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-1 chain

Gene

TUB1

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 5590 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-32674-MONOMER
ReactomeiR-SCE-114608 Platelet degranulation
R-SCE-5610787 Hedgehog 'off' state
R-SCE-5617833 Cilium Assembly
R-SCE-5626467 RHO GTPases activate IQGAPs
R-SCE-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-SCE-983189 Kinesins

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1 chain
Gene namesi
Name:TUB1
Ordered Locus Names:YML085C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML085C
SGDiS000004550 TUB1

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_00000482391 – 447Tubulin alpha-1 chainAdd BLAST447

Proteomic databases

MaxQBiP09733
PaxDbiP09733
PRIDEiP09733

PTM databases

iPTMnetiP09733
SwissPalmiP09733

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.

Protein-protein interaction databases

BioGridi35056, 139 interactors
ComplexPortaliCPX-1424 Tubulin alpha-beta heterodimeric complex, TUB1 variant
DIPiDIP-854N
IntActiP09733, 315 interactors
MINTiP09733
STRINGi4932.YML085C

Structurei

Secondary structure

1447
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi10 – 27Combined sources18
Beta strandi34 – 36Combined sources3
Beta strandi47 – 50Combined sources4
Turni51 – 53Combined sources3
Beta strandi54 – 56Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi62 – 64Combined sources3
Beta strandi66 – 72Combined sources7
Helixi73 – 81Combined sources9
Turni83 – 87Combined sources5
Turni90 – 92Combined sources3
Beta strandi93 – 95Combined sources3
Helixi104 – 108Combined sources5
Helixi112 – 127Combined sources16
Beta strandi135 – 145Combined sources11
Turni146 – 148Combined sources3
Helixi149 – 161Combined sources13
Turni162 – 164Combined sources3
Beta strandi165 – 173Combined sources9
Helixi176 – 178Combined sources3
Helixi184 – 195Combined sources12
Beta strandi196 – 198Combined sources3
Beta strandi200 – 206Combined sources7
Helixi207 – 216Combined sources10
Helixi225 – 239Combined sources15
Helixi241 – 244Combined sources4
Helixi253 – 260Combined sources8
Beta strandi262 – 265Combined sources4
Beta strandi270 – 274Combined sources5
Helixi289 – 295Combined sources7
Helixi299 – 301Combined sources3
Beta strandi302 – 306Combined sources5
Beta strandi313 – 323Combined sources11
Helixi326 – 338Combined sources13
Beta strandi352 – 357Combined sources6
Beta strandi365 – 369Combined sources5
Beta strandi373 – 382Combined sources10
Helixi383 – 385Combined sources3
Helixi386 – 400Combined sources15
Turni401 – 405Combined sources5
Helixi406 – 410Combined sources5
Turni411 – 413Combined sources3
Helixi417 – 436Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FFBX-ray2.88A1-447[»]
4U3JX-ray2.81A1-447[»]
5W3Felectron microscopy3.70A1-447[»]
5W3Helectron microscopy4.00A1-447[»]
5W3Jelectron microscopy4.00A1-447[»]
ProteinModelPortaliP09733
SMRiP09733
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

GeneTreeiENSGT00920000149044
HOGENOMiHOG000165711
InParanoidiP09733
KOiK07374
OMAiGICYQAP
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.

P09733-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREVISINVG QAGCQIGNAC WELYSLEHGI KPDGHLEDGL SKPKGGEEGF
60 70 80 90 100
STFFHETGYG KFVPRAIYVD LEPNVIDEVR NGPYKDLFHP EQLISGKEDA
110 120 130 140 150
ANNYARGHYT VGREILGDVL DRIRKLADQC DGLQGFLFTH SLGGGTGSGL
160 170 180 190 200
GSLLLEELSA EYGKKSKLEF AVYPAPQVST SVVEPYNTVL TTHTTLEHAD
210 220 230 240 250
CTFMVDNEAI YDMCKRNLDI PRPSFANLNN LIAQVVSSVT ASLRFDGSLN
260 270 280 290 300
VDLNEFQTNL VPYPRIHFPL VSYSPVLSKS KAFHESNSVS EITNACFEPG
310 320 330 340 350
NQMVKCDPRD GKYMATCLLY RGDVVTRDVQ RAVEQVKNKK TVQLVDWCPT
360 370 380 390 400
GFKIGICYEP PTATPNSQLA TVDRAVCMLS NTTSIAEAWK RIDRKFDLMY
410 420 430 440
AKRAFVHWYV GEGMEEGEFT EAREDLAALE RDYIEVGADS YAEEEEF
Length:447
Mass (Da):49,800
Last modified:October 1, 1996 - v2
Checksum:iE263B49440F71889
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti94I → L in AAA35180 (PubMed:3025610).Curated1
Sequence conflicti327R → G in AAA35180 (PubMed:3025610).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28429 mRNA Translation: AAA35180.1
Z46660 Genomic DNA Translation: CAA86653.1
BK006946 Genomic DNA Translation: DAA09812.1
PIRiS50871
RefSeqiNP_013625.1, NM_001182444.1

Genome annotation databases

EnsemblFungiiYML085C; YML085C; YML085C
GeneIDi854889
KEGGisce:YML085C

Similar proteinsi

Entry informationi

Entry nameiTBA1_YEAST
AccessioniPrimary (citable) accession number: P09733
Secondary accession number(s): D6W0J8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: June 20, 2018
This is version 169 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

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