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Protein

Tubulin beta chain

Gene

TUB2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1467GTPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • homologous chromosome segregation Source: SGD
  • mitotic sister chromatid segregation Source: SGD
  • nuclear migration along microtubule Source: SGD
  • response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30425-MONOMER.
ReactomeiR-SCE-5610787. Hedgehog 'off' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta chain
Alternative name(s):
Beta-tubulin
Gene namesi
Name:TUB2
Ordered Locus Names:YFL037W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFL037W.
SGDiS000001857. TUB2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic microtubule Source: SGD
  • kinetochore microtubule Source: SGD
  • nuclear microtubule Source: SGD
  • spindle pole body Source: SGD
  • tubulin complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001V → N: Becomes sensitive to rhizoxin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Tubulin beta chainPRO_0000048443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei278 – 2781PhosphoserineCombined sources
Modified residuei280 – 2801PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP02557.
PRIDEiP02557.

PTM databases

iPTMnetiP02557.

Interactioni

Subunit structurei

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Binary interactionsi

WithEntry#Exp.IntActNotes
RBL2P486062EBI-18986,EBI-18991

Protein-protein interaction databases

BioGridi31109. 131 interactions.
DIPiDIP-2340N.
IntActiP02557. 270 interactions.
MINTiMINT-545919.

Structurei

Secondary structure

1
457
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi10 – 2718Combined sources
Helixi42 – 454Combined sources
Helixi46 – 494Combined sources
Beta strandi51 – 533Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 697Combined sources
Helixi70 – 778Combined sources
Helixi80 – 823Combined sources
Beta strandi83 – 853Combined sources
Helixi87 – 893Combined sources
Beta strandi90 – 923Combined sources
Helixi101 – 1055Combined sources
Turni108 – 1125Combined sources
Helixi113 – 12513Combined sources
Beta strandi132 – 14211Combined sources
Helixi143 – 15816Combined sources
Beta strandi162 – 1709Combined sources
Helixi181 – 19515Combined sources
Beta strandi197 – 2037Combined sources
Helixi204 – 2118Combined sources
Helixi222 – 23615Combined sources
Helixi238 – 2414Combined sources
Beta strandi242 – 2443Combined sources
Beta strandi245 – 2473Combined sources
Helixi250 – 2578Combined sources
Beta strandi265 – 2717Combined sources
Helixi286 – 2949Combined sources
Helixi296 – 2983Combined sources
Beta strandi299 – 3035Combined sources
Helixi305 – 3073Combined sources
Beta strandi310 – 32011Combined sources
Helixi323 – 33614Combined sources
Helixi338 – 3403Combined sources
Beta strandi345 – 3473Combined sources
Beta strandi349 – 3557Combined sources
Beta strandi362 – 37110Combined sources
Helixi372 – 3743Combined sources
Helixi375 – 38915Combined sources
Turni390 – 3956Combined sources
Helixi396 – 3994Combined sources
Turni400 – 4023Combined sources
Helixi405 – 42622Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FFBX-ray2.88B1-457[»]
4U3JX-ray2.81B1-457[»]
ProteinModelPortaliP02557.
SMRiP02557. Positions 1-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
InParanoidiP02557.
KOiK07375.
OMAiWVPRSIN.
OrthoDBiEOG7BGHW1.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. 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.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02557-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIIHISTG QCGNQIGAAF WETICGEHGL DFNGTYHGHD DIQKERLNVY
60 70 80 90 100
FNEASSGKWV PRSINVDLEP GTIDAVRNSA IGNLFRPDNY IFGQSSAGNV
110 120 130 140 150
WAKGHYTEGA ELVDSVMDVI RREAEGCDSL QGFQITHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEFP DRMMATFSVL PSPKTSDTVV EPYNATLSVH QLVEHSDETF
210 220 230 240 250
CIDNEALYDI CQRTLKLNQP SYGDLNNLVS SVMSGVTTSL RYPGQLNSDL
260 270 280 290 300
RKLAVNLVPF PRLHFFMVGY APLTAIGSQS FRSLTVPELT QQMFDAKNMM
310 320 330 340 350
AAADPRNGRY LTVAAFFRGK VSVKEVEDEM HKVQSKNSDY FVEWIPNNVQ
360 370 380 390 400
TAVCSVAPQG LDMAATFIAN STSIQELFKR VGDQFSAMFK RKAFLHWYTS
410 420 430 440 450
EGMDELEFSE AESNMNDLVS EYQQYQEATV EDDEEVDENG DFGAPQNQDE

PITENFE
Length:457
Mass (Da):50,923
Last modified:November 1, 1995 - v2
Checksum:i68EBEA7D7A5B8EA1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91T → A in CAA24603 (PubMed:6380751).Curated
Sequence conflicti12 – 121C → Y in CAA24603 (PubMed:6380751).Curated
Sequence conflicti71 – 711G → W in CAA24603 (PubMed:6380751).Curated
Sequence conflicti152 – 1521I → F in CAA24603 (PubMed:6380751).Curated
Sequence conflicti156 – 1561R → K in CAA24603 (PubMed:6380751).Curated
Sequence conflicti159 – 1591F → L in CAA24603 (PubMed:6380751).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01296 Genomic DNA. Translation: CAA24603.1.
D50617 Genomic DNA. Translation: BAA09202.1.
X00209 Genomic DNA. Translation: CAA25035.1.
BK006940 Genomic DNA. Translation: DAA12403.1.
PIRiS56217. UBBYB.
RefSeqiNP_116616.1. NM_001179929.1.

Genome annotation databases

EnsemblFungiiBAA09202; BAA09202; BAA09202.
YFL037W; YFL037W; YFL037W.
GeneIDi850506.
KEGGisce:YFL037W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01296 Genomic DNA. Translation: CAA24603.1.
D50617 Genomic DNA. Translation: BAA09202.1.
X00209 Genomic DNA. Translation: CAA25035.1.
BK006940 Genomic DNA. Translation: DAA12403.1.
PIRiS56217. UBBYB.
RefSeqiNP_116616.1. NM_001179929.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FFBX-ray2.88B1-457[»]
4U3JX-ray2.81B1-457[»]
ProteinModelPortaliP02557.
SMRiP02557. Positions 1-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31109. 131 interactions.
DIPiDIP-2340N.
IntActiP02557. 270 interactions.
MINTiMINT-545919.

PTM databases

iPTMnetiP02557.

Proteomic databases

MaxQBiP02557.
PRIDEiP02557.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09202; BAA09202; BAA09202.
YFL037W; YFL037W; YFL037W.
GeneIDi850506.
KEGGisce:YFL037W.

Organism-specific databases

EuPathDBiFungiDB:YFL037W.
SGDiS000001857. TUB2.

Phylogenomic databases

GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
InParanoidiP02557.
KOiK07375.
OMAiWVPRSIN.
OrthoDBiEOG7BGHW1.

Enzyme and pathway databases

BioCyciYEAST:G3O-30425-MONOMER.
ReactomeiR-SCE-5610787. Hedgehog 'off' state.

Miscellaneous databases

PROiP02557.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. 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.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of the beta-tubulin gene from yeast and demonstration of its essential function in vivo."
    Neff N.F., Thomas J.H., Grisafi P., Botstein D.
    Cell 33:211-219(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product."
    Gallwitz D., Donath C., Sander C.
    Nature 306:704-707(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
  5. "Molecular basis for determining the sensitivity of eucaryotes to the antimitotic drug rhizoxin."
    Takahashi M., Matsumoto S., Iwasaki S., Yahara I.
    Mol. Gen. Genet. 222:169-175(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ANTIBIOTIC RESISTANCE TO RHIZOXIN.
  6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTBB_YEAST
AccessioniPrimary (citable) accession number: P02557
Secondary accession number(s): D6VTJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Rhizoxin, an antibiotic that exhibits potent anti-mitotic activity against most eukaryotic cells except for yeasts, binds to beta tubulin.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.