Q27957 · TPPP_BOVIN
- ProteinTubulin polymerization-promoting protein
- GeneTPPP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids218 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath (By similarity).
Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath (By similarity).
Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes (By similarity).
Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear (By similarity).
In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network (PubMed:14623963).
Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (By similarity).
Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility (By similarity).
Plays a role in cell proliferation by regulating the G1/S-phase transition (By similarity).
Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 (By similarity).
Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath (By similarity).
Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes (By similarity).
Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear (By similarity).
In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network (PubMed:14623963).
Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (By similarity).
Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility (By similarity).
Plays a role in cell proliferation by regulating the G1/S-phase transition (By similarity).
Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 (By similarity).
Catalytic activity
- GTP + H2O = GDP + H+ + phosphateThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTubulin polymerization-promoting protein
- EC number
- Short namesTPPP
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionQ27957
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation (By similarity).
Mainly localizes to the cytoskeleton. Also found in the nucleus; however, nuclear localization is unclear and requires additional evidences. Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies. During mitosis, colocalizes with LIMK2 at the mitotic spindle (By similarity).
Mainly localizes to the cytoskeleton. Also found in the nucleus; however, nuclear localization is unclear and requires additional evidences. Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies. During mitosis, colocalizes with LIMK2 at the mitotic spindle (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 131 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000221134 | 1-218 | Tubulin polymerization-promoting protein | |||
Sequence: MADSRPKPANKTPPKSPGEPAKDKAAKRLSLEAEGAGEGAAAAGAELSALEEAFRKFAVHGDARASGREMHGKNWSKLCRDCQVIDGRSVTVTDVDIVFSKIKGKSCRTITFEQFKEALEELAKKRFKDKSAEEAVREVHKLIEGKAPIISGVTKAISSPTVSRLTDTSKFTGSHKERFDPSGRGKGRAGRVDLVDESGYVPGYKHAGTYDQKVQGGK | ||||||
Modified residue | 12 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 16 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 30 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 91 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 106 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 151 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Modified residue | 158 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 159 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation may alter the tubulin polymerization activity.
Phosphorylated by LIMK1 on serine residues; phosphorylation may alter the tubulin polymerization activity. Phosphorylation by LIMK2, but not LIMK1, regulates astral microtubule organization at early stage of mitosis. Phosphorylation by ROCK1 at Ser-30, Ser-106 and Ser-158 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase. Phosphorylation by CDK1 inhibits the microtubule polymerizing activity.
Degraded by the proteasome; zinc-binding inhibits degradation by the proteasome.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer (By similarity).
Binds tubulin; binding is inhibited by GTP (PubMed:14623963).
Interacts with MAPK1 (PubMed:17693641).
Interacts with GAPDH; the interaction is direct (PubMed:17027006).
Interacts with LIMK1 (via the PDZ domain); the interaction is direct. Interacts with LIMK2. Interacts with HDAC6; thereby inhibiting the tubulin deacetylase activity of HDAC6. Interacts with aggregated SNCA; may have a pro-aggregatory role in synucleinopathies. Interacts with DYNLL1 (By similarity).
Interacts (via C-terminus) with S100A2, S100A6 and S100B; these interactions inhibit TPPP dimerization (By similarity).
Binds tubulin; binding is inhibited by GTP (PubMed:14623963).
Interacts with MAPK1 (PubMed:17693641).
Interacts with GAPDH; the interaction is direct (PubMed:17027006).
Interacts with LIMK1 (via the PDZ domain); the interaction is direct. Interacts with LIMK2. Interacts with HDAC6; thereby inhibiting the tubulin deacetylase activity of HDAC6. Interacts with aggregated SNCA; may have a pro-aggregatory role in synucleinopathies. Interacts with DYNLL1 (By similarity).
Interacts (via C-terminus) with S100A2, S100A6 and S100B; these interactions inhibit TPPP dimerization (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q27957 | GAPDH P10096 | 2 | EBI-7025612, EBI-7025562 |
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-37 | Disordered | ||||
Sequence: MADSRPKPANKTPPKSPGEPAKDKAAKRLSLEAEGAG | ||||||
Region | 1-115 | Mediates interaction with LIMK1 | ||||
Sequence: MADSRPKPANKTPPKSPGEPAKDKAAKRLSLEAEGAGEGAAAAGAELSALEEAFRKFAVHGDARASGREMHGKNWSKLCRDCQVIDGRSVTVTDVDIVFSKIKGKSCRTITFEQF | ||||||
Compositional bias | 17-31 | Basic and acidic residues | ||||
Sequence: PGEPAKDKAAKRLSL | ||||||
Region | 165-192 | Disordered | ||||
Sequence: LTDTSKFTGSHKERFDPSGRGKGRAGRV | ||||||
Compositional bias | 170-192 | Basic and acidic residues | ||||
Sequence: KFTGSHKERFDPSGRGKGRAGRV |
Domain
Most of the protein is composed of disordered regions. Zinc-binding induces structural rearrangement by promoting molten globule state formation.
Sequence similarities
Belongs to the TPPP family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length218
- Mass (Da)23,473
- Last updated1997-11-01 v1
- Checksum55F5DAB42DC3A638
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3Q1M210 | A0A3Q1M210_BOVIN | TPPP | 289 | ||
A0AAF7AK28 | A0AAF7AK28_BOVIN | TPPP | 260 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 17-31 | Basic and acidic residues | ||||
Sequence: PGEPAKDKAAKRLSL | ||||||
Compositional bias | 170-192 | Basic and acidic residues | ||||
Sequence: KFTGSHKERFDPSGRGKGRAGRV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X85738 EMBL· GenBank· DDBJ | CAA59741.1 EMBL· GenBank· DDBJ | mRNA | ||
BC133343 EMBL· GenBank· DDBJ | AAI33344.1 EMBL· GenBank· DDBJ | mRNA |