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General description of the gene and the encoded protein(s) using information from HGNC and Ensembl, as well as predictions made by the Human Protein Atlas project.
Gene namei
Official gene symbol, which is typically a short form of the gene name, according to HGNC.
All transcripts of all genes have been analyzed regarding the location(s) of corresponding protein based on prediction methods for signal peptides and transmembrane regions.
Genes with at least one transcript predicted to encode a secreted protein, according to prediction methods or to UniProt location data, have been further annotated and classified with the aim to determine if the corresponding protein(s) are secreted or actually retained in intracellular locations or membrane-attached.
Remaining genes, with no transcript predicted to encode a secreted protein, will be assigned the prediction-based location(s).
The annotated location overrules the predicted location, so that a gene encoding a predicted secreted protein that has been annotated as intracellular will have intracellular as the final location.
Gene information from Ensembl and Entrez, as well as links to available gene identifiers are displayed here. Information was retrieved from Ensembl if not indicated otherwise.
Chromosome
16
Cytoband
p13.3
Chromosome location (bp)
2771414 - 2777289
Number of transcriptsi
Number of protein-coding transcripts from the gene as defined by Ensembl.
Useful information about the protein provided by UniProt.
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) 1. 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)....show less
Biological process (UniProt)i
Keywords assigned by UniProt to proteins because they are involved in a particular biological process.
This gene encodes the protein elongin B, 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. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene. Pseudogenes have been identified on chromosomes 11 and 13. [provided by RefSeq, Aug 2008]...show less
PROTEIN INFORMATIONi
The protein information section displays alternative protein-coding transcripts (splice variants) encoded by this gene according to the Ensembl database.
The ENSP identifier links to the Ensembl website protein summary, while the ENST identifier links to the Ensembl website transcript summary for the selected splice variant. The data in the UniProt column can be expanded to show links to all matching UniProt identifiers for this protein.
The protein classes assigned to this protein are shown if expanding the data in the protein class column. Parent protein classes are in bold font and subclasses are listed under the parent class.
The Gene Ontology terms assigned to this protein are listed if expanding the Gene ontology column. The length of the protein (amino acid residues according to Ensembl), molecular mass (kDalton), predicted signal peptide (according to a majority of the signal peptide predictors SPOCTOPUS, SignalP 4.0, and Phobius) and the number of predicted transmembrane region(s) (according to MDM) are also reported.
A0A384MDL3 [Target identity:100%; Query identity:100%] Epididymis secretory sperm binding protein
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Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Mapped to neXtProt neXtProt - Evidence at protein level Protein evidence (Kim et al 2014) Protein evidence (Ezkurdia et al 2014)
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GO:0001222[transcription corepressor binding] GO:0005515[protein binding] GO:0005634[nucleus] GO:0005654[nucleoplasm] GO:0005829[cytosol] GO:0006367[transcription initiation at RNA polymerase II promoter] GO:0006368[transcription elongation by RNA polymerase II promoter] GO:0016567[protein ubiquitination] GO:0030891[VCB complex] GO:0031462[Cul2-RING ubiquitin ligase complex] GO:0031466[Cul5-RING ubiquitin ligase complex] GO:0031625[ubiquitin protein ligase binding] GO:0032436[positive regulation of proteasomal ubiquitin-dependent protein catabolic process] GO:0065003[protein-containing complex assembly] GO:0070449[elongin complex]
Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Mapped to neXtProt neXtProt - Evidence at protein level Protein evidence (Kim et al 2014) Protein evidence (Ezkurdia et al 2014)
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GO:0001222[transcription corepressor binding] GO:0005515[protein binding] GO:0005634[nucleus] GO:0005654[nucleoplasm] GO:0005829[cytosol] GO:0006367[transcription initiation at RNA polymerase II promoter] GO:0006368[transcription elongation by RNA polymerase II promoter] GO:0016567[protein ubiquitination] GO:0030891[VCB complex] GO:0031462[Cul2-RING ubiquitin ligase complex] GO:0031466[Cul5-RING ubiquitin ligase complex] GO:0031625[ubiquitin protein ligase binding] GO:0032436[positive regulation of proteasomal ubiquitin-dependent protein catabolic process] GO:0065003[protein-containing complex assembly] GO:0070449[elongin complex]
SCAMPI predicted membrane proteins Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Protein evidence (Ezkurdia et al 2014)
The Human Protein Atlas project is funded
