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P05214

- TBA3_MOUSE

UniProt

P05214 - TBA3_MOUSE

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Protein

Tubulin alpha-3 chain

Gene
Tuba3a, Tuba3
Tuba3b, Tuba7
Organism
Mus musculus (Mouse)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei450 – 4501Involved in polymerization By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTP Reviewed prediction

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. microtubule-based process Source: InterPro
  2. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_199117. Kinesins.
REACT_207679. Separation of Sister Chromatids.
REACT_218773. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_227366. Gap junction assembly.

Names & Taxonomyi

Organism-specific databases

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
Gene namesi
Name:Tuba3a
Synonyms:Tuba3
AND
Name:Tuba3b
Synonyms:Tuba7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6
MGIiMGI:1095406. Tuba3a.
MGI:1095408. Tuba3b.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. microtubule Source: UniProtKB-KW

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Tubulin alpha-3 chainPRO_0000048122Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphoserine By similarity
Modified residuei83 – 831Nitrated tyrosine By similarity
Modified residuei282 – 2821Nitrated tyrosine By similarity
Modified residuei432 – 4321Phosphotyrosine By similarity
Modified residuei439 – 4391Phosphoserine By similarity

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.
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.

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

PRIDEiP05214.

2D gel databases

REPRODUCTION-2DPAGEP05214.

PTM databases

PhosphoSiteiP05214.

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

BgeeiP05214.
CleanExiMM_TUBA3A.
MM_TUBA3B.
GenevestigatoriP05214.

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. 2 interactions.
STRINGi10090.ENSMUSP00000084713.

Structurei

3D structure databases

ProteinModelPortaliP05214.
SMRiP05214. Positions 1-440.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.

Phylogenomic databases

HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP05214.
KOiK07374.
OMAiGTERECI.
OrthoDBiEOG7TBC1W.
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.

P05214-1 [UniParc]FASTAAdd to Basket

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MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN    50
TFFSETGAGK HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA 100
NNYARGHYTI GKEIVDLVLD RIRKLADLCT GLQGFLIFHS FGGGTGSGFA 150
SLLMERLSVD YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC 200
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV 250
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 300
QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG 350
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA 400
KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGVDSV EAEAEEGEEY 450
Length:450
Mass (Da):49,960
Last modified:August 13, 1987 - v1
Checksum:i2A78714CBA782D55
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M13442 mRNA. Translation: AAA40501.1 .
M13443 mRNA. Translation: AAA40504.1 .
BC050769 mRNA. Translation: AAH50769.1 .
BC050770 mRNA. Translation: AAH50770.1 .
CCDSi CCDS39640.1.
CCDS39707.1.
PIRi I77426.
RefSeqi NP_033472.1. NM_009446.2.
NP_033475.1. NM_009449.3.
UniGenei Mm.270295.
Mm.287784.

3D structure databases

ProteinModelPortali P05214.
SMRi P05214. Positions 1-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204374. 2 interactions.
STRINGi 10090.ENSMUSP00000084713.

PTM databases

PhosphoSitei P05214.

2D gel databases

REPRODUCTION-2DPAGE P05214.

Proteomic databases

PRIDEi P05214.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000087445 ; ENSMUSP00000084713 ; ENSMUSG00000067338 .
ENSMUST00000088246 ; ENSMUSP00000085580 ; ENSMUSG00000067702 .
GeneIDi 22144.
22147.
KEGGi mmu:22144.
mmu:22147.
UCSCi uc009dui.1. mouse.

Organism-specific databases

CTDi 22144.
22147.
MGIi MGI:1095406. Tuba3a.
MGI:1095408. Tuba3b.

Phylogenomic databases

HOGENOMi HOG000165711.
HOVERGENi HBG000089.
InParanoidi P05214.
KOi K07374.
OMAi GTERECI.
OrthoDBi EOG7TBC1W.
PhylomeDBi P05214.
TreeFami TF300314.

Enzyme and pathway databases

Reactomei REACT_196550. MHC class II antigen presentation.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_199117. Kinesins.
REACT_207679. Separation of Sister Chromatids.
REACT_218773. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_227366. Gap junction assembly.

Miscellaneous databases

NextBioi 302046.
PROi P05214.
SOURCEi Search...

Gene expression databases

Bgeei P05214.
CleanExi MM_TUBA3A.
MM_TUBA3B.
Genevestigatori P05214.

Family and domain databases

Gene3Di 1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProi IPR002452. 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 ]
PANTHERi PTHR11588. PTHR11588. 1 hit.
Pfami PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view ]
PRINTSi PR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTi SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEi PS00227. TUBULIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.

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: September 3, 2014
This is version 132 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

External Data

Dasty 3

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