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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi143 – 1497GTPSequence analysis

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Tubulin alpha-1 chainPRO_0000048239Add
BLAST

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 interactions.
DIPiDIP-854N.
IntActiP09733. 251 interactions.
MINTiMINT-1529610.

Structurei

Secondary structure

1
447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi10 – 2718Combined sources
Beta strandi34 – 363Combined sources
Beta strandi47 – 504Combined sources
Turni51 – 533Combined sources
Beta strandi54 – 563Combined sources
Beta strandi58 – 603Combined sources
Beta strandi62 – 643Combined sources
Beta strandi66 – 727Combined sources
Helixi73 – 819Combined sources
Turni83 – 875Combined sources
Turni90 – 923Combined sources
Beta strandi93 – 953Combined sources
Helixi104 – 1085Combined sources
Helixi112 – 12716Combined sources
Beta strandi135 – 14511Combined sources
Turni146 – 1483Combined sources
Helixi149 – 16113Combined sources
Turni162 – 1643Combined sources
Beta strandi165 – 1739Combined sources
Helixi176 – 1783Combined sources
Helixi184 – 19512Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi200 – 2067Combined sources
Helixi207 – 21610Combined sources
Helixi225 – 23915Combined sources
Helixi241 – 2444Combined sources
Helixi253 – 2608Combined sources
Beta strandi262 – 2654Combined sources
Beta strandi270 – 2745Combined sources
Helixi289 – 2957Combined sources
Helixi299 – 3013Combined sources
Beta strandi302 – 3065Combined sources
Beta strandi313 – 32311Combined sources
Helixi326 – 33813Combined sources
Beta strandi352 – 3576Combined sources
Beta strandi365 – 3695Combined sources
Beta strandi373 – 38210Combined sources
Helixi383 – 3853Combined sources
Helixi386 – 40015Combined sources
Turni401 – 4055Combined sources
Helixi406 – 4105Combined sources
Turni411 – 4133Combined sources
Helixi417 – 43620Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FFBX-ray2.88A1-447[»]
4U3JX-ray2.81A1-447[»]
ProteinModelPortaliP09733.
SMRiP09733. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

GeneTreeiENSGT00840000130009.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941I → L in AAA35180 (PubMed:3025610).Curated
Sequence conflicti327 – 3271R → G in AAA35180 (PubMed:3025610).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4FFBX-ray2.88A1-447[»]
4U3JX-ray2.81A1-447[»]
ProteinModelPortaliP09733.
SMRiP09733. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35056. 131 interactions.
DIPiDIP-854N.
IntActiP09733. 251 interactions.
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

GeneTreeiENSGT00840000130009.
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: September 7, 2016
This is version 151 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.