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P68369

- TBA1A_MOUSE

UniProt

P68369 - TBA1A_MOUSE

Protein

Tubulin alpha-1A chain

Gene

Tuba1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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
    Sitei451 – 4511Involved in polymerization

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196550. MHC class II antigen presentation.
    REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    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

    Protein namesi
    Recommended name:
    Tubulin alpha-1A chain
    Alternative name(s):
    Alpha-tubulin 1
    Alpha-tubulin isotype M-alpha-1
    Tubulin alpha-1 chain
    Gene namesi
    Name:Tuba1a
    Synonyms:Tuba1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:98869. Tuba1a.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic microtubule Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 451451Tubulin alpha-1A chainPRO_0000048120Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481PhosphoserineBy similarity
    Modified residuei83 – 831Nitrated tyrosineBy similarity
    Modified residuei282 – 2821Nitrated tyrosineBy similarity
    Modified residuei432 – 4321PhosphotyrosineBy similarity
    Modified residuei439 – 4391PhosphoserineBy 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.By similarity

    Keywords - PTMi

    Acetylation, Nitration, Phosphoprotein

    Proteomic databases

    MaxQBiP68369.
    PaxDbiP68369.
    PRIDEiP68369.

    2D gel databases

    SWISS-2DPAGEP68369.

    PTM databases

    PhosphoSiteiP68369.

    Miscellaneous databases

    PMAP-CutDBP68369.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, although primarily in lung and brain.1 Publication

    Gene expression databases

    BgeeiP68369.
    CleanExiMM_TUBA1A.
    GenevestigatoriP68369.

    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CyldQ80TQ25EBI-400542,EBI-943859

    Protein-protein interaction databases

    BioGridi204372. 29 interactions.
    IntActiP68369. 18 interactions.
    MINTiMINT-3288915.
    STRINGi10090.ENSMUSP00000094778.

    Structurei

    3D structure databases

    ProteinModelPortaliP68369.
    SMRiP68369. Positions 1-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    GeneTreeiENSGT00750000117333.
    HOVERGENiHBG000089.
    InParanoidiP68369.
    KOiK07374.
    OMAiTRATHEA.
    OrthoDBiEOG7TBC1W.
    PhylomeDBiP68369.
    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.

    P68369-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN    50
    TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA 100
    NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT 150
    SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC 200
    AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV 250
    DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 300
    QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG 350
    FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA 400
    KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE 450
    Y 451
    Length:451
    Mass (Da):50,136
    Last modified:July 21, 1986 - v1
    Checksum:i00F8429A4A10E5FE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241K → E in BAE40598. (PubMed:16141072)Curated
    Sequence conflicti132 – 1321L → P in BAE26417. (PubMed:16141072)Curated
    Sequence conflicti257 – 2571T → I in BAE37745. (PubMed:16141072)Curated
    Sequence conflicti273 – 2731A → S in AAH83344. (PubMed:15489334)Curated
    Sequence conflicti328 – 3281V → G in BAE26417. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13445 mRNA. Translation: AAA40499.1.
    AK077529 mRNA. Translation: BAC36848.1.
    AK145404 mRNA. Translation: BAE26417.1.
    AK146983 mRNA. Translation: BAE27586.1.
    AK164335 mRNA. Translation: BAE37745.1.
    AK167687 mRNA. Translation: BAE39734.1.
    AK168762 mRNA. Translation: BAE40598.1.
    AK169610 mRNA. Translation: BAE41258.1.
    BC056169 mRNA. Translation: AAH56169.1.
    BC083343 mRNA. Translation: AAH83343.1.
    BC083345 mRNA. Translation: AAH83345.1.
    BC085256 mRNA. Translation: AAH85256.1.
    M28729 mRNA. Translation: AAA40506.1.
    BC083344 mRNA. Translation: AAH83344.1.
    CCDSiCCDS37196.1.
    PIRiI77424.
    RefSeqiNP_035783.1. NM_011653.2.
    UniGeneiMm.405359.

    Genome annotation databases

    EnsembliENSMUST00000097014; ENSMUSP00000094778; ENSMUSG00000072235.
    GeneIDi22142.
    KEGGimmu:22142.
    UCSCiuc007xok.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13445 mRNA. Translation: AAA40499.1 .
    AK077529 mRNA. Translation: BAC36848.1 .
    AK145404 mRNA. Translation: BAE26417.1 .
    AK146983 mRNA. Translation: BAE27586.1 .
    AK164335 mRNA. Translation: BAE37745.1 .
    AK167687 mRNA. Translation: BAE39734.1 .
    AK168762 mRNA. Translation: BAE40598.1 .
    AK169610 mRNA. Translation: BAE41258.1 .
    BC056169 mRNA. Translation: AAH56169.1 .
    BC083343 mRNA. Translation: AAH83343.1 .
    BC083345 mRNA. Translation: AAH83345.1 .
    BC085256 mRNA. Translation: AAH85256.1 .
    M28729 mRNA. Translation: AAA40506.1 .
    BC083344 mRNA. Translation: AAH83344.1 .
    CCDSi CCDS37196.1.
    PIRi I77424.
    RefSeqi NP_035783.1. NM_011653.2.
    UniGenei Mm.405359.

    3D structure databases

    ProteinModelPortali P68369.
    SMRi P68369. Positions 1-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204372. 29 interactions.
    IntActi P68369. 18 interactions.
    MINTi MINT-3288915.
    STRINGi 10090.ENSMUSP00000094778.

    Chemistry

    BindingDBi P68369.

    PTM databases

    PhosphoSitei P68369.

    2D gel databases

    SWISS-2DPAGE P68369.

    Proteomic databases

    MaxQBi P68369.
    PaxDbi P68369.
    PRIDEi P68369.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000097014 ; ENSMUSP00000094778 ; ENSMUSG00000072235 .
    GeneIDi 22142.
    KEGGi mmu:22142.
    UCSCi uc007xok.1. mouse.

    Organism-specific databases

    CTDi 7846.
    MGIi MGI:98869. Tuba1a.

    Phylogenomic databases

    eggNOGi COG5023.
    GeneTreei ENSGT00750000117333.
    HOVERGENi HBG000089.
    InParanoidi P68369.
    KOi K07374.
    OMAi TRATHEA.
    OrthoDBi EOG7TBC1W.
    PhylomeDBi P68369.
    TreeFami TF300314.

    Enzyme and pathway databases

    Reactomei REACT_196550. MHC class II antigen presentation.
    REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    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

    ChiTaRSi TUBA1A. mouse.
    NextBioi 302038.
    PMAP-CutDB P68369.
    PROi P68369.
    SOURCEi Search...

    Gene expression databases

    Bgeei P68369.
    CleanExi MM_TUBA1A.
    Genevestigatori P68369.

    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 transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Heart, Kidney, Placenta, Spinal ganglion and Thymus.
    3. "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].
      Strain: C57BL/6.
      Tissue: Brain and Olfactory epithelium.
    4. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-163; 216-280; 312-320; 327-336; 340-370; 374-401 AND 403-440, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    5. "Five mouse tubulin isotypes and their regulated expression during development."
      Lewis S.A., Lee M.G.-S., Cowan N.J.
      J. Cell Biol. 101:852-861(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 254-451.
    6. Cited for: POLYGLUTAMYLATION.
    7. "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 nameiTBA1A_MOUSE
    AccessioniPrimary (citable) accession number: P68369
    Secondary accession number(s): P02551
    , P05210, P05212, Q3TGF0, Q3TIW2, Q3TPJ1, Q3ULN1, Q5XJF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 108 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