SIRT2
entrez
22933
canonical
uniprot
Q8IXJ6
canonical
ensembl
ENSG00000068903
resolver
ensembl
ENSG00000283100
resolver
ensp
ENSP00000249396
resolver
ensp
ENSP00000351809
resolver
ensp
ENSP00000375931
resolver
ensp
ENSP00000488998
resolver
ensp
ENSP00000542204
resolver
ensp
ENSP00000682053
resolver
enst
ENST00000358931
resolver
enst
ENST00000634707
resolver
genesymbol
SIRT2
resolver
genesymbol_syn
SIR2L
resolver
genesymbol_syn
SIR2L2
resolver
hgnc
HGNC:10886
resolver
uniprot
A0A0A0MRF5
resolver
uniprot
A8K3V1
resolver
uniprot
B2RB45
resolver
uniprot
O95889
resolver
uniprot
Q924Y7
resolver
uniprot
Q9P0G8
resolver
uniprot
Q9UNT0
resolver
uniprot
Q9Y6E9
resolver
uniprot
U5TP13
resolver
uniprot_entry
A0A0A0MRF5_HUMAN
resolver
uniprot_entry
SIR2_HUMAN
resolver
uniprot_sec
A8K3V1
resolver
uniprot_sec
B2RB45
resolver
uniprot_sec
O95889
resolver
uniprot_sec
Q924Y7
resolver
uniprot_sec
Q9P0G8
resolver
uniprot_sec
Q9UNT0
resolver
uniprot_sec
Q9Y6E9
resolver
uniprot_sec
U5TP13
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by Sirtinol, A3 and M15 small molecules (PubMed:11483616). Inhibited by nicotinamide. Inhibited by a macrocyclic peptide inhibitor S2iL5 (PubMed:24389023). Inhibited by EP300-induced acetylation (PubMed:18722353). {ECO:0000269|PubMed:11483616, ECO:0000269|PubMed:18722353, ECO:0000269|PubMed:24389023}.
uniprot
proteins
amino_acid_sequence
MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASIDAQSGAGVPNPSTSASPKKSPPPAKDEARTTEREKPQ
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.286
uniprot
proteins
function
FUNCTION: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors (PubMed:12620231, PubMed:16648462, PubMed:18249187, PubMed:18332217, PubMed:18995842, PubMed:20543840, PubMed:20587414, PubMed:21081649, PubMed:21726808, PubMed:21949390, PubMed:22014574, PubMed:22771473, PubMed:23468428, PubMed:23908241, PubMed:24177535, PubMed:24681946, PubMed:24769394, PubMed:24940000). Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy (PubMed:12620231, PubMed:16648462, PubMed:18249187, PubMed:18332217, PubMed:18995842, PubMed:20543840, PubMed:20587414, PubMed:21081649, PubMed:21726808, PubMed:21949390, PubMed:22014574, PubMed:22771473, PubMed:23468428, PubMed:23908241, PubMed:24177535, PubMed:24681946, PubMed:24769394, PubMed:24940000). Plays a major role in the control of cell cycle progression and genomic stability (PubMed:12697818, PubMed:16909107, PubMed:17488717, PubMed:17726514, PubMed:19282667, PubMed:23468428). Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes (PubMed:12697818, PubMed:16909107, PubMed:17488717, PubMed:17726514, PubMed:19282667, PubMed:23468428). Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis (PubMed:22014574). Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes (PubMed:23468428). Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis (PubMed:23468428). Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression (PubMed:23468428). Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response (PubMed:23468428). Also deacetylates histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition (PubMed:20587414). Upon bacterium Listeria monocytogenes infection, deacetylates 'Lys-18' of histone H3 in a receptor tyrosine kinase MET- and PI3K/Akt-dependent manner, thereby inhibiting transcriptional activity and promoting late stages of listeria infection (PubMed:23908241). During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function (PubMed:24940000). Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to regulate expression of VEGFA, a key regulator of angiogenesis (PubMed:24940000). Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells (PubMed:18332217, PubMed:18995842). Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha-tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation (PubMed:17488717). Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination (PubMed:21949390). Involved in several cellular metabolic pathways (PubMed:20543840, PubMed:21726808, PubMed:24769394). Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability (PubMed:21726808). Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage (PubMed:24769394). Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis (PubMed:20543840). Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity (PubMed:20543840). Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells (PubMed:20543840). Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagy (PubMed:20543840). Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation (By similarity). Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia (PubMed:24681946). Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF stimulation (PubMed:21081649). Inhibits transcriptional activation by deacetylating p53/TP53 and EP300 (PubMed:18249187, PubMed:18995842). Also deacetylates EIF5A (PubMed:22771473). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of N(6)-benzoyl (benzoyl) and N(6)-methacryl (methacryl) acyl groups from lysine residues, leading to histone debenzoylation and demethacrylation, respectively (PubMed:30154464, PubMed:34961760). Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions (PubMed:24769394). Plays a role as tumor suppressor (PubMed:22014574). In addition to protein deacetylase activity, also has activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as ARF6 and KRAS, thereby regulating their association with membranes (PubMed:25704306, PubMed:29239724, PubMed:32103017). {ECO:0000250|UniProtKB:Q8VDQ8, ECO:0000269|PubMed:12620231, ECO:0000269|PubMed:12697818, ECO:0000269|PubMed:16648462, ECO:0000269|PubMed:16909107, ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:17574768, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:18249187, ECO:0000269|PubMed:18332217, ECO:0000269|PubMed:18640115, ECO:0000269|PubMed:18722353, ECO:0000269|PubMed:18995842, ECO:0000269|PubMed:19282667, ECO:0000269|PubMed:20543840, ECO:0000269|PubMed:20587414, ECO:0000269|PubMed:21081649, ECO:0000269|PubMed:21726808, ECO:0000269|PubMed:21949390, ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:22771473, ECO:0000269|PubMed:22819792, ECO:0000269|PubMed:23468428, ECO:0000269|PubMed:23908241, ECO:0000269|PubMed:23932781, ECO:0000269|PubMed:24177535, ECO:0000269|PubMed:24681946, ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:24940000, ECO:0000269|PubMed:25704306, ECO:0000269|PubMed:29239724, ECO:0000269|PubMed:30154464, ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:34961760}.; FUNCTION: [Isoform 1]: Deacetylates EP300, alpha-tubulin and histone H3 and H4. {ECO:0000269|PubMed:24177535}.; FUNCTION: [Isoform 2]: Deacetylates EP300, alpha-tubulin and histone H3 and H4. {ECO:0000269|PubMed:24177535}.; FUNCTION: [Isoform 5]: Lacks deacetylation activity, at least toward known SIRT2 targets. {ECO:0000269|PubMed:24177535}.
uniprot
proteins
mass_dalton
43182
uniprot
proteins
mutagenesis
MUTAGEN 53; /note="S->A: Reduces deacetylase activity."; /evidence="ECO:0000269|PubMed:17516032"; MUTAGEN 97; /note="R->A: No effect on deacetylase activity."; /evidence="ECO:0000269|PubMed:11427894"; MUTAGEN 98; /note="S->A: Inhibits deacetylase activity."; /evidence="ECO:0000269|PubMed:17516032"; MUTAGEN 100; /note="S->A: Reduces deacetylase activity."; /evidence="ECO:0000269|PubMed:17516032"; MUTAGEN 116; /note="E->A: Reduces binding for the peptide inhibitor S2iL5."; /evidence="ECO:0000269|PubMed:24389023"; MUTAGEN 120; /note="E->A: Reduces binding for the peptide inhibitor S2iL5."; /evidence="ECO:0000269|PubMed:24389023"; MUTAGEN 167; /note="Q->A: Reduces deacetylase activity. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-168 and A-187."; /evidence="ECO:0000269|PubMed:11427894, ECO:0000269|PubMed:16909107"; MUTAGEN 168; /note="N->A: Abolishes deacetylation of alpha-tubulin. Inhibits deacetylation of histone H3 at 'Lys-18'. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-167 and A-187."; /evidence="ECO:0000269|PubMed:11427894, ECO:0000269|PubMed:12620231, ECO:0000269|PubMed:16909107, ECO:0000269|PubMed:23908241, ECO:0000269|PubMed:24769394"; MUTAGEN 170; /note="D->A,N: Reduces deacetylase activity."; /evidence="ECO:0000269|PubMed:11427894"; MUTAGEN 187; /note="H->Y,A: Inhibits deacetylase activity toward histone, alpha-tubulin, FZR1 and CDC20. No effect on CDK2-dependent phosphorylation. Does not inhibit interaction with alpha-tubulin, HDAC6, HIF1A and the cyclin E-CDK2 complex. Inhibits interaction with BEX4 and KMT5A. Abolishes deacetylation, dimeric formation and enzymatic activity increase of G6PD. Prevents histone H4 methylation at 'Lys-20'(H4K20me1) in metaphase chromosomes. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-167 and A-168. Strongly reduced activity toward long-chain fatty acyl groups."; /evidence="ECO:0000269|PubMed:10381378, ECO:0000269|PubMed:11427894, ECO:0000269|PubMed:11812793, ECO:0000269|PubMed:12620231, ECO:0000269|PubMed:12697818, ECO:0000269|PubMed:16909107, ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:17516032, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:24681946, ECO:0000269|PubMed:27512957, ECO:0000269|PubMed:29239724"; MUTAGEN 244; /note="F->A: Strongly reduces binding for the peptide inhibitor S2iL5."; /evidence="ECO:0000269|PubMed:24389023"; MUTAGEN 265; /note="Q->A: Reduces binding for the peptide inhibitor S2iL5."; /evidence="ECO:0000269|PubMed:24389023"; MUTAGEN 271; /note="S->A: Reduces binding for the peptide inhibitor S2iL5."; /evidence="ECO:0000269|PubMed:24389023"; MUTAGEN 279; /note="S->A: Reduces deacetylase activity."; /evidence="ECO:0000269|PubMed:17516032"; MUTAGEN 280; /note="T->A: Reduces deacetylase activity."; /evidence="ECO:0000269|PubMed:17516032"; MUTAGEN 294; /note="D->A: Reduces binding for the peptide inhibitor S2iL5."; /evidence="ECO:0000269|PubMed:24389023"; MUTAGEN 311; /note="S->A: Reduces deacetylase activity."; /evidence="ECO:0000269|PubMed:17516032"; MUTAGEN 315; /note="Y->A: Reduces deacetylase activity."; /evidence="ECO:0000269|PubMed:17516032"; MUTAGEN 364; /note="S->A: Abolishes CDK2-dependent phosphorylation."; /evidence="ECO:0000269|PubMed:17516032"; MUTAGEN 368; /note="S->A: Does not affect deacetylase activity. Abolishes CDK2-dependent phosphorylation. Inhibits cellular proliferation delay in the early metaphase to prevent chromosomal instability. Does not inhibit interaction with a cyclin E-CDK2 complex. Does not inhibit interaction with HDAC6 and ubiquitination. Inhibits cell adhesion and migration and neurite outgrowth. Inhibits deacetylase activity; when associated with A-372."; /evidence="ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:17516032, ECO:0000269|PubMed:18332217"; MUTAGEN 368; /note="S->D: Abolishes CDK2-dependent phosphorylation. Inhibits interaction with a cyclin E-CDK2 complex. Reduces strongly histone deacetylation activity."; /evidence="ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:17516032, ECO:0000269|PubMed:18332217"; MUTAGEN 368; /note="S->E: Abolishes CDK2-dependent phosphorylation."; /evidence="ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:17516032, ECO:0000269|PubMed:18332217"; MUTAGEN 372; /note="S->A: Reduces phosphorylation. Does not inhibit interaction with HDAC6, ubiquitination and deacetylase activity. Inhibits deacetylase activity; when associated with A-368."; /evidence="ECO:0000269|PubMed:17516032
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at phosphoserine and phosphothreonine. Phosphorylated at Ser-368 by a mitotic kinase CDK1/cyclin B at the G2/M transition; phosphorylation regulates the delay in cell-cycle progression. Phosphorylated at Ser-368 by a mitotic kinase G1/S-specific cyclin E/Cdk2 complex; phosphorylation inactivates SIRT2-mediated alpha-tubulin deacetylation and thereby negatively regulates cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Phosphorylated by cyclin A/Cdk2 and p35-Cdk5 complexes and to a lesser extent by the cyclin D3/Cdk4 and cyclin B/Cdk1, in vitro. Dephosphorylated at Ser-368 by CDC14A and CDC14B around early anaphase. {ECO:0000269|PubMed:12697818, ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:17516032, ECO:0000269|PubMed:18332217}.; PTM: Acetylated by EP300; acetylation leads both to the decreased of SIRT2-mediated alpha-tubulin deacetylase activity and SIRT2-mediated down-regulation of TP53 transcriptional activity. {ECO:0000269|PubMed:18722353}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:12697818, ECO:0000269|PubMed:17516032}.
uniprot
proteins
protein_family
Class I subfamily
uniprot
proteins
protein_family
Sirtuin family
uniprot
proteins
pubmed
10381378
uniprot
proteins
pubmed
10393250
uniprot
proteins
pubmed
10931946
uniprot
proteins
pubmed
11226170
uniprot
proteins
pubmed
11427894
uniprot
proteins
pubmed
11483616
uniprot
proteins
pubmed
11812793
uniprot
proteins
pubmed
12065666
uniprot
proteins
pubmed
12620231
uniprot
proteins
pubmed
12697818
uniprot
proteins
pubmed
12963026
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15213244
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16079181
uniprot
proteins
pubmed
16648462
uniprot
proteins
pubmed
16909107
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17488717
uniprot
proteins
pubmed
17516032
uniprot
proteins
pubmed
17574768
uniprot
proteins
pubmed
17726514
uniprot
proteins
pubmed
18249187
uniprot
proteins
pubmed
18332217
uniprot
proteins
pubmed
18640115
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18722353
uniprot
proteins
pubmed
18995842
uniprot
proteins
pubmed
19282667
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20543840
uniprot
proteins
pubmed
20587414
uniprot
proteins
pubmed
21081649
uniprot
proteins
pubmed
21726808
uniprot
proteins
pubmed
21791548
uniprot
proteins
pubmed
21949390
uniprot
proteins
pubmed
22014574
uniprot
proteins
pubmed
22771473
uniprot
proteins
pubmed
22819792
uniprot
proteins
pubmed
22943040
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23454361
uniprot
proteins
pubmed
23468428
uniprot
proteins
pubmed
23806683
uniprot
proteins
pubmed
23908241
uniprot
proteins
pubmed
23932781
uniprot
proteins
pubmed
24177535
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24389023
uniprot
proteins
pubmed
24681946
uniprot
proteins
pubmed
24769394
uniprot
proteins
pubmed
24940000
uniprot
proteins
pubmed
25672491
uniprot
proteins
pubmed
25704306
uniprot
proteins
pubmed
27512957
uniprot
proteins
pubmed
29239724
uniprot
proteins
pubmed
30154464
uniprot
proteins
pubmed
32103017
uniprot
proteins
pubmed
34961760
uniprot
proteins
sequence_length
389
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12697818, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:16648462, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:20543840, ECO:0000269|PubMed:23908241, ECO:0000269|PubMed:24177535}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8VDQ8}. Cytoplasm {ECO:0000269|PubMed:12697818, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:16648462, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:20543840, ECO:0000269|PubMed:23908241, ECO:0000269|PubMed:24681946}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12620231}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:17726514}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:17726514}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17488717}. Midbody {ECO:0000269|PubMed:17726514}. Chromosome {ECO:0000269|PubMed:16648462, ECO:0000269|PubMed:23468428}. Perikaryon {ECO:0000250|UniProtKB:Q8VDQ8}. Cell projection {ECO:0000250|UniProtKB:Q8VDQ8}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q8VDQ8}. Myelin membrane {ECO:0000250|UniProtKB:Q8VDQ8}. Note=Localizes in the cytoplasm during most of the cell cycle except in the G2/M transition and during mitosis, where it is localized in association with chromatin and induces deacetylation of histone at 'Lys-16' (H4K16ac) (PubMed:17726514, PubMed:23468428). Colocalizes with KMT5A at mitotic foci (PubMed:23468428). Colocalizes with CDK1 at centrosome during prophase and splindle fibers during metaphase (PubMed:17488717). Colocalizes with Aurora kinase AURKA at centrosome during early prophase and in the centrioles and growing mitotic spindle throughout metaphase (PubMed:17488717). Colocalizes with Aurora kinase AURKB during cytokinesis with the midbody (PubMed:17488717). Colocalizes with microtubules (PubMed:12620231). Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (By similarity). Shuttles between the cytoplasm and the nucleus through the CRM1 export pathway (PubMed:17726514). Colocalizes with EP300 in the nucleus (PubMed:24177535). Translocates to the nucleus and chromatin upon bacterium Listeria monocytogenes infection in interphase cells (PubMed:23908241). Deacetylates FOXO3 in the cytoplasm (By similarity). Colocalizes with PLP1 in internodal regions, at paranodal axoglial junction and Schmidt-Lanterman incisures of myelin sheath (By similarity). Colocalizes with CDK5R1 in the perikaryon, neurites and growth cone of hippocampal neurons (By similarity). Colocalizes with alpha-tubulin in neuronal growth cone (By similarity). Localizes in the cytoplasm and nucleus of germinal vesicle (GV) stage oocytes (By similarity). Colocalizes with alpha-tubulin on the meiotic spindle as the oocytes enter into metaphase, and also during meiotic anaphase and telophase, especially with the midbody (By similarity). Colocalizes with PARD3 in internodal region of axons (By similarity). Colocalizes with acetylated alpha-tubulin in cell projection processes during primary oligodendrocyte precursor (OLP) differentiation (By similarity). {ECO:0000250|UniProtKB:Q8VDQ8, ECO:0000269|PubMed:12620231, ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:23468428, ECO:0000269|PubMed:23908241, ECO:0000269|PubMed:24177535}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:24177535}. Nucleus {ECO:0000269|PubMed:24177535}. Note=Predominantly localized in the cytoplasmic. {ECO:0000269|PubMed:24177535}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:24177535}. Nucleus {ECO:0000269|PubMed:24177535}. Note=Predominantly localized in the cytoplasmic. {ECO:0000269|PubMed:24177535}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:24177535}. Nucleus {ECO:0000269|PubMed:24177535}. Note=Predominantly localized in the nucleus. {ECO:0000269|PubMed:24177535}.
uniprot
proteins