TBCD: Difference between revisions

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{{for|the Telephony Binary-Coded Decimal digital encoding method|Binary-coded decimal}}
{{PBB_Controls
{{Infobox_gene}}
| update_page = yes
'''Tubulin-specific chaperone D''' is a [[protein]] that in humans is encoded by the ''TBCD'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TBCD tubulin folding cofactor D| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6904| accessdate = }}</ref>
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Tubulin folding cofactor D
| HGNCid = 11581
| Symbol = TBCD
| AltSymbols =; KIAA0988
| OMIM = 604649
| ECnumber = 
| Homologene = 4368
| MGIid = 1919686
| GeneAtlas_image1 = PBB_GE_TBCD_201759_at_tn.png
| Function = {{GNF_GO|id=GO:0051087 |text = chaperone binding}}
| Component = {{GNF_GO|id=GO:0005874 |text = microtubule}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0007025 |text = beta-tubulin folding}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6904
    | Hs_Ensembl = ENSG00000141556
    | Hs_RefseqProtein = NP_001028224
    | Hs_RefseqmRNA = NM_001033052
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 78303227
    | Hs_GenLoc_end = 78494345
    | Hs_Uniprot = Q9BTW9
    | Mm_EntrezGene = 108903
    | Mm_Ensembl = ENSMUSG00000039230
    | Mm_RefseqmRNA = NM_029878
    | Mm_RefseqProtein = NP_084154
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 121268039
    | Mm_GenLoc_end = 121433254
    | Mm_Uniprot = Q8R199
  }}
}}
'''Tubulin folding cofactor D''', also known as '''TBCD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TBCD tubulin folding cofactor D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6904| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: TBCD tubulin folding cofactor D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6904| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
TBCD has been shown to [[Protein-protein interaction|interact]] with [[ARL2]].<ref name=pmid12912990>{{cite journal | vauthors = Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA | title = Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A | journal = J. Biol. Chem. | volume = 278 | issue = 42 | pages = 40829–36 | date = October 2003 | pmid = 12912990 | doi = 10.1074/jbc.M308678200 }}</ref><ref name=pmid10831612>{{cite journal | vauthors = Bhamidipati A, Lewis SA, Cowan NJ | title = ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin | journal = J. Cell Biol. | volume = 149 | issue = 5 | pages = 1087–96 | date = May 2000 | pmid = 10831612 | pmc = 2174823 | doi = 10.1083/jcb.149.5.1087 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Lewis SA, Tian G, Vainberg IE, Cowan NJ | title = Chaperonin-mediated folding of actin and tubulin | journal = J. Cell Biol. | volume = 132 | issue = 1–2 | pages = 1–4 | year = 1996 | pmid = 8567715 | pmc = 2120700 | doi = 10.1083/jcb.132.1.1 }}
| citations =
* {{cite journal | vauthors = Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA | title = A "double adaptor" method for improved shotgun library construction | journal = Anal. Biochem. | volume = 236 | issue = 1 | pages = 107–13 | year = 1996 | pmid = 8619474 | doi = 10.1006/abio.1996.0138 }}
*{{cite journal | author=Lewis SA, Tian G, Vainberg IE, Cowan NJ |title=Chaperonin-mediated folding of actin and tubulin. |journal=J. Cell Biol. |volume=132 |issue= 1-2 |pages= 1-4 |year= 1996 |pmid= 8567715 |doi= }}
* {{cite journal | vauthors = Tian G, Huang Y, Rommelaere H, Vandekerckhove J, Ampe C, Cowan NJ | title = Pathway leading to correctly folded beta-tubulin | journal = Cell | volume = 86 | issue = 2 | pages = 287–96 | year = 1996 | pmid = 8706133 | doi = 10.1016/S0092-8674(00)80100-2 }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
* {{cite journal | vauthors = Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA | title = Large-scale concatenation cDNA sequencing | journal = Genome Res. | volume = 7 | issue = 4 | pages = 353–8 | year = 1997 | pmid = 9110174 | pmc = 139146 | doi = 10.1101/gr.7.4.353 }}
*{{cite journal | author=Tian G, Huang Y, Rommelaere H, ''et al.'' |title=Pathway leading to correctly folded beta-tubulin. |journal=Cell |volume=86 |issue= 2 |pages= 287-96 |year= 1996 |pmid= 8706133 |doi= }}
* {{cite journal | vauthors = Tian G, Lewis SA, Feierbach B, Stearns T, Rommelaere H, Ampe C, Cowan NJ | title = Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors | journal = J. Cell Biol. | volume = 138 | issue = 4 | pages = 821–32 | year = 1997 | pmid = 9265649 | pmc = 2138046 | doi = 10.1083/jcb.138.4.821 }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
* {{cite journal | vauthors = Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = 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 | journal = DNA Res. | volume = 6 | issue = 1 | pages = 63–70 | year = 1999 | pmid = 10231032 | doi = 10.1093/dnares/6.1.63 }}
*{{cite journal | author=Tian G, Lewis SA, Feierbach B, ''et al.'' |title=Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors. |journal=J. Cell Biol. |volume=138 |issue= 4 |pages= 821-32 |year= 1997 |pmid= 9265649 |doi= }}
* {{cite journal | vauthors = Martín L, Fanarraga ML, Aloria K, Zabala JC | title = Tubulin folding cofactor D is a microtubule destabilizing protein | journal = FEBS Lett. | volume = 470 | issue = 1 | pages = 93–5 | year = 2000 | pmid = 10722852 | doi = 10.1016/S0014-5793(00)01293-X }}
*{{cite journal | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=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. |journal=DNA Res. |volume=6 |issue= 1 |pages= 63-70 |year= 1999 |pmid= 10231032 |doi= }}
* {{cite journal | vauthors = Bhamidipati A, Lewis SA, Cowan NJ | title = ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin | journal = J. Cell Biol. | volume = 149 | issue = 5 | pages = 1087–96 | year = 2000 | pmid = 10831612 | pmc = 2174823 | doi = 10.1083/jcb.149.5.1087 }}
*{{cite journal | author=Martín L, Fanarraga ML, Aloria K, Zabala JC |title=Tubulin folding cofactor D is a microtubule destabilizing protein. |journal=FEBS Lett. |volume=470 |issue= 1 |pages= 93-5 |year= 2000 |pmid= 10722852 |doi= }}
* {{cite journal | vauthors = Schubert A, Cattaruzza M, Hecker M, Darmer D, Holtz J, Morawietz H | title = Shear stress-dependent regulation of the human beta-tubulin folding cofactor D gene | journal = Circ. Res. | volume = 87 | issue = 12 | pages = 1188–94 | year = 2001 | pmid = 11110777 | doi = 10.1161/01.res.87.12.1188 }}
*{{cite journal | author=Bhamidipati A, Lewis SA, Cowan NJ |title=ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin. |journal=J. Cell Biol. |volume=149 |issue= 5 |pages= 1087-96 |year= 2000 |pmid= 10831612 |doi= }}
* {{cite journal | vauthors = Wistow G, Bernstein SL, Wyatt MK, Fariss RN, Behal A, Touchman JW, Bouffard G, Smith D, Peterson K | title = Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants | journal = Mol. Vis. | volume = 8 | issue =  | pages = 205–20 | year = 2002 | pmid = 12107410 | doi =  }}
*{{cite journal | author=Schubert A, Cattaruzza M, Hecker M, ''et al.'' |title=Shear stress-dependent regulation of the human beta-tubulin folding cofactor D gene. |journal=Circ. Res. |volume=87 |issue= 12 |pages= 1188-94 |year= 2001 |pmid= 11110777 |doi= }}
* {{cite journal | vauthors = Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA | title = Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A | journal = J. Biol. Chem. | volume = 278 | issue = 42 | pages = 40829–36 | year = 2003 | pmid = 12912990 | doi = 10.1074/jbc.M308678200 }}
*{{cite journal | author=Wistow G, Bernstein SL, Wyatt MK, ''et al.'' |title=Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants. |journal=Mol. Vis. |volume=8 |issue=  |pages= 205-20 |year= 2002 |pmid= 12107410 |doi=  }}
* {{cite journal | vauthors = Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM | title = Functional proteomics mapping of a human signaling pathway | journal = Genome Res. | volume = 14 | issue = 7 | pages = 1324–32 | year = 2004 | pmid = 15231748 | pmc = 442148 | doi = 10.1101/gr.2334104 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = 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 | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | year = 2005 | pmid = 16189514 | doi = 10.1038/nature04209 }}
*{{cite journal  | author=Shern JF, Sharer JD, Pallas DC, ''et al.'' |title=Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A. |journal=J. Biol. Chem. |volume=278 |issue= 42 |pages= 40829-36 |year= 2003 |pmid= 12912990 |doi= 10.1074/jbc.M308678200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Colland F, Jacq X, Trouplin V, ''et al.'' |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324-32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 11:38, 15 September 2017

For the Telephony Binary-Coded Decimal digital encoding method, see Binary-coded decimal.
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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Tubulin-specific chaperone D is a protein that in humans is encoded by the TBCD gene.[1]

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.[1]

Interactions

TBCD has been shown to interact with ARL2.[2][3]

References

  1. ↑ 1.0 1.1 "Entrez Gene: TBCD tubulin folding cofactor D".
  2. ↑ 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.
  3. ↑ 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


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