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P05213

- TBA1B_MOUSE

UniProt

P05213 - TBA1B_MOUSE

Protein

Tubulin alpha-1B chain

Gene

Tuba1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (23 Nov 2004)
      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. double-stranded RNA binding Source: MGI
    2. GTPase activity Source: InterPro
    3. GTP binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. structural constituent of cytoskeleton Source: MGI

    GO - Biological processi

    1. cellular response to interleukin-4 Source: MGI
    2. microtubule cytoskeleton organization Source: MGI
    3. protein folding Source: Reactome
    4. protein polymerization Source: InterPro

    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

    Protein namesi
    Recommended name:
    Tubulin alpha-1B chain
    Alternative name(s):
    Alpha-tubulin 2
    Alpha-tubulin isotype M-alpha-2
    Tubulin alpha-2 chain
    Gene namesi
    Name:Tuba1b
    Synonyms:Tuba2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:107804. Tuba1b.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic microtubule Source: MGI
    2. cytosol Source: Reactome
    3. microtubule Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 451451Tubulin alpha-1B chainPRO_0000048121Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481PhosphoserineBy similarity
    Modified residuei83 – 831Nitrated tyrosineBy similarity
    Modified residuei232 – 2321PhosphoserineBy similarity
    Modified residuei282 – 2821Nitrated tyrosineBy similarity
    Cross-linki326 – 326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei339 – 3391Omega-N-methylarginineBy similarity
    Cross-linki370 – 370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By 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, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP05213.
    PaxDbiP05213.
    PRIDEiP05213.

    2D gel databases

    REPRODUCTION-2DPAGEP05213.

    PTM databases

    PhosphoSiteiP05213.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with highest levels in spleen, thymus and immature brain.

    Gene expression databases

    BgeeiP05213.
    CleanExiMM_TUBA1B.
    GenevestigatoriP05213.

    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

    BioGridi204373. 18 interactions.
    IntActiP05213. 14 interactions.
    MINTiMINT-1869669.

    Structurei

    3D structure databases

    ProteinModelPortaliP05213.
    SMRiP05213. Positions 1-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    GeneTreeiENSGT00750000117333.
    HOGENOMiHOG000165711.
    HOVERGENiHBG000089.
    InParanoidiP05213.
    KOiK07374.
    OMAiCVRARTI.
    OrthoDBiEOG7TBC1W.
    PhylomeDBiP05213.
    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.

    P05213-1 [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 ISQIVSSITA SLRFDGALNV 250
    DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 300
    QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG 350
    FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA 400
    KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE 450
    Y 451
    Length:451
    Mass (Da):50,152
    Last modified:November 23, 2004 - v2
    Checksum:i94355B4EC2086429
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551E → G in BAE30708. (PubMed:16141072)Curated
    Sequence conflicti55 – 551E → G in BAE31107. (PubMed:16141072)Curated
    Sequence conflicti114 – 1141I → T in BAE34741. (PubMed:16141072)Curated
    Sequence conflicti119 – 1191L → P in BAE29999. (PubMed:16141072)Curated
    Sequence conflicti119 – 1191L → P in BAE30196. (PubMed:16141072)Curated
    Sequence conflicti135 – 1362FL → LF in AAA40507. (PubMed:3839797)Curated
    Sequence conflicti340 – 3401S → T(PubMed:3785200)Curated
    Sequence conflicti340 – 3401S → T in AAA40507. (PubMed:3839797)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13446 mRNA. Translation: AAA40500.1.
    AK075955 mRNA. Translation: BAC36080.1.
    AK137885 mRNA. Translation: BAE23512.1.
    AK150128 mRNA. Translation: BAE29327.1.
    AK150179 mRNA. Translation: BAE29362.1.
    AK150968 mRNA. Translation: BAE29999.1.
    AK151199 mRNA. Translation: BAE30196.1.
    AK151809 mRNA. Translation: BAE30708.1.
    AK152298 mRNA. Translation: BAE31107.1.
    AK153064 mRNA. Translation: BAE31690.1.
    AK153254 mRNA. Translation: BAE31845.1.
    AK158958 mRNA. Translation: BAE34741.1.
    AK164428 mRNA. Translation: BAE37783.1.
    AK168770 mRNA. Translation: BAE40606.1.
    AK169075 mRNA. Translation: BAE40860.1.
    AK169092 mRNA. Translation: BAE40875.1.
    AK169130 mRNA. Translation: BAE40909.1.
    AK169665 mRNA. Translation: BAE41287.1.
    BC002219 mRNA. Translation: AAH02219.1.
    BC008117 mRNA. Translation: AAH08117.1.
    BC063777 mRNA. Translation: AAH63777.1.
    BC083120 mRNA. Translation: AAH83120.1.
    BC098321 mRNA. Translation: AAH98321.1.
    BC108337 mRNA. Translation: AAI08338.1.
    BC108394 mRNA. Translation: AAI08395.1.
    M28727 mRNA. Translation: AAA40507.1.
    CCDSiCCDS37195.1.
    PIRiI77425.
    S29013. A61275.
    RefSeqiNP_035784.1. NM_011654.2.
    UniGeneiMm.392113.
    Mm.491454.

    Genome annotation databases

    EnsembliENSMUST00000077577; ENSMUSP00000076777; ENSMUSG00000023004.
    GeneIDi22143.
    KEGGimmu:22143.
    UCSCiuc007xoj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13446 mRNA. Translation: AAA40500.1 .
    AK075955 mRNA. Translation: BAC36080.1 .
    AK137885 mRNA. Translation: BAE23512.1 .
    AK150128 mRNA. Translation: BAE29327.1 .
    AK150179 mRNA. Translation: BAE29362.1 .
    AK150968 mRNA. Translation: BAE29999.1 .
    AK151199 mRNA. Translation: BAE30196.1 .
    AK151809 mRNA. Translation: BAE30708.1 .
    AK152298 mRNA. Translation: BAE31107.1 .
    AK153064 mRNA. Translation: BAE31690.1 .
    AK153254 mRNA. Translation: BAE31845.1 .
    AK158958 mRNA. Translation: BAE34741.1 .
    AK164428 mRNA. Translation: BAE37783.1 .
    AK168770 mRNA. Translation: BAE40606.1 .
    AK169075 mRNA. Translation: BAE40860.1 .
    AK169092 mRNA. Translation: BAE40875.1 .
    AK169130 mRNA. Translation: BAE40909.1 .
    AK169665 mRNA. Translation: BAE41287.1 .
    BC002219 mRNA. Translation: AAH02219.1 .
    BC008117 mRNA. Translation: AAH08117.1 .
    BC063777 mRNA. Translation: AAH63777.1 .
    BC083120 mRNA. Translation: AAH83120.1 .
    BC098321 mRNA. Translation: AAH98321.1 .
    BC108337 mRNA. Translation: AAI08338.1 .
    BC108394 mRNA. Translation: AAI08395.1 .
    M28727 mRNA. Translation: AAA40507.1 .
    CCDSi CCDS37195.1.
    PIRi I77425.
    S29013. A61275.
    RefSeqi NP_035784.1. NM_011654.2.
    UniGenei Mm.392113.
    Mm.491454.

    3D structure databases

    ProteinModelPortali P05213.
    SMRi P05213. Positions 1-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204373. 18 interactions.
    IntActi P05213. 14 interactions.
    MINTi MINT-1869669.

    PTM databases

    PhosphoSitei P05213.

    2D gel databases

    REPRODUCTION-2DPAGE P05213.

    Proteomic databases

    MaxQBi P05213.
    PaxDbi P05213.
    PRIDEi P05213.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000077577 ; ENSMUSP00000076777 ; ENSMUSG00000023004 .
    GeneIDi 22143.
    KEGGi mmu:22143.
    UCSCi uc007xoj.1. mouse.

    Organism-specific databases

    CTDi 10376.
    MGIi MGI:107804. Tuba1b.

    Phylogenomic databases

    eggNOGi COG5023.
    GeneTreei ENSGT00750000117333.
    HOGENOMi HOG000165711.
    HOVERGENi HBG000089.
    InParanoidi P05213.
    KOi K07374.
    OMAi CVRARTI.
    OrthoDBi EOG7TBC1W.
    PhylomeDBi P05213.
    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 302042.
    PROi P05213.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05213.
    CleanExi MM_TUBA1B.
    Genevestigatori P05213.

    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].
    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 and NOD.
      Tissue: Amnion, Bone marrow, Eye, Kidney, Liver, Thymus and Visual cortex.
    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/6J, Czech II and FVB/N.
      Tissue: Limb, Mammary tumor, Olfactory epithelium and Salivary gland.
    4. Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-163; 216-304; 312-320; 327-336; 340-370; 374-390; 395-401 AND 403-432, 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 100-451.
    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 nameiTBA1B_MOUSE
    AccessioniPrimary (citable) accession number: P05213
    Secondary accession number(s): Q3TY23
    , Q3U8B1, Q3UAW8, Q4KMW2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 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