TPPP
entrez
11076
canonical
uniprot
O94811
canonical
ensembl
ENSG00000171368
resolver
ensp
ENSP00000353785
resolver
ensp
ENSP00000559110
resolver
ensp
ENSP00000559111
resolver
ensp
ENSP00000559112
resolver
ensp
ENSP00000559113
resolver
ensp
ENSP00000559115
resolver
ensp
ENSP00000559116
resolver
ensp
ENSP00000559117
resolver
ensp
ENSP00000611455
resolver
ensp
ENSP00000611456
resolver
ensp
ENSP00000611457
resolver
ensp
ENSP00000611458
resolver
enst
ENST00000360578
resolver
enst
ENST00000889051
resolver
enst
ENST00000889052
resolver
enst
ENST00000889053
resolver
enst
ENST00000889054
resolver
enst
ENST00000889056
resolver
enst
ENST00000889057
resolver
enst
ENST00000889058
resolver
enst
ENST00000941396
resolver
enst
ENST00000941397
resolver
enst
ENST00000941398
resolver
enst
ENST00000941399
resolver
genesymbol
FREP1
resolver
genesymbol
TPPP
resolver
genesymbol_syn
TPPP
resolver
genesymbol_syn
TPPP1
resolver
hgnc
HGNC:24164
resolver
uniprot
Q4L233
resolver
uniprot_entry
Q4L233_HUMAN
resolver
uniprot_entry
TPPP_HUMAN
resolver
amino_acid_sequence
MADKAKPAKAANRTPPKSPGDPSKDRAAKRLSLESEGAGEGAAASPELSALEEAFRRFAVHGDARATGREMHGKNWSKLCKDCQVIDGRNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGKAPIISGVTKAISSPTVSRLTDTTKFTGSHKERFDPSGKGKGKAGRVDLVDESGYVSGYKHAGTYDQKVQGGK
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
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). {ECO:0000269|PubMed:17105200, ECO:0000269|PubMed:17693641, ECO:0000269|PubMed:18028908, ECO:0000269|PubMed:20308065, ECO:0000269|PubMed:21316364, ECO:0000269|PubMed:21995432, ECO:0000269|PubMed:22328514, ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:26289831, ECO:0000269|PubMed:31522887}.
uniprot
proteins
mass_dalton
23694
uniprot
proteins
mutagenesis
MUTAGEN 14; /note="T->A: In 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-18, A-45 and A-160."; /evidence="ECO:0000269|PubMed:23355470"; MUTAGEN 14; /note="T->E: In 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-18, E-45 and E-160."; /evidence="ECO:0000269|PubMed:23355470"; MUTAGEN 18; /note="S->A: In 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-14, A-45 and A-160."; /evidence="ECO:0000269|PubMed:23355470"; MUTAGEN 18; /note="S->E: In 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-14, E-45 and E-160."; /evidence="ECO:0000269|PubMed:23355470"; MUTAGEN 32; /note="S->A: In 3Ala; abolished phosphorylation by ROCK1, leading to delayed entry into S-phase; when associated with A-107 and A-159."; /evidence="ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470"; MUTAGEN 32; /note="S->E: In 3Glu; phosphomimetic mutant, leading to decreased transition of the G1/S-phase; when associated with E-07 and E-159."; /evidence="ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470"; MUTAGEN 45; /note="S->A: In 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-14, A-18 and A-160."; /evidence="ECO:0000269|PubMed:23355470"; MUTAGEN 45; /note="S->E: In 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-14, E-18 and E-160."; /evidence="ECO:0000269|PubMed:23355470"; MUTAGEN 107; /note="S->A: In 3Ala; abolished phosphorylation by ROCK1, leading to delayed entry into S-phase; when associated with A-32 and A-159."; /evidence="ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470"; MUTAGEN 107; /note="S->E: In 3Glu; phosphomimetic mutant, leading to decreased transition of the G1/S-phase; when associated with E-32 and E-159."; /evidence="ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470"; MUTAGEN 159; /note="S->A: In 3Ala; abolished phosphorylation by ROCK1, leading to delayed entry into S-phase; when associated with A-32 and A-107."; /evidence="ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470"; MUTAGEN 159; /note="S->E: In 3Glu; phosphomimetic mutant, leading to decreased transition of the G1/S-phase; when associated with E-32 and E-107."; /evidence="ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470"; MUTAGEN 160; /note="S->A: In 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-14, A-18 and A-45."; /evidence="ECO:0000269|PubMed:23355470"; MUTAGEN 160; /note="S->E: In 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-14, E-18 and E-45."; /evidence="ECO:0000269|PubMed:23355470
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by LIMK1 on serine residues; phosphorylation may alter the tubulin polymerization activity (PubMed:17693641, PubMed:18028908). Phosphorylation by LIMK2, but not LIMK1, regulates astral microtubule organization at early stage of mitosis (PubMed:22328514). Phosphorylation by ROCK1 at Ser-32, Ser-107 and Ser-159 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase (PubMed:23093407, PubMed:23355470). Phosphorylation by CDK1 inhibits the microtubule polymerizing activity (PubMed:23355470). {ECO:0000269|PubMed:17693641, ECO:0000269|PubMed:18028908, ECO:0000269|PubMed:22328514, ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470}.; PTM: Degraded by the proteasome; zinc-binding inhibits degradation by the proteasome. {ECO:0000269|PubMed:25445539}.
uniprot
proteins
protein_family
TPPP family
uniprot
proteins
pubmed
10083737
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15590652
uniprot
proteins
pubmed
17027006
uniprot
proteins
pubmed
17105200
uniprot
proteins
pubmed
17693641
uniprot
proteins
pubmed
18028908
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20308065
uniprot
proteins
pubmed
21316364
uniprot
proteins
pubmed
21565174
uniprot
proteins
pubmed
21995432
uniprot
proteins
pubmed
22328514
uniprot
proteins
pubmed
22484033
uniprot
proteins
pubmed
23093407
uniprot
proteins
pubmed
23355470
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25445539
uniprot
proteins
pubmed
26289831
uniprot
proteins
pubmed
31505170
uniprot
proteins
pubmed
31522887
uniprot
proteins
pubmed
33831707
uniprot
proteins
sequence_length
219
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi outpost {ECO:0000250|UniProtKB:D3ZQL7}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:D3ZQL7}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17105200}. Nucleus {ECO:0000269|PubMed:18028908}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22328514}. 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 (PubMed:18028908). Also found in the nucleus; however, nuclear localization is unclear and requires additional evidence (PubMed:18028908). Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies (PubMed:15590652, PubMed:17027006). During mitosis, colocalizes with LIMK2 at the mitotic spindle (PubMed:22328514). {ECO:0000250|UniProtKB:D3ZQL7, ECO:0000269|PubMed:15590652, ECO:0000269|PubMed:17027006, ECO:0000269|PubMed:18028908, ECO:0000269|PubMed:22328514}.
uniprot
proteins