Human Gene TUBB6 (ENST00000317702.10_4) from GENCODE V47lift37
  Description: tubulin beta 6 class V, transcript variant 1 (from RefSeq NM_032525.3)
Gencode Transcript: ENST00000317702.10_4
Gencode Gene: ENSG00000176014.13_9
Transcript (Including UTRs)
   Position: hg19 chr18:12,308,240-12,326,615 Size: 18,376 Total Exon Count: 4 Strand: +
Coding Region
   Position: hg19 chr18:12,308,292-12,326,129 Size: 17,838 Coding Exon Count: 4 

Page IndexSequence and LinksUniProtKB CommentsPrimersMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2024-08-22 23:36:26

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr18:12,308,240-12,326,615)mRNA (may differ from genome)Protein (446 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
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UniProtKBBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: TBB6_HUMAN
DESCRIPTION: RecName: Full=Tubulin beta-6 chain;
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 (By similarity).
SUBUNIT: Dimer of alpha and beta chains (By similarity).
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
TISSUE SPECIFICITY: Ubiquitous. Maximal expression in breast and lung, where it represents around 10% of all beta-tubulins. Largely decreased expression in most cancerous tissues.
DOMAIN: The highly acidic C-terminal region may bind cations such as calcium.
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
PTM: Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules (Probable).
SIMILARITY: Belongs to the tubulin family.

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  MalaCards Disease Associations
  MalaCards Gene Search: TUBB6
Diseases sorted by gene-association score: anonychia congenita (3)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 101.25 RPKM in Esophagus - Muscularis
Total median expression: 1499.02 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -9.8052-0.188 Picture PostScript Text
3' UTR -109.50486-0.225 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR013838 - Beta-tubulin_BS
IPR002453 - Beta_tubulin
IPR008280 - Tub_FtsZ_C
IPR000217 - Tubulin
IPR018316 - Tubulin/FtsZ_2-layer-sand-dom
IPR023123 - Tubulin_C
IPR017975 - Tubulin_CS
IPR003008 - Tubulin_FtsZ_GTPase

Pfam Domains:
PF00091 - Tubulin/FtsZ family, GTPase domain
PF03953 - Tubulin C-terminal domain

SCOP Domains:
52490 - Tubulin nucleotide-binding domain-like
55307 - Tubulin C-terminal domain-like

ModBase Predicted Comparative 3D Structure on Q9BUF5
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologNo orthologNo orthologNo orthologNo ortholog
Gene DetailsGene Details    
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-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0000166 nucleotide binding
GO:0003674 molecular_function
GO:0003924 GTPase activity
GO:0005200 structural constituent of cytoskeleton
GO:0005525 GTP binding

Biological Process:
GO:0007010 cytoskeleton organization
GO:0007017 microtubule-based process

Cellular Component:
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
GO:0005874 microtubule
GO:0070062 extracellular exosome


-  Descriptions from all associated GenBank mRNAs
  AK311364 - Homo sapiens cDNA, FLJ18406.
AK092677 - Homo sapiens cDNA FLJ35358 fis, clone PUAEN2000497, highly similar to Tubulin beta-6 chain.
AK001295 - Homo sapiens cDNA FLJ10433 fis, clone NT2RP1000478, highly similar to Tubulin beta-6 chain.
AK304616 - Homo sapiens cDNA FLJ52847 complete cds, highly similar to Tubulin beta-6 chain.
AK022340 - Homo sapiens cDNA FLJ12278 fis, clone MAMMA1001735, highly similar to TUBULIN BETA-5 CHAIN.
AK098440 - Homo sapiens cDNA FLJ25574 fis, clone JTH07516, highly similar to TUBULIN BETA-5 CHAIN.
BC002654 - Homo sapiens tubulin, beta 6, mRNA (cDNA clone MGC:4083 IMAGE:3605559), complete cds.
AK298196 - Homo sapiens cDNA FLJ52712 complete cds, highly similar to Tubulin beta-6 chain.
BC039717 - Homo sapiens mRNA similar to tubulin beta-5 (cDNA clone IMAGE:5745167).
AB590145 - Synthetic construct DNA, clone: pFN21AE1530, Homo sapiens TUBB6 gene for tubulin, beta 6, without stop codon, in Flexi system.
DQ896394 - Synthetic construct Homo sapiens clone IMAGE:100010854; FLH193926.01L; RZPDo839D0769D tubulin, beta 6 (TUBB6) gene, encodes complete protein.
DQ893486 - Synthetic construct clone IMAGE:100006116; FLH193930.01X; RZPDo839D0779D tubulin, beta 6 (TUBB6) gene, encodes complete protein.
KJ895010 - Synthetic construct Homo sapiens clone ccsbBroadEn_04404 TUBB6 gene, encodes complete protein.
JD474669 - Sequence 455693 from Patent EP1572962.
JD150169 - Sequence 131193 from Patent EP1572962.
JD552405 - Sequence 533429 from Patent EP1572962.
JD204264 - Sequence 185288 from Patent EP1572962.
JD361339 - Sequence 342363 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein Q9BUF5 (Reactome details) participates in the following event(s):

R-HSA-389980 unfolded actin/tubulin associates with prefoldin
R-HSA-389970 Actin/tubulin:prefoldin complex associates with CCT/TriC
R-HSA-389954 Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC
R-HSA-389961 ADP is exchanged for ATP in the (ADP:CCT/TriC):tubulin complex
R-HSA-389956 Beta-tubulin:GTP + Cofactor A -> Beta-tubulin:GTP: Cofactor A
R-HSA-389969 Beta-tubulin:GTP + Cofactor D -> Beta-tubulin:GTP: Cofactor D
R-HSA-389974 Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E:Cofactor C-> Beta-tubulin:GDP :alpha-tubulin:GTP heterodimer +Cofactor E+ Cofactor D+ Cofactor C+ Pi
R-HSA-8955706 TTL ligates L-Tyr to the carboxy terminus of alpha-tubulin
R-HSA-8955712 TTCP hydrolyzes the terminal L-Tyr residue from alpha-tubulin
R-HSA-389955 Beta-tubulin:GTP: Cofactor A+ Cofactor D -> Beta-tubulin:GTP:Cofactor D + Cofactor A
R-HSA-389976 Beta-tubulin:GTP:Cofactor D+alpha-tubulin:GTP:Cofactor E-> Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E
R-HSA-389964 Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E+ Cofactor C-> Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E:Cofactor C
R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-389958 Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding
R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977 Post-chaperonin tubulin folding pathway
R-HSA-8955332 Carboxyterminal post-translational modifications of tubulin
R-HSA-390466 Chaperonin-mediated protein folding
R-HSA-391251 Protein folding
R-HSA-597592 Post-translational protein modification
R-HSA-392499 Metabolism of proteins

-  Other Names for This Gene
  Alternate Gene Symbols: B3KM76, ENST00000317702.1, ENST00000317702.2, ENST00000317702.3, ENST00000317702.4, ENST00000317702.5, ENST00000317702.6, ENST00000317702.7, ENST00000317702.8, ENST00000317702.9, NM_032525, Q9BUF5, Q9HA42, TBB6_HUMAN, uc317qhq.1, uc317qhq.2
UCSC ID: ENST00000317702.10_4
RefSeq Accession: NM_032525.3
Protein: Q9BUF5 (aka TBB6_HUMAN)

-  Gene Model Information
  Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.