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0TBB4_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTUBB4
DescriptionTubulin beta-4 chain (tubulin 5 beta).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0051082 unfolded protein binding (ISS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This domain is found in all tubulin chains.swell as the bacterial FtsZ family of proteins. These proteinsare involved in polymer formation. Tubulin is the major componentof microtubules.hile FtsZ is the polymer-forming proteinof bacterial cell division.t is part of a ring in the middle of thedividing cell that is required for constriction of cell membrane andcell envelope to yield two daughter cells. FtsZ and tubulin are GTPases.his entry is the GTPase domain.FtsZ can polymerise into tubes.heets.nd rings in vitro and isubiquitous in bacteria and archaea.
  IPR003008:Tubulin/FtsZ, GTPase
This domain is found in the tubulin alpha.eta and gamma chains.swell as the bacterial FtsZ family of proteins. These proteinsare GTPases and are involved in polymer formation. Tubulin is the major componentof microtubules.hile FtsZ is the polymer-forming proteinof bacterial cell division.t is part of a ring in the middle of thedividing cell that is required for constriction of cell membrane andcell envelope to yield two daughter cells. FtsZ can polymerise into tubes.heets.nd rings in vitro and isubiquitous in bacteria and archaea. This is the C-terminal domain.
  IPR008280:Tubulin/FtsZ, C-terminal
Microtubules are polymers of tubulin. dimer of two 55-kDa subunits.esignated alpha and beta . Within the microtubule lattice.lpha-beta heterodimers associate in a head-to-tail fashion.iving rise to microtubule polarity. Fluorescent labelling studies have suggested that tubulin is oriented in microtubules with beta-tubulin toward the plus end . For maximal rate and extent of polymerisation into microtubules.ubulin requires GTP. Two molecules of GTP are bound at different sites.ermed N and E. At the E (Exchangeable) site.TP is hydrolysed during incorporationinto the microtubule. Close to the E site is an invariant region rich in glycine residues.hich is found in both chains and is thought to controlaccess of the nucleotide to its binding site .Most species.xcepting simple eukaryotes.xpress a variety of closely-related alpha- and beta-isotypes. A third family member.amma tubulin.asalso been identified in a number of species. Gamma tubulin is found at microtubule-organising centres.uch as the spindle poles or the centrosome.uggesting that it is involved in minus-end nucleation of microtubule assembly .
  IPR000217:Tubulin
Microtubules are polymers of tubulin. dimer of two 55 kD subunits.esignated alpha and beta . Within the microtubule lattice.lpha-betaheterodimers associate in a head-to-tail fashion.iving rise to microtubule polarity. Fluorescent labelling studies have suggested that tubulin isoriented in microtubules with beta-tubulin toward the plus end . For maximal rate and extent of polymerisation into microtubules.ubulin requires GTP. Two molecules of GTP are bound at different sites.ermed N and E. At the E (Exchangeable) site.TP is hydrolysed during incorporationinto the microtubule. Close to the E site is an invariant region rich in glycine residues.hich is found in both chains and is thought to controlaccess of the nucleotide to its binding site . Most species.xcepting simple eukaryotes.xpress a variety of closely related alpha- and beta-isotypes. A third family member.amma tubulin.asalso been identified in a number of species .British type familial amyloidosis is an autosomal dominant disease characterised by progressive dementia.pastic paralysis and ataxia. Amyloid deposits from the brain tissue of an individual who died with this disease have been characterised. Trypsin digestion and subsequent N-terminalsequence analysis yielded a number of short sequences.ll of which aretryptic fragments of the C-termini of human alpha- and beta-tubulin. Consistent with the definition of amyloid.ynthetic peptides based on the sequences of these fragments formed fibrils in vitro.uggesting that theC-termini of both alpha- and beta-tubulin are closely associated with theamyloid deposits of this type of amyloidosis . The amino acid sequences encoded by beta tubulin genes have revealed a high level of overall similarity.ut significant divergence between theirC-termini . The pattern of expression of the beta-tubulin genes has been studied in several different human cell lines and has revealed varying levels of and differential expression in different cell lines. Itappears that distinct human beta-tubulin isotypes are encoded by geneswhose exon size and number has been conserved evolutionarily.ut whose pattern of expression may be regulated either co-ordinately or uniquely .
  IPR002453:Beta tubulin
IPR003008:Tubulin 
Evalue:-109.958610534668 
Location:45-244IPR008280:Tubulin_C 
Evalue:-81.0222778320313 
Location:246-383IPR000217:TUBULIN 
Evalue:0 
Location:10-30IPR002453:BETATUBULIN 
Evalue:0 
Location:412-430IPR013838:TUBULIN_B_AUTOREG 
Evalue:0 
Location:1-4
SequencesProtein: TBB4_HUMAN (444 aa)
mRNA: NM_006087
Local Annotation
Synapse Ontology
microtubules of the presynaptic compartment function as the tracks for the intense traffic of organelles from cell body to axon terminals and vice versa. It is generally excluded from the presynaptic vesicle cluster.Microtubules do not directly regulate synapse morphology or function
sdb:0087 microtubules  (Evidence:keywords)
KO assignmentK07375
  Level 3 annotation:
    tubulin, beta
  Level 2 annotation:
    Gap junction
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 635 residues, 6445329-6447232Exon2: 39 residues, 6452297-6452408Exon3: 38 residues, 6452525-6452634Exon4: 56 residues, 6453166-6453330Exon5: 2 residues, -Jump to TBB4_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4358 6377049-6384790 ~-8K 17799(-)Loci: 4359 6391074-6410781 ~-20K 17803(-)Loci: 4360 6445329-6453330 ~-8K 17809(TUBB4)(-)Loci: 3083 6312462-6319915 ~-7K 17793(CLPP)(+)Link out to UCSC