O44388 (TBB_TRITR) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 8, 2011.
Version 55.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Tubulin beta chain Alternative name(s): Beta-tubulin |
| Organism | Trichuris trichiura (Whipworm) |
| Taxonomic identifier | 36087 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Nematoda › Enoplea › Trichocephalida › Trichuridae › Trichuris |
Protein attributes
| Sequence length | 444 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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. |
| Subcellular location | |
| Sequence similarities | Belongs to the tubulin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Cytoskeleton Microtubule |
| Ligand | GTP-binding Nucleotide-binding |
| Gene Ontology (GO) | |
| Biological process | microtubule-based movement Inferred from electronic annotation. Source: InterPro protein polymerizationInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW 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 structural molecule activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "A beta-tubulin gene from Trichuris trichiura." Bennett A.B., Barker G.C., Bundy D.A.P. Mol. Biochem. Parasitol. 103:111-116(1999) [PubMed: 10514087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF034219 Genomic DNA. Translation: AAB99949.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FFX based on UniProtKB P02554. |
| ProteinModelPortal | O44388. |
| SMR | O44388. Positions 1-427. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| 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] |
| Gene3D | G3DSA:3.30.1330.20. Tubulin/FtsZ_2-layer-sand-dom. 1 hit. G3DSA:1.10.287.600. Tubulin_C. 1 hit. G3DSA:3.40.50.1440. Tubulin_FtsZ. 1 hit. |
| PANTHER | PTHR11588. Tubulin. 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 | |
| DrugBank | DB00643. Mebendazole. |
Entry information
| Entry name | TBB_TRITR | ||||||||
| Accession | Primary (citable) accession number: O44388 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with