P22012 (TBB_ASPFL) Reviewed, UniProtKB/Swiss-Prot
Last modified
July 27, 2011.
Version 66.
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 | Aspergillus flavus |
| Taxonomic identifier | 5059 [NCBI] |
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 448 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
| ||||||||||||||||||
References
| [1] | "Isolation and sequence analysis of a beta-tubulin gene from Aspergillus flavus and its use as a selectable marker." Seip E., Woloshuk C., Payne G., Curtis S. Appl. Environ. Microbiol. 56:3686-3692(1990) [PubMed: 2128007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M38265 Genomic DNA. Translation: AAA32689.1. |
| PIR | A43794. |
3D structure databases | |
| ProteinModelPortal | P22012. |
| SMR | P22012. Positions 1-427. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P22012. |
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. |
| 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... |
Entry information
| Entry name | TBB_ASPFL | ||||||||
| Accession | Primary (citable) accession number: P22012 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with