Alpha-tubulin 3C

TUBA3C
Identifiers
Aliases	TUBA3C , TUBA2, bA408E5.3, Alpha-tubulin 3C, tubulin alpha 3c
External IDs	OMIM: 602528 HomoloGene: 134742 GeneCards: TUBA3C
Gene location (Human)
Chr.	Chromosome 13 (human)
End	19,181,824 bp
RNA expression pattern
	Top expressed in
	oocyte; ; sperm; ; triceps brachii muscle; ; pons; ; vena cava; ; secondary oocyte; ; cerebellar vermis; ; right ventricle; ; internal globus pallidus; ; subthalamic nucleus;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	nucleotide binding ; GTP binding ; structural constituent of cytoskeleton ; protein binding ; GTPase activity ;
Cellular component	cytoplasm ; microtubule ; cytoskeleton ; nucleus ; microtubule cytoskeleton ; cilium ; ciliary basal body ;
Biological process	microtubule-based process ; cytoskeleton organization ;
	Sources:Amigo / QuickGO
Orthologs
	7278
	n/a
	ENSG00000198033
	n/a
	Q1ZYQ1 ; P0DPH8
	n/a
	NM_079836 ; NM_006001
	n/a
	NP_525125 ; NP_005992
	n/a
	Wikidata
View/Edit Human

Last updated January 25, 2024

Tubulin alpha-3C/D chain is a protein that in humans is encoded by the TUBA3C gene.^[3]^[4]

Function

Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulin. The genes encoding these microtubule constituents are part of the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes and they are highly conserved among and between species. This gene is an alpha tubulin gene that encodes a protein 99% to the mouse testis-specific Tuba3 and Tuba7 gene products. This gene is located in the 13q11 region, which is associated with the genetic diseases Clouston hidrotic ectodermal dysplasia and Kabuki syndrome. Alternative splicing has been observed for this gene and two variants have been identified.^[4]

Interactions

Alpha-tubulin 3C has been shown to interact with FYN ^[5] and NMI.^[6]

Related Research Articles

Microtubules are polymers of tubulin that form part of the cytoskeleton and provide structure and shape to eukaryotic cells. Microtubules can be as long as 50 micrometres, as wide as 23 to 27 nm and have an inner diameter between 11 and 15 nm. They are formed by the polymerization of a dimer of two globular proteins, alpha and beta tubulin into protofilaments that can then associate laterally to form a hollow tube, the microtubule. The most common form of a microtubule consists of 13 protofilaments in the tubular arrangement.

The cytoskeleton is a complex, dynamic network of interlinking protein filaments present in the cytoplasm of all cells, including those of bacteria and archaea. In eukaryotes, it extends from the cell nucleus to the cell membrane and is composed of similar proteins in the various organisms. It is composed of three main components: microfilaments, intermediate filaments, and microtubules, and these are all capable of rapid growth or disassembly depending on the cell's requirements.

Tubulin in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. α- and β-tubulins polymerize into microtubules, a major component of the eukaryotic cytoskeleton. Microtubules function in many essential cellular processes, including mitosis. Tubulin-binding drugs kill cancerous cells by inhibiting microtubule dynamics, which are required for DNA segregation and therefore cell division.

Stathmin, also known as metablastin and oncoprotein 18 is a protein that in humans is encoded by the STMN1 gene.

In cell biology, microtubule nucleation is the event that initiates de novo formation of microtubules (MTs). These filaments of the cytoskeleton typically form through polymerization of α- and β-tubulin dimers, the basic building blocks of the microtubule, which initially interact to nucleate a seed from which the filament elongates.

Proto-oncogene tyrosine-protein kinase Fyn is an enzyme that in humans is encoded by the FYN gene.

Gamma-aminobutyric acid receptor-associated protein is a protein that in humans is encoded by the GABARAP gene.

Actin, cytoplasmic 2, or gamma-actin is a protein that in humans is encoded by the ACTG1 gene. Gamma-actin is widely expressed in cellular cytoskeletons of many tissues; in adult striated muscle cells, gamma-actin is localized to Z-discs and costamere structures, which are responsible for force transduction and transmission in muscle cells. Mutations in ACTG1 have been associated with nonsyndromic hearing loss and Baraitser-Winter syndrome, as well as susceptibility of adolescent patients to vincristine toxicity.

In enzymology, an alpha-tubulin N-acetyltransferase is an enzyme which is encoded by the ATAT1 gene.

Tubulin alpha-4A chain is a protein that in humans is encoded by the TUBA4A gene.

Tubulin alpha-1A chain is a protein that in humans is encoded by the TUBA1A gene.

Tubulin alpha-1B chain is a protein that in humans is encoded by the TUBA1B gene.

FYN binding protein (FYB-120/130), also known as FYB, ADAP, and SLAP-130 is a protein that is encoded by the FYB gene in humans. The protein is expressed in T cells, monocytes, mast cells, macrophages, NK cells, but not B cells. FYB is a multifunctional protein involved in post-activation T cell signaling, lymphocyte cytokine production, cell adhesion, and actin remodeling.

Tubulin beta-4A chain is a protein that in humans is encoded by the TUBB4A gene. Two tubulin beta-4 chain proteins are encoded in the human genome by the genes TUBB4A and TUBB4B. Tubulin is the major constituent of microtubules, a key components of the cytoskeleton. It binds two molecules of GTP, one at an exchangeable site on the beta-chain and one at a non-exchangeable site on the alpha-chain. TUBB4A is preferentially and highly expressed in the central nervous system.

Src kinase-associated phosphoprotein 2 is an enzyme that in humans is encoded by the SKAP2 gene.

Pericentrin (kendrin), also known as PCNT and pericentrin-B (PCNTB), is a protein which in humans is encoded by the PCNT gene on chromosome 21. This protein localizes to the centrosome and recruits proteins to the pericentriolar matrix (PCM) to ensure proper centrosome and mitotic spindle formation, and thus, uninterrupted cell cycle progression. This gene is implicated in many diseases and disorders, including congenital disorders such as microcephalic osteodysplastic primordial dwarfism type II (MOPDII) and Seckel syndrome.

Tubulin alpha-8 chain is a protein that in humans is encoded by the TUBA8 gene.

Src kinase-associated phosphoprotein 1 is an adapter protein that in humans is encoded by the SKAP1 gene.

Tubulin beta chain is a protein that in humans is encoded by the TUBB gene.

<span class="mw-page-title-main">TUBG1</span> Tubulin protein

Tubulin, gamma 1 is a protein in humans that is encoded by the TUBG1 gene. This gene encodes a member of the tubulin superfamily. The encoded protein localizes to the centrosome where it binds to microtubules as part of a complex referred to as the gamma-tubulin ring complex. The protein mediates microtubule nucleation and is required for microtubule formation and progression of the cell cycle.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000198033 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Dodé C, Weil D, Levilliers J, Crozet F, Chaïb H, Levi-Acobas F, Guilford P, Petit C (Jan 1998). "Sequence characterization of a newly identified human alpha-tubulin gene (TUBA2)". Genomics. 47 (1): 125–30. doi:10.1006/geno.1997.5081. PMID 9465305.
1 2 "Entrez Gene: TUBA3C tubulin, alpha 3c".
↑ Klein C, Kramer EM, Cardine AM, Schraven B, Brandt R, Trotter J (Feb 2002). "Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau". The Journal of Neuroscience. 22 (3): 698–707. doi:10.1523/JNEUROSCI.22-03-00698.2002. PMC 6758498 . PMID 11826099.
↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

External links

Human TUBA3C genome location and TUBA3C gene details page in the UCSC Genome Browser .

Desai A, Mitchison TJ (Jul 1998). "Tubulin and FtsZ structures: functional and therapeutic implications". BioEssays. 20 (7): 523–7. doi:10.1002/(SICI)1521-1878(199807)20:7<523::AID-BIES1>3.0.CO;2-L. PMID 9722999.
Oakley BR (Dec 2000). "An abundance of tubulins". Trends in Cell Biology. 10 (12): 537–42. doi:10.1016/S0962-8924(00)01857-2. PMID 11121746.
Dutcher SK (Feb 2001). "The tubulin fraternity: alpha to eta". Current Opinion in Cell Biology. 13 (1): 49–54. doi:10.1016/S0955-0674(00)00173-3. PMID 11163133.
Alexandrova N, Niklinski J, Bliskovsky V, Otterson GA, Blake M, Kaye FJ, Zajac-Kaye M (Sep 1995). "The N-terminal domain of c-Myc associates with alpha-tubulin and microtubules in vivo and in vitro". Molecular and Cellular Biology. 15 (9): 5188–95. doi:10.1128/MCB.15.9.5188. PMC 230766 . PMID 7651436.
Guilford P, Dodé C, Crozet F, Blanchard S, Chaïb H, Levilliers J, Levi-Acobas F, Weil D, Weissenbach J, Cohen D (Sep 1995). "A YAC contig and an EST map in the pericentromeric region of chromosome 13 surrounding the loci for neurosensory nonsyndromic deafness (DFNB1 and DFNA3) and limb-girdle muscular dystrophy type 2C (LGMD2C)". Genomics. 29 (1): 163–9. doi:10.1006/geno.1995.1227. PMID 8530067.
Marie-Cardine A, Kirchgessner H, Eckerskorn C, Meuer SC, Schraven B (Dec 1995). "Human T lymphocyte activation induces tyrosine phosphorylation of alpha-tubulin and its association with the SH2 domain of the p59fyn protein tyrosine kinase". European Journal of Immunology. 25 (12): 3290–7. doi:10.1002/eji.1830251214. PMID 8566014. S2CID 37614803.
Crépieux P, Kwon H, Leclerc N, Spencer W, Richard S, Lin R, Hiscott J (Dec 1997). "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Molecular and Cellular Biology. 17 (12): 7375–85. doi:10.1128/MCB.17.12.7375. PMC 232593 . PMID 9372968.
Kibar Z, Lafrenière RG, Chakravarti A, Wang JC, Chevrette M, Der Kaloustian VM, Rouleau GA (Feb 1999). "A radiation hybrid map of 48 loci including the clouston hidrotic ectodermal dysplasia locus in the pericentromeric region of chromosome 13q". Genomics. 56 (1): 127–30. doi:10.1006/geno.1998.5698. PMID 10036193.
Herreros L, Rodríguez-Fernandez JL, Brown MC, Alonso-Lebrero JL, Cabañas C, Sánchez-Madrid F, Longo N, Turner CE, Sánchez-Mateos P (Aug 2000). "Paxillin localizes to the lymphocyte microtubule organizing center and associates with the microtubule cytoskeleton". The Journal of Biological Chemistry. 275 (34): 26436–40. doi: 10.1074/jbc.M003970200 . hdl: 10261/135387 . PMID 10840040.
Watts NR, Sackett DL, Ward RD, Miller MW, Wingfield PT, Stahl SS, Steven AC (Jul 2000). "HIV-1 rev depolymerizes microtubules to form stable bilayered rings". The Journal of Cell Biology. 150 (2): 349–60. doi:10.1083/jcb.150.2.349. PMC 2180222 . PMID 10908577.
Takeoka A, Shimizu M, Horio T (Dec 2000). "Identification of an alpha-tubulin mutant of fission yeast from gamma-tubulin-interacting protein screening: genetic evidence for alpha-/gamma-tubulin interaction". Journal of Cell Science. 113 (24): 4557–62. doi:10.1242/jcs.113.24.4557. PMID 11082048.
Germani A, Bruzzoni-Giovanelli H, Fellous A, Gisselbrecht S, Varin-Blank N, Calvo F (Dec 2000). "SIAH-1 interacts with alpha-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis". Oncogene. 19 (52): 5997–6006. doi:10.1038/sj.onc.1204002. PMID 11146551. S2CID 41279377.
Kourmouli N, Dialynas G, Petraki C, Pyrpasopoulou A, Singh PB, Georgatos SD, Theodoropoulos PA (Apr 2001). "Binding of heterochromatin protein 1 to the nuclear envelope is regulated by a soluble form of tubulin". The Journal of Biological Chemistry. 276 (16): 13007–14. doi: 10.1074/jbc.M007135200 . PMID 11278332.
Rommelaere H, De Neve M, Neirynck K, Peelaers D, Waterschoot D, Goethals M, Fraeyman N, Vandekerckhove J, Ampe C (Nov 2001). "Prefoldin recognition motifs in the nonhomologous proteins of the actin and tubulin families". The Journal of Biological Chemistry. 276 (44): 41023–8. doi: 10.1074/jbc.M106591200 . PMID 11535601.
Klein C, Kramer EM, Cardine AM, Schraven B, Brandt R, Trotter J (Feb 2002). "Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau". The Journal of Neuroscience. 22 (3): 698–707. doi: 10.1523/JNEUROSCI.22-03-00698.2002 . PMC 6758498 . PMID 11826099.
Saugstad JA, Yang S, Pohl J, Hall RA, Conn PJ (Mar 2002). "Interaction between metabotropic glutamate receptor 7 and alpha tubulin". Journal of Neurochemistry. 80 (6): 980–8. doi:10.1046/j.0022-3042.2002.00778.x. PMC 2925652 . PMID 11953448.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000198033 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9465305-3] Dodé C, Weil D, Levilliers J, Crozet F, Chaïb H, Levi-Acobas F, Guilford P, Petit C (Jan 1998). "Sequence characterization of a newly identified human alpha-tubulin gene (TUBA2)". Genomics. 47 (1): 125–30. doi:10.1006/geno.1997.5081. PMID 9465305.

[entrez-4] 1 2 "Entrez Gene: TUBA3C tubulin, alpha 3c".

[pmid11826099-5] Klein C, Kramer EM, Cardine AM, Schraven B, Brandt R, Trotter J (Feb 2002). "Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau". The Journal of Neuroscience. 22 (3): 698–707. doi:10.1523/JNEUROSCI.22-03-00698.2002. PMC 6758498 . PMID 11826099.

[pmid16189514-6] Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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