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TBCD
Identifiers
Aliases	TBCD, SSD-1, tfcD, tubulin folding cofactor D, PEBAT
External IDs	OMIM: 604649; MGI: 1919686; HomoloGene: 4368; GeneCards: TBCD; OMA:TBCD - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17q25.3 Start 82,752,042 bp End 82,945,914 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 E2 Start 121,342,775 bp End 121,507,990 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of thyroid gland apex of heart right hemisphere of cerebellum left lobe of thyroid gland canal of the cervix anterior pituitary right uterine tube granulocyte ectocervix ventricular zone Top expressed in epithelium of lens Epithelium of choroid plexus facial motor nucleus hair follicle Paneth cell stroma of bone marrow trigeminal ganglion endothelial cell of lymphatic vessel lacrimal gland condyle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function chaperone binding GTPase activator activity protein binding beta-tubulin binding Cellular component cytoplasm lateral plasma membrane membrane bicellular tight junction adherens junction plasma membrane cell junction microtubule centrosome microtubule organizing center cytoskeleton Biological process negative regulation of cell-substrate adhesion negative regulation of microtubule polymerization adherens junction assembly protein folding bicellular tight junction assembly positive regulation of GTPase activity post-chaperonin tubulin folding pathway mitotic cell cycle cell morphogenesis involved in neuron differentiation tubulin complex assembly microtubule cytoskeleton organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6904 108903 Ensembl ENSG00000278759 ENSG00000141556 ENSMUSG00000039230 UniProt Q9BTW9 Q8BYA0 RefSeq (mRNA) NM_001033052 NM_005993 NM_029878 RefSeq (protein) NP_005984 NP_084154 Location (UCSC) Chr 17: 82.75 – 82.95 Mb Chr 11: 121.34 – 121.51 Mb PubMed search
Wikidata
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Tubulin-specific chaperone D is a protein that in humans is encoded by the TBCD gene.

Function

Cofactor D 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.

Interactions

TBCD has been shown to interact with ARL2.

References

1. ^ ENSG00000141556 GRCh38: Ensembl release 89: ENSG00000278759, ENSG00000141556 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000039230 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ "Entrez Gene: TBCD tubulin folding cofactor D".
6. Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA (October 2003). "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. doi:10.1074/jbc.M308678200. PMID 12912990.
7. Bhamidipati A, Lewis SA, Cowan NJ (May 2000). "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. doi:10.1083/jcb.149.5.1087. PMC 2174823. PMID 10831612.

Further reading

• Lewis SA, Tian G, Vainberg IE, Cowan NJ (1996). "Chaperonin-mediated folding of actin and tubulin". J. Cell Biol. 132 (1–2): 1–4. doi:10.1083/jcb.132.1.1. PMC 2120700. PMID 8567715.
• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Tian G, Huang Y, Rommelaere H, Vandekerckhove J, Ampe C, Cowan NJ (1996). "Pathway leading to correctly folded beta-tubulin". Cell. 86 (2): 287–96. doi:10.1016/S0092-8674(00)80100-2. PMID 8706133. S2CID 18359371.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Tian G, Lewis SA, Feierbach B, Stearns T, Rommelaere H, Ampe C, Cowan NJ (1997). "Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors". J. Cell Biol. 138 (4): 821–32. doi:10.1083/jcb.138.4.821. PMC 2138046. PMID 9265649.
• Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (1999). "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (1): 63–70. doi:10.1093/dnares/6.1.63. PMID 10231032.
• Martín L, Fanarraga ML, Aloria K, Zabala JC (2000). "Tubulin folding cofactor D is a microtubule destabilizing protein". FEBS Lett. 470 (1): 93–5. doi:10.1016/S0014-5793(00)01293-X. PMID 10722852. S2CID 35012741.
• Bhamidipati A, Lewis SA, Cowan NJ (2000). "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. doi:10.1083/jcb.149.5.1087. PMC 2174823. PMID 10831612.
• Schubert A, Cattaruzza M, Hecker M, Darmer D, Holtz J, Morawietz H (2001). "Shear stress-dependent regulation of the human beta-tubulin folding cofactor D gene". Circ. Res. 87 (12): 1188–94. doi:10.1161/01.res.87.12.1188. PMID 11110777.
• Wistow G, Bernstein SL, Wyatt MK, Fariss RN, Behal A, Touchman JW, Bouffard G, Smith D, Peterson K (2002). "Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants". Mol. Vis. 8: 205–20. PMID 12107410.
• Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA (2003). "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. doi:10.1074/jbc.M308678200. PMID 12912990.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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