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Protein
Submitted name:

TuBulin, Alpha

Gene

tba-1

Organism
Caenorhabditis elegans
Status
Unreviewed-Annotation score: Annotation score: 4 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.UniRule annotationSAAS annotation

GO - Molecular functioni

GO - Biological processi

  • embryo development ending in birth or egg hatching Source: WormBase
  • establishment of mitotic spindle orientation Source: WormBase
  • regulation of cytokinesis Source: WormBase
Complete GO annotation...

Keywords - Ligandi

GTP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Submitted name:
TuBulin, AlphaImported
Gene namesi
Name:tba-1Imported
ORF Names:CELE_F26E4.8Imported, F26E4.8Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiF26E4.8a; CE09692; WBGene00006528; tba-1.

Subcellular locationi

  • Cytoplasm SAAS annotation
  • Cytoplasmcytoskeleton SAAS annotation

GO - Cellular componenti

  • axon Source: WormBase
  • cytoplasm Source: UniProtKB-KW
  • dendrite Source: WormBase
  • meiotic spindle Source: WormBase
  • microtubule Source: UniProtKB-KW
  • mitotic spindle Source: WormBase
  • neuronal cell body Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, CytoskeletonSAAS annotation, MicrotubuleUniRule annotationSAAS annotation

PTM / Processingi

Proteomic databases

EPDiO18688.
PaxDbiO18688.

Expressioni

Gene expression databases

ExpressionAtlasiO18688. baseline.

Interactioni

Subunit structurei

Dimer of alpha and beta chains.UniRule annotation
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.SAAS annotation

Protein-protein interaction databases

DIPiDIP-25114N.
IntActiO18688. 1 interaction.
MINTiMINT-1064720.
STRINGi6239.F26E4.8b.

Structurei

3D structure databases

ProteinModelPortaliO18688.
SMRiO18688. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 244198TubulinInterPro annotationAdd
BLAST
Domaini246 – 391146Tubulin_CInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the tubulin family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
PhylomeDBiO18688.

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.

O18688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREVISIHVG QAGVQIGNAC WELYCLEHGI QPDGTMPSDQ QADGESFTTF
60 70 80 90 100
FSDTGNGRYV PRSIFVDLEP TVVDEIRTGT YKKLFHPEQM ITGKEDAANN
110 120 130 140 150
YARGHYTVGK ELIDTVLDRI RRLADNCSGL QGFFVFHSFG GGTGSGFTSL
160 170 180 190 200
LMERLSVDYG KKSKLEFSIY PAPQVSTAVV EPYNSILTTH TTLEHSDCAF
210 220 230 240 250
MVDNEAIYDI CRRNLSVDRP SYTNLNRIIS QVVSSITASL RFDGALNVDL
260 270 280 290 300
NEFQTNLVPY PRIHFPLAAY TPLISADKAY HEALSVNDIT NSCFEPANQM
310 320 330 340 350
VKCDPRHGKY MAVCLLYRGD VVPKDVNTAI AAIKTKRTIQ FVDWCPTGFK
360 370 380 390 400
VGINYQPPTV VPGGDLAKVP RAVCMLSNTT AIAEAWSRLD YKFDLMYAKR
410 420 430 440
AFVHWYVGEG MEEGEFTEAR EDLAALEKDY EEVGADSNEG GNEEEGEEY
Length:449
Mass (Da):50,009
Last modified:January 1, 1998 - v1
Checksum:i991D292EDC04BDB2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284601 Genomic DNA. Translation: CAB03001.1.
PIRiT21415.
RefSeqiNP_001251213.1. NM_001264284.1.
UniGeneiCel.38859.

Genome annotation databases

EnsemblMetazoaiF26E4.8a; F26E4.8a; WBGene00006528.
GeneIDi172831.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284601 Genomic DNA. Translation: CAB03001.1.
PIRiT21415.
RefSeqiNP_001251213.1. NM_001264284.1.
UniGeneiCel.38859.

3D structure databases

ProteinModelPortaliO18688.
SMRiO18688. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-25114N.
IntActiO18688. 1 interaction.
MINTiMINT-1064720.
STRINGi6239.F26E4.8b.

Proteomic databases

EPDiO18688.
PaxDbiO18688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF26E4.8a; F26E4.8a; WBGene00006528.
GeneIDi172831.

Organism-specific databases

CTDi172831.
WormBaseiF26E4.8a; CE09692; WBGene00006528; tba-1.

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
PhylomeDBiO18688.

Gene expression databases

ExpressionAtlasiO18688. baseline.

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...

Publicationsi

  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    Caenorhabditis elegans Sequencing Consortium
    Sulson J.E., Waterston R.
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2Imported.

Entry informationi

Entry nameiO18688_CAEEL
AccessioniPrimary (citable) accession number: O18688
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.