ELOC
Elongin-C
Also known as: ELOC_HUMAN, SIII, TCEB1
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q15369
- Gene
- ELOC
- Ensembl
- ENSG00000154582
- Chromosome
- 8
- Canonical length
- 112 aa
- Protein class
- Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoli,Vesicles,Cell Junctions
OverviewNCBI Gene
This gene encodes the protein elongin C, which is a subunit of the transcription factor B (SIII) complex. The SIII complex is composed of elongins A/A2, B and C. It activates elongation by RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. Elongin A functions as the transcriptionally active component of the SIII complex, whereas elongins B and C are regulatory subunits. Elongin A2 is specifically expressed in the testis, and capable of forming a stable complex with elongins B and C. The von Hippel-Lindau tumor suppressor protein binds to elongins B and C, and thereby inhibits transcription elongation. Multiple alternatively spliced transcript variants encoding two distinct isoforms have been identified. [provided by RefSeq, Mar 2011]
Canonical amino-acid sequenceUniProt
112 residues, UniProt reviewed canonical sequence.
>Q15369|ELOC
1 MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG QFAENETNEV
61 NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA LELLMAANFL DCLocalizationUniProt · AlphaFold · HPA
Whether an antibody against ELOC can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.36
- Highest tissue expression
- 191 nTPM
Expression across tissuesHPA
Tissue
- skeletal muscle: 191 nTPM
- heart muscle: 138 nTPM
- tongue: 121 nTPM
- cerebral cortex: 118 nTPM
- testis: 112 nTPM
- amygdala: 111 nTPM
Single-cell type
- esophageal apical cells: 992 nCPM
- late primary spermatocytes: 919 nCPM
- early spermatids: 636 nCPM
- late spermatids: 588 nCPM
- extravillous trophoblasts: 445 nCPM
- esophageal suprabasal cells: 439 nCPM
Immune cell
- basophil: 144 nTPM
- plasmacytoid DC: 124 nTPM
- T-reg: 103 nTPM
- eosinophil: 89 nTPM
- memory B-cell: 87 nTPM
- neutrophil: 82 nTPM
Brain region
- cerebral cortex: 88 nTPM
- hippocampal formation: 85 nTPM
- white matter: 82 nTPM
- basal ganglia: 80 nTPM
- cerebellum: 79 nTPM
- hypothalamus: 76 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about ELOC.
Disease | ImmuneIEDB
Conditions an epitope on ELOC was assayed in.
- skin melanoma T cell
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.66
- gnomAD pLI
- 0.74
- DepMap mean gene effect
- -1.25
- DepMap dependency class
- common
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 15% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- protein ubiquitination
- regulation of transcription by RNA polymerase II
- target-directed miRNA degradation
- transcription initiation at RNA polymerase II promoter
- ubiquitin-dependent protein catabolic process
- ubiquitin-dependent protein catabolic process via the C-end degron rule pathway
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of ELOC in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads ELOC as an antibody target. Whether an autoantibody or antibody against ELOC could matter depends on whether native ELOC is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
ELOC is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label ELOC as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
Loading the interactive Seroatlas protein explorer...