Tubulin beta chain (Sus scrofa) - Revision history

Wu3857: /* Reference */

2019-08-19T23:18:59Z

‎Reference

Wu3857: /* Protein Function */

2019-07-30T21:25:36Z

‎Protein Function

Wu3857: /* Cys Function & Property */

2019-07-30T21:19:53Z

‎Cys Function & Property

Wu3857: /* Cys Function & Property */

2019-07-30T21:19:41Z

‎Cys Function & Property

Wu3857: /* Cys Function & Property */

2019-07-30T21:19:22Z

‎Cys Function & Property

Wu3857: /* Cys Function & Property */

2019-07-30T21:17:15Z

‎Cys Function & Property

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|TUBB, Beta-tubulin|[https://www.uniprot.org/uniprot/P02554 P02554]|Sus scrofa|Cys239, Cys354|[http://pfam.xfam...."

2019-07-30T21:03:47Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|TUBB, Beta-tubulin|[https://www.uniprot.org/uniprot/P02554 P02554]|Sus scrofa|Cys239, Cys354|[http://pfam.xfam...."

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{| align="left"
| __TOC__
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{{#invoke:InfoboxforTarget|run|TUBB, Beta-tubulin|[https://www.uniprot.org/uniprot/P02554 P02554]|Sus scrofa|Cys239, Cys354|[http://pfam.xfam.org/family/PF00091 Tubulin family]|[[:Category:Tubulin beta chain (Sus scrofa)|Ligand list]]|Structural protein}}
==Summary==

===Protein Function ===
Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. (From Uniprot) 
Tubulin (tubul- + -in) in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. The tubulin superfamily contains six families of tubulins (alpha-, beta-, gamma-, delta-, epsilon and zeta-tubulins). Tubulin is also used to specifically refer to α-tubulin and β-tubulin, the proteins that make up microtubules in eukaryotic cells. Each has a molecular weight of approximately 50,000 Daltons. Tubulin was long thought to be specific to eukaryotes. Recently, however, the prokaryotic cell division protein FtsZ was shown to be related to tubulin. 
The Tubulin/FtsZ family, GTPase domain is an evolutionary conserved protein domain. This GTPase protein domain is found in all tubulin chains, as well as the bacterial FtsZ family of proteins. These proteins are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division that forms part of a ring in the middle of the dividing cell that is required for constriction of the cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerise into tubes, sheets, and rings in vitro, and is ubiquitous in bacteria and archaea. 
Microtubules are assembled from dimers of α- and β-tubulin. These subunits are slightly acidic with an isoelectric point between 5.2 and 5.8. To form microtubules, the dimers of α- and β-tubulin bind to GTP and assemble onto the (+) ends of microtubules while in the GTP-bound state. The β-tubulin subunit is exposed on the plus end of the microtubule while the α-tubulin subunit is exposed on the minus end. After the dimer is incorporated into the microtubule, the molecule of GTP bound to the β-tubulin subunit eventually hydrolyzes into GDP through inter-dimer contacts along the microtubule protofilament. Whether the β-tubulin member of the tubulin dimer is bound to GTP or GDP influences the stability of the dimer in the microtubule. Dimers bound to GTP tend to assemble into microtubules, while dimers bound to GDP tend to fall apart; thus, this GTP cycle is essential for the dynamic instability of the microtubule. (From Wiki)
 

===Cys Function & Property===
Cys354 and Cys239 is close to the interface. alpha,beta-Unsaturated carbonyl compounds such as 6-shogaol could react with sulfhydryl groups of cysteine residues in tubulin, and impair tubulin polymerization. (PMID: 18805415) 

* Hydrophobic property:
:[[File:503-hydro.png||600px]]
* SASA：
:Cys239: 0.497 A^2
:Cys354: 0.73 A^2

==Protein Sequence==

MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY 
YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 
WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL 
LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY 
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTT'''C'''L RFPGQLNADL 
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM 
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK 
TAV'''C'''DIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 
EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEG EEDEA 


==Structural Information==
*Known structure with covalent ligand: 
:Unknown 

*Protein structure:
[[File:503-2.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko04145 Phagosome] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04540 Gap junction] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05130 Pathogenic Escherichia coli infection] 

==Experimental Evidence==
:DTNB Method, Immunocytochemical Staining

==Reference==
# Ishiguro K, Ando T, Watanabe O, et al. '''Specific reaction of α, β-unsaturated carbonyl compounds such as 6-shogaol with sulfhydryl groups in tubulin leading to microtubule damage[J].''' FEBS letters, 2008, 582(23-24): 3531-3536. [https://www.ncbi.nlm.nih.gov/pubmed/?term=18805415 18805415] 

[[Category:Targets|Targets]]
[[Category:Sus scrofa|Sus scrofa]]
[[Category:Structural protein|Structural protein]]
[[Category:Tubulin family|Tubulin family]]
[[Category:Phagosome|Phagosome]]
[[Category:Gap junction|Gap junction]]
[[Category:Pathogenic Escherichia coli infection|Pathogenic Escherichia coli infection]]

@@ Line 53: / Line 53: @@
 # Ishiguro K, Ando T, Watanabe O, et al. '''Specific reaction of α, β-unsaturated carbonyl compounds such as 6-shogaol with sulfhydryl groups in tubulin leading to microtubule damage[J].''' FEBS letters, 2008, 582(23-24): 3531-3536. [https://www.ncbi.nlm.nih.gov/pubmed/?term=18805415 18805415]<br/>
-[[Category:Targets|Targets]]
+[[Category:Targets]]
-[[Category:Sus scrofa|Sus scrofa]]
+[[Category:Sus scrofa]]
-[[Category:Structural protein|Structural protein]]
+[[Category:Structural protein]]
-[[Category:Tubulin family|Tubulin family]]
+[[Category:Tubulin family]]
-[[Category:Phagosome|Phagosome]]
+[[Category:Phagosome]]
-[[Category:Gap junction|Gap junction]]
+[[Category:Gap junction]]
-[[Category:Pathogenic Escherichia coli infection|Pathogenic Escherichia coli infection]]
+[[Category:Pathogenic Escherichia coli infection]]

@@ Line 7: / Line 7: @@
 ===Protein Function ===
 Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. (From Uniprot)<br/>
-Tubulin (tubul- + -in) in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. The tubulin superfamily contains six families of tubulins (alpha-, beta-, gamma-, delta-, epsilon and zeta-tubulins). Tubulin is also used to specifically refer to α-tubulin and β-tubulin, the proteins that make up microtubules in eukaryotic cells. Each has a molecular weight of approximately 50,000 Daltons. Tubulin was long thought to be specific to eukaryotes. Recently, however, the prokaryotic cell division protein FtsZ was shown to be related to tubulin. <br/>
+Tubulin in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. The tubulin superfamily contains six families of tubulins (alpha-, beta-, gamma-, delta-, epsilon and zeta-tubulins). Tubulin is also used to specifically refer to α-tubulin and β-tubulin, the proteins that make up microtubules in eukaryotic cells. Each has a molecular weight of approximately 50,000 Daltons. Tubulin was long thought to be specific to eukaryotes. Recently, however, the prokaryotic cell division protein FtsZ was shown to be related to tubulin. <br/>
 The Tubulin/FtsZ family, GTPase domain is an evolutionary conserved protein domain. This GTPase protein domain is found in all tubulin chains, as well as the bacterial FtsZ family of proteins. These proteins are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division that forms part of a ring in the middle of the dividing cell that is required for constriction of the cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerise into tubes, sheets, and rings in vitro, and is ubiquitous in bacteria and archaea. <br/>
 Microtubules are assembled from dimers of α- and β-tubulin. These subunits are slightly acidic with an isoelectric point between 5.2 and 5.8. To form microtubules, the dimers of α- and β-tubulin bind to GTP and assemble onto the (+) ends of microtubules while in the GTP-bound state. The β-tubulin subunit is exposed on the plus end of the microtubule while the α-tubulin subunit is exposed on the minus end. After the dimer is incorporated into the microtubule, the molecule of GTP bound to the β-tubulin subunit eventually hydrolyzes into GDP through inter-dimer contacts along the microtubule protofilament. Whether the β-tubulin member of the tubulin dimer is bound to GTP or GDP influences the stability of the dimer in the microtubule. Dimers bound to GTP tend to assemble into microtubules, while dimers bound to GDP tend to fall apart; thus, this GTP cycle is essential for the dynamic instability of the microtubule. (From Wiki)

@@ Line 13: / Line 13: @@
 ===Cys Function & Property===
-Cys354 and Cys239 are close to the interface. Alpha,Beta-unsaturated carbonyl compounds such as 6-shogaol could react with sulfhydryl groups of cysteine residues in tubulin, and impair tubulin polymerization. (PMID: 18805415)<br/>
+Cys354 and Cys239 are close to the interface.<br/>
 * Hydrophobic property:

@@ Line 13: / Line 13: @@
 ===Cys Function & Property===
-Cys354 and Cys239 are close to the interface. Alpha,beta-Unsaturated carbonyl compounds such as 6-shogaol could react with sulfhydryl groups of cysteine residues in tubulin, and impair tubulin polymerization. (PMID: 18805415)<br/>
+Cys354 and Cys239 are close to the interface. Alpha,Beta-unsaturated carbonyl compounds such as 6-shogaol could react with sulfhydryl groups of cysteine residues in tubulin, and impair tubulin polymerization. (PMID: 18805415)<br/>
 * Hydrophobic property:

@@ Line 13: / Line 13: @@
 ===Cys Function & Property===
-Cys354 and Cys239 are close to the interface. alpha,beta-Unsaturated carbonyl compounds such as 6-shogaol could react with sulfhydryl groups of cysteine residues in tubulin, and impair tubulin polymerization. (PMID: 18805415)<br/>
+Cys354 and Cys239 are close to the interface. Alpha,beta-Unsaturated carbonyl compounds such as 6-shogaol could react with sulfhydryl groups of cysteine residues in tubulin, and impair tubulin polymerization. (PMID: 18805415)<br/>
 * Hydrophobic property:

Tubulin beta chain (Sus scrofa) - Revision history

Wu3857: /* Reference */

Wu3857: /* Protein Function */

Wu3857: /* Cys Function & Property */

Wu3857: /* Cys Function & Property */

Wu3857: /* Cys Function & Property */

Wu3857: /* Cys Function & Property */

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|TUBB, Beta-tubulin|[https://www.uniprot.org/uniprot/P02554 P02554]|Sus scrofa|Cys239, Cys354|[http://pfam.xfam...."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|TUBB, Beta-tubulin|[https://www.uniprot.org/uniprot/P02554 P02554]|Sus scrofa|Cys239, Cys354|[http://pfam.xfam...."