TUB2/YFL037W Summary Help

Standard Name TUB2 1
Systematic Name YFL037W
Alias ARM10 , SHE8 2
Feature Type ORF, Verified
Description Beta-tubulin; associates with alpha-tubulin (Tub1p and Tub3p) to form tubulin dimer, which polymerizes to form microtubules; mutation in human ortholog is associated with congenital fibrosis of the extraocular muscles (CFEOM) with polymicrogyria (1, 3 and see Summary Paragraph)
Name Description TUBulin 1
Chromosomal Location
ChrVI:56336 to 57709 | ORF Map | GBrowse
Genetic position: -59 cM
Gene Ontology Annotations All TUB2 GO evidence and references
  View Computational GO annotations for TUB2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 5 genes
Classical genetics
reduction of function
Large-scale survey
reduction of function
175 total interaction(s) for 121 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 65
  • Affinity Capture-RNA: 5
  • Affinity Capture-Western: 7
  • Co-crystal Structure: 4
  • Co-fractionation: 1
  • Co-localization: 1
  • Co-purification: 1
  • PCA: 1
  • Reconstituted Complex: 11
  • Two-hybrid: 10

Genetic Interactions
  • Dosage Rescue: 8
  • Negative Genetic: 4
  • Phenotypic Enhancement: 3
  • Phenotypic Suppression: 5
  • Synthetic Growth Defect: 4
  • Synthetic Lethality: 36
  • Synthetic Rescue: 9

Expression Summary
Length (a.a.) 457
Molecular Weight (Da) 50,922
Isoelectric Point (pI) 4.46
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVI:56336 to 57709 | ORF Map | GBrowse
Genetic position: -59 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1374 56336..57709 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001857

In S. cerevisiae, TUB2 encodes the single essential beta-tubulin (1). Tub2p belongs to the tubulin superfamily, which includes alpha- and gamma-tubulin and the prokaryotic tubulin-like gene FtsZ (reviewed in 4, 5). Beta- and alpha-tubulin form tubulin heterodimers, which polymerize into microtubules. Microtubules are conserved cytoskeletal elements that function in nuclear processes: chromosome segregation in mitosis and meiosis, spindle orientation, and nuclear migration during mitosis and mating (6; for reviews, see 7, 8). All microtubules in S. cerevisiae emanate from a microtubule organizing center called the spindle pole body (SPB), which is embedded in the nuclear envelope (for review, see 9). Microtubules extend from both faces of the SPB, generating two types of microtubules: nuclear and cytoplasmic microtubules (10; for review, see 9). The distribution and length of these two types of microtubules is regulated throughout the cell cycle (10; reviewed in 11).

TUB2 was cloned based on its strong homology with its counterparts in other eukaryotes (1). There is an abundance of tub2 conditional mutants resulting from genetic screens for chromosome loss and sensitivity/resistance to anti-microtubule drugs (such as benomyl), suppressor analysis, and in vitro mutagenesis (12, 13, 14, 15). One benomyl-resistant allele of TUB2, tub2-150, actually requires benomyl for growth at high temperatures, suggesting that microtubules in this mutant are hyper-stable (14, 16). Most conditional tub2 mutants are cold sensitive, presumably reflecting the intrinsic cold-sensitivity of the microtubule polymer. Tub2p interacts with numerous proteins involved in the regulation of microtubules, such as microtubule motors, SPB components, kinetochore components, tubulin biogenesis factors, and alpha-tubulin (encoded by TUB1 and TUB3) (reviewed in 7, 8).

Tub2p is a GTP-binding protein (for review, see 17). Tub2p hydrolyzes its GTP following tubulin dimer addition to the microtubule end, whereas the GTP bound to Tub1p and Tub3p is non-hydrolyzable (17). The structure of tubulin has been crystallized in the polymerized state; Tub3p and Tub1p, rather than Tub2p, are believed to interact directly with the SPB (18).

Last updated: 2003-12-18 Contact SGD

References cited on this page View Complete Literature Guide for TUB2
1) Neff NF, et al.  (1983) Isolation of the beta-tubulin gene from yeast and demonstration of its essential function in vivo. Cell 33(1):211-9
2) Espinet C, et al.  (1995) An efficient method to isolate yeast genes causing overexpression-mediated growth arrest. Yeast 11(1):25-32
3) Cederquist GY, et al.  (2012) An inherited TUBB2B mutation alters a kinesin-binding site and causes polymicrogyria, CFEOM and axon dysinnervation. Hum Mol Genet 21(26):5484-99
4) McKean PG, et al.  (2001) The extended tubulin superfamily. J Cell Sci 114(Pt 15):2723-33
5) Nogales E, et al.  (1998) Tubulin and FtsZ form a distinct family of GTPases. Nat Struct Biol 5(6):451-8
6) Jacobs CW, et al.  (1988) Functions of microtubules in the Saccharomyces cerevisiae cell cycle. J Cell Biol 107(4):1409-26
7) Winsor B and Schiebel E  (1997) Review: an overview of the Saccharomyces cerevisiae microtubule and microfilament cytoskeleton. Yeast 13(5):399-434
8) Botstein D, et al.  (1997) "The yeast cytoskeleton." Pp. 1-90 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Cell Cycle and Cell Biology, edited by Pringle JR, Broach JR and Jones EW. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
9) Knop M, et al.  (1999) Microtubule organization by the budding yeast spindle pole body. Biol Cell 91(4-5):291-304
10) Kilmartin JV and Adams AE  (1984) Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces. J Cell Biol 98(3):922-33
11) Carminati JL and Stearns T  (1999) Cytoskeletal dynamics in yeast. Methods Cell Biol 58:87-105
12) Hoyt MA, et al.  (1990) Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes. Mol Cell Biol 10(1):223-34
13) Stearns T, et al.  (1990) Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function. Genetics 124(2):251-62
14) Thomas JH, et al.  (1985) Isolation and characterization of mutations in the beta-tubulin gene of Saccharomyces cerevisiae. Genetics 111(4):715-34
15) Huffaker TC, et al.  (1988) Diverse effects of beta-tubulin mutations on microtubule formation and function. J Cell Biol 106(6):1997-2010
16) Machin NA, et al.  (1995) Microtubule stability in budding yeast: characterization and dosage suppression of a benomyl-dependent tubulin mutant. Mol Biol Cell 6(9):1241-59
17) Mandelkow E and Mandelkow EM  (1989) Microtubular structure and tubulin polymerization. Curr Opin Cell Biol 1(1):5-9
18) Nogales E, et al.  (1999) High-resolution model of the microtubule. Cell 96(1):79-88