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Q3ZCM7

- TBB8_HUMAN

UniProt

Q3ZCM7 - TBB8_HUMAN

Protein

Tubulin beta-8 chain

Gene

TUBB8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (26 Feb 2008)
      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 By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi140 – 1467GTPSequence Analysis

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin beta-8 chain
    Gene namesi
    Name:TUBB8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:20773. TUBB8.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. extracellular vesicular exosome Source: UniProt
    3. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Tubulin beta-8 chainPRO_0000320631Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei172 – 1721Phosphoserine; by CDK1By similarity

    Post-translational modificationi

    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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ3ZCM7.
    PRIDEiQ3ZCM7.

    PTM databases

    PhosphoSiteiQ3ZCM7.

    Expressioni

    Gene expression databases

    BgeeiQ3ZCM7.
    GenevestigatoriQ3ZCM7.

    Organism-specific databases

    HPAiHPA043640.
    HPA046280.

    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

    BioGridi131462. 11 interactions.
    IntActiQ3ZCM7. 4 interactions.
    MINTiMINT-1144251.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3ZCM7.
    SMRiQ3ZCM7. Positions 1-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    HOGENOMiHOG000165710.
    HOVERGENiHBG000089.
    InParanoidiQ3ZCM7.
    KOiK07375.
    OMAiLTQIGQC.
    PhylomeDBiQ3ZCM7.
    TreeFamiTF300298.

    Family and domain databases

    Gene3Di1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProiIPR013838. Beta-tubulin_BS.
    IPR002453. Beta_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]
    PRINTSiPR01163. BETATUBULIN.
    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.
    PS00228. TUBULIN_B_AUTOREG. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q3ZCM7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREIVLTQIG QCGNQIGAKF WEVISDEHAI DSAGTYHGDS HLQLERINVY    50
    YNEASGGRYV PRAVLVDLEP GTMDSVRSGP FGQVFRPDNF IFGQCGAGNN 100
    WAKGHYTEGA ELMESVMDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL 150
    LLSKIREEYP DRIINTFSIL PSPKVSDTVV EPYNATLSVH QLIENADETF 200
    CIDNEALYDI CSKTLKLPTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 250
    RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVAELT QQMFDAKNMM 300
    AACDPRHGRY LTAAAIFRGR MPMREVDEQM FNIQDKNSSY FADWLPNNVK 350
    TAVCDIPPRG LKMSATFIGN NTAIQELFKR VSEQFTAMFR RKAFLHWYTG 400
    EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDEEYAE EEVA 444
    Length:444
    Mass (Da):49,776
    Last modified:February 26, 2008 - v2
    Checksum:i3EC4AC10946BF590
    GO

    Sequence cautioni

    The sequence CAI16221.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti345 – 3451L → F.
    Corresponds to variant rs4880608 [ dbSNP | Ensembl ].
    VAR_039240

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF355127 Genomic DNA. Translation: AAL32434.1.
    CR590375 mRNA. No translation available.
    AL713922 Genomic DNA. Translation: CAI16221.1. Sequence problems.
    CH471072 Genomic DNA. Translation: EAW86545.1.
    BC101270 mRNA. Translation: AAI01271.1.
    BC101271 mRNA. Translation: AAI01272.1.
    CCDSiCCDS7051.1.
    RefSeqiNP_817124.1. NM_177987.2.
    UniGeneiHs.532659.

    Genome annotation databases

    EnsembliENST00000309812; ENSP00000311042; ENSG00000173876.
    GeneIDi347688.
    KEGGihsa:347688.
    UCSCiuc001ifi.2. human.

    Polymorphism databases

    DMDMi182705285.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF355127 Genomic DNA. Translation: AAL32434.1 .
    CR590375 mRNA. No translation available.
    AL713922 Genomic DNA. Translation: CAI16221.1 . Sequence problems.
    CH471072 Genomic DNA. Translation: EAW86545.1 .
    BC101270 mRNA. Translation: AAI01271.1 .
    BC101271 mRNA. Translation: AAI01272.1 .
    CCDSi CCDS7051.1.
    RefSeqi NP_817124.1. NM_177987.2.
    UniGenei Hs.532659.

    3D structure databases

    ProteinModelPortali Q3ZCM7.
    SMRi Q3ZCM7. Positions 1-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 131462. 11 interactions.
    IntActi Q3ZCM7. 4 interactions.
    MINTi MINT-1144251.

    Chemistry

    BindingDBi Q3ZCM7.
    ChEMBLi CHEMBL2095182.

    PTM databases

    PhosphoSitei Q3ZCM7.

    Polymorphism databases

    DMDMi 182705285.

    Proteomic databases

    MaxQBi Q3ZCM7.
    PRIDEi Q3ZCM7.

    Protocols and materials databases

    DNASUi 347688.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309812 ; ENSP00000311042 ; ENSG00000173876 .
    GeneIDi 347688.
    KEGGi hsa:347688.
    UCSCi uc001ifi.2. human.

    Organism-specific databases

    CTDi 347688.
    GeneCardsi GC10M000093.
    H-InvDB HIX0029368.
    HGNCi HGNC:20773. TUBB8.
    HPAi HPA043640.
    HPA046280.
    neXtProti NX_Q3ZCM7.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000165710.
    HOVERGENi HBG000089.
    InParanoidi Q3ZCM7.
    KOi K07375.
    OMAi LTQIGQC.
    PhylomeDBi Q3ZCM7.
    TreeFami TF300298.

    Miscellaneous databases

    GenomeRNAii 347688.
    NextBioi 99218.
    PROi Q3ZCM7.

    Gene expression databases

    Bgeei Q3ZCM7.
    Genevestigatori Q3ZCM7.

    Family and domain databases

    Gene3Di 1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProi IPR013838. Beta-tubulin_BS.
    IPR002453. Beta_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 PR01163. BETATUBULIN.
    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.
    PS00228. TUBULIN_B_AUTOREG. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A cascade of complex subtelomeric duplications during the evolution of the hominoid and Old World monkey genomes."
      van Geel M., Eichler E.E., Beck A.F., Shan Z., Haaf T., van der Maarel S.M., Frants R.R., de Jong P.J.
      Am. J. Hum. Genet. 70:269-278(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Fetal brain.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] OF 4-444.
    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.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTBB8_HUMAN
    AccessioniPrimary (citable) accession number: Q3ZCM7
    Secondary accession number(s): Q5SQX9, Q8WZ78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 85 of the entry and version 2 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 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3