Search Results

Overview

Uniprot IDO94811
Protein NameTubulin polymerization-promoting protein
Gene NameTPPP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
147 VHRLIEGKAPIISGV
156 PIISGVTKAISSPTV
17 AANRTPPKSPGDPSK
171 SRLTDTTKFTGSHKE
185 ERFDPSGKGKGKAGR
187 FDPSGKGKGKAGRVD
206 SGYVSGYKHAGTYDQ
214 HAGTYDQKVQGGK**
4 ****MADKAKPAKAA
81 KNWSKLCKDCQVIDG

Function

Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath (PubMed:31522887). 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 (PubMed:31522887, PubMed:33831707). Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes (PubMed:31522887). Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear (PubMed:21316364, PubMed:21995432). 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:17105200, PubMed:17693641, PubMed:18028908, PubMed:26289831). Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (PubMed:20308065, PubMed:23093407). Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility (PubMed:23093407). Plays a role in cell proliferation by regulating the G1/S-phase transition (PubMed:23355470). Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 (PubMed:22328514)

Protein Sequence

10 MADKAKPAKA 20 ANRTPPKSPG 30 DPSKDRAAKR 40 LSLESEGAGE 50 GAAASPELSA 60 LEEAFRRFAV 70 HGDARATGRE 80 MHGKNWSKLC 90 KDCQVIDGRN 100 VTVTDVDIVF 110 SKIKGKSCRT 120 ITFEQFQEAL 130 EELAKKRFKD 140 KSSEEAVREV 150 HRLIEGKAPI 160 ISGVTKAISS 170 PTVSRLTDTT 180 KFTGSHKERF 190 DPSGKGKGKA 200 GRVDLVDESG 210 YVSGYKHAGT YDQKVQGGK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005874 microtubule
Cellular Component GO:0005815 microtubule organizing center
Cellular Component GO:0072686 mitotic spindle
Cellular Component GO:0005634 nucleus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0150051 postsynaptic Golgi apparatus
Molecular Function GO:0003924 GTPase activity
Molecular Function GO:0000287 magnesium ion binding
Molecular Function GO:0008017 microtubule binding
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0015631 tubulin binding
Biological Process GO:0030953 astral microtubule organization
Biological Process GO:0051301 cell division
Biological Process GO:0001578 microtubule bundle formation
Biological Process GO:0051418 microtubule nucleation by microtubule organizing center
Biological Process GO:0046785 microtubule polymerization
Biological Process GO:0032288 myelin assembly
Biological Process GO:1904428 negative regulation of tubulin deacetylation
Biological Process GO:0014003 oligodendrocyte development
Biological Process GO:0048709 oligodendrocyte differentiation
Biological Process GO:0031643 positive regulation of myelination
Biological Process GO:0032273 positive regulation of protein polymerization
Biological Process GO:0031334 positive regulation of protein-containing complex assembly
Biological Process GO:0070507 regulation of microtubule cytoskeleton organization

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.