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Protein

Tubulin beta-1 chain

Gene

betaTub56D

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-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 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1467GTPSequence analysis

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • structural constituent of cytoskeleton Source: FlyBase

GO - Biological processi

  • centrosome duplication Source: FlyBase
  • muscle attachment Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-1 chain
Alternative name(s):
Beta-1-tubulin
Gene namesi
Name:betaTub56D
ORF Names:CG9277
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003887. betaTub56D.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • microtubule Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Tubulin beta-1 chainPRO_0000048276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401Phosphoserine1 Publication
Modified residuei339 – 3391Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ24560.
PRIDEiQ24560.

PTM databases

iPTMnetiQ24560.

Expressioni

Gene expression databases

BgeeiQ24560.
ExpressionAtlasiQ24560. differential.
GenevisibleiQ24560. DM.

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. Interacts with mgr and Vhl.1 Publication

Protein-protein interaction databases

BioGridi62900. 66 interactions.
DIPiDIP-43956N.
IntActiQ24560. 2 interactions.
MINTiMINT-786821.
STRINGi7227.FBpp0085721.

Structurei

3D structure databases

ProteinModelPortaliQ24560.
SMRiQ24560. Positions 1-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
InParanoidiQ24560.
KOiK07375.
OrthoDBiEOG71ZP1H.
PhylomeDBiQ24560.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_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]
PRINTSiPR01163. BETATUBULIN.
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.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q24560-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEIISDEHGI DATGAYHGDS DLQLERINVY
60 70 80 90 100
YNEASGGKYV PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTYSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS LTMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNIQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQEATA DEDAEFEEEQ EAEVDEN
Length:447
Mass (Da):50,147
Last modified:November 15, 2002 - v2
Checksum:i9E6F66C5C96731DB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351A → T in AAA28989 (PubMed:3119300).Curated
Sequence conflicti163 – 1631I → S in AAA28989 (PubMed:3119300).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20419 mRNA. Translation: AAA28989.1.
AE013599 Genomic DNA. Translation: AAF57555.1.
BT003242 mRNA. Translation: AAO24999.1.
RefSeqiNP_523795.2. NM_079071.3.
UniGeneiDm.7174.

Genome annotation databases

EnsemblMetazoaiFBtr0086536; FBpp0085720; FBgn0003887.
GeneIDi37238.
KEGGidme:Dmel_CG9277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20419 mRNA. Translation: AAA28989.1.
AE013599 Genomic DNA. Translation: AAF57555.1.
BT003242 mRNA. Translation: AAO24999.1.
RefSeqiNP_523795.2. NM_079071.3.
UniGeneiDm.7174.

3D structure databases

ProteinModelPortaliQ24560.
SMRiQ24560. Positions 1-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62900. 66 interactions.
DIPiDIP-43956N.
IntActiQ24560. 2 interactions.
MINTiMINT-786821.
STRINGi7227.FBpp0085721.

PTM databases

iPTMnetiQ24560.

Proteomic databases

PaxDbiQ24560.
PRIDEiQ24560.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086536; FBpp0085720; FBgn0003887.
GeneIDi37238.
KEGGidme:Dmel_CG9277.

Organism-specific databases

CTDi37238.
FlyBaseiFBgn0003887. betaTub56D.

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
InParanoidiQ24560.
KOiK07375.
OrthoDBiEOG71ZP1H.
PhylomeDBiQ24560.

Miscellaneous databases

ChiTaRSibetaTub56D. fly.
GenomeRNAii37238.
PROiQ24560.

Gene expression databases

BgeeiQ24560.
ExpressionAtlasiQ24560. differential.
GenevisibleiQ24560. DM.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_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]
PRINTSiPR01163. BETATUBULIN.
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.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Testis-specific beta 2 tubulins are identical in Drosophila melanogaster and D. hydei but differ from the ubiquitous beta 1 tubulin."
    Michiels F., Falkenburg D., Mueller A.M., Hinz U., Otto U., Bellmann R., Glaetzer K.H., Brand R., Bialojan S., Renkawitz-Pohl R.
    Chromosoma 95:387-395(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-339, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  6. Cited for: INTERACTION WITH MGR AND VHL.

Entry informationi

Entry nameiTBB1_DROME
AccessioniPrimary (citable) accession number: Q24560
Secondary accession number(s): Q53YG6, Q9V8V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: June 8, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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.