TBCA

Tubulin-specific chaperone A is a protein that in humans is encoded by the TBCA gene.^[5][6][7]

TBCA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1H7C
Identifiers
Aliases	TBCA, tubulin folding cofactor A
External IDs	OMIM: 610058; MGI: 107549; HomoloGene: 3388; GeneCards: TBCA; OMA:TBCA - orthologs
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q14.1 Start 77,691,166 bp[1] End 77,868,780 bp[1]
Gene location (Mouse) Chr. Chromosome 13 (mouse)[2] Band 13|13 C3 Start 94,925,418 bp[2] End 94,979,430 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right adrenal cortex left adrenal gland left adrenal cortex ganglionic eminence ventricular zone left ovary islet of Langerhans anterior pituitary gastric mucosa tibial arteries Top expressed in cumulus cell endocardial cushion facial motor nucleus supraoptic nucleus medial ganglionic eminence atrioventricular valve mandibular prominence maxillary prominence abdominal wall trigeminal ganglion More reference expression data BioGPS More reference expression data
Gene ontology Molecular function chaperone binding protein binding beta-tubulin binding RNA binding Cellular component cytoplasm microtubule cytoskeleton nucleolus microtubule cytoskeleton extracellular exosome Biological process post-chaperonin tubulin folding pathway tubulin complex assembly protein folding Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6902 21371 Ensembl ENSG00000171530 ENSMUSG00000042043 UniProt O75347 P48428 RefSeq (mRNA) NM_004607 NM_001297738 NM_001297740 NM_009321 RefSeq (protein) NP_001284667 NP_001284669 NP_004598 NP_033347 Location (UCSC) Chr 5: 77.69 – 77.87 Mb Chr 13: 94.93 – 94.98 Mb PubMed search [3] [4]
Wikidata
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The product of this gene is one of four proteins (cofactors A, D, E, and C) involved in the pathway leading to correctly folded beta-tubulin from folding intermediates. Cofactors A and D are believed to play a role in capturing and stabilizing beta-tubulin intermediates in a quasi-native confirmation. Cofactor E binds to the cofactor D/beta-tubulin complex; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state. This gene encodes chaperonin cofactor A.^[7]