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Protein

Tubulin alpha-3 chain

Gene

Tuba3a

more
Organism
Mus musculus (Mouse)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei450Involved in polymerizationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi142 – 148GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1445148. Translocation of GLUT4 to the plasma membrane.
R-MMU-5610787. Hedgehog 'off' state.
R-MMU-5620924. Intraflagellar transport.
R-MMU-5632684. Hedgehog 'on' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-3 chain
Alternative name(s):
Alpha-tubulin 3/7
Alpha-tubulin isotype M-alpha-3/7
Tubulin alpha-3/alpha-7 chain
Cleaved into the following chain:
Gene namesi
Name:Tuba3a
Synonyms:Tuba3
AND
Name:Tuba3b
Synonyms:Tuba7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1095406. Tuba3a.
MGI:1095408. Tuba3b.

Subcellular locationi

GO - Cellular componenti

  • ciliary basal body Source: MGI
  • cilium Source: MGI
  • cytoplasm Source: UniProtKB-KW
  • microtubule Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000481221 – 450Tubulin alpha-3 chainAdd BLAST450
ChainiPRO_00004374011 – 449Detyrosinated tubulin alpha-3 chain2 PublicationsAdd BLAST449

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6-acetyllysineBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei83Nitrated tyrosineBy similarity1
Modified residuei432PhosphotyrosineBy similarity1
Modified residuei439PhosphoserineBy similarity1
Modified residuei4503'-nitrotyrosineBy similarity1

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear.1 Publication
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity).By similarity1 Publication
Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly.By similarity
Nitration of Tyr-450 is irreversible and interferes with normal dynein intracellular distribution.By similarity
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.4 Publications
Tubulin alpha-3 chain: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (PubMed:16954346, PubMed:19564401). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).By similarity2 Publications
Detyrosinated tubulin alpha-3 chain: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle (PubMed:26446751). In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (PubMed:27102488).By similarity2 Publications

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

PaxDbiP05214.
PeptideAtlasiP05214.
PRIDEiP05214.

2D gel databases

REPRODUCTION-2DPAGEP05214.

PTM databases

iPTMnetiP05214.
PhosphoSitePlusiP05214.

Expressioni

Tissue specificityi

Alpha-3 and alpha-7 are identical but coded by two different genes, they are testis-specific.1 Publication

Gene expression databases

BgeeiENSMUSG00000067338.
CleanExiMM_TUBA3A.
MM_TUBA3B.
ExpressionAtlasiP05214. baseline and differential.
GenevisibleiP05214. MM.

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

BioGridi204374. 70 interactors.
IntActiP05214. 69 interactors.
STRINGi10090.ENSMUSP00000085580.

Structurei

3D structure databases

ProteinModelPortaliP05214.
SMRiP05214.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP05214.
KOiK07374.
OMAiXERECIS.
OrthoDBiEOG091G0736.
PhylomeDBiP05214.
TreeFamiTF300314.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN
60 70 80 90 100
TFFSETGAGK HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIVDLVLD RIRKLADLCT GLQGFLIFHS FGGGTGSGFA
160 170 180 190 200
SLLMERLSVD YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGVDSV EAEAEEGEEY
Length:450
Mass (Da):49,960
Last modified:August 13, 1987 - v1
Checksum:i2A78714CBA782D55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13442 mRNA. Translation: AAA40501.1.
M13443 mRNA. Translation: AAA40504.1.
BC050769 mRNA. Translation: AAH50769.1.
BC050770 mRNA. Translation: AAH50770.1.
CCDSiCCDS39640.1.
CCDS39707.1.
PIRiI77426.
RefSeqiNP_033472.1. NM_009446.2.
NP_033475.1. NM_009449.3.
UniGeneiMm.270295.
Mm.287784.

Genome annotation databases

EnsembliENSMUST00000087445; ENSMUSP00000084713; ENSMUSG00000067338.
ENSMUST00000088246; ENSMUSP00000085580; ENSMUSG00000067702.
GeneIDi22144.
22147.
KEGGimmu:22144.
mmu:22147.
UCSCiuc009dui.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13442 mRNA. Translation: AAA40501.1.
M13443 mRNA. Translation: AAA40504.1.
BC050769 mRNA. Translation: AAH50769.1.
BC050770 mRNA. Translation: AAH50770.1.
CCDSiCCDS39640.1.
CCDS39707.1.
PIRiI77426.
RefSeqiNP_033472.1. NM_009446.2.
NP_033475.1. NM_009449.3.
UniGeneiMm.270295.
Mm.287784.

3D structure databases

ProteinModelPortaliP05214.
SMRiP05214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204374. 70 interactors.
IntActiP05214. 69 interactors.
STRINGi10090.ENSMUSP00000085580.

PTM databases

iPTMnetiP05214.
PhosphoSitePlusiP05214.

2D gel databases

REPRODUCTION-2DPAGEP05214.

Proteomic databases

PaxDbiP05214.
PeptideAtlasiP05214.
PRIDEiP05214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087445; ENSMUSP00000084713; ENSMUSG00000067338.
ENSMUST00000088246; ENSMUSP00000085580; ENSMUSG00000067702.
GeneIDi22144.
22147.
KEGGimmu:22144.
mmu:22147.
UCSCiuc009dui.1. mouse.

Organism-specific databases

CTDi22144.
22147.
MGIiMGI:1095406. Tuba3a.
MGI:1095408. Tuba3b.

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP05214.
KOiK07374.
OMAiXERECIS.
OrthoDBiEOG091G0736.
PhylomeDBiP05214.
TreeFamiTF300314.

Enzyme and pathway databases

ReactomeiR-MMU-1445148. Translocation of GLUT4 to the plasma membrane.
R-MMU-5610787. Hedgehog 'off' state.
R-MMU-5620924. Intraflagellar transport.
R-MMU-5632684. Hedgehog 'on' state.

Miscellaneous databases

ChiTaRSiTuba3a. mouse.
PROiP05214.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000067338.
CleanExiMM_TUBA3A.
MM_TUBA3B.
ExpressionAtlasiP05214. baseline and differential.
GenevisibleiP05214. MM.

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 nameiTBA3_MOUSE
AccessioniPrimary (citable) accession number: P05214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 2, 2016
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.