View source for Tubulin beta chain (Homo sapiens)

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{{#invoke:InfoboxforTarget|run|TUBB|[https://www.uniprot.org/uniprot/P07437 P07437]|Homo sapiens|Cys12, Cys211, Cys239|[http://pfam.xfam.org/family/PF00091 Tubulin family]|[[:Category:Tubulin beta chain (Homo sapiens)|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) <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)
<br/>

===Cys Function & Property===
From the homologous structures, these residues are all very close to the interface.<br/>

* Hydrophobic property:
:[[File:506-hydro.png||600px]]
* SASA：
:Unknown<br/>

==Protein Sequence==
<font face="Courier">
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY <br/>
YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN <br/>
WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL <br/>
LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY <br/>
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTT<span style="background:#ffff00">'''C'''</span>L RFPGQLNADL <br/>
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM <br/>
AA<span style="background:#ffff00">'''C'''</span>DPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK <br/>
TAV<span style="background:#ffff00">'''C'''</span>DIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG <br/>
EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA      <br/> 
</font>

==Structural Information==
*Known structure with covalent ligand: <br/>
:Unknown<br/>  

*Protein structure:
:Unknown<br/>

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

==Experimental Evidence==
:SDS-PAGE, Cys-directed Mutation

==Reference==
# Li Y M, Broome J D. '''Arsenic targets tubulins to induce apoptosis in myeloid leukemia cells[J].''' Cancer Research, 1999, 59(4): 776-780. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10029061 10029061]<br/> 
# Banerjee R, Pace N J, Brown D R, et al. '''1, 3, 5-Triazine as a modular scaffold for covalent inhibitors with streamlined target identification[J].''' Journal of the American Chemical Society, 2013, 135(7): 2497-2500. [https://www.ncbi.nlm.nih.gov/pubmed/?term=23379904 23379904]<br/>

[[Category:Targets]]
[[Category:Homo sapiens]]
[[Category:Structural protein]]
[[Category:Tubulin family]]
[[Category:Phagosome]]
[[Category:Gap junction]]
[[Category:Pathogenic Escherichia coli infection]]