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Details on Person UniProt:Q6P9V9 Tuba1b
| Class:Id | ReferenceGeneProduct:250592 |
|---|---|
| _chainChangeLog | chain:1-451 added on Sat February 7 2015;chain:1-450 added on Fri November 4 2016 |
| _displayName | UniProt:Q6P9V9 Tuba1b |
| _timestamp | 2025-08-15 21:49:35 |
| chain | chain:1-451 chain:1-450 |
| checksum | 94355B4EC2086429 |
| comment | FUNCTION Tubulin is the major constituent of microtubules, protein filaments consisting 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).CATALYTIC ACTIVITY GTP + H2O = GDP + phosphate + H(+)COFACTOR Heterodimer of alpha- and beta-tubulin (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). Interacts with gamma-tubulin; the interaction allows microtubules to nucleate from the gamma-tubulin ring complex (gTuRC) (By similarity). Nascent microtubule interacts (via alpha-tubulin MREC motif) with TTC5/STRAP; this interaction may result in tubulin mRNA-targeted degradation (By similarity). Component of sperm flagellar doublet microtubules (By similarity).SUBCELLULAR LOCATION The MREC motif mediates interaction with TTC5/STRAP and may be critical for tubulin autoregulation.PTM Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation 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 polyglycylation levels increases polyglutamylation, and reciprocally. Cilia and flagella glycylation is required for their stability and maintenance. Flagella glycylation controls sperm motility.PTM Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). Glutamylation is also involved in cilia motility (By similarity).PTM Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly.PTM Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.PTM Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution.PTM Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (MATCAP1, VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively.PTM Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).PTM Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (By similarity).SIMILARITY Belongs to the tubulin family. |
| created | [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53 |
| description | recommendedName: Tubulin alpha-1B chain ecNumber evidence="3"3.6.5.- alternativeName: Alpha-tubulin 2 alternativeName: Tubulin alpha-2 chain component recommendedName: Detyrosinated tubulin alpha-1B chain /component |
| geneName | Tuba1b Tuba2 |
| identifier | Q6P9V9 |
| isSequenceChanged | FALSE |
| keyword | Acetylation Cytoplasm Cytoskeleton Direct protein sequencing GTP-binding Hydrolase Isopeptide bond Magnesium Metal-binding Methylation Microtubule Nitration Nucleotide-binding Phosphoprotein Reference proteome Ubl conjugation |
| modified | [InstanceEdit:354386] Schmidt, EE, 2008-06-18 04:45:12 [InstanceEdit:384350] Kanapin, AA, 2008-11-26 14:00:39 [InstanceEdit:392885] Kanapin, AA, 2009-03-09 12:07:18 [InstanceEdit:400710] Schmidt, EE, 2009-03-25 05:33:35 [InstanceEdit:423310] Kanapin, AA [InstanceEdit:435478] Kanapin, AA [InstanceEdit:435871] Kanapin, AA [InstanceEdit:447347] Kanapin, AA [InstanceEdit:525883] Kanapin, AA [InstanceEdit:613449] Kanapin, AA [InstanceEdit:797602] Kanapin, AA [InstanceEdit:937368] Yung, CK [InstanceEdit:1042053] Yung, CK [InstanceEdit:1220657] Yung, CK [InstanceEdit:1300696] Yung, CK [InstanceEdit:1301627] Yung, CK [InstanceEdit:1551960] Weiser, JD [InstanceEdit:1995863] Weiser, JD [InstanceEdit:2132304] Weiser, JD [InstanceEdit:2265580] Weiser, JD [InstanceEdit:3132113] Weiser, JD [InstanceEdit:5263031] Weiser, JD [InstanceEdit:5433710] Weiser, JD [InstanceEdit:5618415] Weiser, JD [InstanceEdit:5634237] Weiser, JD [InstanceEdit:5673015] Weiser, JD [InstanceEdit:8944791] Weiser, JD [InstanceEdit:9037114] Weiser, JD [InstanceEdit:9627708] Weiser, JD [InstanceEdit:9637257] Weiser, JD [InstanceEdit:9657908] Weiser, JD [InstanceEdit:9676415] Weiser, JD [InstanceEdit:9767224] Weiser, Joel [InstanceEdit:9773244] Weiser, Joel [InstanceEdit:9819394] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | Tuba1b |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| secondaryIdentifier | TBA1B_RAT |
| sequenceLength | 451 |
| species | [Species:48895] Rattus norvegicus |
| (referenceEntity) | [EntityWithAccessionedSequence:444963] Tubulin alpha-1B chain [cytosol] [Rattus norvegicus] |
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No pathways have been reviewed or authored by UniProt:Q6P9V9 Tuba1b (250592)
