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Q9BQE3

- TBA1C_HUMAN

UniProt

Q9BQE3 - TBA1C_HUMAN

Protein

Tubulin alpha-1C chain

Gene

TUBA1C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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
    Sitei449 – 4491Involved 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: UniProt
    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. microtubule-based process Source: BHF-UCL
    6. protein folding Source: Reactome
    7. 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-1C chain
    Alternative name(s):
    Alpha-tubulin 6
    Tubulin alpha-6 chain
    Gene namesi
    Name:TUBA1C
    Synonyms:TUBA6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:20768. TUBA1C.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic microtubule Source: Ensembl
    2. microtubule Source: BHF-UCL
    3. nucleus Source: UniProt
    4. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162407345.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 449449Tubulin alpha-1C chainPRO_0000048112Add
    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 – 4321Phosphotyrosine1 Publication
    Modified residuei439 – 4391Phosphoserine6 Publications

    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

    MaxQBiQ9BQE3.
    PRIDEiQ9BQE3.

    2D gel databases

    REPRODUCTION-2DPAGEQ9BQE3.

    PTM databases

    PhosphoSiteiQ9BQE3.

    Miscellaneous databases

    PMAP-CutDBQ9BQE3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BQE3.
    BgeeiQ9BQE3.
    CleanExiHS_TUBA1C.
    GenevestigatoriQ9BQE3.

    Organism-specific databases

    HPAiHPA039247.
    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.

    Protein-protein interaction databases

    BioGridi124259. 67 interactions.
    IntActiQ9BQE3. 46 interactions.
    MINTiMINT-3060519.
    STRINGi9606.ENSP00000301072.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BQE3.
    SMRiQ9BQE3. Positions 1-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    HOVERGENiHBG000089.
    InParanoidiQ9BQE3.
    KOiK07374.
    PhylomeDBiQ9BQE3.
    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.

    Q9BQE3-1 [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 AYHEQLTVAE ITNACFEPAN 300
    QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG 350
    FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAVAEAWAR LDHKFDLMYA 400
    KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGADSA DGEDEGEEY 449
    Length:449
    Mass (Da):49,895
    Last modified:June 1, 2001 - v1
    Checksum:i0CFE7212CB5E14F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC004949 mRNA. Translation: AAH04949.1.
    BC005946 mRNA. Translation: AAH05946.1.
    BC011790 mRNA. Translation: AAH11790.1.
    BC019298 mRNA. Translation: AAH19298.1.
    BC021088 mRNA. Translation: AAH21088.1.
    BC051297 mRNA. Translation: AAH51297.1.
    BC063036 mRNA. Translation: AAH63036.1.
    CCDSiCCDS8782.1.
    RefSeqiNP_116093.1. NM_032704.3.
    UniGeneiHs.652390.

    Genome annotation databases

    EnsembliENST00000301072; ENSP00000301072; ENSG00000167553.
    GeneIDi84790.
    KEGGihsa:84790.
    UCSCiuc001rtt.1. human.

    Polymorphism databases

    DMDMi20455322.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC004949 mRNA. Translation: AAH04949.1 .
    BC005946 mRNA. Translation: AAH05946.1 .
    BC011790 mRNA. Translation: AAH11790.1 .
    BC019298 mRNA. Translation: AAH19298.1 .
    BC021088 mRNA. Translation: AAH21088.1 .
    BC051297 mRNA. Translation: AAH51297.1 .
    BC063036 mRNA. Translation: AAH63036.1 .
    CCDSi CCDS8782.1.
    RefSeqi NP_116093.1. NM_032704.3.
    UniGenei Hs.652390.

    3D structure databases

    ProteinModelPortali Q9BQE3.
    SMRi Q9BQE3. Positions 1-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124259. 67 interactions.
    IntActi Q9BQE3. 46 interactions.
    MINTi MINT-3060519.
    STRINGi 9606.ENSP00000301072.

    Chemistry

    ChEMBLi CHEMBL2095182.

    PTM databases

    PhosphoSitei Q9BQE3.

    Polymorphism databases

    DMDMi 20455322.

    2D gel databases

    REPRODUCTION-2DPAGE Q9BQE3.

    Proteomic databases

    MaxQBi Q9BQE3.
    PRIDEi Q9BQE3.

    Protocols and materials databases

    DNASUi 84790.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301072 ; ENSP00000301072 ; ENSG00000167553 .
    GeneIDi 84790.
    KEGGi hsa:84790.
    UCSCi uc001rtt.1. human.

    Organism-specific databases

    CTDi 84790.
    GeneCardsi GC12P049658.
    HGNCi HGNC:20768. TUBA1C.
    HPAi HPA039247.
    HPA043684.
    neXtProti NX_Q9BQE3.
    PharmGKBi PA162407345.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG000089.
    InParanoidi Q9BQE3.
    KOi K07374.
    PhylomeDBi Q9BQE3.
    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

    ChiTaRSi TUBA1C. human.
    GeneWikii TUBA1C.
    GenomeRNAii 84790.
    NextBioi 74948.
    PMAP-CutDB Q9BQE3.
    PROi Q9BQE3.

    Gene expression databases

    ArrayExpressi Q9BQE3.
    Bgeei Q9BQE3.
    CleanExi HS_TUBA1C.
    Genevestigatori Q9BQE3.

    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. "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: Bone marrow, Duodenum, Lymph and Skin.
    2. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 65-79 AND 244-280, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    3. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    4. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: GLYCYLATION.
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-432 AND SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTBA1C_HUMAN
    AccessioniPrimary (citable) accession number: Q9BQE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 134 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3