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Q71U36

- TBA1A_HUMAN

UniProt

Q71U36 - TBA1A_HUMAN

Protein

Tubulin alpha-1A chain

Gene

TUBA1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (05 Jul 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 polymerizationBy similarity

    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
    5. structural molecule activity Source: BHF-UCL

    GO - Biological processi

    1. 'de novo' posttranslational protein folding Source: Reactome
    2. cell division Source: BHF-UCL
    3. cellular protein metabolic process Source: Reactome
    4. cytoskeleton-dependent intracellular transport Source: BHF-UCL
    5. G2/M transition of mitotic cell cycle Source: Reactome
    6. microtubule-based process Source: BHF-UCL
    7. mitotic cell cycle Source: Reactome
    8. protein folding Source: Reactome
    9. protein polymerization Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
    REACT_121399. MHC class II antigen presentation.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
    REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
    REACT_16967. Post-chaperonin tubulin folding pathway.
    REACT_22365. Recycling pathway of L1.
    REACT_25201. Kinesins.
    REACT_682. Mitotic Prometaphase.
    REACT_9509. Gap junction assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin alpha-1A chain
    Alternative name(s):
    Alpha-tubulin 3
    Tubulin B-alpha-1
    Tubulin alpha-3 chain
    Gene namesi
    Name:TUBA1A
    Synonyms:TUBA3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:20766. TUBA1A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic microtubule Source: Ensembl
    2. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. microtubule Source: UniProtKB
    6. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Lissencephaly 3 (LIS3) [MIM:611603]: A classic type lissencephaly associated with psychomotor retardation and seizures. Features include agyria or pachygyria or laminar heterotopia, severe mental retardation, motor delay, variable presence of seizures, and abnormalities of corpus callosum, hippocampus, cerebellar vermis and brainstem.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti188 – 1881I → L in LIS3. 1 Publication
    VAR_039332
    Natural varianti263 – 2631P → T in LIS3. 1 Publication
    VAR_039333
    Natural varianti264 – 2641R → C in LIS3. 1 Publication
    VAR_039334
    Natural varianti286 – 2861L → F in LIS3. 1 Publication
    VAR_039335
    Natural varianti402 – 4021R → C in LIS3. 1 Publication
    VAR_039336
    Natural varianti402 – 4021R → H in LIS3. 1 Publication
    VAR_039337
    Natural varianti419 – 4191S → L in LIS3. 1 Publication
    VAR_039338

    Keywords - Diseasei

    Disease mutation, Lissencephaly

    Organism-specific databases

    MIMi611603. phenotype.
    Orphaneti171680. Lissencephaly due to TUBA1A mutation.
    PharmGKBiPA162407319.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 451451Tubulin alpha-1A chainPRO_0000048111Add
    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 polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation 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 glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules Probable.Curated
    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

    MaxQBiQ71U36.
    PaxDbiQ71U36.
    PRIDEiQ71U36.

    PTM databases

    PhosphoSiteiQ71U36.

    Miscellaneous databases

    PMAP-CutDBQ71U36.

    Expressioni

    Tissue specificityi

    Expressed at a high level in fetal brain.1 Publication

    Gene expression databases

    ArrayExpressiQ71U36.
    BgeeiQ71U36.
    CleanExiHS_TUBA1A.
    GenevestigatoriQ71U36.

    Organism-specific databases

    HPAiCAB008686.
    HPA039247.
    HPA043684.

    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
    CYLDQ9NQC76EBI-302552,EBI-2117940

    Protein-protein interaction databases

    BioGridi113603. 133 interactions.
    DIPiDIP-32773N.
    IntActiQ71U36. 77 interactions.
    MINTiMINT-156132.
    STRINGi9606.ENSP00000301071.

    Structurei

    3D structure databases

    ProteinModelPortaliQ71U36.
    SMRiQ71U36. Positions 1-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    HOGENOMiHOG000165711.
    HOVERGENiHBG000089.
    InParanoidiQ71U36.
    KOiK07374.
    OMAiTRATHEA.
    OrthoDBiEOG7TBC1W.
    PhylomeDBiQ71U36.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q71U36-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « 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 5, 2004 - v1
    Checksum:i00F8429A4A10E5FE
    GO
    Isoform 2 (identifier: Q71U36-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-35: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:416
    Mass (Da):46,297
    Checksum:iBF1E2C9AC0754A68
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1311G → R in CAA25855. (PubMed:3839072)Curated
    Sequence conflicti131 – 1311G → R in AAA91575. (PubMed:6646120)Curated
    Sequence conflicti290 – 2901E → D in AAA91575. (PubMed:6646120)Curated
    Sequence conflicti308 – 3081R → G in CAA25855. (PubMed:3839072)Curated
    Sequence conflicti308 – 3081R → G in AAA91575. (PubMed:6646120)Curated
    Sequence conflicti438 – 4381D → H in CAA25855. (PubMed:3839072)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti188 – 1881I → L in LIS3. 1 Publication
    VAR_039332
    Natural varianti263 – 2631P → T in LIS3. 1 Publication
    VAR_039333
    Natural varianti264 – 2641R → C in LIS3. 1 Publication
    VAR_039334
    Natural varianti286 – 2861L → F in LIS3. 1 Publication
    VAR_039335
    Natural varianti402 – 4021R → C in LIS3. 1 Publication
    VAR_039336
    Natural varianti402 – 4021R → H in LIS3. 1 Publication
    VAR_039337
    Natural varianti419 – 4191S → L in LIS3. 1 Publication
    VAR_039338
    Natural varianti447 – 4471E → K.
    Corresponds to variant rs1065730 [ dbSNP | Ensembl ].
    VAR_034540

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3535Missing in isoform 2. CuratedVSP_046782Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01703 Genomic DNA. Translation: CAA25855.1.
    AF141347 mRNA. Translation: AAD33871.1.
    AK289483 mRNA. Translation: BAF82172.1.
    AC010173 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW58052.1.
    CH471111 Genomic DNA. Translation: EAW58054.1.
    CH471111 Genomic DNA. Translation: EAW58055.1.
    BC006468 mRNA. Translation: AAH06468.1.
    BC050637 mRNA. Translation: AAH50637.1.
    K00557 mRNA. Translation: AAA91575.1.
    CCDSiCCDS58226.1. [Q71U36-2]
    CCDS58227.1. [Q71U36-1]
    CCDS8781.1. [Q71U36-1]
    RefSeqiNP_001257328.1. NM_001270399.1. [Q71U36-1]
    NP_001257329.1. NM_001270400.1. [Q71U36-2]
    NP_006000.2. NM_006009.3. [Q71U36-1]
    UniGeneiHs.654422.

    Genome annotation databases

    EnsembliENST00000295766; ENSP00000439020; ENSG00000167552. [Q71U36-1]
    ENST00000301071; ENSP00000301071; ENSG00000167552. [Q71U36-1]
    ENST00000550767; ENSP00000446637; ENSG00000167552. [Q71U36-2]
    GeneIDi7846.
    KEGGihsa:7846.
    UCSCiuc001rtp.4. human. [Q71U36-1]

    Polymorphism databases

    DMDMi55977864.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01703 Genomic DNA. Translation: CAA25855.1 .
    AF141347 mRNA. Translation: AAD33871.1 .
    AK289483 mRNA. Translation: BAF82172.1 .
    AC010173 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW58052.1 .
    CH471111 Genomic DNA. Translation: EAW58054.1 .
    CH471111 Genomic DNA. Translation: EAW58055.1 .
    BC006468 mRNA. Translation: AAH06468.1 .
    BC050637 mRNA. Translation: AAH50637.1 .
    K00557 mRNA. Translation: AAA91575.1 .
    CCDSi CCDS58226.1. [Q71U36-2 ]
    CCDS58227.1. [Q71U36-1 ]
    CCDS8781.1. [Q71U36-1 ]
    RefSeqi NP_001257328.1. NM_001270399.1. [Q71U36-1 ]
    NP_001257329.1. NM_001270400.1. [Q71U36-2 ]
    NP_006000.2. NM_006009.3. [Q71U36-1 ]
    UniGenei Hs.654422.

    3D structure databases

    ProteinModelPortali Q71U36.
    SMRi Q71U36. Positions 1-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113603. 133 interactions.
    DIPi DIP-32773N.
    IntActi Q71U36. 77 interactions.
    MINTi MINT-156132.
    STRINGi 9606.ENSP00000301071.

    Chemistry

    BindingDBi Q71U36.
    ChEMBLi CHEMBL2095182.

    PTM databases

    PhosphoSitei Q71U36.

    Polymorphism databases

    DMDMi 55977864.

    Proteomic databases

    MaxQBi Q71U36.
    PaxDbi Q71U36.
    PRIDEi Q71U36.

    Protocols and materials databases

    DNASUi 7846.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295766 ; ENSP00000439020 ; ENSG00000167552 . [Q71U36-1 ]
    ENST00000301071 ; ENSP00000301071 ; ENSG00000167552 . [Q71U36-1 ]
    ENST00000550767 ; ENSP00000446637 ; ENSG00000167552 . [Q71U36-2 ]
    GeneIDi 7846.
    KEGGi hsa:7846.
    UCSCi uc001rtp.4. human. [Q71U36-1 ]

    Organism-specific databases

    CTDi 7846.
    GeneCardsi GC12M049578.
    HGNCi HGNC:20766. TUBA1A.
    HPAi CAB008686.
    HPA039247.
    HPA043684.
    MIMi 602529. gene.
    611603. phenotype.
    neXtProti NX_Q71U36.
    Orphaneti 171680. Lissencephaly due to TUBA1A mutation.
    PharmGKBi PA162407319.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5023.
    HOGENOMi HOG000165711.
    HOVERGENi HBG000089.
    InParanoidi Q71U36.
    KOi K07374.
    OMAi TRATHEA.
    OrthoDBi EOG7TBC1W.
    PhylomeDBi Q71U36.
    TreeFami TF300314.

    Enzyme and pathway databases

    Reactomei REACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
    REACT_121399. MHC class II antigen presentation.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
    REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
    REACT_16967. Post-chaperonin tubulin folding pathway.
    REACT_22365. Recycling pathway of L1.
    REACT_25201. Kinesins.
    REACT_682. Mitotic Prometaphase.
    REACT_9509. Gap junction assembly.

    Miscellaneous databases

    ChiTaRSi TUBA1A. human.
    GeneWikii TUBA1A.
    GenomeRNAii 7846.
    NextBioi 30260.
    PMAP-CutDB Q71U36.
    PROi Q71U36.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q71U36.
    Bgeei Q71U36.
    CleanExi HS_TUBA1A.
    Genevestigatori Q71U36.

    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. "Structural features and restricted expression of a human alpha-tubulin gene."
      Hall J.L., Cowan N.J.
      Nucleic Acids Res. 13:207-223(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site."
      Crabtree D.V., Ojima I., Geng X., Adler A.J.
      Bioorg. Med. Chem. 9:1967-1976(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retina.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Cerebellum.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Muscle and Skin.
    7. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 85-105; 113-121; 157-163; 216-304; 312-320; 327-336; 340-352; 374-390; 395-401 AND 403-430, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    8. "Expression of human alpha-tubulin genes: interspecies conservation of 3' untranslated regions."
      Cowan N.J., Dobner P., Fuchs E.V., Cleveland D.W.
      Mol. Cell. Biol. 3:1738-1745(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-451.
      Tissue: Fetal brain.
    9. Cited for: TISSUE SPECIFICITY, VARIANTS LIS3 LEU-188; THR-263; CYS-264; PHE-286; HIS-402; CYS-402 AND LEU-419.
    10. "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: GLYCYLATION.

    Entry informationi

    Entry nameiTBA1A_HUMAN
    AccessioniPrimary (citable) accession number: Q71U36
    Secondary accession number(s): A8K0B8
    , G3V1U9, P04687, P05209
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3