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Protein

Tubulin alpha-1 chain

Gene

TUB1

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)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
Complete GO annotation...

Keywords - Ligandi

GTP-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. Assembly of the primary cilium.
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

GO - Cellular componenti

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

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.
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. 131 interactors.
DIPiDIP-854N.
IntActiP09733. 251 interactors.
MINTiMINT-1529610.

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[»]
ProteinModelPortaliP09733.
SMRiP09733.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

GeneTreeiENSGT00860000134462.
HOGENOMiHOG000165711.
InParanoidiP09733.
KOiK07374.
OMAiPRPSFAN.
OrthoDBiEOG092C2JRV.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_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]
PRINTSiPR01162. ALPHATUBULIN.
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.
[Graphical view]

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.

Cross-referencesi

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.

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[»]
ProteinModelPortaliP09733.
SMRiP09733.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35056. 131 interactors.
DIPiDIP-854N.
IntActiP09733. 251 interactors.
MINTiMINT-1529610.

PTM databases

iPTMnetiP09733.
SwissPalmiP09733.

Proteomic databases

MaxQBiP09733.
PRIDEiP09733.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML085C; YML085C; YML085C.
GeneIDi854889.
KEGGisce:YML085C.

Organism-specific databases

EuPathDBiFungiDB:YML085C.
SGDiS000004550. TUB1.

Phylogenomic databases

GeneTreeiENSGT00860000134462.
HOGENOMiHOG000165711.
InParanoidiP09733.
KOiK07374.
OMAiPRPSFAN.
OrthoDBiEOG092C2JRV.

Enzyme and pathway databases

BioCyciYEAST:G3O-32674-MONOMER.
ReactomeiR-SCE-114608. Platelet degranulation.
R-SCE-5610787. Hedgehog 'off' state.
R-SCE-5617833. Assembly of the primary cilium.
R-SCE-5626467. RHO GTPases activate IQGAPs.
R-SCE-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-SCE-983189. Kinesins.

Miscellaneous databases

PROiP09733.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_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]
PRINTSiPR01162. ALPHATUBULIN.
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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTBA1_YEAST
AccessioniPrimary (citable) accession number: P09733
Secondary accession number(s): D6W0J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5590 molecules/cell in log phase SD medium.1 Publication

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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: 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.