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) (PubMed:7638163). 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-2 and cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes), which mediate the ubiquitination of target proteins (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694, PubMed:26138980, PubMed:29775578, PubMed:29779948, PubMed:33268465, PubMed:37844242, PubMed:38326650, PubMed:39039081, PubMed:35512830, PubMed:39039081, PubMed:40440427, PubMed:40963025). 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 (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694). Component the von Hippel-Lindau ubiquitination complex CBC(VHL) (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694). 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 (PubMed:26138980, PubMed:29775578, PubMed:29779948, PubMed:36805027, PubMed:37844242, PubMed:38177675). The ECS(ASB9) complex mediates ubiquitination and degradation of CKB (PubMed:33268465). As part of a multisubunit ubiquitin ligase complex, polyubiquitinates monoubiquitinated POLR2A (PubMed:19920177). 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 (PubMed:35512830). The ECS(ASB7) complex acts a negative regulator of H3K9me3 histone mark by mediating ubiquitination and degradation of SUV39H1 (PubMed:40440427). As part of the ECS(LRRC58) complex, mediates CDO1 ubiquitination and degradation, regulating cysteine catabolism (PubMed:40963025). {ECO:0000250|UniProtKB:P62869, ECO:0000269|PubMed:10205047, ECO:0000269|PubMed:12004076, ECO:0000269|PubMed:12050673, ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:33268465, ECO:0000269|PubMed:35512830, ECO:0000269|PubMed:36805027, ECO:0000269|PubMed:37844242, ECO:0000269|PubMed:38177675, ECO:0000269|PubMed:39039081, ECO:0000269|PubMed:40440427, ECO:0000269|PubMed:40963025}. (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 (PubMed:18562529, PubMed:20532212, PubMed:22190037, PubMed:24225024, PubMed:24402281, PubMed:36754086). The complex can also ubiquitinate APOBEC3H to some extent (PubMed:37640699). {ECO:0000269|PubMed:18562529, ECO:0000269|PubMed:20532212, ECO:0000269|PubMed:22190037, ECO:0000269|PubMed:24225024, ECO:0000269|PubMed:24402281, ECO:0000269|PubMed:36754086, ECO:0000269|PubMed:37640699}. This is the function of Ensembl gene identifier ENSG00000103363 (ELOB, elongin B).