Q15369 · ELOC_HUMAN
- ProteinElongin-C
- GeneELOC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids112 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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) (PubMed:7821821).
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).
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 (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694, PubMed:21199876, PubMed:26138980, PubMed:29775578, PubMed:29779948, PubMed:30166453, PubMed:33268465).
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).
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).
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).
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).
(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).
The complex can also ubiquitinate APOBEC3H to some extent (PubMed:37640699).
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Cul2-RING ubiquitin ligase complex | |
Cellular Component | Cul5-RING ubiquitin ligase complex | |
Cellular Component | cytosol | |
Cellular Component | elongin complex | |
Cellular Component | nucleoplasm | |
Molecular Function | protein-macromolecule adaptor activity | |
Molecular Function | transcription corepressor binding | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of transcription by RNA polymerase II | |
Biological Process | target-directed miRNA degradation | |
Biological Process | transcription initiation at RNA polymerase II promoter | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameElongin-C
- Short namesEloC
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ15369
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 99 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000187258 | 1-112 | Elongin-C | |||
Sequence: MDGEEKTYGGCEGPDAMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC |
Post-translational modification
Ubiquitinated by the DCX(AMBRA1) complex, leading to its degradation by the proteasome.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Overexpressed in prostate cancer cell line PC-3 and breast cancer cell line SK-BR-3.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Heterotrimer of an A (ELOA, ELOA2 or ELOA3P), ELOB and ELOC subunit (PubMed:17997974).
The elongin BC complex interacts with EPOP; leading to recruit the elongin BC complex to Polycomb group (PcG) target genes, thereby restricting excessive activity of the PRC2/EED-EZH2 complex (By similarity).
Component of multiple cullin-RING E3 ubiquitin-protein ligase complexes composed of Elongin BC (ELOB and ELOC), a cullin (CUL2 or CUL5), a catalytic subunit (RBX1 or RNF7/RBX2), as well as a substrate adapter protein that can be either ASB2, ASB9, ASB11, KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B, FEM1C, LRR1, PCMTD1, SOCS1, SOCS2, SOCS5, SPSB1, SPSB3, ELOA, VHL, WSB1 or ZYG11B (PubMed:10205047, PubMed:11006129, PubMed:12004076, PubMed:12050673, PubMed:15590694, PubMed:17189197, PubMed:17304241, PubMed:19920177, PubMed:21980433, PubMed:23102700, PubMed:23837592, PubMed:24337577, PubMed:25505247, PubMed:26138980, PubMed:29775578, PubMed:29779948, PubMed:31182716, PubMed:31387940, PubMed:32513959, PubMed:33268465, PubMed:34700328, PubMed:34857742, PubMed:35486881, PubMed:37816714, PubMed:38418882).
Interacts with TMF1 (PubMed:15467733).
As part of the Elongin BC E3 ubiquitin ligase complex; interacts with NRBP1 (PubMed:22510880).
The elongin BC complex interacts with EPOP; leading to recruit the elongin BC complex to Polycomb group (PcG) target genes, thereby restricting excessive activity of the PRC2/EED-EZH2 complex (By similarity).
Component of multiple cullin-RING E3 ubiquitin-protein ligase complexes composed of Elongin BC (ELOB and ELOC), a cullin (CUL2 or CUL5), a catalytic subunit (RBX1 or RNF7/RBX2), as well as a substrate adapter protein that can be either ASB2, ASB9, ASB11, KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B, FEM1C, LRR1, PCMTD1, SOCS1, SOCS2, SOCS5, SPSB1, SPSB3, ELOA, VHL, WSB1 or ZYG11B (PubMed:10205047, PubMed:11006129, PubMed:12004076, PubMed:12050673, PubMed:15590694, PubMed:17189197, PubMed:17304241, PubMed:19920177, PubMed:21980433, PubMed:23102700, PubMed:23837592, PubMed:24337577, PubMed:25505247, PubMed:26138980, PubMed:29775578, PubMed:29779948, PubMed:31182716, PubMed:31387940, PubMed:32513959, PubMed:33268465, PubMed:34700328, PubMed:34857742, PubMed:35486881, PubMed:37816714, PubMed:38418882).
Interacts with TMF1 (PubMed:15467733).
As part of the Elongin BC E3 ubiquitin ligase complex; interacts with NRBP1 (PubMed:22510880).
(Microbial infection) Interacts with HIV-1 Vif; forming an active cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex).
(Microbial infection) Substrate adapter protein can be a viral protein such as HIV Vif.
(Microbial infection) Interacts with human respiratory syncytial virus (HRSV) protein NS1.
(Microbial infection) Interacts with molluscum contagiosum virus MC132.
(Microbial infection) Interacts with herpes virus 8 virus protein LANA1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q15369 | ASB9 Q96DX5 | 5 | EBI-301231, EBI-745641 | |
BINARY | Q15369 | COMMD1 Q8N668 | 2 | EBI-301231, EBI-1550112 | |
BINARY | Q15369 | CUL2 Q13617 | 10 | EBI-301231, EBI-456179 | |
BINARY | Q15369 | CUL3 Q13618 | 3 | EBI-301231, EBI-456129 | |
BINARY | Q15369 | ELOB Q15370 | 20 | EBI-301231, EBI-301238 | |
XENO | Q15369 | GAMMAHV.ORF73 O41974 | 2 | EBI-301231, EBI-6933128 | |
BINARY | Q15369 | MED8 Q96G25 | 3 | EBI-301231, EBI-394405 | |
BINARY | Q15369 | METTL21C Q5VZV1 | 9 | EBI-301231, EBI-10236049 | |
XENO | Q15369 | ORF10 A0A663DJA2 | 4 | EBI-301231, EBI-25475906 | |
BINARY | Q15369 | PRAME P78395 | 12 | EBI-301231, EBI-348325 | |
BINARY | Q15369 | SOCS1 O15524 | 4 | EBI-301231, EBI-968198 | |
BINARY | Q15369 | SOCS2 O14508 | 2 | EBI-301231, EBI-617737 | |
BINARY | Q15369 | SPSB2 Q99619 | 4 | EBI-301231, EBI-2323209 | |
BINARY | Q15369 | SPSB4 Q96A44 | 3 | EBI-301231, EBI-2323233 | |
XENO | Q15369 | vif P12504 | 5 | EBI-301231, EBI-779991 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q15369-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length112
- Mass (Da)12,473
- Last updated1996-11-01 v1
- Checksum98D88696E883538B
Q15369-2
- Name2
- Differences from canonical
- 1-16: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8J9AD82 | A0A8J9AD82_HUMAN | ELOC | 135 | ||
R4GMY8 | R4GMY8_HUMAN | ELOC | 65 | ||
A0A8I5KYG1 | A0A8I5KYG1_HUMAN | ELOC | 133 | ||
E5RHG8 | E5RHG8_HUMAN | ELOC | 89 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045955 | 1-16 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L34587 EMBL· GenBank· DDBJ | AAA67650.1 EMBL· GenBank· DDBJ | mRNA | ||
BX649138 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AC022868 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC013809 EMBL· GenBank· DDBJ | AAH13809.1 EMBL· GenBank· DDBJ | mRNA | ||
BC093065 EMBL· GenBank· DDBJ | AAH93065.1 EMBL· GenBank· DDBJ | mRNA | ||
BC100028 EMBL· GenBank· DDBJ | AAI00029.1 EMBL· GenBank· DDBJ | mRNA | ||
BC100283 EMBL· GenBank· DDBJ | AAI00284.1 EMBL· GenBank· DDBJ | mRNA |