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Protein

Tubulin beta chain

Gene

TUB2

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

Functioni

Tubulin is the major constituent of microtubules (PubMed:28013290). 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.1 Publication

Miscellaneous

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi140 – 146GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

  • cytoskeleton organization Source: UniProtKB
  • homologous chromosome segregation Source: SGD
  • microtubule-based process Source: UniProtKB
  • mitotic sister chromatid segregation Source: SGD
  • nuclear migration along microtubule Source: SGD
  • positive regulation of intracellular protein transport Source: UniProtKB
  • response to antibiotic Source: UniProtKB-KW

Keywordsi

Biological processAntibiotic resistance
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30425-MONOMER
ReactomeiR-SCE-5610787 Hedgehog 'off' state
R-SCE-5617833 Cilium Assembly
R-SCE-5626467 RHO GTPases activate IQGAPs
R-SCE-6798695 Neutrophil degranulation
R-SCE-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-SCE-983189 Kinesins

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi100V → N: Becomes sensitive to rhizoxin. 1
Mutagenesisi390K → Q: Decreased microtubule stability. 1 Publication1
Mutagenesisi421E → K: Increased microtubule polymerization and depolymerization rates. Increased microtubule stability. Decreased kinesin KIP3 subcellular location at microtubule plus ends. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000484431 – 457Tubulin beta chainAdd BLAST457

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei278PhosphoserineCombined sources1
Modified residuei280PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP02557
PaxDbiP02557
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, 435 interactors
DIPiDIP-2340N
IntActiP02557, 339 interactors
MINTiP02557
STRINGi4932.YFL037W

Structurei

Secondary structure

1457
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi10 – 27Combined sources18
Helixi42 – 45Combined sources4
Helixi46 – 49Combined sources4
Beta strandi51 – 53Combined sources3
Beta strandi59 – 61Combined sources3
Beta strandi63 – 69Combined sources7
Helixi70 – 77Combined sources8
Helixi80 – 82Combined sources3
Beta strandi83 – 85Combined sources3
Helixi87 – 89Combined sources3
Beta strandi90 – 92Combined sources3
Helixi101 – 105Combined sources5
Turni108 – 112Combined sources5
Helixi113 – 125Combined sources13
Beta strandi132 – 142Combined sources11
Helixi143 – 158Combined sources16
Beta strandi162 – 170Combined sources9
Helixi181 – 195Combined sources15
Beta strandi197 – 203Combined sources7
Helixi204 – 211Combined sources8
Helixi222 – 236Combined sources15
Helixi238 – 241Combined sources4
Beta strandi242 – 244Combined sources3
Beta strandi245 – 247Combined sources3
Helixi250 – 257Combined sources8
Beta strandi265 – 271Combined sources7
Helixi286 – 294Combined sources9
Helixi296 – 298Combined sources3
Beta strandi299 – 303Combined sources5
Helixi305 – 307Combined sources3
Beta strandi310 – 320Combined sources11
Helixi323 – 336Combined sources14
Helixi338 – 340Combined sources3
Beta strandi345 – 347Combined sources3
Beta strandi349 – 355Combined sources7
Beta strandi362 – 371Combined sources10
Helixi372 – 374Combined sources3
Helixi375 – 389Combined sources15
Turni390 – 395Combined sources6
Helixi396 – 399Combined sources4
Turni400 – 402Combined sources3
Helixi405 – 426Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FFBX-ray2.88B1-457[»]
4U3JX-ray2.81B1-457[»]
5W3Felectron microscopy3.70B1-457[»]
5W3Helectron microscopy4.00B1-457[»]
5W3Jelectron microscopy4.00B1-457[»]
ProteinModelPortaliP02557
SMRiP02557
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000119061
HOGENOMiHOG000165710
InParanoidiP02557
KOiK07375
OMAiEVGANKY
OrthoDBiEOG092C2U1W

Family and domain databases

Gene3Di1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
InterProiView protein in InterPro
IPR013838 Beta-tubulin_BS
IPR002453 Beta_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase
PANTHERiPTHR11588 PTHR11588, 1 hit
PTHR11588:SF256 PTHR11588:SF256, 1 hit
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01163 BETATUBULIN
PR01161 TUBULIN
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227 TUBULIN, 1 hit
PS00228 TUBULIN_B_AUTOREG, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti9T → A in CAA24603 (PubMed:6380751).Curated1
Sequence conflicti12C → Y in CAA24603 (PubMed:6380751).Curated1
Sequence conflicti71G → W in CAA24603 (PubMed:6380751).Curated1
Sequence conflicti152I → F in CAA24603 (PubMed:6380751).Curated1
Sequence conflicti156R → K in CAA24603 (PubMed:6380751).Curated1
Sequence conflicti159F → L in CAA24603 (PubMed:6380751).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiTBB_YEAST
AccessioniPrimary (citable) accession number: P02557
Secondary accession number(s): D6VTJ3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 178 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health