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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.
Assigned HPA protein class(es) for the encoded protein(s).
Plasma proteins
Predicted locationi
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
6
Cytoband
q25.3
Chromosome location (bp)
159778498 - 159789703
Number of transcriptsi
Number of protein-coding transcripts from the gene as defined by Ensembl.
Useful information about the protein provided by UniProt.
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis 1. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance 2. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia 3. The TRiC complex plays a role in the folding of actin and tubulin (Probable)....show less
Molecular function (UniProt)i
Keywords assigned by UniProt to proteins due to their particular molecular function.
Chaperone
Ligand (UniProt)i
Keywords assigned by UniProt to proteins because they bind, are associated with, or whose activity is dependent of some molecule.
ATP-binding, Nucleotide-binding
Gene summary (Entrez)i
Useful information about the gene from Entrez
The protein encoded by this gene is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized. In addition, three pseudogenes that appear to be derived from this gene have been found. [provided by RefSeq, Jun 2010]...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.
P17987 [Direct mapping] T-complex protein 1 subunit alpha
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Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Plasma proteins 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:0000166[nucleotide binding] GO:0000242[pericentriolar material] GO:0000792[heterochromatin] GO:0001669[acrosomal vesicle] GO:0002199[zona pellucida receptor complex] GO:0003723[RNA binding] GO:0005515[protein binding] GO:0005524[ATP binding] GO:0005737[cytoplasm] GO:0005794[Golgi apparatus] GO:0005813[centrosome] GO:0005815[microtubule organizing center] GO:0005829[cytosol] GO:0005832[chaperonin-containing T-complex] GO:0005856[cytoskeleton] GO:0005874[microtubule] GO:0006457[protein folding] GO:0007021[tubulin complex assembly] GO:0007339[binding of sperm to zona pellucida] GO:0016887[ATP hydrolysis activity] GO:0031625[ubiquitin protein ligase binding] GO:0032212[positive regulation of telomere maintenance via telomerase] GO:0044053[translocation of peptides or proteins into host cell cytoplasm] GO:0044183[protein folding chaperone] GO:0044297[cell body] GO:0050821[protein stabilization] GO:0051082[unfolded protein binding] GO:0051973[positive regulation of telomerase activity] GO:0061077[chaperone-mediated protein folding] GO:0070062[extracellular exosome] GO:0090666[scaRNA localization to Cajal body] GO:0140662[ATP-dependent protein folding chaperone] GO:1901998[toxin transport] GO:1904851[positive regulation of establishment of protein localization to telomere] GO:1904871[positive regulation of protein localization to Cajal body] GO:1904874[positive regulation of telomerase RNA localization to Cajal body] GO:2000109[regulation of macrophage apoptotic process]
E7EQR6 [Direct mapping] T-complex protein 1 subunit alpha
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Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Protein evidence (Kim et al 2014) Protein evidence (Ezkurdia et al 2014)
The Human Protein Atlas project is funded
