Human Gene TUBA1C (ENST00000301072.11_5) from GENCODE V47lift37
  Description: tubulin alpha 1c, transcript variant 5 (from RefSeq NM_032704.5)
Gencode Transcript: ENST00000301072.11_5
Gencode Gene: ENSG00000167553.17_9
Transcript (Including UTRs)
   Position: hg19 chr12:49,658,865-49,668,383 Size: 9,519 Total Exon Count: 4 Strand: +
Coding Region
   Position: hg19 chr12:49,658,965-49,667,010 Size: 8,046 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 (chr12:49,658,865-49,668,383)mRNA (may differ from genome)Protein (449 aa)
Gene SorterGenome BrowserOther Species FASTAGene interactionsTable SchemaAlphaFold
BioGPSEnsemblEntrez GeneExonPrimerGeneCardsHGNC
MalacardsMGIPubMedReactomeUniProtKBWikipedia
BioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: TBA1C_HUMAN
DESCRIPTION: RecName: Full=Tubulin alpha-1C chain; AltName: Full=Alpha-tubulin 6; AltName: Full=Tubulin alpha-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.
SUBUNIT: Dimer of alpha and beta chains.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively (By similarity).
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).
PTM: Acetylation of alpha-tubulins at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity).
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: TUBA1C
Diseases sorted by gene-association score: distal hereditary motor neuropathy, type ii (2)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  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: 146.76 RPKM in Esophagus - Mucosa
Total median expression: 1212.32 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 -19.30100-0.193 Picture PostScript Text
3' UTR -521.701373-0.380 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
IPR002452 - Alpha_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 Q9BQE3
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 orthologGenome BrowserNo ortholog
Gene DetailsGene Details  Gene Details 
Gene SorterGene Sorter  Gene Sorter 
 RGD  WormBase 
    Protein Sequence 
    Alignment 

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0000166 nucleotide binding
GO:0003924 GTPase activity
GO:0005198 structural molecule activity
GO:0005200 structural constituent of cytoskeleton
GO:0005515 protein binding
GO:0005525 GTP binding

Biological Process:
GO:0007010 cytoskeleton organization
GO:0007017 microtubule-based process
GO:0030705 cytoskeleton-dependent intracellular transport
GO:0051301 cell division

Cellular Component:
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
GO:0005874 microtubule
GO:0015630 microtubule cytoskeleton
GO:0031982 vesicle


-  Descriptions from all associated GenBank mRNAs
  AK293589 - Homo sapiens cDNA FLJ55956 complete cds, highly similar to Tubulin alpha-6 chain.
D28390 - Homo sapiens mRNA for tubulin alpha-1, 5'UTR region.
BC005946 - Homo sapiens tubulin, alpha 1c, mRNA (cDNA clone MGC:14580 IMAGE:4134187), complete cds.
AK223024 - Homo sapiens mRNA for tubulin alpha 6 variant, clone: JTH01540.
BC011790 - Homo sapiens tubulin, alpha 1c, mRNA (cDNA clone MGC:19827 IMAGE:4025017), complete cds.
BC063036 - Homo sapiens tubulin, alpha 1c, mRNA (cDNA clone MGC:64889 IMAGE:4397636), complete cds.
BC004949 - Homo sapiens tubulin, alpha 1c, mRNA (cDNA clone MGC:10851 IMAGE:3617714), complete cds.
BC033064 - Homo sapiens tubulin, alpha 1c, mRNA (cDNA clone MGC:45598 IMAGE:3926854), complete cds.
BC051297 - Homo sapiens tubulin, alpha 1c, mRNA (cDNA clone MGC:59688 IMAGE:3832363), complete cds.
BC019298 - Homo sapiens tubulin, alpha 1c, mRNA (cDNA clone MGC:4112 IMAGE:2905506), complete cds.
BC021088 - Homo sapiens tubulin, alpha 1c, mRNA (cDNA clone MGC:1754 IMAGE:3543481), complete cds.
CU678818 - Synthetic construct Homo sapiens gateway clone IMAGE:100019456 5' read TUBA1C mRNA.
CU676808 - Synthetic construct Homo sapiens gateway clone IMAGE:100017294 5' read TUBA1C mRNA.
CU675203 - Synthetic construct Homo sapiens gateway clone IMAGE:100017296 5' read TUBA1C mRNA.
DQ896235 - Synthetic construct Homo sapiens clone IMAGE:100010695; FLH191421.01L; RZPDo839D0167D tubulin, alpha 6 (TUBA6) gene, encodes complete protein.
DQ892986 - Synthetic construct clone IMAGE:100005616; FLH191425.01X; RZPDo839D0177D tubulin, alpha 6 (TUBA6) gene, encodes complete protein.
KJ899828 - Synthetic construct Homo sapiens clone ccsbBroadEn_09222 TUBA1C gene, encodes complete protein.
KJ906372 - Synthetic construct Homo sapiens clone ccsbBroadEn_16042 TUBA1C gene, encodes complete protein.
KJ906373 - Synthetic construct Homo sapiens clone ccsbBroadEn_16043 TUBA1C gene, encodes complete protein.
JD034886 - Sequence 15910 from Patent EP1572962.
DL492088 - Novel nucleic acids.
DL490632 - Novel nucleic acids.
JD035670 - Sequence 16694 from Patent EP1572962.
JD032220 - Sequence 13244 from Patent EP1572962.
DQ589802 - Homo sapiens piRNA piR-56914, complete sequence.
JD024485 - Sequence 5509 from Patent EP1572962.
JD027061 - Sequence 8085 from Patent EP1572962.
JD035518 - Sequence 16542 from Patent EP1572962.
JD029285 - Sequence 10309 from Patent EP1572962.
JD029721 - Sequence 10745 from Patent EP1572962.
JD033115 - Sequence 14139 from Patent EP1572962.
JD027868 - Sequence 8892 from Patent EP1572962.
JD060811 - Sequence 41835 from Patent EP1572962.
JD545462 - Sequence 526486 from Patent EP1572962.
JD220127 - Sequence 201151 from Patent EP1572962.
JD481273 - Sequence 462297 from Patent EP1572962.
JD430912 - Sequence 411936 from Patent EP1572962.
JD442902 - Sequence 423926 from Patent EP1572962.
JD558728 - Sequence 539752 from Patent EP1572962.
JD558727 - Sequence 539751 from Patent EP1572962.
JD442901 - Sequence 423925 from Patent EP1572962.
JD166446 - Sequence 147470 from Patent EP1572962.
JD563479 - Sequence 544503 from Patent EP1572962.
JD508277 - Sequence 489301 from Patent EP1572962.

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

Protein Q9BQE3 (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-389972 alpha-tubulin:GTP + Cofactor B -> alpha-tubulin:GTP: Cofactor B
R-HSA-389978 alpha-tubulin:GTP + Cofactor E -> alpha-tubulin:GTP:Cofactor E
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-8955712 TTCP hydrolyzes the terminal L-Tyr residue from alpha-tubulin
R-HSA-8955706 TTL ligates L-Tyr to the carboxy terminus of alpha-tubulin
R-HSA-389963 alpha-tubulin:GTP:Cofactor B +Cofactor E -> alpha-tubulin:GTP: Cofactor E +Cofactor B
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: ENST00000301072.1, ENST00000301072.10, ENST00000301072.2, ENST00000301072.3, ENST00000301072.4, ENST00000301072.5, ENST00000301072.6, ENST00000301072.7, ENST00000301072.8, ENST00000301072.9, NM_032704, Q9BQE3, TBA1C_HUMAN, TUBA6, uc317msr.1, uc317msr.2
UCSC ID: ENST00000301072.11_5
RefSeq Accession: NM_032704.5
Protein: Q9BQE3 (aka TBA1C_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.