TBCD

TBCD
Identifiers
Aliases	TBCD, SSD-1, tfcD, tubulin folding cofactor D, PEBAT
External IDs	OMIM: 604649 MGI: 1919686 HomoloGene: 4368 GeneCards: TBCD
Gene location (Human)
Chr.	Chromosome 17 (human)[1]
End	82,945,914 bp[1]
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)[2]
End	121,617,164 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• chaperone binding; • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity; • GO:0001948 protein binding; • beta-tubulin binding;
Cellular component	• cytoplasm; • lateral plasma membrane; • membrane; • bicellular tight junction; • adherens junction; • cell membrane; • cell junction; • microtubules; • 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; • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity; • post-chaperonin tubulin folding pathway; • GO:0007067 mitotic cell cycle; • cell morphogenesis involved in neuron differentiation; • tubulin complex assembly; • microtubule cytoskeleton organization;
	Sources:Amigo / QuickGO
Orthologs
	6904
	108903
	ENSG00000278759; ENSG00000141556
	ENSMUSG00000039230
	Q9BTW9
	Q8BYA0
	NM_001033052; NM_005993
	NM_029878
	NP_005984
	NP_084154
	Wikidata
View/Edit Human	View/Edit Mouse

Tubulin-specific chaperone D is a protein that in humans is encoded by the TBCD gene.[5]

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.[5]

Interactions

TBCD has been shown to interact with ARL2.[6][7]

References

ENSG00000141556 GRCh38: Ensembl release 89: ENSG00000278759, ENSG00000141556 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000039230 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: TBCD tubulin folding cofactor D".
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.
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.

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. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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[refGRCh38Ensembl-1] ENSG00000141556 GRCh38: Ensembl release 89: ENSG00000278759, ENSG00000141556 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[entrez-5] "Entrez Gene: TBCD tubulin folding cofactor D".

[pmid12912990-6] 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.

[pmid10831612-7] 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.

TBCD

Function

Interactions

References

Further reading