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Protein

Tubulin beta chain

Gene

tbb-1

Organism
Caenorhabditis elegans
Status
Unreviewed-Annotation score: Annotation score: 2 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

Keywordsi

LigandGTP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta chainUniRule annotation
Gene namesi
Name:tbb-1Imported
ORF Names:CELE_K01G5.7Imported, K01G5.7Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiK01G5.7; CE16197; WBGene00006536; tbb-1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, CytoskeletonSAAS annotation, MicrotubuleUniRule annotationSAAS annotation

PTM / Processingi

Proteomic databases

EPDiO17921.
PaxDbiO17921.
PeptideAtlasiO17921.

Expressioni

Gene expression databases

BgeeiWBGene00006536.

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.UniRule annotation

Protein-protein interaction databases

DIPiDIP-24741N.
IntActiO17921. 1 interactor.
MINTiMINT-1077993.
STRINGi6239.K01G5.7.2.

Structurei

3D structure databases

ProteinModelPortaliO17921.
SMRiO17921.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 244TubulinInterPro annotationAdd BLAST198
Domaini246 – 383Tubulin_CInterPro annotationAdd BLAST138

Sequence similaritiesi

Belongs to the tubulin family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
InParanoidiO17921.
KOiK07375.
OMAiAYHGEND.
OrthoDBiEOG091G06U2.
PhylomeDBiO17921.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiView protein in InterPro
IPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR037103. Tubulin/FtsZ_C_sf.
IPR036525. Tubulin/FtsZ_GTPase_sf.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiView protein in Pfam
PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
PRINTSiPR01163. BETATUBULIN.
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.
PS00228. TUBULIN_B_AUTOREG. 1 hit.

Sequencei

Sequence statusi: Complete.

O17921-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHVQAG QCGNQIGSKF WEVISDEHGI QPDGTFKGES DLQLERIDVY
60 70 80 90 100
YNEANNGKYV PRAVLVDLEP GTMDSVRSGP FGQLFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDNVLDVI RKEAEGCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEFP DRIMSSFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CYRTLKLTNP TYGDLNHLVS LTMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLSAKGAQA YRALTVAELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVAAMFRGR MSMREVDEQM LSVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMAATFVGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLIS EYQQYQEATA EDEPLDEFAG EGETYESEQ
Length:449
Mass (Da):50,239
Last modified:January 1, 1998 - v1
Checksum:i4BE6D4163F2FE520
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284603 Genomic DNA. Translation: CAB07246.1.
PIRiT23201.
RefSeqiNP_499367.1. NM_066966.6.
UniGeneiCel.10334.

Genome annotation databases

EnsemblMetazoaiK01G5.7.1; K01G5.7.1; WBGene00006536.
K01G5.7.2; K01G5.7.2; WBGene00006536.
GeneIDi176501.
KEGGicel:CELE_K01G5.7.

Similar proteinsi

Entry informationi

Entry nameiO17921_CAEEL
AccessioniPrimary (citable) accession number: O17921
Entry historyiIntegrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: October 25, 2017
This is version 142 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported