophobic BC-box pocket mapped to residues including Y76, L102, A107 in peptide/HDX studies; ELOC is the central adaptor subunit of the ELOB/C module. (fischer2023decipheringthemolecular pages 76-79, fischer2023decipheringthemolecular pages 79-82)	Kim et al., 2025, https://doi.org/10.1038/s41598-025-88166-2; Fischer, 2023, https://doi.org/10.17192/z2023.0625; Beringer et al., 2016, https://doi.org/10.1016/j.molcel.2016.10.018 (kim2025identificationofnovel pages 4-6, fischer2023decipheringthemolecular pages 76-79, fischer2023decipheringthemolecular pages 51-54)	No robust gene-specific kinetics reported here; role is primarily structural/adaptor rather than catalytic. (kim2025identificationofnovel pages 4-6, fischer2023decipheringthemolecular pages 51-54)
CRL2^VHL (VHL–ELOB/C–CUL2–RBX1)	ELOC is the adaptor that bridges VHL-box substrate receptors such as pVHL to CUL2, enabling assembly of the CRL2^VHL E3 ligase that targets HIF-α for ubiquitination and proteasomal degradation. Loss or mutation of ELOC destabilizes this pathway and phenocopies VHL deficiency. (kim2025identificationofnovel pages 4-6, fischer2023decipheringthemolecular pages 54-57, andreou2022elonginc(eloctceb1)associated pages 4-7, andreou2022elonginc(eloctceb1)associated pages 2-4)	ELOC residues Glu64, Met105, Phe109 contact CUL2; Tyr79 is a conserved hotspot residue in ELOC that hydrogen-bonds with pVHL Pro154; BC-box/VHL-box interactions position VHL on ELOC. (kim2025identificationofnovel pages 4-6, fischer2023decipheringthemolecular pages 67-70, andreou2022elonginc(eloctceb1)associated pages 2-4, andreou2022elonginc(eloctceb1)associated media cca6df01)	Andreou et al., 2022, https://doi.org/10.1093/hmg/ddac066; Wang et al., 2024, https://doi.org/10.1038/s41594-023-01167-5; Coffey & Simon, 2024, https://doi.org/10.1038/s41581-023-00800-2 (andreou2022elonginc(eloctceb1)associated pages 4-7, andreou2022elonginc(eloctceb1)associated pages 2-4, coffey2024metabolicalterationsin pages 4-6, wang2024cand1inhibitscullin2ring pages 3-4, wang2024cand1inhibitscullin2ring pages 6-8)	In RCC cohorts, ELOC is deleted in ~40% of ccRCC and inactivating ELOC mutations occur in ~3% of ccRCC; ELOC and VHL mutations are mutually exclusive. In the 100,000 Genomes RCC cohort, 8/1336 RCCs had candidate pathogenic somatic ELOC variants; 4 carried p.Tyr79Cys. Belzutifan data cited for VHL-associated ccRCC: 49% tumor shrinkage, 49% stable disease over 2 years; 14 active/recruiting Belzutifan RCC trials. CRL2^VHL assembly kinetics: kon,fast = 1.1×10^6 M^-1 s^-1, kon,slow = 0.015 s^-1, koff = 5.7×10^-4 s^-1, t1/2 ≈ 20 min. (andreou2022elonginc(eloctceb1)associated pages 2-4, coffey2024metabolicalterationsin pages 4-6, wang2024cand1inhibitscullin2ring pages 9-11, wang2024cand1inhibitscullin2ring pages 6-8)
CRL5^SOCS / SOCS-box ligases	ELOC, as part of the ELOB/C adaptor, recruits SOCS-box proteins to CUL5/RBX2 complexes, linking cytokine-signaling substrate receptors to CRL5-mediated ubiquitination. This places ELOC in pathways such as JAK/STAT and broader cytokine signaling. (kim2025identificationofnovel pages 4-6, fischer2023decipheringthemolecular pages 57-59, andreou2022elonginc(eloctceb1)associated pages 4-7)	SOCS-box proteins use a BC-box to bind ELOB/C and a CUL5-box (including LPΦP motif features) to bind CUL5; ELOC is the BC-box-engaging adaptor within this bipartite recruitment system. (fischer2023decipheringthemolecular pages 65-67, fischer2023decipheringthemolecular pages 57-59)	Zhou et al., 2024, https://doi.org/10.1038/s41467-024-50556-x; Ramachandran et al., 2023, https://doi.org/10.1038/s41467-023-41894-3; Fischer, 2023, https://doi.org/10.17192/z2023.0625 (fischer2023decipheringthemolecular pages 57-59, fischer2023decipheringthemolecular pages 65-67)	No direct ELOC-specific kinetic constants reported in the cited SOCS-focused excerpts, but structural work confirms conserved EloBC recruitment by SOCS-box receptors and CRL5 assembly logic. (fischer2023decipheringthemolecular pages 57-59, fischer2023decipheringthemolecular pages 65-67)
Other CRL cross-regulation / CRL2 control	ELOC is itself regulated as a shared CRL component: CRL4^AMBRA1 can polyubiquitinate and degrade ELOC, thereby attenuating CRL5 complex assembly/activity. In CRL2, ELOC-containing VBC assembly is additionally controlled by CAND1 and cullin neddylation, which regulate complex disassembly/reassembly and substrate selectivity. (chen2018crl4ambra1targetselongin pages 1-2, wang2024cand1inhibitscullin2ring pages 3-4, wang2024cand1inhibitscullin2ring pages 9-11, wang2024cand1inhibitscullin2ring pages 6-8)	CAND1 binds unneddylated CUL2 and is incompatible with stable VBC occupancy; VBC plus neddylation promote CUL2•CAND1 disassembly. ELOC isoform usage also affects CUL2 affinity. (wang2024cand1inhibitscullin2ring pages 3-4, wang2024cand1inhibitscullin2ring pages 8-9, wang2024cand1inhibitscullin2ring pages 4-6, wang2024cand1inhibitscullin2ring pages 6-8)	Wang et al., 2024, https://doi.org/10.1038/s41594-023-01167-5; Chen et al., 2018, https://doi.org/10.15252/embj.201797508; Lin & Komives, 2024, https://doi.org/10.1016/j.sbi.2024.102879 (chen2018crl4ambra1targetselongin pages 1-2, lin2024diversityofstructure pages 3-5, wang2024cand1inhibitscullin2ring pages 3-4, wang2024cand1inhibitscullin2ring pages 6-8)	CAND1 knockout accelerated ARV-771-induced BRD2 degradation with 34% lower t1/2 and 42% lower plateau; after 18 h BRD2 levels were 50–60% lower. Natural CRL2 substrate half-lives were reduced by 57% (CODD) and 87% (MIC19) in DKO cells. CAND1 increased VBC dissociation from 5.7×10^-4 s^-1 to 0.15 s^-1 (KM ≈ 60 nM); neddylation increased CRL2^VHL t1/2 ~3.5-fold and reduced CUL2•CAND1 half-life from 20 min to 4 min when combined with VBC. ELOC17-112 weakened CUL2•VBC affinity ~10-fold versus ELOC1-112. (wang2024cand1inhibitscullin2ring pages 3-4, wang2024cand1inhibitscullin2ring pages 8-9, wang2024cand1inhibitscullin2ring pages 9-11, wang2024cand1inhibitscullin2ring pages 4-6, wang2024cand1inhibitscullin2ring pages 6-8)
Viral hijacking / host-pathogen interactions	Viral proteins exploit or perturb ELOC-containing ligases. HIV-1 Vif uses CRL5 containing ELOC/ELOB; La Crosse virus NSs functionally depends in part on ELOC for RNAPII RPB1 degradation and relocalizes ELOC from nucleolar speckles. (chen2018crl4ambra1targetselongin pages 1-2, fischer2023decipheringthemolecular pages 65-67, schoen2020elonginccontributes pages 7-8, schoen2020elonginccontributes pages 1-2)	Viral BC-box-like interactions with EloBC are documented for Vif; in LACV infection, ELOC relocalizes from nucleolin-overlapping nucleolar speckles and this can be partially trapped by leptomycin B, implying CRM1-dependent export/redistribution. (fischer2023decipheringthemolecular pages 65-67, schoen2020elonginccontributes pages 7-8, schoen2020elonginccontributes pages 8-11, schoen2020elonginccontributes pages 11-12)	Schoen et al., 2020, https://doi.org/10.1128/jvi.02134-19; Chen et al., 2018, https://doi.org/10.15252/embj.201797508; Fischer, 2023, https://doi.org/10.17192/z2023.0625 (chen2018crl4ambra1targetselongin pages 1-2, fischer2023decipheringthemolecular pages 65-67, schoen2020elonginccontributes pages 7-8, schoen2020elonginccontributes pages 8-11)	In HuH-7 cells, endogenous ELOC shows nucleolar/nuclear speckles with 1:1 overlap with nucleolin; redistribution was observed after wild-type LACV infection at MOI 1, while α-amanitin (10 µg/mL, 16 h) dissolved speckles but preserved nuclear signal. LMB (16 nM, 1 h pretreatment) partially trapped ELOC in nucleoli. RPB1 degradation began by 1 h post-infection; ELOC depletion partially rescued RNAPII transcription and IFN-β expression. (schoen2020elonginccontributes pages 7-8, schoen2020elonginccontributes pages 8-11, schoen2020elonginccontributes pages 11-12, schoen2020elonginccontributes pages 1-2)

Table: This table summarizes the main experimentally supported roles of human ELOC/TCEB1 across transcription, CRL2/CRL5 ubiquitin ligases, regulatory cross-talk, and viral hijacking. It also captures key interfaces and recent quantitative findings useful for functional annotation.

Key visual evidence (structure)

A structural view of the ELOC–pVHL interface highlighting ELOC Tyr79 (hotspot mutated to Cys in RCC/VHL-like phenotypes) is available in Andreou et al. 2022 (Figure 3D). (andreou2022elonginc(eloctceb1)associated media cca6df01)

Selected references (publication date + URL)

Andreou A. et al. 2022-03. Elongin C (ELOC/TCEB1)-associated von Hippel–Lindau disease. Human Molecular Genetics. https://doi.org/10.1093/hmg/ddac066 (andreou2022elonginc(eloctceb1)associated pages 2-4, andreou2022elonginc(eloctceb1)associated media cca6df01)
Fischer S. 2023-07. Deciphering the Molecular Mechanisms of Cancer and Developing Precision Therapeutics. https://doi.org/10.17192/z2023.0625 (fischer2023decipheringthemolecular pages 54-57)
Coffey N.J., Simon M.C. 2024-01. Metabolic alterations in hereditary and sporadic renal cell carcinoma. Nature Reviews Nephrology. https://doi.org/10.1038/s41581-023-00800-2 (coffey2024metabolicalterationsin pages 4-6)
Wang K. et al. 2024-01. CAND1 inhibits Cullin-2-RING ubiquitin ligases for enhanced substrate specificity. Nature Structural & Molecular Biology. https://doi.org/10.1038/s41594-023-01167-5 (wang2024cand1inhibitscullin2ring pages 3-4, wang2024cand1inhibitscullin2ring pages 6-8)
Zhang X. et al. 2024-11. Genomic alterations and diagnosis of renal cancer. Virchows Archiv. https://doi.org/10.1007/s00428-023-03700-9 (zhang2024genomicalterationsand pages 1-3)
Lin C.P., Komives E.A. 2024-10. Diversity of structure and function in Cullin E3 ligases. Current Opinion in Structural Biology. https://doi.org/10.1016/j.sbi.2024.102879 (lin2024diversityofstructure pages 3-5)
Schoen A. et al. 2020-03. Elongin C contributes to RNA Polymerase II degradation by the interferon antagonist NSs of La Crosse Orthobunyavirus. Journal of Virology. https://doi.org/10.1128/jvi.02134-19 (schoen2020elonginccontributes pages 7-8)

References

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(fischer2023decipheringthemolecular pages 54-57): Sabrina Fischer. Deciphering the molecular mechanisms of cancer and developing precision therapeutics. Text, Jul 2023. URL: https://doi.org/10.17192/z2023.0625, doi:10.17192/z2023.0625. This article has 0 citations and is from a peer-reviewed journal.
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(fischer2023decipheringthemolecular pages 57-59): Sabrina Fischer. Deciphering the molecular mechanisms of cancer and developing precision therapeutics. Text, Jul 2023. URL: https://doi.org/10.17192/z2023.0625, doi:10.17192/z2023.0625. This article has 0 citations and is from a peer-reviewed journal.
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(wang2024cand1inhibitscullin2ring pages 6-8): Kankan Wang, Stephanie Diaz, Lihong Li, Jeremy R. Lohman, and Xing Liu. Cand1 inhibits cullin-2-ring ubiquitin ligases for enhanced substrate specificity. Nature Structural & Molecular Biology, pages 1-13, Jan 2024. URL: https://doi.org/10.1038/s41594-023-01167-5, doi:10.1038/s41594-023-01167-5. This article has 5 citations and is from a highest quality peer-reviewed journal.
(andreou2022elonginc(eloctceb1)associated pages 4-7): Avgi Andreou, Bryndis Yngvadottir, Laia Bassaganyas, Graeme Clarke, Ezequiel Martin, J. Whitworth, A. Cornish, R. Houlston, P. Rich, C. Egan, S. Hodgson, A. Warren, K. Snape, and E. Maher. Elongin c (eloc/tceb1)-associated von hippel–lindau disease. Human Molecular Genetics, 31:2728-2737, Mar 2022. URL: https://doi.org/10.1093/hmg/ddac066, doi:10.1093/hmg/ddac066. This article has 40 citations and is from a domain leading peer-reviewed journal.
(andreou2022elonginc(eloctceb1)associated pages 2-4): Avgi Andreou, Bryndis Yngvadottir, Laia Bassaganyas, Graeme Clarke, Ezequiel Martin, J. Whitworth, A. Cornish, R. Houlston, P. Rich, C. Egan, S. Hodgson, A. Warren, K. Snape, and E. Maher. Elongin c (eloc/tceb1)-associated von hippel–lindau disease. Human Molecular Genetics, 31:2728-2737, Mar 2022. URL: https://doi.org/10.1093/hmg/ddac066, doi:10.1093/hmg/ddac066. This article has 40 citations and is from a domain leading peer-reviewed journal.
(andreou2022elonginc(eloctceb1)associated media cca6df01): Avgi Andreou, Bryndis Yngvadottir, Laia Bassaganyas, Graeme Clarke, Ezequiel Martin, J. Whitworth, A. Cornish, R. Houlston, P. Rich, C. Egan, S. Hodgson, A. Warren, K. Snape, and E. Maher. Elongin c (eloc/tceb1)-associated von hippel–lindau disease. Human Molecular Genetics, 31:2728-2737, Mar 2022. URL: https://doi.org/10.1093/hmg/ddac066, doi:10.1093/hmg/ddac066. This article has 40 citations and is from a domain leading peer-reviewed journal.
(chen2018crl4ambra1targetselongin pages 1-2): Si‐Han Chen, Gwendolyn M Jang, Ruth Hüttenhain, David E Gordon, Dan Du, Billy W Newton, Jeffrey R Johnson, Joseph Hiatt, Judd F Hultquist, Tasha L Johnson, Yi‐Liang Liu, Lily A Burton, Jordan Ye, Kurt M Reichermeier, Robert M Stroud, Alexander Marson, Jayanta Debnath, John D Gross, and Nevan J Krogan. Crl4ambra1 targets elongin c for ubiquitination and degradation to modulate crl5 signaling. The EMBO Journal, Aug 2018. URL: https://doi.org/10.15252/embj.201797508, doi:10.15252/embj.201797508. This article has 29 citations.
(schoen2020elonginccontributes pages 7-8): Andreas Schoen, Simone Lau, Paul Verbruggen, and Friedemann Weber. Elongin c contributes to rna polymerase ii degradation by the interferon antagonist nss of la crosse orthobunyavirus. Journal of Virology, Mar 2020. URL: https://doi.org/10.1128/jvi.02134-19, doi:10.1128/jvi.02134-19. This article has 28 citations and is from a domain leading peer-reviewed journal.
(schoen2020elonginccontributes pages 8-11): Andreas Schoen, Simone Lau, Paul Verbruggen, and Friedemann Weber. Elongin c contributes to rna polymerase ii degradation by the interferon antagonist nss of la crosse orthobunyavirus. Journal of Virology, Mar 2020. URL: https://doi.org/10.1128/jvi.02134-19, doi:10.1128/jvi.02134-19. This article has 28 citations and is from a domain leading peer-reviewed journal.
(wang2024cand1inhibitscullin2ring pages 3-4): Kankan Wang, Stephanie Diaz, Lihong Li, Jeremy R. Lohman, and Xing Liu. Cand1 inhibits cullin-2-ring ubiquitin ligases for enhanced substrate specificity. Nature Structural & Molecular Biology, pages 1-13, Jan 2024. URL: https://doi.org/10.1038/s41594-023-01167-5, doi:10.1038/s41594-023-01167-5. This article has 5 citations and is from a highest quality peer-reviewed journal.
(wang2024cand1inhibitscullin2ring pages 9-11): Kankan Wang, Stephanie Diaz, Lihong Li, Jeremy R. Lohman, and Xing Liu. Cand1 inhibits cullin-2-ring ubiquitin ligases for enhanced substrate specificity. Nature Structural & Molecular Biology, pages 1-13, Jan 2024. URL: https://doi.org/10.1038/s41594-023-01167-5, doi:10.1038/s41594-023-01167-5. This article has 5 citations and is from a highest quality peer-reviewed journal.
(zhang2024genomicalterationsand pages 1-3): Xingming Zhang, Hella A. Bolck, Niels J. Rupp, and Holger Moch. Genomic alterations and diagnosis of renal cancer. Virchows Archiv, 484:323-337, Nov 2024. URL: https://doi.org/10.1007/s00428-023-03700-9, doi:10.1007/s00428-023-03700-9. This article has 20 citations and is from a peer-reviewed journal.
(zhang2024genomicalterationsand pages 5-6): Xingming Zhang, Hella A. Bolck, Niels J. Rupp, and Holger Moch. Genomic alterations and diagnosis of renal cancer. Virchows Archiv, 484:323-337, Nov 2024. URL: https://doi.org/10.1007/s00428-023-03700-9, doi:10.1007/s00428-023-03700-9. This article has 20 citations and is from a peer-reviewed journal.
(coffey2024metabolicalterationsin pages 4-6): Nathan J. Coffey and M. Celeste Simon. Metabolic alterations in hereditary and sporadic renal cell carcinoma. Nature reviews. Nephrology, 20:233-250, Jan 2024. URL: https://doi.org/10.1038/s41581-023-00800-2, doi:10.1038/s41581-023-00800-2. This article has 46 citations.
(zhang2024genomicalterationsand pages 3-5): Xingming Zhang, Hella A. Bolck, Niels J. Rupp, and Holger Moch. Genomic alterations and diagnosis of renal cancer. Virchows Archiv, 484:323-337, Nov 2024. URL: https://doi.org/10.1007/s00428-023-03700-9, doi:10.1007/s00428-023-03700-9. This article has 20 citations and is from a peer-reviewed journal.
(schoen2020elonginccontributes pages 11-12): Andreas Schoen, Simone Lau, Paul Verbruggen, and Friedemann Weber. Elongin c contributes to rna polymerase ii degradation by the interferon antagonist nss of la crosse orthobunyavirus. Journal of Virology, Mar 2020. URL: https://doi.org/10.1128/jvi.02134-19, doi:10.1128/jvi.02134-19. This article has 28 citations and is from a domain leading peer-reviewed journal.
(fischer2023decipheringthemolecular pages 51-54): Sabrina Fischer. Deciphering the molecular mechanisms of cancer and developing precision therapeutics. Text, Jul 2023. URL: https://doi.org/10.17192/z2023.0625, doi:10.17192/z2023.0625. This article has 0 citations and is from a peer-reviewed journal.
(bi2026dysregulationofthe pages 4-5): Yege Bi, Rui Wang, Lu Li, Lili Wang, Xingwang Chen, Xiaomei Nie, Jia Meng, and Shanjun Cai. Dysregulation of the ubiquitin-proteasome system in von hippel-lindau syndrome: molecular insights and clinical perspectives. Clinical and Experimental Medicine, Dec 2026. URL: https://doi.org/10.1007/s10238-025-01978-4, doi:10.1007/s10238-025-01978-4. This article has 1 citations and is from a peer-reviewed journal.
(fischer2023decipheringthemolecular pages 76-79): Sabrina Fischer. Deciphering the molecular mechanisms of cancer and developing precision therapeutics. Text, Jul 2023. URL: https://doi.org/10.17192/z2023.0625, doi:10.17192/z2023.0625. This article has 0 citations and is from a peer-reviewed journal.
(fischer2023decipheringthemolecular pages 79-82): Sabrina Fischer. Deciphering the molecular mechanisms of cancer and developing precision therapeutics. Text, Jul 2023. URL: https://doi.org/10.17192/z2023.0625, doi:10.17192/z2023.0625. This article has 0 citations and is from a peer-reviewed journal.
(fischer2023decipheringthemolecular pages 67-70): Sabrina Fischer. Deciphering the molecular mechanisms of cancer and developing precision therapeutics. Text, Jul 2023. URL: https://doi.org/10.17192/z2023.0625, doi:10.17192/z2023.0625. This article has 0 citations and is from a peer-reviewed journal.
(wang2024cand1inhibitscullin2ring pages 8-9): Kankan Wang, Stephanie Diaz, Lihong Li, Jeremy R. Lohman, and Xing Liu. Cand1 inhibits cullin-2-ring ubiquitin ligases for enhanced substrate specificity. Nature Structural & Molecular Biology, pages 1-13, Jan 2024. URL: https://doi.org/10.1038/s41594-023-01167-5, doi:10.1038/s41594-023-01167-5. This article has 5 citations and is from a highest quality peer-reviewed journal.
(wang2024cand1inhibitscullin2ring pages 4-6): Kankan Wang, Stephanie Diaz, Lihong Li, Jeremy R. Lohman, and Xing Liu. Cand1 inhibits cullin-2-ring ubiquitin ligases for enhanced substrate specificity. Nature Structural & Molecular Biology, pages 1-13, Jan 2024. URL: https://doi.org/10.1038/s41594-023-01167-5, doi:10.1038/s41594-023-01167-5. This article has 5 citations and is from a highest quality peer-reviewed journal.
(schoen2020elonginccontributes pages 1-2): Andreas Schoen, Simone Lau, Paul Verbruggen, and Friedemann Weber. Elongin c contributes to rna polymerase ii degradation by the interferon antagonist nss of la crosse orthobunyavirus. Journal of Virology, Mar 2020. URL: https://doi.org/10.1128/jvi.02134-19, doi:10.1128/jvi.02134-19. This article has 28 citations and is from a domain leading peer-reviewed journal.

Citations

fischer2023decipheringthemolecular pages 54-57
fischer2023decipheringthemolecular pages 57-59
schoen2020elonginccontributes pages 7-8
schoen2020elonginccontributes pages 8-11
zhang2024genomicalterationsand pages 1-3
zhang2024genomicalterationsand pages 5-6
coffey2024metabolicalterationsin pages 4-6
lin2024diversityofstructure pages 3-5
kim2025identificationofnovel pages 4-6
fischer2023decipheringthemolecular pages 65-67
zhang2024genomicalterationsand pages 3-5
schoen2020elonginccontributes pages 11-12
fischer2023decipheringthemolecular pages 51-54
bi2026dysregulationofthe pages 4-5
fischer2023decipheringthemolecular pages 76-79
fischer2023decipheringthemolecular pages 79-82
fischer2023decipheringthemolecular pages 67-70
schoen2020elonginccontributes pages 1-2
https://doi.org/10.1038/s41598-025-88166-2;
https://doi.org/10.17192/z2023.0625;
https://doi.org/10.1016/j.molcel.2016.10.018
https://doi.org/10.1093/hmg/ddac066;
https://doi.org/10.1038/s41594-023-01167-5;
https://doi.org/10.1038/s41581-023-00800-2
https://doi.org/10.1038/s41467-024-50556-x;
https://doi.org/10.1038/s41467-023-41894-3;
https://doi.org/10.17192/z2023.0625
https://doi.org/10.15252/embj.201797508;
https://doi.org/10.1016/j.sbi.2024.102879
https://doi.org/10.1128/jvi.02134-19;
https://doi.org/10.1093/hmg/ddac066
https://doi.org/10.1038/s41594-023-01167-5
https://doi.org/10.1007/s00428-023-03700-9
https://doi.org/10.1128/jvi.02134-19
https://doi.org/10.1038/s41598-025-88166-2,
https://doi.org/10.17192/z2023.0625,
https://doi.org/10.1016/j.sbi.2024.102879,
https://doi.org/10.1038/s41594-023-01167-5,
https://doi.org/10.1093/hmg/ddac066,
https://doi.org/10.15252/embj.201797508,
https://doi.org/10.1128/jvi.02134-19,
https://doi.org/10.1007/s00428-023-03700-9,
https://doi.org/10.1038/s41581-023-00800-2,
https://doi.org/10.1007/s10238-025-01978-4,

📄 View Raw YAML

id: Q15369
gene_symbol: ELOC
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: ELOC encodes Elongin C, the SKP1-like adaptor subunit of the Elongin BC module. Together with ELOB, ELOC bridges BC-box, VHL-box, and SOCS-box substrate receptors to Cul2 or Cul5 Cullin-RING ubiquitin ligase scaffolds, while also participating in Elongin transcription elongation complexes.
alternative_products:
- name: '1'
  id: Q15369-1
- name: '2'
  id: Q15369-2
  sequence_note: VSP_045955
existing_annotations:
- term:
    id: GO:0006511
    label: ubiquitin-dependent protein catabolic process
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Accepted as a pathway-level consequence. ELOC-containing CRL2/CRL5 complexes target substrates for ubiquitination and downstream proteasomal degradation.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: "A central and well-established role of ELOC is within the **VHL\u2013ELOB/ELOC\u2013CUL2\u2013RBX1** E3 ubiquitin ligase"
- term:
    id: GO:0070449
    label: elongin complex
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Correct. ELOC is Elongin C, the SKP1-like subunit of the Elongin BC module and Elongin complex.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**ELOC (Elongin C)** forms a heterodimer with **ELOB (Elongin B)**, commonly referred to as the **Elongin BC** module.'
- term:
    id: GO:0030674
    label: protein-macromolecule adaptor activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Correct and informative. ELOC acts as a protein-macromolecule adaptor within Elongin BC, bridging BC-box/VHL-box/SOCS-box substrate receptors to Cul2/Cul5 CRL scaffolds.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: The literature retrieved here consistently uses **ELOC** as the human gene encoding **Elongin C** (also called **TCEB1**) and describes it as the **Elongin B/C adaptor subunit** that binds **BC-box/VHL-box/SOCS-box** motifs and bridges substrate receptors to **CUL2** or **CUL5** in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
- term:
    id: GO:0000151
    label: ubiquitin ligase complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  review:
    summary: Correct but broad. ELOC is better captured as an adaptor subunit in specific Cul2/Cul5 ubiquitin ligase complexes rather than by the generic ubiquitin ligase complex term alone.
    action: MARK_AS_OVER_ANNOTATED
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: More specific Cul2-RING, Cul5-RING, and Elongin complex annotations capture the supported complex membership.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: Supported. ELOC has nuclear functions in Elongin/CRL assemblies and has experimentally observed nuclear/nucleolar localization.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  review:
    summary: Correct but less precise than the available cytosol and nuclear/nucleoplasm localization annotations.
    action: MARK_AS_OVER_ANNOTATED
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Use cytosol and nucleus/nucleoplasm annotations where available rather than generic cytoplasm.
- term:
    id: GO:0006511
    label: ubiquitin-dependent protein catabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: Accepted as a pathway-level consequence. ELOC-containing CRL2/CRL5 complexes target substrates for ubiquitination and downstream proteasomal degradation.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: "A central and well-established role of ELOC is within the **VHL\u2013ELOB/ELOC\u2013CUL2\u2013RBX1** E3 ubiquitin ligase"
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:10205047
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:12004076
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:12050673
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:12149480
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:15601820
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16189514
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16643902
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17183367
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19159283
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19322197
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19327355
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:20211142
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21145461
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21516116
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21822215
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21988832
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:22190034
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:23460923
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:23563313
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25416956
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:28514442
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:31515488
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:31980649
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32296183
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32353859
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:33060197
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:33827988
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:33961781
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:36217030
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:40205054
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0016567
    label: protein ubiquitination
  evidence_type: IEA
  original_reference_id: GO_REF:0000041
  review:
    summary: Accepted. ELOC is not the catalytic ubiquitin-transfer subunit, but it is required as an Elongin BC adaptor component of CRL2/CRL5 ligases that mediate substrate ubiquitination.
    action: ACCEPT
    reason: Keep the process annotation because ELOC is a direct required module in
      CRL ubiquitination complexes. Do not add GO:1990756 for ELOC itself, because
      substrate recognition is supplied by SOCS-box, VHL-box, or related substrate
      receptor proteins rather than by ELOC.
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: "ELOC\u2019s primary biochemical function in these contexts is **protein\u2013protein interaction and complex assembly**, not ubiquitin transfer catalysis per se."
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0070449
    label: elongin complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: Correct. ELOC is Elongin C, the SKP1-like subunit of the Elongin BC module and Elongin complex.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**ELOC (Elongin C)** forms a heterodimer with **ELOB (Elongin B)**, commonly referred to as the **Elongin BC** module.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:40963025
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0000122
    label: negative regulation of transcription by RNA polymerase II
  evidence_type: NAS
  original_reference_id: PMID:28591624
  review:
    summary: Kept as non-core. Negative transcriptional regulation can arise in specific Elongin-associated contexts, but it is not the central ELOC molecular function.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: The literature retrieved here consistently uses **ELOC** as the human gene encoding **Elongin C** (also called **TCEB1**) and describes it as the **Elongin B/C adaptor subunit** that binds **BC-box/VHL-box/SOCS-box** motifs and bridges substrate receptors to **CUL2** or **CUL5** in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
- term:
    id: GO:0043161
    label: proteasome-mediated ubiquitin-dependent protein catabolic process
  evidence_type: NAS
  original_reference_id: PMID:31273098
  review:
    summary: Supported as a non-core consequence of ELOC-containing CRL activity. ELOC is an adaptor/regulatory subunit rather than the proteasome or catalytic ubiquitin-transfer component.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: "A central and well-established role of ELOC is within the **VHL\u2013ELOB/ELOC\u2013CUL2\u2013RBX1** E3 ubiquitin ligase"
- term:
    id: GO:0140627
    label: ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
  evidence_type: NAS
  original_reference_id: PMID:15601820
  review:
    summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL2** uses **CUL2** as scaffold and **RBX1** as the RING component, and uniquely uses **ELOB/ELOC** as adaptor proteins for substrate receptors like VHL.'
- term:
    id: GO:0140627
    label: ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
  evidence_type: NAS
  original_reference_id: PMID:21822215
  review:
    summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL2** uses **CUL2** as scaffold and **RBX1** as the RING component, and uniquely uses **ELOB/ELOC** as adaptor proteins for substrate receptors like VHL.'
- term:
    id: GO:0140627
    label: ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
  evidence_type: NAS
  original_reference_id: PMID:22649776
  review:
    summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL2** uses **CUL2** as scaffold and **RBX1** as the RING component, and uniquely uses **ELOB/ELOC** as adaptor proteins for substrate receptors like VHL.'
- term:
    id: GO:0140627
    label: ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
  evidence_type: NAS
  original_reference_id: PMID:29779948
  review:
    summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL2** uses **CUL2** as scaffold and **RBX1** as the RING component, and uniquely uses **ELOB/ELOC** as adaptor proteins for substrate receptors like VHL.'
- term:
    id: GO:0140627
    label: ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
  evidence_type: NAS
  original_reference_id: PMID:33398168
  review:
    summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL2** uses **CUL2** as scaffold and **RBX1** as the RING component, and uniquely uses **ELOB/ELOC** as adaptor proteins for substrate receptors like VHL.'
- term:
    id: GO:0140627
    label: ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
  evidence_type: NAS
  original_reference_id: PMID:34743205
  review:
    summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL2** uses **CUL2** as scaffold and **RBX1** as the RING component, and uniquely uses **ELOB/ELOC** as adaptor proteins for substrate receptors like VHL.'
- term:
    id: GO:1990116
    label: ribosome-associated ubiquitin-dependent protein catabolic process
  evidence_type: NAS
  original_reference_id: PMID:33909987
  review:
    summary: Supported as a non-core specialized CRL pathway context. ELOC contributes through Elongin BC adaptor function in substrate-specific ligase assemblies.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: The literature retrieved here consistently uses **ELOC** as the human gene encoding **Elongin C** (also called **TCEB1**) and describes it as the **Elongin B/C adaptor subunit** that binds **BC-box/VHL-box/SOCS-box** motifs and bridges substrate receptors to **CUL2** or **CUL5** in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
- term:
    id: GO:2000104
    label: negative regulation of DNA-templated DNA replication
  evidence_type: NAS
  original_reference_id: PMID:22649776
  review:
    summary: Kept as non-core. Negative regulation of DNA-templated DNA replication is likely a downstream substrate-specific consequence of ELOC-containing ligase activity rather than ELOC's primary molecular role.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: "ELOC\u2019s primary biochemical function in these contexts is **protein\u2013protein interaction and complex assembly**, not ubiquitin transfer catalysis per se."
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:39039081
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:40440427
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0031462
    label: Cul2-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:37844242
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul2-RING ligase assemblies such as CRL2-VHL.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL2** uses **CUL2** as scaffold and **RBX1** as the RING component, and uniquely uses **ELOB/ELOC** as adaptor proteins for substrate receptors like VHL.'
- term:
    id: GO:0140627
    label: ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
  evidence_type: IDA
  original_reference_id: PMID:37844242
  review:
    summary: Supported as a non-core specialized CRL2 pathway context. ELOC participates through the shared Elongin BC adaptor module, not as the substrate receptor itself.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL2** uses **CUL2** as scaffold and **RBX1** as the RING component, and uniquely uses **ELOB/ELOC** as adaptor proteins for substrate receptors like VHL.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:35512830
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:37816714
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:34857742
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:21980433
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:25505247
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:38418882
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:31387940
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:32513959
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:23837592
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:33268465
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0140958
    label: target-directed miRNA degradation
  evidence_type: IMP
  original_reference_id: PMID:33184237
  review:
    summary: Kept as non-core. Target-directed miRNA degradation is a specialized pathway context for an ELOC-containing CRL assembly rather than the general function of ELOC itself.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: The literature retrieved here consistently uses **ELOC** as the human gene encoding **Elongin C** (also called **TCEB1**) and describes it as the **Elongin B/C adaptor subunit** that binds **BC-box/VHL-box/SOCS-box** motifs and bridges substrate receptors to **CUL2** or **CUL5** in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:22510880
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0001222
    label: transcription corepressor binding
  evidence_type: IPI
  original_reference_id: PMID:7660122
  review:
    summary: Kept as non-core. ELOC can participate in transcriptional regulatory complexes, but its primary role is the Elongin BC adaptor/regulatory module.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: The literature retrieved here consistently uses **ELOC** as the human gene encoding **Elongin C** (also called **TCEB1**) and describes it as the **Elongin B/C adaptor subunit** that binds **BC-box/VHL-box/SOCS-box** motifs and bridges substrate receptors to **CUL2** or **CUL5** in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
- term:
    id: GO:0006367
    label: transcription initiation at RNA polymerase II promoter
  evidence_type: IDA
  original_reference_id: PMID:7660122
  review:
    summary: Remove. The cited PMID:7660122 paper concerns VHL inhibition of Elongin-dependent
      RNA polymerase II transcription elongation, not transcription initiation.
    action: REMOVE
    reason: 'Evidence-term mismatch: PMID:7660122 supports transcription elongation biology,
      not GO:0006367 transcription initiation at RNA polymerase II promoter.'
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0070449
    label: elongin complex
  evidence_type: IDA
  original_reference_id: PMID:7660122
  review:
    summary: Correct. ELOC is Elongin C, the SKP1-like subunit of the Elongin BC module and Elongin complex.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**ELOC (Elongin C)** forms a heterodimer with **ELOB (Elongin B)**, commonly referred to as the **Elongin BC** module.'
- term:
    id: GO:0016567
    label: protein ubiquitination
  evidence_type: IDA
  original_reference_id: PMID:30166453
  review:
    summary: Accepted. ELOC is not the catalytic ubiquitin-transfer subunit, but it is required as an Elongin BC adaptor component of CRL2/CRL5 ligases that mediate substrate ubiquitination.
    action: ACCEPT
    reason: Keep the process annotation because ELOC is a direct required module in
      CRL ubiquitination complexes. Do not add GO:1990756 for ELOC itself, because
      substrate recognition is supplied by SOCS-box, VHL-box, or related substrate
      receptor proteins rather than by ELOC.
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: "ELOC\u2019s primary biochemical function in these contexts is **protein\u2013protein interaction and complex assembly**, not ubiquitin transfer catalysis per se."
- term:
    id: GO:0031466
    label: Cul5-RING ubiquitin ligase complex
  evidence_type: IDA
  original_reference_id: PMID:30166453
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul5-RING ligase assemblies recruited by SOCS-box proteins.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL5** uses **CUL5** and **RBX2/SAG**, and commonly uses **SOCS-box** substrate receptors that recruit **ELOB/ELOC** as adaptors.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21119685
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0031462
    label: Cul2-RING ubiquitin ligase complex
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  review:
    summary: Correct. ELOC is the adaptor subunit of Elongin BC in Cul2-RING ligase assemblies such as CRL2-VHL.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: '**CRL2** uses **CUL2** as scaffold and **RBX1** as the RING component, and uniquely uses **ELOB/ELOC** as adaptor proteins for substrate receptors like VHL.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21199876
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1234159
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1234163
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1234173
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1234175
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1234177
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1234183
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-180540
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-180555
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-180603
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8952039
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8952044
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8952625
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8952626
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8955241
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8955289
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8956040
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8956099
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8956103
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8956106
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9705738
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9755303
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9833107
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9833155
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9954721
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9954723
  review:
    summary: Supported. ELOC-containing CRL2/CRL5 complexes and their substrate receptor assemblies operate in cytosolic as well as nuclear contexts.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md

- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-112379
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-112385
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-112392
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-112395
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-112396
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-112435
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-112436
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-113411
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-113412
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-113413
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-113414
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-113429
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1234169
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1234172
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1234175
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6797606
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6797616
  review:
    summary: Supported. ELOC has a prominent nuclear/nucleoplasmic pool consistent with Elongin transcriptional and nuclear CRL functions.
    action: ACCEPT
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: In human **HuH-7** cells, endogenous Elongin C shows **nuclear/nucleolar-like speckles** with **1:1 overlap with nucleolin**.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:15590694
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:10851083
  review:
    summary: Protein binding is too generic for ELOC. The informative annotation is Elongin BC adaptor activity and specific Cul2/Cul5 ligase complex membership.
    action: REMOVE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    reason: Replace generic binding with specific adaptor and CRL complex annotations.
- term:
    id: GO:0006357
    label: regulation of transcription by RNA polymerase II
  evidence_type: TAS
  original_reference_id: PMID:7660129
  review:
    summary: Kept as non-core. Regulation of RNA polymerase II transcription is a supported broader context, but ELOC is best captured by Elongin BC adaptor and CRL complex roles.
    action: KEEP_AS_NON_CORE
    additional_reference_ids:
    - file:human/ELOC/ELOC-deep-research-falcon.md
    supported_by:
    - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
      supporting_text: The literature retrieved here consistently uses **ELOC** as the human gene encoding **Elongin C** (also called **TCEB1**) and describes it as the **Elongin B/C adaptor subunit** that binds **BC-box/VHL-box/SOCS-box** motifs and bridges substrate receptors to **CUL2** or **CUL5** in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO terms
  findings: []
- id: GO_REF:0000024
  title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000041
  title: Gene Ontology annotation based on UniPathway vocabulary mapping
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
  findings: []
- id: GO_REF:0000107
  title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  findings: []
- id: PMID:10205047
  title: 'Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function.'
  findings: []
- id: PMID:10851083
  title: Tracheal development and the von Hippel-Lindau tumor suppressor homolog in Drosophila.
  findings: []
- id: PMID:12004076
  title: 'Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling.'
  findings: []
- id: PMID:12050673
  title: Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL.
  findings: []
- id: PMID:12149480
  title: Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase.
  findings: []
- id: PMID:15590694
  title: Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling.
  findings: []
- id: PMID:15601820
  title: VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases.
  findings: []
- id: PMID:16189514
  title: Towards a proteome-scale map of the human protein-protein interaction network.
  findings: []
- id: PMID:16643902
  title: The E3 ubiquitin ligase HOIL-1 induces the polyubiquitination and degradation of SOCS6 associated proteins.
  findings: []
- id: PMID:17183367
  title: COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase.
  findings: []
- id: PMID:19159283
  title: 'Array MAPPIT: high-throughput interactome analysis in mammalian cells.'
  findings: []
- id: PMID:19322197
  title: Termination of NF-kappaB activity through a gammaherpesvirus protein that assembles an EC5S ubiquitin-ligase.
  findings: []
- id: PMID:19327355
  title: Requirement for microtubule integrity in the SOCS1-mediated intracellular dynamics of HIV-1 Gag.
  findings: []
- id: PMID:20211142
  title: An atlas of combinatorial transcriptional regulation in mouse and man.
  findings: []
- id: PMID:21119685
  title: Notch-induced Asb2 expression promotes protein ubiquitination by forming non-canonical E3 ligase complexes.
  findings: []
- id: PMID:21145461
  title: Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics.
  findings: []
- id: PMID:21199876
  title: Regulation of inducible nitric-oxide synthase by the SPRY domain- and SOCS box-containing proteins.
  findings: []
- id: PMID:21516116
  title: Next-generation sequencing to generate interactome datasets.
  findings: []
- id: PMID:21822215
  title: The tumour antigen PRAME is a subunit of a Cul2 ubiquitin ligase and associates with active NFY promoters.
  findings: []
- id: PMID:21980433
  title: The SOCS2 ubiquitin ligase complex regulates growth hormone receptor levels.
  findings: []
- id: PMID:21988832
  title: Toward an understanding of the protein interaction network of the human liver.
  findings: []
- id: PMID:22190034
  title: Global landscape of HIV-human protein complexes.
  findings: []
- id: PMID:22510880
  title: Nuclear receptor binding protein 1 regulates intestinal progenitor cell homeostasis and tumour formation.
  findings: []
- id: PMID:22649776
  title: The Role of Elongin BC-Containing Ubiquitin Ligases.
  findings: []
- id: PMID:23460923
  title: PRAME is a golgi-targeted protein that associates with the Elongin BC complex and is upregulated by interferon-gamma and bacterial PAMPs.
  findings: []
- id: PMID:23563313
  title: "CCDC22 deficiency in humans blunts activation of proinflammatory NF-\u03BAB signaling."
  findings: []
- id: PMID:23837592
  title: 'Multimeric complexes among ankyrin-repeat and SOCS-box protein 9 (ASB9), ElonginBC, and Cullin 5: insights into the structure and assembly of ECS-type Cullin-RING E3 ubiquitin ligases.'
  findings: []
- id: PMID:25416956
  title: A proteome-scale map of the human interactome network.
  findings: []
- id: PMID:25505247
  title: 'Biophysical studies on interactions and assembly of full-size E3 ubiquitin ligase: suppressor of cytokine signaling 2 (SOCS2)-elongin BC-cullin 5-ring box protein 2 (RBX2).'
  findings: []
- id: PMID:28514442
  title: Architecture of the human interactome defines protein communities and disease networks.
  findings: []
- id: PMID:28591624
  title: Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex.
  findings: []
- id: PMID:29779948
  title: "The Eukaryotic Proteome Is Shaped by E3\_Ubiquitin Ligases Targeting C-Terminal Degrons."
  findings: []
- id: PMID:30166453
  title: CRL4(AMBRA1) targets Elongin C for ubiquitination and degradation to modulate CRL5 signaling.
  findings: []
- id: PMID:31273098
  title: A glycine-specific N-degron pathway mediates the quality control of protein N-myristoylation.
  findings: []
- id: PMID:31387940
  title: BIK ubiquitination by the E3 ligase Cul5-ASB11 determines cell fate during cellular stress.
  findings: []
- id: PMID:31515488
  title: Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
  findings: []
- id: PMID:31980649
  title: Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).
  findings: []
- id: PMID:32296183
  title: A reference map of the human binary protein interactome.
  findings: []
- id: PMID:32353859
  title: A SARS-CoV-2 protein interaction map reveals targets for drug repurposing.
  findings: []
- id: PMID:32513959
  title: Structure and dynamics of the ASB9 CUL-RING E3 Ligase.
  findings: []
- id: PMID:33060197
  title: Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms.
  findings: []
- id: PMID:33184237
  title: The ZSWIM8 ubiquitin ligase mediates target-directed microRNA degradation.
  findings: []
- id: PMID:33268465
  title: The Mechanism of NEDD8 Activation of CUL5 Ubiquitin E3 Ligases.
  findings: []
- id: PMID:33398168
  title: Molecular basis for arginine C-terminal degron recognition by Cul2(FEM1) E3 ligase.
  findings: []
- id: PMID:33827988
  title: ORF10-Cullin-2-ZYG11B complex is not required for SARS-CoV-2 infection.
  findings: []
- id: PMID:33909987
  title: Convergence of mammalian RQC and C-end rule proteolytic pathways via alanine tailing.
  findings: []
- id: PMID:33961781
  title: Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
  findings: []
- id: PMID:34743205
  title: CRL2-KLHDC3 E3 ubiquitin ligase complex suppresses ferroptosis through promoting p14(ARF) degradation.
  findings: []
- id: PMID:34857742
  title: Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands.
  findings: []
- id: PMID:35512830
  title: Rab40c regulates focal adhesions and PP6 activity by controlling ANKRD28 ubiquitylation.
  findings: []
- id: PMID:36217030
  title: A comprehensive SARS-CoV-2-human protein-protein interactome reveals COVID-19 pathobiology and potential host therapeutic targets.
  findings: []
- id: PMID:37816714
  title: Structure-based design of a phosphotyrosine-masked covalent ligand targeting the E3 ligase SOCS2.
  findings: []
- id: PMID:37844242
  title: Molecular basis for C-degron recognition by CRL2(APPBP2) ubiquitin ligase.
  findings: []
- id: PMID:38418882
  title: The CRL5-SPSB3 ubiquitin ligase targets nuclear cGAS for degradation.
  findings: []
- id: PMID:39039081
  title: Molecular insights into degron recognition by CRL5(ASB7) ubiquitin ligase.
  findings: []
- id: PMID:40205054
  title: Multimodal cell maps as a foundation for structural and functional genomics.
  findings: []
- id: PMID:40440427
  title: ASB7 is a negative regulator of H3K9me3 homeostasis.
  findings: []
- id: PMID:40963025
  title: Covariation MS uncovers a protein that controls cysteine catabolism.
  findings: []
- id: PMID:7660122
  title: Inhibition of transcription elongation by the VHL tumor suppressor protein.
  findings: []
- id: PMID:7660129
  title: 'Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II.'
  findings: []
- id: Reactome:R-HSA-112379
  title: Recruitment of elongation factors to form elongation complex
  findings: []
- id: Reactome:R-HSA-112385
  title: Addition of nucleotides leads to transcript elongation
  findings: []
- id: Reactome:R-HSA-112392
  title: Resumption of elongation after recovery from pausing
  findings: []
- id: Reactome:R-HSA-112395
  title: Abortive termination of elongation after arrest
  findings: []
- id: Reactome:R-HSA-112396
  title: Separation of elongating transcript from template
  findings: []
- id: Reactome:R-HSA-112435
  title: Formation of Elongin BC complex
  findings: []
- id: Reactome:R-HSA-112436
  title: Formation of Elongin complex
  findings: []
- id: Reactome:R-HSA-113411
  title: 2-4 nt.backtracking of Pol II complex on the template leading to elongation pausing
  findings: []
- id: Reactome:R-HSA-113412
  title: Pol II elongation complex moves on the template as transcript elongates
  findings: []
- id: Reactome:R-HSA-113413
  title: TFIIS-mediated recovery of elongation from arrest
  findings: []
- id: Reactome:R-HSA-113414
  title: 7-14 nt. Backtracking of Pol II complex on the template leading to elongation arrest
  findings: []
- id: Reactome:R-HSA-113429
  title: Elongating transcript encounters a lesion in the template
  findings: []
- id: Reactome:R-HSA-1234159
  title: Proteasome proteolyzes ub-HIF-alpha
  findings: []
- id: Reactome:R-HSA-1234163
  title: Cytosolic VBC complex ubiquitinylates hydroxyprolyl-HIF-alpha
  findings: []
- id: Reactome:R-HSA-1234169
  title: Nuclear VHL:EloB,C:CUL2:RBX1 binds hydroxyprolyl-HIF-alpha
  findings: []
- id: Reactome:R-HSA-1234172
  title: Nuclear VBC complex ubiquitinylates HIF-alpha
  findings: []
- id: Reactome:R-HSA-1234173
  title: Cytosolic PHD2,3 hydroxylates proline residues on HIF3A
  findings: []
- id: Reactome:R-HSA-1234175
  title: ub-hydroxyPro-HIF-alpha:VHL:EloB,C:CUL2:RBX1 translocates from the nucleus to the cytosol
  findings: []
- id: Reactome:R-HSA-1234177
  title: Cytosolic PHD2,3 hydroxylates proline residues on HIF1A
  findings: []
- id: Reactome:R-HSA-1234183
  title: Cytosolic VHL:EloB,C:CUL2:RBX1 binds hydroxyprolyl-HIF-alpha
  findings: []
- id: Reactome:R-HSA-180540
  title: Multi-ubiquitination of APOBEC3G
  findings: []
- id: Reactome:R-HSA-180555
  title: Association of APOBEC3G:Vif with the Cul5-SCF complex
  findings: []
- id: Reactome:R-HSA-180603
  title: Proteosome-mediated degradation of APOBEC3G
  findings: []
- id: Reactome:R-HSA-6797606
  title: CDK12 phosphorylates RNA Pol II CTD at DNA repair genes
  findings: []
- id: Reactome:R-HSA-6797616
  title: CCNK:CDK12 binds RNA Pol II at DNA repair genes
  findings: []
- id: Reactome:R-HSA-8952039
  title: NEDD8:AcM-UBE2F binds CRL5 E3 ubiquitin ligase complex
  findings: []
- id: Reactome:R-HSA-8952044
  title: AcM-UBE2F transfers NEDD8 to CRL5 E3 ubiquitin ligase complex
  findings: []
- id: Reactome:R-HSA-8952625
  title: NEDD8:AcM-UBE2M binds CRL2 E3 ubiquitin ligase complex
  findings: []
- id: Reactome:R-HSA-8952626
  title: AcM-UBE2M transfers NEDD8 to CRL2 E3 ubiquitin ligase complex
  findings: []
- id: Reactome:R-HSA-8955241
  title: CAND1 binds cytosolic CRL E3 ubiquitin ligases
  findings: []
- id: Reactome:R-HSA-8955289
  title: COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes
  findings: []
- id: Reactome:R-HSA-8956040
  title: COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes
  findings: []
- id: Reactome:R-HSA-8956099
  title: VHL:EloB,C:NEDD8-CUL2:RBX1 complex binds UBXN7
  findings: []
- id: Reactome:R-HSA-8956103
  title: VHL:EloB,C:NEDD8-CUL2:RBX1 complex binds hydroxyprolyl-HIF-alpha
  findings: []
- id: Reactome:R-HSA-8956106
  title: VHL:EloB,C:NEDD8-CUL2:RBX1 complex ubiquitinylates HIF-alpha
  findings: []
- id: Reactome:R-HSA-9705738
  title: SOCS1,3 ubiquitinates CSF3R in SOCS1,3:p-4Y-CSF3R:CSF3 dimer:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2:CUL5:ELOB:ELOC:RNF7
  findings: []
- id: Reactome:R-HSA-9755303
  title: 26S proteasome degrades HIFalpha
  findings: []
- id: Reactome:R-HSA-9833107
  title: Association of NS1 (1C) with Cul5 and SCF
  findings: []
- id: Reactome:R-HSA-9833155
  title: Ubiquitination of STAT2
  findings: []
- id: Reactome:R-HSA-9954721
  title: NEDD8-K699-CUL2:ELOB:ELOC:RBX1:KLHDC10 K48 polyubiquitinates alanine-tailed nascent peptide
  findings: []
- id: Reactome:R-HSA-9954723
  title: NEDD8-K699-CUL2:ELOB:ELOC:RBX1:KLHDC10 binds alanine-tailed nascent peptide
  findings: []
- id: file:human/ELOC/ELOC-deep-research-falcon.md
  title: Falcon deep research report for human ELOC
  findings: []
core_functions:
- description: ELOC is the SKP1-like adaptor subunit of Elongin BC that enables substrate-receptor coupling and assembly of Elongin, CRL2, and CRL5 complexes rather than acting as a ubiquitin-transfer enzyme itself.
  supported_by:
  - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
    supporting_text: The literature retrieved here consistently uses **ELOC** as the human gene encoding **Elongin C** (also called **TCEB1**) and describes it as the **Elongin B/C adaptor subunit** that binds **BC-box/VHL-box/SOCS-box** motifs and bridges substrate receptors to **CUL2** or **CUL5** in Cullin-RING ubiquitin ligases (CRLs), matching the UniProt-provided identity and SKP1-like adaptor role.
  - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
    supporting_text: '**ELOC (Elongin C)** forms a heterodimer with **ELOB (Elongin B)**, commonly referred to as the **Elongin BC** module.'
  - reference_id: file:human/ELOC/ELOC-deep-research-falcon.md
    supporting_text: "ELOC\u2019s primary biochemical function in these contexts is **protein\u2013protein interaction and complex assembly**, not ubiquitin transfer catalysis per se."
  molecular_function:
    id: GO:0030674
    label: protein-macromolecule adaptor activity
  directly_involved_in:
  - id: GO:0016567
    label: protein ubiquitination
  - id: GO:0006511
    label: ubiquitin-dependent protein catabolic process
  locations:
  - id: GO:0005654
    label: nucleoplasm
  - id: GO:0005829
    label: cytosol
  in_complex:
    id: GO:0070449
    label: elongin complex
proposed_new_terms: []
suggested_questions:
- question: Which ELOC-containing CRL assemblies are most sensitive to ELOC interface variants such as Y79C, and how do these differ from VHL loss?
  experts: []
- question: How separable are ELOC roles in classical Elongin transcription elongation from its dominant CRL2/CRL5 adaptor functions across human cell types?
  experts: []
suggested_experiments:
- hypothesis: ELOC interface residues differentially support CRL2-VHL, CRL5-SOCS, and Elongin transcription elongation assemblies.
  description: Rescue ELOC-depleted cells with interface mutants and compare VHL-HIF turnover, SOCS-box CRL5 substrate degradation, and RNA polymerase II elongation readouts.
- hypothesis: ELOC promotes ubiquitin-dependent substrate degradation through adaptor-mediated complex assembly rather than catalytic ubiquitin transfer.
  description: Reconstitute ELOBC-containing CRL2 and CRL5 complexes with wild-type and mutant ELOC and measure complex formation, substrate receptor recruitment, and ubiquitination kinetics.

Gene Description

Existing Annotations Review

Core Functions

ELOC is the SKP1-like adaptor subunit of Elongin BC that enables substrate-receptor coupling and assembly of Elongin, CRL2, and CRL5 complexes rather than acting as a ubiquitin-transfer enzyme itself.

References

Suggested Questions for Experts

Suggested Experiments

Deep Research

Falcon

Research report: Human ELOC (TCEB1) / Elongin-C (UniProt Q15369)—functional annotation and recent research

0) Target verification (gene/protein identity)

1) Key concepts and definitions (current understanding)

1.1 Elongin BC is an adaptor module; ELOC provides the BC-box binding surface

1.2 Canonical CRL architectures relevant to ELOC

1.3 ELOC is not the catalytic enzyme; it is a structural adaptor controlling assembly and specificity

2) Molecular functions, complexes, and pathways

2.1 CRL2^VHL: oxygen sensing via HIFα degradation

2.3 Cross-regulation of CRL signaling: ELOC as a regulated subunit

2.4 Host–pathogen interactions and subcellular trafficking (localization-linked function)

3) Recent developments (prioritizing 2023–2024)

3.1 2024: CAND1 as a conditional inhibitor of CRL2^VHL—implications for ELOC-containing ligase dynamics

3.2 2024: ELOC-mutated RCC as a molecularly defined entity in the WHO 2022 classification—diagnostic integration of NGS

3.3 2024: Clinical and epidemiologic framing of ELOC lesions in renal cancer and therapeutic inference from VHL syndrome (HIF-2α inhibitors)

4) Current applications and real-world implementations

4.1 Molecular pathology: ELOC-mutated RCC diagnosis and classification

4.2 Precision therapeutics: HIF-2α inhibitors as mechanism-based therapy for ELOC pathway disruption

4.3 Targeted protein degradation (TPD/PROTACs): engineering VHL-recruiting degraders and accounting for CRL2 regulation

5) Subcellular localization (evidence-based summary)

6) Expert opinion and analysis (authoritative synthesis)

6.1 Why ELOC is “central” in CRL2/CRL5 biology

6.2 Interpreting ELOC-mutant tumors mechanistically

Summary table of ELOC functions and evidence

Key visual evidence (structure)

Selected references (publication date + URL)

Citations

📄 View Raw YAML

ELOC

Gene Description

Existing Annotations Review

Core Functions

ELOC is the SKP1-like adaptor subunit of Elongin BC that enables substrate-receptor coupling and assembly of Elongin, CRL2, and CRL5 complexes rather than acting as a ubiquitin-transfer enzyme itself.

References

Suggested Questions for Experts

Suggested Experiments

Deep Research

Falcon

Research report: Human ELOC (TCEB1) / Elongin-C (UniProt Q15369)—functional annotation and recent research

0) Target verification (gene/protein identity)

1) Key concepts and definitions (current understanding)

1.1 Elongin BC is an adaptor module; ELOC provides the BC-box binding surface

1.2 Canonical CRL architectures relevant to ELOC

1.3 ELOC is not the catalytic enzyme; it is a structural adaptor controlling assembly and specificity

2) Molecular functions, complexes, and pathways

2.1 CRL2^VHL: oxygen sensing via HIFα degradation

2.2 CRL5^SOCS: cytokine signaling regulation (JAK/STAT-related)

2.3 Cross-regulation of CRL signaling: ELOC as a regulated subunit

2.4 Host–pathogen interactions and subcellular trafficking (localization-linked function)

3) Recent developments (prioritizing 2023–2024)

3.1 2024: CAND1 as a conditional inhibitor of CRL2^VHL—implications for ELOC-containing ligase dynamics

3.2 2024: ELOC-mutated RCC as a molecularly defined entity in the WHO 2022 classification—diagnostic integration of NGS

3.3 2024: Clinical and epidemiologic framing of ELOC lesions in renal cancer and therapeutic inference from VHL syndrome (HIF-2α inhibitors)

4) Current applications and real-world implementations

4.1 Molecular pathology: ELOC-mutated RCC diagnosis and classification

4.2 Precision therapeutics: HIF-2α inhibitors as mechanism-based therapy for ELOC pathway disruption

4.3 Targeted protein degradation (TPD/PROTACs): engineering VHL-recruiting degraders and accounting for CRL2 regulation

5) Subcellular localization (evidence-based summary)

6) Expert opinion and analysis (authoritative synthesis)

6.1 Why ELOC is “central” in CRL2/CRL5 biology

6.2 Interpreting ELOC-mutant tumors mechanistically

Summary table of ELOC functions and evidence

Key visual evidence (structure)

Selected references (publication date + URL)

Citations

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