Reviewed,
UniProtKB/Swiss-Prot Q13509 (TBB3_HUMAN)
Last modified
October 13, 2009.
Version 90.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Tubulin beta-3 chain Alternative name(s): Tubulin beta-III Tubulin beta-4 | ||||
| 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 | 450 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. |
| 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 |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | microtubule-based movement Inferred from electronic annotation. Source: InterPro protein polymerizationInferred from electronic annotation. Source: InterPro |
| Cellular component | microtubule Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activityInferred from electronic annotation. Source: InterPro structural molecule activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 450 | 450 | Tubulin beta-3 chain | PRO_0000048250 | |||||
Regions | |||||||||
| Nucleotide binding | 140 – 146 | 7 | GTP Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 58 | 1 | N6-acetyllysine Ref.7 | ||||||
Experimental info | |||||||||
| Sequence conflict | 275 | 1 | A → R in AAC52035. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and sequencing of human betaIII-tubulin cDNA: induction of betaIII isotype in human prostate carcinoma cells by acute exposure to antimicrotubule agents." Ranganathan S., Dexter D.W., Benetatos C.A., Hudes G.R. Biochim. Biophys. Acta 1395:237-245(1998) [PubMed: 9473684] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | Banerjee A. Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary cancer. |
| [3] | "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: Lung. |
| [4] | Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 63-77; 104-121; 242-251; 163-174 AND 381-390, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex. |
| [5] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [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: 19524510] [Abstract] Cited for: GLYCYLATION. |
| [7] | "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
Sequence databases | |
|---|---|
| U47634 mRNA. Translation: AAC52035.1. AF427491 mRNA. Translation: AAL28094.1. BC000748 mRNA. Translation: AAH00748.1. BC003021 mRNA. Translation: AAH03021.2. | |
| IPI | IPI00013683. |
| RefSeq | NP_006077.2. |
| UniGene | Hs.511743 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FFX based on UniProtKB P02554. |
| SMR | Q13509. Positions 2-427. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q13509. 4 interactions. |
| STRING | Q13509. |
PTM databases | |
| PhosphoSite | Q13509. |
2-D gel databases | |
| OGP | Q13509. |
Proteomic databases | |
| PRIDE | Q13509. |
Genome annotation databases | |
| Ensembl | ENST00000304984; ENSP00000302777; ENSG00000198211; Homo sapiens. [Genome view] ENST00000315491; ENSP00000320295; ENSG00000198211; Homo sapiens. [Genome view] |
| GeneID | 10381. |
| KEGG | hsa:10381. |
| UCSC | uc002fph.1. human. |
Organism-specific databases | |
| CTD | 10381. |
| GeneCards | GC16P088514. |
| HGNC | HGNC:20772. TUBB3. |
| HPA | CAB011512. |
| MIM | 602661. gene. |
| PharmGKB | PA134953867. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | Q13509. |
Enzyme and pathway databases | |
| Reactome | REACT_17015. Metabolism of proteins. |
Gene expression databases | |
| ArrayExpress | Q13509. |
| Bgee | Q13509. |
| CleanEx | HS_TUBB3. HS_TUBB4. |
| Genevestigator | Q13509. |
| GermOnline | ENSG00000198211. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR013838. Beta-tubulin_BS. IPR002453. Beta_tubulin. IPR000217. Tubulin. IPR018316. Tubulin/FtsZ_2-layer-sand-dom. IPR017975. Tubulin_CS. IPR003008. Tubulin_FtsZ_GTPase. [Graphical view] |
| Gene3D | G3DSA:3.30.1330.20. Tubulin/FtsZ_2-layer-sand-dom. 1 hit. G3DSA:3.40.50.1440. Tubulin_FtsZ. 1 hit. |
| PANTHER | PTHR11588:SF9. Beta_tubulin. 1 hit. PTHR11588. Tubulin. 1 hit. |
| Pfam | PF00091. Tubulin. 1 hit. PF03953. Tubulin_C. 1 hit. [Graphical view] |
| PRINTS | PR01163. BETATUBULIN. PR01161. TUBULIN. |
| PROSITE | PS00227. TUBULIN. 1 hit. PS00228. TUBULIN_B_AUTOREG. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 39327. |
| SOURCE | Search... |
Entry information
| Entry name | TBB3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q13509 Secondary accession number(s): Q9BTZ0, Q9BW10 | ||||||||
| 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 16 Human chromosome 16: 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 |

Clusters with


