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P07437

- TBB5_HUMAN

UniProt

P07437 - TBB5_HUMAN

Protein

Tubulin beta chain

Gene

TUBB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 2 (21 Dec 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.

    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. MHC class I protein binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. structural constituent of cytoskeleton Source: Ensembl
    6. structural molecule activity Source: BHF-UCL

    GO - Biological processi

    1. cell division Source: BHF-UCL
    2. cellular component movement Source: UniProtKB
    3. cellular process Source: DFLAT
    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. natural killer cell mediated cytotoxicity Source: UniProtKB
    9. protein polymerization Source: InterPro
    10. spindle assembly Source: Ensembl

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_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_160315. Regulation of PLK1 Activity at G2/M Transition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin beta chain
    Alternative name(s):
    Tubulin beta-5 chain
    Gene namesi
    Name:TUBB
    Synonyms:TUBB5
    ORF Names:OK/SW-cl.56
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:20778. TUBB.

    Subcellular locationi

    GO - Cellular componenti

    1. cell body Source: DFLAT
    2. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    3. cytoskeleton Source: UniProtKB
    4. cytosol Source: Reactome
    5. extracellular vesicular exosome Source: UniProtKB
    6. microtubule Source: UniProtKB
    7. nuclear envelope lumen Source: DFLAT
    8. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA358.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Tubulin beta chainPRO_0000048243Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei58 – 581N6-acetyllysine; alternate1 Publication
    Modified residuei58 – 581N6-succinyllysine; alternateBy similarity
    Cross-linki58 – 58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
    Modified residuei172 – 1721Phosphoserine; by CDK1By similarity
    Modified residuei318 – 3181Omega-N-methylarginine1 Publication
    Cross-linki324 – 324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

    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

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP07437.
    PaxDbiP07437.
    PRIDEiP07437.

    2D gel databases

    OGPiP07437.
    REPRODUCTION-2DPAGEP07437.
    SWISS-2DPAGEP07437.
    UCD-2DPAGEP07437.

    PTM databases

    PhosphoSiteiP07437.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with highest levels in spleen, thymus and immature brain.1 Publication

    Gene expression databases

    ArrayExpressiP07437.
    BgeeiP07437.
    CleanExiHS_TUBB.
    GenevestigatoriP07437.

    Organism-specific databases

    HPAiCAB005417.
    CAB012406.
    HPA043640.
    HPA046280.

    Interactioni

    Subunit structurei

    May interact with RNABP10 By similarity. Interacts with MX1 By similarity. 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. Interacts with PIFO.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EBNA-LPQ8AZK73EBI-350864,EBI-1185167From a different organism.
    LRRK2Q5S0074EBI-350864,EBI-5323863

    Protein-protein interaction databases

    BioGridi128444. 157 interactions.
    DIPiDIP-32772N.
    IntActiP07437. 76 interactions.
    MINTiMINT-1146393.
    STRINGi9606.ENSP00000410071.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QNZX-ray2.20C429-438[»]
    3QO0X-ray2.30C422-441[»]
    ProteinModelPortaliP07437.
    SMRiP07437. Positions 2-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The highly acidic C-terminal region may bind cations such as calcium.

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    HOVERGENiHBG000089.
    InParanoidiP07437.
    KOiK07375.
    OMAiTPPPHIF.
    PhylomeDBiP07437.
    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.

    P07437-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY    50
    YNEATGGKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 100
    WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL 150
    LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY 200
    CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 250
    RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM 300
    AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK 350
    TAVCDIPPRG LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 400
    EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDFGEEA EEEA 444
    Length:444
    Mass (Da):49,671
    Last modified:December 21, 2004 - v2
    Checksum:i1E6CD0A36773A103
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti216 – 2161K → R(PubMed:6688039)Curated
    Sequence conflicti216 – 2161K → R(PubMed:6865944)Curated
    Sequence conflicti231 – 2311A → G(PubMed:6688039)Curated
    Sequence conflicti231 – 2311A → G(PubMed:6865944)Curated
    Sequence conflicti234 – 2352SG → EC(PubMed:6688039)Curated
    Sequence conflicti234 – 2352SG → EC(PubMed:6865944)Curated
    Sequence conflicti288 – 2881E → D(PubMed:6688039)Curated
    Sequence conflicti288 – 2881E → D(PubMed:6865944)Curated
    Sequence conflicti298 – 2981N → D in AAH20946. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00314 Genomic DNA. Translation: AAB59507.1.
    AF141349 mRNA. Translation: AAD33873.1.
    AF070561 mRNA. Translation: AAC28642.1.
    AF070593 mRNA. Translation: AAC28650.1.
    AF070600 mRNA. Translation: AAC28654.1.
    BA000025 Genomic DNA. Translation: BAB63321.1.
    AB088100 Genomic DNA. Translation: BAC54932.1.
    AB062393 mRNA. Translation: BAB93480.1.
    BC001938 mRNA. Translation: AAH01938.1.
    BC002347 mRNA. Translation: AAH02347.1.
    BC005838 mRNA. Translation: AAH05838.1.
    BC007605 mRNA. Translation: AAH07605.1.
    BC013374 mRNA. Translation: AAH13374.1.
    BC019924 mRNA. Translation: AAH19924.1.
    BC020946 mRNA. Translation: AAH20946.1.
    BC021909 mRNA. Translation: AAH21909.1.
    BC070326 mRNA. Translation: AAH70326.1.
    CCDSiCCDS4687.1.
    PIRiA26561.
    RefSeqiNP_821133.1. NM_178014.3.
    UniGeneiHs.636480.

    Genome annotation databases

    EnsembliENST00000327892; ENSP00000339001; ENSG00000196230.
    ENST00000383564; ENSP00000373058; ENSG00000183311.
    ENST00000419792; ENSP00000401317; ENSG00000235067.
    ENST00000421473; ENSP00000399155; ENSG00000224156.
    ENST00000422650; ENSP00000400663; ENSG00000229684.
    ENST00000422674; ENSP00000406811; ENSG00000227739.
    ENST00000432462; ENSP00000410829; ENSG00000232421.
    ENST00000436628; ENSP00000410071; ENSG00000232575.
    GeneIDi203068.
    KEGGihsa:203068.
    UCSCiuc003nrl.3. human.

    Polymorphism databases

    DMDMi56757569.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Tubulin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00314 Genomic DNA. Translation: AAB59507.1 .
    AF141349 mRNA. Translation: AAD33873.1 .
    AF070561 mRNA. Translation: AAC28642.1 .
    AF070593 mRNA. Translation: AAC28650.1 .
    AF070600 mRNA. Translation: AAC28654.1 .
    BA000025 Genomic DNA. Translation: BAB63321.1 .
    AB088100 Genomic DNA. Translation: BAC54932.1 .
    AB062393 mRNA. Translation: BAB93480.1 .
    BC001938 mRNA. Translation: AAH01938.1 .
    BC002347 mRNA. Translation: AAH02347.1 .
    BC005838 mRNA. Translation: AAH05838.1 .
    BC007605 mRNA. Translation: AAH07605.1 .
    BC013374 mRNA. Translation: AAH13374.1 .
    BC019924 mRNA. Translation: AAH19924.1 .
    BC020946 mRNA. Translation: AAH20946.1 .
    BC021909 mRNA. Translation: AAH21909.1 .
    BC070326 mRNA. Translation: AAH70326.1 .
    CCDSi CCDS4687.1.
    PIRi A26561.
    RefSeqi NP_821133.1. NM_178014.3.
    UniGenei Hs.636480.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QNZ X-ray 2.20 C 429-438 [» ]
    3QO0 X-ray 2.30 C 422-441 [» ]
    ProteinModelPortali P07437.
    SMRi P07437. Positions 2-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128444. 157 interactions.
    DIPi DIP-32772N.
    IntActi P07437. 76 interactions.
    MINTi MINT-1146393.
    STRINGi 9606.ENSP00000410071.

    Chemistry

    BindingDBi P07437.
    ChEMBLi CHEMBL5444.
    DrugBanki DB01394. Colchicine.
    DB00570. Vinblastine.
    DB00541. Vincristine.
    DB00361. Vinorelbine.
    GuidetoPHARMACOLOGYi 2640.

    PTM databases

    PhosphoSitei P07437.

    Polymorphism databases

    DMDMi 56757569.

    2D gel databases

    OGPi P07437.
    REPRODUCTION-2DPAGE P07437.
    SWISS-2DPAGE P07437.
    UCD-2DPAGE P07437.

    Proteomic databases

    MaxQBi P07437.
    PaxDbi P07437.
    PRIDEi P07437.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327892 ; ENSP00000339001 ; ENSG00000196230 .
    ENST00000383564 ; ENSP00000373058 ; ENSG00000183311 .
    ENST00000419792 ; ENSP00000401317 ; ENSG00000235067 .
    ENST00000421473 ; ENSP00000399155 ; ENSG00000224156 .
    ENST00000422650 ; ENSP00000400663 ; ENSG00000229684 .
    ENST00000422674 ; ENSP00000406811 ; ENSG00000227739 .
    ENST00000432462 ; ENSP00000410829 ; ENSG00000232421 .
    ENST00000436628 ; ENSP00000410071 ; ENSG00000232575 .
    GeneIDi 203068.
    KEGGi hsa:203068.
    UCSCi uc003nrl.3. human.

    Organism-specific databases

    CTDi 203068.
    GeneCardsi GC06P030687.
    GC06Pi30696.
    GC06Pj30677.
    GC06Pk30678.
    GC06Pl30732.
    GC06Pm30766.
    GC06Pn30677.
    GC06Po30679.
    HGNCi HGNC:20778. TUBB.
    HPAi CAB005417.
    CAB012406.
    HPA043640.
    HPA046280.
    MIMi 191130. gene.
    neXtProti NX_P07437.
    PharmGKBi PA358.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5023.
    HOVERGENi HBG000089.
    InParanoidi P07437.
    KOi K07375.
    OMAi TPPPHIF.
    PhylomeDBi P07437.
    TreeFami TF300298.

    Enzyme and pathway databases

    Reactomei 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_160315. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    ChiTaRSi TUBB. human.
    GeneWikii TUBB.
    GenomeRNAii 203068.
    NextBioi 90324.
    PROi P07437.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07437.
    Bgeei P07437.
    CleanExi HS_TUBB.
    Genevestigatori P07437.

    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. "Evolutionary history of a multigene family: an expressed human beta-tubulin gene and three processed pseudogenes."
      Lee M.G.-S., Lewis S.A., Wilde C.D., Cowan N.J.
      Cell 33:477-487(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Identification of two human beta-tubulin isotypes."
      Hall J.L., Dudley L., Dobner P.R., Lewis S.A., Cowan N.J.
      Mol. Cell. Biol. 3:854-862(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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].
      Tissue: Retina.
    4. Yu W., Gibbs R.A.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
      Shiina S., Tamiya G., Oka A., Inoko H.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Genome diversity in HLA: a new strategy for detection of genetic polymorphisms in expressed genes within the HLA class III and class I regions."
      Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon adenocarcinoma.
    8. "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: Brain, Eye, Lung, Muscle and Placenta.
    9. Bienvenut W.V., Campbell A., Ozanne B.W., Lourenco F., Olson M.F.
      Submitted (DEC-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-19; 47-77; 104-174; 242-276; 283-297; 310-359 AND 363-390, METHYLATION AT ARG-318, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Foreskin fibroblast and Mammary carcinoma.
    10. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 3-19; 47-58; 63-77; 104-121; 163-174; 242-251; 253-276; 283-297; 310-318; 325-336 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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.
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: TISSUE SPECIFICITY.
    15. Cited for: INTERACTION WITH PIFO.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTBB5_HUMAN
    AccessioniPrimary (citable) accession number: P07437
    Secondary accession number(s): P05218, Q8WUC1, Q9CY33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 173 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3