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0TBB2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTUBB2
DescriptionTubulin beta-2 chain.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0042288 MHC class I protein binding (IEP)
0042267 natural killer cell mediated cytotoxicity (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
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
In bacteria.tsZ is an essential cell division protein which appears to be involved in the initiation of this event. It assembles into a cytokinetic ring on the inner surface of the cytoplasmicmembrane at the place where division will occur. The ring serves as a scaffoldthat is disassembled when septation is completed. FtsZ ring formation is initiated at a singlesite on one side of the bacterium and appears to grow bidirectionally. In Escherichia coli.inCD .ncoded by the MinB locus.orm a complex which appears to block the formation of FtsZ rings at the cell poles.t the ancient mid cell divisionsites.hilst MinE.ncoded at the same locus.pecifically prevents the action of MinCD at mid cell. FtsZ is a GTP bindingprotein with a GTPase activity.It undergoes GTP-dependent polymerization intofilaments (or tubules) that seem to form a cytoskeleton involved in septumsynthesis. The structure and the properties ofFtsZ clearly provide it with the capacity for the cytoskeletal.erhaps motor role.ecessary for "contraction" along the division plane. In addition.owever.he FtsZring structure provides the framework for the recruitment or assembly of the ten or so membrane and cytoplasmic proteins.niquely required for cell division inE. coli or Bacillus subtilis.ome of which are required for biogenesis of the new hemispherical poles of the two daughter cells. FtsZ can polymerize into various structures.or example a single linear polymer of FtsZ monomers.alled aprotofilament. Protofilaments can associate laterally to form pairs (sometimes called thick filaments.undles (ill-defined linear associations of multipleprotofilaments or thick filaments.heets (parallel or anti-parallel two-dimensional associations of thick filaments and tubes(anti-parallel associations of thick filaments in a circular fashion to form a tubular structure). In addition.mallcircles of FtsZ monomers (a short protofilament bent around to join itself.pparently head to tail) have been observed and termed mini-rings. FtsZ is a protein of about 400 residues which is well conserved acrossbacterial species and which is also present in the chloroplast of plants as well as in archaebacteria . FtsZ shows structural similarity witheukaryotic tubulins. This similarity is probably both evolutionary andfunctionally significant.
  IPR000158:Cell division protein FtsZ
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:-111.031517028809 
Location:45-244IPR008280:Tubulin_C 
Evalue:-81.0555191040039 
Location:246-383IPR000217:TUBULIN 
Evalue:0 
Location:10-30IPR002453:BETATUBULIN 
Evalue:0 
Location:412-430IPR013838:TUBULIN_B_AUTOREG 
Evalue:0 
Location:1-4
SequencesProtein: TBB2_HUMAN (444 aa)
mRNA: NM_178014
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: 62 residues, 1935034-1935218Exon2: 38 residues, 1937191-1937300Exon3: 39 residues, 1937572-1937683Exon4: 694 residues, 1937994-1940072Exon5: 2 residues, -Jump to TBB2_HUMANLoci index, Chromosomal location, Length, Possible relational loci clusterExon1: 62 residues, 30796135-30796319Exon2: 38 residues, 30798292-30798401Exon3: 39 residues, 30798673-30798784Exon4: 694 residues, 30799095-30801172Exon5: 2 residues, -Jump to TBB2_HUMANLoci index, Chromosomal location, Length, Possible relational loci clusterExon1: 62 residues, 2136731-2136915Exon2: 38 residues, 2138888-2138997Exon3: 39 residues, 2139269-2139380Exon4: 694 residues, 2139691-2141768Exon5: 2 residues, -Jump to TBB2_HUMAN  
Loci Cluster (Details)Loci: 3576 882132-897414 ~-15K 32584(MOG)(+)Loci: 4860 1368158-1375605 ~-7K 32610(TRIM10)(-)Loci: 3577 1541880-1558353 ~-16K 32616(+)Loci: 4861 1914463-1929833 ~-15K 32644(MDC1)(-)Loci: 3578 1935034-1940072 ~-5K 32647(TUBB2)(+)Loci: 3579 2099260-2114867 ~-16K 32653(DDR1)(+)Loci: 4862 2381927-2388269 ~-6K 32673(POU5F1)(-)Loci: 3580 2744366-2745636 ~-1K 32685(MCCD1)(+)Loci: 3581 2790934-2793697 ~-3K 32694(TNF)(+)Loci: 3582 2836184-2853121 ~-17K 32708(BAT2)(+)Loci: 4863 2902325-2918686 ~-16K 32722(BAT5)(-)Loci: 4864 2945936-2951926 ~-6K 32734(CLIC1)(-)Loci: 4865 3074690-3078421 ~-4K 32743(NEU1)(-)Loci: 4866 3167604-3174600 ~-7K 32757(RDBP)(-)Loci: 4867 3377585-3406812 ~-29K 32798(NOTCH4)(-)Loci: 4859 827283-858139 ~-31K 32580(GABBR1)(-)Link out to UCSC  
Loci: 3524 30403018-30419484 ~-16K 30623(+)Loci: 4778 30775563-30790934 ~-15K 30651(MDC1)(-)Loci: 3525 30796135-30801172 ~-5K 30654(TUBB2)(+)Loci: 3526 30960305-30975910 ~-16K 30660(DDR1)(+)Loci: 4779 31240107-31246432 ~-6K 30683(POU5F1)(-)Loci: 3527 31651328-31654089 ~-3K 30704(TNF)(+)Loci: 3528 31696575-31713516 ~-17K 30718(BAT2)(+)Loci: 4780 31762714-31779067 ~-16K 30732(BAT5)(-)Loci: 4781 31806338-31812320 ~-6K 30744(CLIC1)(-)Loci: 4782 31934931-31938662 ~-4K 30760(NEU1)(-)Loci: 4783 32027843-32034843 ~-7K 30774(RDBP)(-)Loci: 4784 32116910-32185131 ~-68K 30791(TNXB)(-)Loci: 4785 32191022-32204008 ~-13K 30793(CREBL1)(-)Loci: 4786 32270598-32299822 ~-29K 30822(NOTCH4)(-)Loci: 4777 30229242-30236690 ~-7K 30617(TRIM10)(-)Link out to UCSC  
Loci: 3568 1080116-1095456 ~-15K 32266(MOG)(+)Loci: 4846 1569907-1577353 ~-7K 32295(TRIM10)(-)Loci: 3569 1743552-1760022 ~-16K 32299(+)Loci: 4847 2116160-2131531 ~-15K 32327(MDC1)(-)Loci: 3570 2136731-2141768 ~-5K 32330(TUBB2)(+)Loci: 3571 2300931-2316538 ~-16K 32336(DDR1)(+)Loci: 4848 2583391-2589717 ~-6K 32358(POU5F1)(-)Loci: 3572 2942907-2944177 ~-1K 32370(MCCD1)(+)Loci: 3573 2989472-2992233 ~-3K 32379(TNF)(+)Loci: 3574 3034720-3051660 ~-17K 32394(BAT2)(+)Loci: 4849 3100861-3117213 ~-16K 32408(BAT5)(-)Loci: 4850 3144482-3150469 ~-6K 32420(CLIC1)(-)Loci: 4851 3273206-3276937 ~-4K 32436(NEU1)(-)Loci: 4852 3366127-3373127 ~-7K 32450(RDBP)(-)Loci: 4853 3416089-3484322 ~-68K 32465(TNXB)(-)Loci: 4854 3490215-3503197 ~-13K 32467(CREBL1)(-)Loci: 4855 3569805-3599027 ~-29K 32497(NOTCH4)(-)Loci: 4845 1025321-1056177 ~-31K 32256(GABBR1)(-)Link out to UCSC