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Protein

Tubulin alpha-3 chain

Gene

TUBA3

Organism
Arabidopsis thaliana (Mouse-ear cress)
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei450 – 4501Involved in polymerization

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTPSequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_277547. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_304635. Formation of tubulin folding intermediates by CCT/TriC.
REACT_306784. Post-chaperonin tubulin folding pathway.
REACT_342512. Kinesins.
REACT_342811. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-3 chain
Gene namesi
Name:TUBA3
Synonyms:TUA3
Ordered Locus Names:At5g19770
ORF Names:T29J13.190
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G19770.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Tubulin alpha-3 chainPRO_0000048138Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei349 – 3491Phosphothreonine1 Publication

Post-translational modificationi

Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ56WH1.

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

BioGridi17373. 1 interaction.
17374. 2 interactions.
IntActiQ56WH1. 1 interaction.
STRINGi3702.AT5G19780.1.

Structurei

3D structure databases

ProteinModelPortaliQ56WH1.
SMRiQ56WH1. Positions 1-436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
InParanoidiQ56WH1.
KOiK07374.
PhylomeDBiQ56WH1.

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.
IPR013838. Beta-tubulin_BS.
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.

Q56WH1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIISIHIG QAGIQVGNSC WELYCLEHGI QPDGMMPSDT TVGVAHDAFN
60 70 80 90 100
TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLISGKEDAA
110 120 130 140 150
NNFARGHYTV GKEIVDLCLD RVRKLADNCT GLQGFLVFNA VGGGTGSGLG
160 170 180 190 200
SLLLERLSVD YGKKSKLGFT IYPSPQVSTA VVEPYNSVLS THSLLEHTDV
210 220 230 240 250
AVLLDNEAIY DICRRSLDIE RPTYTNLNRL ISQIISSLTT SLRFDGAINV
260 270 280 290 300
DITEFQTNLV PYPRIHFMLS SYAPVISAAK AYHEQLSVPE ITNAVFEPAS
310 320 330 340 350
MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVGTIKTKRT VQFVDWCPTG
360 370 380 390 400
FKCGINYQPP TVVPGGDLAK VQRAVCMISN NTAVAEVFSR IDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGAEGG DDEEDEGEDY
Length:450
Mass (Da):49,654
Last modified:October 3, 2012 - v2
Checksum:iB6AD6D00244CFB71
GO

Sequence cautioni

The sequence BAD94893.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti308 – 3081R → K in BAD94893 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17189 Genomic DNA. Translation: AAA32888.1.
AF296838 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92747.1.
AF367301 mRNA. Translation: AAK32888.1.
AY065164 mRNA. Translation: AAL38340.1.
AY143895 mRNA. Translation: AAN28834.1.
BT000718 mRNA. Translation: AAN31860.1.
BT000719 mRNA. Translation: AAN31861.1.
BT001197 mRNA. Translation: AAN65084.1.
AK222069 mRNA. Translation: BAD94893.1. Different initiation.
PIRiA32712.
RefSeqiNP_197478.1. NM_121982.3.
NP_197479.1. NM_121983.3.
UniGeneiAt.23553.
At.49039.
At.75628.

Genome annotation databases

EnsemblPlantsiAT5G19770.1; AT5G19770.1; AT5G19770.
AT5G19780.1; AT5G19780.1; AT5G19780.
GeneIDi832097.
832098.
KEGGiath:AT5G19770.
ath:AT5G19780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17189 Genomic DNA. Translation: AAA32888.1.
AF296838 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92747.1.
AF367301 mRNA. Translation: AAK32888.1.
AY065164 mRNA. Translation: AAL38340.1.
AY143895 mRNA. Translation: AAN28834.1.
BT000718 mRNA. Translation: AAN31860.1.
BT000719 mRNA. Translation: AAN31861.1.
BT001197 mRNA. Translation: AAN65084.1.
AK222069 mRNA. Translation: BAD94893.1. Different initiation.
PIRiA32712.
RefSeqiNP_197478.1. NM_121982.3.
NP_197479.1. NM_121983.3.
UniGeneiAt.23553.
At.49039.
At.75628.

3D structure databases

ProteinModelPortaliQ56WH1.
SMRiQ56WH1. Positions 1-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17373. 1 interaction.
17374. 2 interactions.
IntActiQ56WH1. 1 interaction.
STRINGi3702.AT5G19780.1.

Proteomic databases

PRIDEiQ56WH1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G19770.1; AT5G19770.1; AT5G19770.
AT5G19780.1; AT5G19780.1; AT5G19780.
GeneIDi832097.
832098.
KEGGiath:AT5G19770.
ath:AT5G19780.

Organism-specific databases

TAIRiAT5G19770.

Phylogenomic databases

eggNOGiCOG5023.
InParanoidiQ56WH1.
KOiK07374.
PhylomeDBiQ56WH1.

Enzyme and pathway databases

ReactomeiREACT_277547. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_304635. Formation of tubulin folding intermediates by CCT/TriC.
REACT_306784. Post-chaperonin tubulin folding pathway.
REACT_342512. Kinesins.
REACT_342811. Platelet degranulation.

Miscellaneous databases

PROiQ56WH1.

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.
IPR013838. Beta-tubulin_BS.
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

« Hide 'large scale' publications
  1. "Characterization of the alpha-tubulin gene family of Arabidopsis thaliana."
    Ludwig S.R., Oppenheimer D.G., Silflow C.D., Snustad D.P.
    Proc. Natl. Acad. Sci. U.S.A. 84:5833-5837(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 255-450.
    Strain: cv. Columbia.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Root.
  7. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  8. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTBA3_ARATH
AccessioniPrimary (citable) accession number: Q56WH1
Secondary accession number(s): P20363
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: October 3, 2012
Last modified: July 22, 2015
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

There are six genes coding for alpha-tubulin. The sequences coded by genes 3 and 5 are identical.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.