Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tubulin alpha-3 chain

Gene

TUB3

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. 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.

Miscellaneous

Present with 12300 molecules/cell in log phase SD medium.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi143 – 149GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

  • homologous chromosome segregation Source: SGD
  • mitotic sister chromatid segregation Source: SGD
  • nuclear migration along microtubule Source: SGD

Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32703-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-3 chain
Gene namesi
Name:TUB3
Ordered Locus Names:YML124C
ORF Names:YM7056.02C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML124C
SGDiS000004593 TUB3

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000482401 – 445Tubulin alpha-3 chainAdd BLAST445

Proteomic databases

MaxQBiP09734
PaxDbiP09734
PRIDEiP09734

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. Interacts with NUM1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NUM1Q004022EBI-18981,EBI-12386

Protein-protein interaction databases

BioGridi35081, 217 interactors
DIPiDIP-2206N
IntActiP09734, 95 interactors
MINTiP09734
STRINGi4932.YML124C

Structurei

3D structure databases

ProteinModelPortaliP09734
SMRiP09734
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

GeneTreeiENSGT00910000144648
HOGENOMiHOG000165711
InParanoidiP09734
OMAiICNEPSA
OrthoDBiEOG092C2JRV

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
IPR002452 Alpha_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
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01162 ALPHATUBULIN
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

Sequencei

Sequence statusi: Complete.

P09734-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREVISINVG QAGCQIGNAC WELYSLEHGI KEDGHLEDGL SKPKGGEEGF
60 70 80 90 100
STFFHETGYG KFVPRAIYVD LEPNVIDEVR TGRFKELFHP EQLINGKEDA
110 120 130 140 150
ANNYARGHYT VGREIVDEVE ERIRKMADQC DGLQGFLFTH SLGGGTGSGL
160 170 180 190 200
GSLLLENLSY EYGKKSKLEF AVYPAPQLST SVVEPYNTVL TTHTTLEHAD
210 220 230 240 250
CTFMVDNEAI YDICKRNLGI SRPSFSNLNG LIAQVISSVT ASLRFDGSLN
260 270 280 290 300
VDLNEFQTNL VPYPRIHFPL VSYAPILSKK RATHESNSVS EITNACFEPG
310 320 330 340 350
NQMVKCDPTK GKYMANCLLY RGDVVTRDVQ RAVEQVKNKK TVQMVDWCPT
360 370 380 390 400
GFKIGICYEP PSVIPSSELA NVDRAVCMLS NTTAIADAWK RIDQKFDLMY
410 420 430 440
AKRAFVHWYV GEGMEEGEFT EAREDLAALE RDYIEVGADS YAEEF
Length:445
Mass (Da):49,694
Last modified:July 1, 1989 - v1
Checksum:i189889B795E72448
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28428 mRNA Translation: AAA35181.1
Z49218 Genomic DNA Translation: CAA89156.1
D90346 Genomic DNA No translation available.
BK006946 Genomic DNA Translation: DAA09775.1
PIRiB25076
RefSeqiNP_013582.1, NM_001182487.1

Genome annotation databases

EnsemblFungiiYML124C; YML124C; YML124C
GeneIDi854915
KEGGisce:YML124C

Similar proteinsi

Entry informationi

Entry nameiTBA3_YEAST
AccessioniPrimary (citable) accession number: P09734
Secondary accession number(s): D6W0G1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 23, 2018
This is version 163 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health