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Q13748

- TBA3C_HUMAN

UniProt

Q13748 - TBA3C_HUMAN

Protein

Tubulin alpha-3C/D chain

Gene

TUBA3C

more
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (02 May 2002)
      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
    Sitei450 – 4501Involved 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. 'de novo' posttranslational protein folding Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. microtubule-based process Source: InterPro
    4. protein folding Source: Reactome
    5. 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_15510. Recruitment of NuMA to mitotic centrosomes.
    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-3C/D chain
    Alternative name(s):
    Alpha-tubulin 2
    Alpha-tubulin 3C/D
    Tubulin alpha-2 chain
    Gene namesi
    Name:TUBA3C
    Synonyms:TUBA2
    AND
    Name:TUBA3D
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:12408. TUBA3C.
    HGNC:24071. TUBA3D.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. microtubule Source: UniProtKB-KW
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162407346.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 450450Tubulin alpha-3C/D chainPRO_0000048110Add
    BLAST

    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

    Proteomic databases

    MaxQBiQ13748.
    PRIDEiQ13748.

    PTM databases

    PhosphoSiteiQ13748.

    Miscellaneous databases

    PMAP-CutDBQ13748.

    Expressioni

    Tissue specificityi

    Testis specific.1 Publication

    Gene expression databases

    ArrayExpressiQ13748.
    BgeeiQ13748.
    CleanExiHS_TUBA3C.
    HS_TUBA3D.
    GenevestigatoriQ13748.

    Organism-specific databases

    HPAiCAB004972.
    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
    NMIQ132872EBI-355068,EBI-372942

    Protein-protein interaction databases

    BioGridi113129. 20 interactions.
    125248. 7 interactions.
    DIPiDIP-34513N.
    IntActiQ13748. 10 interactions.
    MINTiMINT-1157262.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13748.
    SMRiQ13748. Positions 1-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    HOGENOMiHOG000165711.
    HOVERGENiHBG000089.
    InParanoidiQ13748.
    KOiK07374.
    OMAiGTERECI.
    OrthoDBiEOG7TBC1W.
    PhylomeDBiQ13748.
    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: Q13748-1) [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 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:May 2, 2002 - v3
    Checksum:i2A78714CBA782D55
    GO
    Isoform 2 (identifier: Q13748-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         393-424: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:418
    Mass (Da):46,112
    Checksum:iB103B8C73F95D81B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti305 – 3051C → Y in AAH57810. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti75 – 751V → L.
    Corresponds to variant rs36215077 [ dbSNP | Ensembl ].
    VAR_034541
    Natural varianti392 – 3921D → V.
    Corresponds to variant rs17076703 [ dbSNP | Ensembl ].
    VAR_052666
    Natural varianti440 – 4401V → M.
    Corresponds to variant rs1803092 [ dbSNP | Ensembl ].
    VAR_022068

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei393 – 42432Missing in isoform 2. 1 PublicationVSP_006678Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005392 Genomic DNA. Translation: AAC39578.1.
    AL139327 Genomic DNA. Translation: CAH73534.1.
    CH471075 Genomic DNA. Translation: EAX08210.1.
    BC011721 mRNA. Translation: AAH11721.1.
    BC057810 mRNA. Translation: AAH57810.1.
    L11645 mRNA. Translation: AAA35521.1.
    CCDSiCCDS33290.1. [Q13748-1]
    CCDS9284.1. [Q13748-1]
    RefSeqiNP_005992.1. NM_006001.2. [Q13748-1]
    NP_525125.2. NM_080386.3. [Q13748-1]
    UniGeneiHs.349695.
    Hs.503749.

    Genome annotation databases

    EnsembliENST00000321253; ENSP00000326042; ENSG00000075886. [Q13748-1]
    ENST00000400113; ENSP00000382982; ENSG00000198033. [Q13748-1]
    GeneIDi113457.
    7278.
    KEGGihsa:113457.
    hsa:7278.
    UCSCiuc002tsu.4. human. [Q13748-1]

    Polymorphism databases

    DMDMi20455316.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Tubulin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005392 Genomic DNA. Translation: AAC39578.1 .
    AL139327 Genomic DNA. Translation: CAH73534.1 .
    CH471075 Genomic DNA. Translation: EAX08210.1 .
    BC011721 mRNA. Translation: AAH11721.1 .
    BC057810 mRNA. Translation: AAH57810.1 .
    L11645 mRNA. Translation: AAA35521.1 .
    CCDSi CCDS33290.1. [Q13748-1 ]
    CCDS9284.1. [Q13748-1 ]
    RefSeqi NP_005992.1. NM_006001.2. [Q13748-1 ]
    NP_525125.2. NM_080386.3. [Q13748-1 ]
    UniGenei Hs.349695.
    Hs.503749.

    3D structure databases

    ProteinModelPortali Q13748.
    SMRi Q13748. Positions 1-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113129. 20 interactions.
    125248. 7 interactions.
    DIPi DIP-34513N.
    IntActi Q13748. 10 interactions.
    MINTi MINT-1157262.

    Chemistry

    ChEMBLi CHEMBL2095182.

    PTM databases

    PhosphoSitei Q13748.

    Polymorphism databases

    DMDMi 20455316.

    Proteomic databases

    MaxQBi Q13748.
    PRIDEi Q13748.

    Protocols and materials databases

    DNASUi 113457.
    7278.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321253 ; ENSP00000326042 ; ENSG00000075886 . [Q13748-1 ]
    ENST00000400113 ; ENSP00000382982 ; ENSG00000198033 . [Q13748-1 ]
    GeneIDi 113457.
    7278.
    KEGGi hsa:113457.
    hsa:7278.
    UCSCi uc002tsu.4. human. [Q13748-1 ]

    Organism-specific databases

    CTDi 113457.
    7278.
    GeneCardsi GC02P132233.
    GC13M019747.
    H-InvDB HIX0002464.
    HIX0011150.
    HGNCi HGNC:12408. TUBA3C.
    HGNC:24071. TUBA3D.
    HPAi CAB004972.
    HPA039247.
    HPA043684.
    MIMi 602528. gene.
    neXtProti NX_Q13748.
    PharmGKBi PA162407346.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000165711.
    HOVERGENi HBG000089.
    InParanoidi Q13748.
    KOi K07374.
    OMAi GTERECI.
    OrthoDBi EOG7TBC1W.
    PhylomeDBi Q13748.
    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_15510. Recruitment of NuMA to mitotic centrosomes.
    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

    GeneWikii Alpha-tubulin_3C.
    NextBioi 28463.
    PMAP-CutDB Q13748.
    PROi Q13748.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13748.
    Bgeei Q13748.
    CleanExi HS_TUBA3C.
    HS_TUBA3D.
    Genevestigatori Q13748.

    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. "Sequence characterization of a newly identified human alpha-tubulin gene (TUBA2)."
      Dode C., Weil D., Levilliers J., Crozet F., Chaib H., Levi-Acobas F., Guilford P., Petit C.
      Genomics 47:125-130(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    2. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Skin and Testis.
    5. "The alpha-tubulin gene on chromosome 13 (TUBA2) encodes a testis-specific isotype."
      Bonaldo M., Su L., Lawton L.N., Soares M.B.
      Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 352-449 (ISOFORM 1), TISSUE SPECIFICITY.
    6. "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 nameiTBA3C_HUMAN
    AccessioniPrimary (citable) accession number: Q13748
    Secondary accession number(s): A6NJQ0
    , Q5W099, Q6PEY3, Q96F18
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: May 2, 2002
    Last modified: October 1, 2014
    This is version 148 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3