P52275 · TBB2_CAEEL
- ProteinTubulin beta-2 chain
- Genetbb-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids450 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (By similarity).
Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (By similarity).
Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (By similarity).
Required for the normal dynamic behavior of the non-centrosomal microtubules in the epidermal syncytium (PubMed:31995031).
Involved in the redistribution of microtubule end-binding protein EB1/ebp-2 caused by wounding (PubMed:31995031).
Required to modulate expression in the epidermis of antimicrobial peptides, such as nlp-29, after wounding, or fungal infection (PubMed:31995031).
Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (By similarity).
Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (By similarity).
Required for the normal dynamic behavior of the non-centrosomal microtubules in the epidermal syncytium (PubMed:31995031).
Involved in the redistribution of microtubule end-binding protein EB1/ebp-2 caused by wounding (PubMed:31995031).
Required to modulate expression in the epidermis of antimicrobial peptides, such as nlp-29, after wounding, or fungal infection (PubMed:31995031).
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11 | GTP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 69 | GTP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 69 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 138 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 142 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 143 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 144 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 204 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 226 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | microtubule | |
Cellular Component | spindle microtubule | |
Cellular Component | tubulin complex | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | metal ion binding | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | meiotic spindle organization | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | mitotic cell cycle |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTubulin beta-2 chain
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionP52275
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown abolishes recruitment of microtubule end-binding protein EB1/ebp-2 to a wound site (PubMed:31995031).
Almost completely abolishes induction of nlp-29 expression upon infection with Drechmeria coniospora (PubMed:31995031).
Almost completely abolishes induction of nlp-29 expression upon infection with Drechmeria coniospora (PubMed:31995031).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 404 | Partial reduction in ced-3-mediated cleavage; when associated with E-417 and E-435. | ||||
Sequence: D → E | ||||||
Mutagenesis | 417 | Partial reduction in ced-3-mediated cleavage; when associated with E-404 and E-435. | ||||
Sequence: D → E | ||||||
Mutagenesis | 435 | Partial reduction in ced-3-mediated cleavage; when associated with E-404 and E-417. | ||||
Sequence: D → E | ||||||
Mutagenesis | 439 | In sb26; no effect on thick filament organization in body wall muscles. Partially restores thick filament organization in a mel-26 (ct61sb4) mutant background. | ||||
Sequence: E → K |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000048287 | 1-450 | Tubulin beta-2 chain | |||
Sequence: MREIVHVQAGQCGNQIGSKFWEVISDEHGIQPDGTFKGETDLQLERIDVYYNEANNGKYVPRAVLVDLEPGTMDSVRSGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDNVLDVIRKEAEGCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMSSFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICYRTLKLTNPTYGDLNHLVSLTMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLSAKGTQAYRALTVAELTQQMFDAKNMMAACDPRHGRYLTVAAMFRGRMSMREVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFVGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLISEYQQYQEATAEDDVDGYAEGEAGETYESEQ |
Post-translational modification
Cleaved by caspase ced-3 in vitro.
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Dimer of alpha and beta chains (By similarity).
A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nm (By similarity).
Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity (By similarity).
Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells (By similarity).
A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nm (By similarity).
Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity (By similarity).
Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 428-450 | Disordered | ||||
Sequence: ATAEDDVDGYAEGEAGETYESEQ | ||||||
Compositional bias | 432-450 | Acidic residues | ||||
Sequence: DDVDGYAEGEAGETYESEQ |
Sequence similarities
Belongs to the tubulin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length450
- Mass (Da)50,345
- Last updated1996-10-01 v1
- Checksum8F04D0D2AB165006
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 432-450 | Acidic residues | ||||
Sequence: DDVDGYAEGEAGETYESEQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z35597 EMBL· GenBank· DDBJ | CAA84648.1 EMBL· GenBank· DDBJ | Genomic DNA |