SCUBA

ELOC — Elongin C

ELOC belongs to a gene co-expression module in 9 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

ELOC's module in each cell type

Cell typeModuleShares the module with
CD8⁺ T cellsMitochondrial Housekeeping
Housekeeping
AURKAIP1, CCDC167, ITGB1BP1, MRPL57, NDUFB7, PDCD5, RBM17, SNRPA1 +2 moreView in SCUBA
EndothelialStress RNA Processing
RNA processing & translation
ARF4, CACYBP, ENY2, EWSR1, GNA14, HNRNPDL, HNRNPF, MAP3K13 +5 moreView in SCUBA
FibroblastsER Stress UPR
Stress
ARF4, B4GALT1, BTG3, BZW1, CYCS, EFHD2, LDHA, LITAF +6 moreView in SCUBA
Gamma-delta T cellsGPCR-AKT-MAPK Signaling
TCR Signaling
ADNP, AKT1, ALYREF, B3GALT6, BRD4, BRI3, BTBD6, CENPB +29 more
Glial cellsActin Cytoskeletal Organization
Cytoskeletal
ACTB, ACTG1, CALM1, CFL1, CIRBP, DYNLL1, MORF4L2, PPIA +1 moreView in SCUBA
Goblet cellsBasal Transcription
Housekeeping
ACTB, ACTG1, CALM2, DYNLL1, ENY2, GTF2A2, LSM8, POLR2K +2 moreView in SCUBA
Innate lymphoid cellsTRiC Chaperonin Folding
Protein processing & ER
ATP6V0D1, CACYBP, CCT2, CCT3, CCT4, CCT5, EIF5A, FAM162A +9 moreView in SCUBA
Lymphatic endothelialNotch TGF-β Endothelial
endothelial development
ARF6, ARL4C, C16orf87, CCNL1, CLK1, DEDD2, GPBP1, HEY1 +11 moreView in SCUBA
MacrophagesGlycolytic Redox Metabolism
Lipid metabolism
AGPAT2, ANXA5, ATP6V1F, BCKDK, BRI3, C1orf122, CLIC1, ENO1 +18 moreView in SCUBA

About the gene

SynonymsSIII, TCEB1
Chromosome8: 73939169-73972307
Predicted locationIntracellular
Essential geneYes
Protein classEssential proteins, Plasma proteins, Predicted intracellular proteins
Biological processHost-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway

Function

SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity). Core component of multiple cullin-RING-based ECS (ElonginB/C- CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. By binding to BC- box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes. Component the von Hippel-Lindau ubiquitination complex CBC(VHL). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The ECS(ASB9) complex mediates ubiquitination and degradation of CKB. As part of a multisubunit ubiquitin ligase complex, polyubiquitinates monoubiquitinated POLR2A. ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity). As part of the ECS(RAB40C) complex, mediates ANKRD28 ubiquitination and degradation, thereby inhibiting protein phosphatase 6 (PP6) complex activity and focal adhesion assembly during cell migration. (Microbial infection) Following infection by HIV-1 virus, component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, which catalyzes ubiquitination and degradation of APOBEC3F and APOBEC3G. The complex can also ubiquitinate APOBEC3H to some extent.

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.