Reviewed,
UniProtKB/Swiss-Prot P07437 (TBB5_HUMAN)
Last modified
November 3, 2009.
Version 120.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Tubulin beta chain Alternative name(s): Tubulin beta-5 chain | ||||||
| Gene names |
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| Organism | Homo sapiens (Human) [Complete proteome] | ||||||
| Taxonomic identifier | 9606 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 444 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | 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. |
| Subunit structure | Dimer of alpha and beta chains. |
| Tissue specificity | Ubiquitously expressed with highest levels in spleen, thymus and immature brain. |
| Domain | The highly acidic C-terminal region may bind cations such as calcium. |
| Post-translational modification | 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. |
| Sequence similarities | Belongs to the tubulin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Microtubule |
| Ligand | GTP-binding Nucleotide-binding |
| PTM | Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell motion Traceable author statement. Source: UniProtKB microtubule-based movementInferred from electronic annotation. Source: InterPro natural killer cell mediated cytotoxicityNon-traceable author statement. Source: UniProtKB protein polymerizationInferred from electronic annotation. Source: InterPro |
| Cellular component | cytosol Inferred from Experiment. Source: Reactome microtubuleInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activityInferred from electronic annotation. Source: InterPro MHC class I protein bindingInferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 444 | 444 | Tubulin beta chain | PRO_0000048243 | |||||
Regions | |||||||||
| Nucleotide binding | 140 – 146 | 7 | GTP Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 36 | 1 | Phosphotyrosine Ref.11 | ||||||
| Modified residue | 48 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 55 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 58 | 1 | N6-acetyllysine Ref.17 | ||||||
| Modified residue | 318 | 1 | Omega-N-methylarginine Ref.9 | ||||||
| Modified residue | 340 | 1 | Phosphotyrosine Ref.16 | ||||||
| Modified residue | 429 | 1 | Phosphothreonine Ref.12 | ||||||
| Cross-link | 58 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13 | |||||||
| Cross-link | 324 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13 | |||||||
Experimental info | |||||||||
| Sequence conflict | 216 | 1 | K → R Ref.1 | ||||||
| Sequence conflict | 216 | 1 | K → R Ref.2 | ||||||
| Sequence conflict | 231 | 1 | A → G Ref.1 | ||||||
| Sequence conflict | 231 | 1 | A → G Ref.2 | ||||||
| Sequence conflict | 234 – 235 | 2 | SG → EC Ref.1 | ||||||
| Sequence conflict | 234 – 235 | 2 | SG → EC Ref.2 | ||||||
| Sequence conflict | 288 | 1 | E → D Ref.1 | ||||||
| Sequence conflict | 288 | 1 | E → D Ref.2 | ||||||
| Sequence conflict | 298 | 1 | N → D in AAH20946. Ref.8 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 6688039] [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: 6865944] [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: 11504633] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Eye, Lung, Muscle and Placenta. |
| [9] | Bienvenut W.V., Campbell A., Ozanne B.W. Submitted (JUN-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, MASS SPECTROMETRY. Tissue: Foreskin fibroblast. |
| [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, 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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, MASS SPECTROMETRY. |
| [12] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-55 AND THR-429, MASS SPECTROMETRY. |
| [13] | "Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-324, MASS SPECTROMETRY. |
| [14] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [15] | "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: 19524510] [Abstract] Cited for: GLYCYLATION. |
| [16] | "An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-340, MASS SPECTROMETRY. Tissue: Mammary epithelium. |
| [17] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Entry information
| Entry name | TBB5_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P07437 Secondary accession number(s): P05218, Q8WUC1, Q9CY33 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |
