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0TBA8_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTUBA8
DescriptionTubulin alpha-8 chain (alpha-tubulin 8).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
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 . Several alpha-tubulin isotypes have been described.ach distinguished by the presence of unique amino acid substitutions within the coding region. Most of these isotype-specific amino acids are clustered at the C-terminus.Patterns of developmental expression of the various alpha-tubulin isotypeshave been studied. Results suggest that individual tubulin isotypes confer functional specificity on different kinds of microtubules .
  IPR002452:Alpha tubulin
IPR003008:Tubulin 
Evalue:-101.522880554199 
Location:47-246IPR008280:Tubulin_C 
Evalue:-77.3467864990234 
Location:248-393IPR000217:TUBULIN 
Evalue:0 
Location:10-30IPR002452:ALPHATUBULIN 
Evalue:0 
Location:422-438
SequencesProtein: TBA8_HUMAN (449 aa)
mRNA: NM_018943
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 assignmentK07374
  Level 3 annotation:
    tubulin, alpha
  Level 2 annotation:
    Gap junction
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 26 residues, 16973558-16973634Exon2: 76 residues, 16984245-16984468Exon3: 51 residues, 16986922-16987071Exon4: 229 residues, 16989120-16989801Exon5: 298 residues, 16993609-16994498Exon6: 2 residues, -Jump to TBA8_HUMAN  
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Loci Cluster (Details)Loci: 4555 16596905-16637258 ~-40K 24143(BID)(-)Loci: 3295 16973558-16994498 ~-21K 24153(TUBA8)(+)Loci: 4556 17280294-17304066 ~-24K 24158(PRODH)(-)Loci: 4557 17543094-17546285 ~-3K 24164(SLC25A1)(-)Loci: 4558 17698223-17799219 ~-101K 24167(HIRA)(-)Loci: 3296 18081986-18090842 ~-9K 24176(SEPT5)(+)Loci: 4559 18243045-18309515 ~-66K 24188(TXNRD2)(-)Loci: 3297 18309308-18336528 ~-27K 24191(COMT)(+)Loci: 3294 16423182-16453647 ~-30K 24138(SLC25A18)(+)Link out to UCSC