P07437 (TBB5_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 158.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames 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) [Reference 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. |
| 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. May interact with RNABP10 By similarity. Interacts with PIFO. Interacts with MX1 By similarity. Ref.16 |
| Subcellular location | |
| Tissue specificity | Ubiquitously expressed with highest levels in spleen, thymus and immature brain. Ref.15 |
| 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
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 | 58 | 1 | N6-acetyllysine; alternate Ref.14 | ||||||
| Modified residue | 172 | 1 | Phosphoserine; by CDK1 By similarity | ||||||
| Modified residue | 318 | 1 | Omega-N-methylarginine Ref.9 | ||||||
| Modified residue | 340 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 382 | 1 | Phosphoserine By similarity | ||||||
| Cross-link | 58 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.12 | |||||||
| Cross-link | 324 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12 | |||||||
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] [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, 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, 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] | "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] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-324, MASS SPECTROMETRY. |
| [13] | "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. |
| [14] | "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, MASS SPECTROMETRY. |
| [15] | "Tumoral and tissue-specific expression of the major human beta-tubulin isotypes." Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C., Lopez-Jimenez E., Leton R., Cascon A., Robledo M., Rodriguez-Antona C. Cytoskeleton 67:214-223(2010) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [16] | "Pitchfork regulates primary cilia disassembly and left-right asymmetry." Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H. Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIFO. |
| [17] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Web resources
| Wikipedia Tubulin entry |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | 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. | ||||||||||||||||||
| IPI | IPI01019113. | ||||||||||||||||||
| PIR | A26561. | ||||||||||||||||||
| RefSeq | NP_821133.1. NM_178014.2. | ||||||||||||||||||
| UniGene | Hs.636480. Hs.714425. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P07437. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | P07437. 62 interactions. | ||||||||||||||||||
| MINT | MINT-1146393. | ||||||||||||||||||
| STRING | 9606.ENSP00000410071. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | P07437. | ||||||||||||||||||
Polymorphism databases | |||||||||||||||||||
| DMDM | 56757569. | ||||||||||||||||||
2D gel databases | |||||||||||||||||||
| OGP | P07437. | ||||||||||||||||||
| REPRODUCTION-2DPAGE | P07437. | ||||||||||||||||||
| SWISS-2DPAGE | P07437. | ||||||||||||||||||
| UCD-2DPAGE | P07437. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PaxDb | P07437. | ||||||||||||||||||
| PRIDE | P07437. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000327892; ENSP00000339001; ENSG00000196230. ENST00000383564; ENSP00000373058; ENSG00000183311. ENST00000419792; ENSP00000401317; ENSG00000235067. ENST00000421473; ENSP00000399155; ENSG00000224156. ENST00000422650; ENSP00000400663; ENSG00000229684. ENST00000422674; ENSP00000406811; ENSG00000227739. ENST00000432462; ENSP00000410829; ENSG00000232421. ENST00000436628; ENSP00000410071; ENSG00000232575. | ||||||||||||||||||
| GeneID | 203068. | ||||||||||||||||||
| KEGG | hsa:203068. | ||||||||||||||||||
| UCSC | uc003nrl.3. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 203068. | ||||||||||||||||||
| GeneCards | GC06P030687. | ||||||||||||||||||
| HGNC | HGNC:20778. TUBB. | ||||||||||||||||||
| HPA | CAB005417. CAB012406. HPA043640. HPA046280. | ||||||||||||||||||
| MIM | 191130. gene. | ||||||||||||||||||
| neXtProt | NX_P07437. | ||||||||||||||||||
| PharmGKB | PA358. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | COG5023. | ||||||||||||||||||
| HOVERGEN | HBG000089. | ||||||||||||||||||
| InParanoid | P07437. | ||||||||||||||||||
| KO | K07375. | ||||||||||||||||||
| OMA | RYQGEND. | ||||||||||||||||||
| OrthoDB | EOG4DFPNJ. | ||||||||||||||||||
| PhylomeDB | P07437. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| Reactome | REACT_115566. Cell Cycle. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | P07437. | ||||||||||||||||||
| Bgee | P07437. | ||||||||||||||||||
| CleanEx | HS_TUBB. | ||||||||||||||||||
| Genevestigator | P07437. | ||||||||||||||||||
| GermOnline | ENSG00000196230. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 1.10.287.600. 1 hit. 3.30.1330.20. 1 hit. 3.40.50.1440. 1 hit. | ||||||||||||||||||
| InterPro | 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] | ||||||||||||||||||
| PANTHER | PTHR11588. PTHR11588. 1 hit. | ||||||||||||||||||
| Pfam | PF00091. Tubulin. 1 hit. PF03953. Tubulin_C. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR01163. BETATUBULIN. PR01161. TUBULIN. | ||||||||||||||||||
| SMART | SM00864. Tubulin. 1 hit. SM00865. Tubulin_C. 1 hit. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF55307. Tub_FtsZ_C. 1 hit. SSF52490. Tubulin_FtsZ. 1 hit. | ||||||||||||||||||
| PROSITE | PS00227. TUBULIN. 1 hit. PS00228. TUBULIN_B_AUTOREG. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| BindingDB | P07437. | ||||||||||||||||||
| ChEMBL | CHEMBL5444. | ||||||||||||||||||
| ChiTaRS | TUBB. human. | ||||||||||||||||||
| DrugBank | DB01394. Colchicine. DB00570. Vinblastine. DB00541. Vincristine. DB00361. Vinorelbine. | ||||||||||||||||||
| GenomeRNAi | 203068. | ||||||||||||||||||
| NextBio | 90324. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
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 program | Chordata Protein Annotation Program | ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
