Product: TUBA1/3/4 Antibody
Catalog: AF6944
Description: Rabbit polyclonal antibody to TUBA1/3/4
Application: ELISA(peptide)
Reactivity: Human, Mouse
Mol.Wt.: 50kD(Calculated).
Uniprot: Q71U36 | P68363 | Q9BQE3 | Q6PEY2 | P68366
RRID: AB_2847734

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse
Clonality:
Polyclonal
Specificity:
TUBA1/3/4 Antibody detects endogenous levels of total TUBA1/3/4.
RRID:
AB_2847734
Cite Format: Affinity Biosciences Cat# AF6944, RRID:AB_2847734.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Alpha tubulin ubiquitous; Alpha-tubulin ubiquitous; K alpha 1; TBA1B_HUMAN; TUBA1B; Tubulin alpha 1B; Tubulin alpha 1B chain; Tubulin alpha ubiquitous; Tubulin alpha ubiquitous chain; Tubulin alpha-1B chain; Tubulin alpha-ubiquitous chain; Tubulin K alpha 1; Tubulin K-alpha-1; Alpha-tubulin 1; ALS22; B ALPHA 1; bA408E5.3; H2 ALPHA; Hum a tub1; Hum a tub2; LIS3; MGC171407; MGC55332; TBA4A_HUMAN; Testis-specific alpha-tubulin; TUBA1; TUBA1A; tuba1l; Tuba4a; Tubulin alpha 1 chain; Tubulin alpha; Tubulin alpha-1 chain; tubulin alpha-1B chain; Tubulin alpha-4A chain; Tubulin H2-alpha; Tubulin, alpha 1 (testis specific); tubulin, alpha 1, like; Tubulin, alpha 4a; Tubulin, alpha, testis-specific; Tubulin, alpha-1; Alpha-tubulin 2; Alpha-tubulin 3C/D; alpha-tubulin isotype H2-alpha; H2-ALPHA; TBA3C_HUMAN; TUBA2; TUBA3C; TUBA3D; Tubulin alpha 2; Tubulin alpha 2 chain; Tubulin alpha 3c; Tubulin alpha-2 chain; Tubulin alpha-3C/D chain; Alpha tubulin 3; Alpha-tubulin 3; B alpha 1; FLJ25113; LIS3; TBA1A_HUMAN; TUBA1A; TUB

Immunogens

Immunogen:

A synthesized peptide derived from human TUBA1/3/4.

Uniprot:
Gene(ID):
Expression:
Q71U36 TBA1A_HUMAN:

Expressed at a high level in fetal brain.

Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY

MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY

MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAVAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGADSADGEDEGEEY

MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYAKWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEVGVDSVEAEAEEGEAY

MRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGIDSYEDEDEGEE

PTMs - Q71U36/P68363/Q9BQE3/Q6PEY2/P68366 As Substrate

Site PTM Type Enzyme
S6 Phosphorylation
Y24 Phosphorylation
S38 Phosphorylation
K40 Acetylation
K40 Methylation
K40 Ubiquitination
T41 Phosphorylation
S48 Phosphorylation
T51 Phosphorylation
S54 Phosphorylation
T56 Phosphorylation
K60 Acetylation
K60 Sumoylation
K60 Ubiquitination
T73 Phosphorylation
T80 Phosphorylation
T82 Phosphorylation
Y83 Phosphorylation
T94 Phosphorylation
K96 Acetylation
K96 Sumoylation
K96 Ubiquitination
Y103 Phosphorylation
Y108 Phosphorylation
T109 Phosphorylation
K112 Acetylation
K112 Sumoylation
K112 Ubiquitination
K124 Acetylation
K124 Ubiquitination
S151 Phosphorylation
S158 Phosphorylation
Y161 Phosphorylation
K163 Acetylation
K163 Methylation
K163 Ubiquitination
K164 Ubiquitination
S165 Phosphorylation
K166 Ubiquitination
Y172 Phosphorylation
Y185 Phosphorylation
S187 Phosphorylation
T190 Phosphorylation
T191 Phosphorylation
T193 Phosphorylation
T194 Phosphorylation
S198 Phosphorylation
Y210 Phosphorylation
T223 Phosphorylation
Y224 Phosphorylation
T225 Phosphorylation
S236 Phosphorylation
S237 Phosphorylation
T253 Phosphorylation
T257 Phosphorylation
Y262 Phosphorylation
T271 Phosphorylation
Y272 Phosphorylation
S277 Phosphorylation
K280 Ubiquitination
Y282 Phosphorylation
S287 Phosphorylation
T292 Phosphorylation
K304 Ubiquitination
K311 Acetylation
K311 Ubiquitination
Y312 Phosphorylation
Y319 Phosphorylation
K326 Acetylation
K326 Sumoylation
K326 Ubiquitination
T334 Phosphorylation
K336 Acetylation
K336 Sumoylation
K336 Ubiquitination
T337 Phosphorylation
K338 Methylation
K338 Ubiquitination
T340 Phosphorylation
T349 Phosphorylation
K352 Acetylation
K352 Sumoylation
K352 Ubiquitination
Y357 Phosphorylation
T361 Phosphorylation
K370 Acetylation
K370 Sumoylation
K370 Ubiquitination
S379 Phosphorylation
K394 Acetylation
K394 Sumoylation
K394 Ubiquitination
Y399 Phosphorylation
K401 Acetylation
K401 Sumoylation
K401 Ubiquitination
Y408 Phosphorylation
S419 Phosphorylation
K430 Ubiquitination
Y432 Phosphorylation
S439 Phosphorylation
Y451 Phosphorylation
Site PTM Type Enzyme
S6 Phosphorylation
Y24 Phosphorylation
S38 Phosphorylation
K40 Acetylation
K40 Methylation
K40 Ubiquitination
T41 Phosphorylation
S48 Phosphorylation
T51 Phosphorylation
S54 Phosphorylation
T56 Phosphorylation
K60 Acetylation
K60 Sumoylation
K60 Ubiquitination
T73 Phosphorylation
T80 Phosphorylation
T82 Phosphorylation
Y83 Phosphorylation
T94 Phosphorylation
K96 Acetylation
K96 Sumoylation
K96 Ubiquitination
Y103 Phosphorylation
Y108 Phosphorylation
T109 Phosphorylation
K112 Acetylation
K112 Sumoylation
K112 Ubiquitination
K124 Acetylation
K124 Ubiquitination
S151 Phosphorylation
S158 Phosphorylation
Y161 Phosphorylation
K163 Acetylation
K163 Methylation
K163 Ubiquitination
K164 Ubiquitination
K166 Ubiquitination
Y172 Phosphorylation
Y185 Phosphorylation
S187 Phosphorylation
T190 Phosphorylation
T191 Phosphorylation
T193 Phosphorylation
T194 Phosphorylation
S198 Phosphorylation
Y210 Phosphorylation
T223 Phosphorylation
Y224 Phosphorylation
T225 Phosphorylation
S232 Phosphorylation
S236 Phosphorylation
S237 Phosphorylation
T239 Phosphorylation
S241 Phosphorylation
T253 Phosphorylation
T257 Phosphorylation
Y262 Phosphorylation
T271 Phosphorylation
Y272 Phosphorylation
S277 Phosphorylation
K280 Acetylation
K280 Ubiquitination
Y282 Phosphorylation
S287 Phosphorylation
T292 Phosphorylation
C295 S-Nitrosylation
K304 Ubiquitination
K311 Acetylation
K311 Ubiquitination
Y312 Phosphorylation
C315 S-Nitrosylation
C316 S-Nitrosylation
Y319 Phosphorylation
K326 Acetylation
K326 Sumoylation
K326 Ubiquitination
T334 Phosphorylation
K336 Acetylation
K336 Sumoylation
K336 Ubiquitination
T337 Phosphorylation
K338 Methylation
K338 Ubiquitination
R339 Methylation
S340 Phosphorylation
C347 S-Nitrosylation
T349 Phosphorylation
K352 Acetylation
K352 Sumoylation
K352 Ubiquitination
Y357 Phosphorylation
T361 Phosphorylation
K370 Acetylation
K370 Sumoylation
K370 Ubiquitination
C376 S-Nitrosylation
S379 Phosphorylation
K394 Acetylation
K394 Methylation
K394 Sumoylation
K394 Ubiquitination
Y399 Phosphorylation
K401 Acetylation
K401 Sumoylation
K401 Ubiquitination
Y408 Phosphorylation
S419 Phosphorylation
K430 Ubiquitination
Y432 Phosphorylation
S439 Phosphorylation
Y451 Phosphorylation
Site PTM Type Enzyme
S6 Phosphorylation
Y24 Phosphorylation
S38 Phosphorylation
K40 Acetylation
K40 Ubiquitination
T41 Phosphorylation
S48 Phosphorylation
T51 Phosphorylation
S54 Phosphorylation
T56 Phosphorylation
K60 Acetylation
K60 Sumoylation
K60 Ubiquitination
R79 Methylation
T80 Phosphorylation
T82 Phosphorylation
T94 Phosphorylation
R105 Methylation
Y108 Phosphorylation
T109 Phosphorylation
R156 Methylation
Y185 Phosphorylation
S187 Phosphorylation
T190 Phosphorylation
T193 Phosphorylation
T194 Phosphorylation
S198 Phosphorylation
Y210 Phosphorylation
T223 Phosphorylation
Y224 Phosphorylation
T225 Phosphorylation
S236 Phosphorylation
S237 Phosphorylation
T253 Phosphorylation
T257 Phosphorylation
Y262 Phosphorylation
T271 Phosphorylation
Y272 Phosphorylation
S277 Phosphorylation
K280 Ubiquitination
Y282 Phosphorylation
S287 Phosphorylation
T292 Phosphorylation
K304 Ubiquitination
K326 Acetylation
K326 Sumoylation
K326 Ubiquitination
T334 Phosphorylation
K336 Acetylation
K336 Sumoylation
K336 Ubiquitination
T337 Phosphorylation
K338 Methylation
K338 Ubiquitination
T340 Phosphorylation
T349 Phosphorylation
K352 Acetylation
K352 Sumoylation
K352 Ubiquitination
Y357 Phosphorylation
T361 Phosphorylation
K370 Acetylation
K370 Sumoylation
K370 Ubiquitination
S379 Phosphorylation
Y399 Phosphorylation
K401 Ubiquitination
Y408 Phosphorylation
S419 Phosphorylation
Site PTM Type Enzyme
S6 Phosphorylation
Y24 Phosphorylation
S38 Phosphorylation
K40 Acetylation
T41 Phosphorylation
S48 Phosphorylation
C54 S-Nitrosylation
K60 Ubiquitination
T73 Phosphorylation
T94 Phosphorylation
K96 Acetylation
K96 Sumoylation
K96 Ubiquitination
Y103 Phosphorylation
Y108 Phosphorylation
T109 Phosphorylation
K112 Acetylation
K112 Sumoylation
K112 Ubiquitination
K124 Methylation
K124 Ubiquitination
S158 Phosphorylation
Y161 Phosphorylation
K163 Acetylation
K163 Methylation
K163 Ubiquitination
K164 Ubiquitination
K166 Ubiquitination
Y172 Phosphorylation
Y185 Phosphorylation
S187 Phosphorylation
T190 Phosphorylation
T191 Phosphorylation
T193 Phosphorylation
T194 Phosphorylation
S198 Phosphorylation
Y210 Phosphorylation
T223 Phosphorylation
Y224 Phosphorylation
T225 Phosphorylation
S232 Phosphorylation
S236 Phosphorylation
S237 Phosphorylation
T239 Phosphorylation
S241 Phosphorylation
T253 Phosphorylation
T257 Phosphorylation
Y262 Phosphorylation
T271 Phosphorylation
Y272 Phosphorylation
S277 Phosphorylation
K280 Acetylation
K280 Ubiquitination
Y282 Phosphorylation
S287 Phosphorylation
T292 Phosphorylation
C295 S-Nitrosylation
K304 Ubiquitination
K311 Acetylation
K311 Ubiquitination
Y312 Phosphorylation
Y319 Phosphorylation
K326 Ubiquitination
K336 Sumoylation
K336 Ubiquitination
K338 Ubiquitination
R339 Methylation
S340 Phosphorylation
C347 S-Nitrosylation
T349 Phosphorylation
K352 Acetylation
K352 Sumoylation
K352 Ubiquitination
Y357 Phosphorylation
T361 Phosphorylation
K370 Acetylation
K370 Sumoylation
K370 Ubiquitination
C376 S-Nitrosylation
S379 Phosphorylation
K394 Acetylation
K394 Sumoylation
K394 Ubiquitination
Y399 Phosphorylation
K401 Acetylation
K401 Sumoylation
K401 Ubiquitination
Y408 Phosphorylation
S419 Phosphorylation
Y432 Phosphorylation P43405 (SYK)
S439 Phosphorylation
Y440 Phosphorylation

Research Backgrounds

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.

PTMs:

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. 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.

Some glutamate residues at the C-terminus are 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). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).

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.

Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.

Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution.

Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively.

Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1. 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.

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. 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).

Subcellular Location:

Cytoplasm>Cytoskeleton.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed at a high level in fetal brain.

Subunit Structure:

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. 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. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with SETD2; the interaction is independent on alpha-tubulin acetylation on Lys-40.

Family&Domains:

Belongs to the tubulin family.

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.

PTMs:

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. 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.

Some glutamate residues at the C-terminus are 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). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).

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.

Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.

Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution.

Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively.

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).

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. 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).

Subcellular Location:

Cytoplasm>Cytoskeleton.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. 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. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Family&Domains:

Belongs to the tubulin family.

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.

PTMs:

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. 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.

Some glutamate residues at the C-terminus are 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). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).

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.

Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.

Nitration of Tyr-449 is irreversible and interferes with normal dynein intracellular distribution.

Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively.

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).

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. 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).

Subcellular Location:

Cytoplasm>Cytoskeleton.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. 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. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Family&Domains:

Belongs to the tubulin family.

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 (By similarity).

PTMs:

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. 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.

Some glutamate residues at the C-terminus are 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). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).

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.

Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.

Nitration of Tyr-450 is irreversible and interferes with normal dynein intracellular distribution.

Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively.

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).

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. 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).

Subcellular Location:

Cytoplasm>Cytoskeleton.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. 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. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Family&Domains:

Belongs to the tubulin family.

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.

PTMs:

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. 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.

Some glutamate residues at the C-terminus are 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). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).

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.

Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.

Subcellular Location:

Cytoplasm>Cytoskeleton.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. 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. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with CFAP157 (By similarity).

Family&Domains:

Belongs to the tubulin family.

Research Fields

· Cellular Processes > Transport and catabolism > Phagosome.   (View pathway)

· Cellular Processes > Cell growth and death > Apoptosis.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Tight junction.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Gap junction.   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.

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