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P05214 (TBA3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:Tuba3a
Synonyms:Tuba3
AND
Name:Tuba3b
Synonyms:Tuba7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

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

Post-translational modification

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.

Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or 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 such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules.

Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling By similarity.

Sequence similarities

Belongs to the tubulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Tubulin alpha-3 chain
PRO_0000048122

Regions

Nucleotide binding142 – 1487GTP Potential

Sites

Site4501Involved in polymerization By similarity

Amino acid modifications

Modified residue481Phosphoserine By similarity
Modified residue831Nitrated tyrosine By similarity
Modified residue2821Nitrated tyrosine By similarity
Modified residue4321Phosphotyrosine By similarity
Modified residue4391Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P05214 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 2A78714CBA782D55

FASTA45049,960
        10         20         30         40         50         60 
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK 

        70         80         90        100        110        120 
HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLVLD 

       130        140        150        160        170        180 
RIRKLADLCT GLQGFLIFHS FGGGTGSGFA SLLMERLSVD YGKKSKLEFA IYPAPQVSTA 

       190        200        210        220        230        240 
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA 

       250        260        270        280        290        300 
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 

       310        320        330        340        350        360 
QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP 

       370        380        390        400        410        420 
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 

       430        440        450 
AREDLAALEK DYEEVGVDSV EAEAEEGEEY 

« Hide

References

« Hide 'large scale' references
[1]"Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-specific expression of two sister genes."
Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.
Mol. Cell. Biol. 6:2409-2419(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]Lubec G., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 230-280, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Hippocampus.
[4]"Tubulin polyglutamylase enzymes are members of the TTL domain protein family."
Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M., Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S., Gaertig J., Edde B.
Science 308:1758-1762(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYGLUTAMYLATION.
[5]"Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYGLYCYLATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13442 mRNA. Translation: AAA40501.1.
M13443 mRNA. Translation: AAA40504.1.
BC050769 mRNA. Translation: AAH50769.1.
BC050770 mRNA. Translation: AAH50770.1.
CCDSCCDS39640.1.
CCDS39707.1.
PIRI77426.
RefSeqNP_033472.1. NM_009446.2.
NP_033475.1. NM_009449.3.
UniGeneMm.270295.
Mm.287784.

3D structure databases

ProteinModelPortalP05214.
SMRP05214. Positions 1-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204374. 2 interactions.
STRING10090.ENSMUSP00000084713.

PTM databases

PhosphoSiteP05214.

2D gel databases

REPRODUCTION-2DPAGEP05214.

Proteomic databases

PRIDEP05214.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000087445; ENSMUSP00000084713; ENSMUSG00000067338.
ENSMUST00000088246; ENSMUSP00000085580; ENSMUSG00000067702.
GeneID22144.
22147.
KEGGmmu:22144.
mmu:22147.
UCSCuc009dui.1. mouse.

Organism-specific databases

CTD22144.
22147.
MGIMGI:1095406. Tuba3a.
MGI:1095408. Tuba3b.

Phylogenomic databases

HOGENOMHOG000165711.
HOVERGENHBG000089.
InParanoidP05214.
KOK07374.
OMAGTERECI.
OrthoDBEOG7TBC1W.
PhylomeDBP05214.
TreeFamTF300314.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_209837. Membrane Trafficking.

Gene expression databases

BgeeP05214.
CleanExMM_TUBA3A.
MM_TUBA3B.
GenevestigatorP05214.

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR002452. 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]
PANTHERPTHR11588. PTHR11588. 1 hit.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio302046.
PROP05214.
SOURCESearch...

Entry information

Entry nameTBA3_MOUSE
AccessionPrimary (citable) accession number: P05214
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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