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NAD-dependent protein deacetylase sirtuin-2 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2)

 SIR2_MACFA              Reviewed;         389 AA.
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
05-DEC-2018, entry version 77.
RecName: Full=NAD-dependent protein deacetylase sirtuin-2;
EC=3.5.1.- {ECO:0000250|UniProtKB:Q8IXJ6};
AltName: Full=Regulatory protein SIR2 homolog 2;
AltName: Full=SIR2-like protein 2;
Name=SIRT2; ORFNames=QtsA-13614;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
International consortium for macaque cDNA sequencing and analysis;
"DNA sequences of macaque genes expressed in brain or testis and its
evolutionary implications.";
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
-!- 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. 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. Plays a
major role in the control of cell cycle progression and genomic
stability. Functions in the antephase checkpoint preventing
precocious mitotic entry in response to microtubule stress agents,
and hence allowing proper inheritance of chromosomes. Positively
regulates the anaphase promoting complex/cyclosome (APC/C)
ubiquitin ligase complex activity by deacetylating CDC20 and FZR1,
then allowing progression through mitosis. Associates both with
chromatin at transcriptional start sites (TSSs) and enhancers of
active genes. 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. 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.
Deacetylates KMT5A modulating KMT5A chromatin localization during
the mitotic stress response. Deacetylates also histone H3 at 'Lys-
57' (H3K56ac) during the mitotic G2/M transition. 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. Deacetylates histone H4 at 'Lys-16'
(H4K16ac) at the VEGFA promoter and thereby contributes to
regulate expression of VEGFA, a key regulator of angiogenesis.
Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal
motility, oligodendroglial cell arbor projection processes and
proliferation of non-neuronal cells. 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. Deacetylates PARD3 and participates in the
regulation of Schwann cell peripheral myelination formation during
early postnatal development and during postinjury remyelination.
Involved in several cellular metabolic pathways. Plays a role in
the regulation of blood glucose homeostasis by deacetylating and
stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in
response to low nutrient availability. 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. Maintains energy homeostasis in response to
nutrient deprivation as well as energy expenditure by inhibiting
adipogenesis and promoting lipolysis. Attenuates adipocyte
differentiation by deacetylating and promoting FOXO1 interaction
to PPARG and subsequent repression of PPARG-dependent
transcriptional activity. Plays a role in the regulation of
lysosome-mediated degradation of protein aggregates by autophagy
in neuronal cells. Deacetylates FOXO1 in response to oxidative
stress or serum deprivation, thereby negatively regulating FOXO1-
mediated autophagy (By similarity). 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. Deacetylates RELA
in the cytoplasm inhibiting NF-kappaB-dependent transcription
activation upon TNF-alpha stimulation. Inhibits transcriptional
activation by deacetylating p53/TP53 and EP300. Deacetylates also
EIF5A. Functions as a negative regulator on oxidative stress-
tolerance in response to anoxia-reoxygenation conditions. Plays a
role as tumor suppressor (By similarity).
{ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8}.
Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-
acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q8IXJ6};
-!- ACTIVITY REGULATION: Inhibited by Sirtinol, A3 and M15 small
molecules. Inhibited by nicotinamide (By similarity).
-!- SUBUNIT: Interacts with CDC20, FOXO3 and FZR1 (By similarity).
Associates with microtubules in primary cortical mature neurons
(By similarity). Homotrimer. Interacts (via both phosphorylated,
unphosphorylated, active or inactive forms) with HDAC6; the
interaction is necessary for the complex to interact with alpha-
tubulin, suggesting that these proteins belong to a large complex
that deacetylates the cytoskeleton. Interacts with FOXO1; the
interaction is disrupted upon serum-starvation or oxidative
stress, leading to increased level of acetylated FOXO1 and
induction of autophagy (By similarity). Interacts with RELA; the
interaction occurs in the cytoplasm and is increased in a TNF-
alpha-dependent manner. Interacts with HOXA10; the interaction is
direct. Interacts with YWHAB and YWHAG; the interactions occur in
a AKT-dependent manner and increase SIRT2-dependent TP53
deacetylation. Interacts with MAPK1/ERK2 and MAPK3/ERK1; the
interactions increase SIRT2 stability and deacetylation activity.
Interacts (phosphorylated form) with KMT5A isoform 2; the
interaction is direct, stimulates KMT5A-mediated methyltransferase
activity on histone at 'Lys-20' (H4K20me1) and is increased in a
H(2)O(2)-induced oxidative stress-dependent manner. Interacts with
G6PD; the interaction is enhanced by H(2)O(2) treatment. Interacts
with a G1/S-specific cyclin E-CDK2 complex. Interacts with AURKA,
CDK5R1 (p35 form) and CDK5 and HIF1A. Interacts with the tRNA
ligase SARS; recruited to the VEGFA promoter via interaction with
SARS (By similarity). Interacts with BEX4; negatively regulates
alpha-tubulin deacetylation by SIRT2 (By similarity).
{ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8VDQ8}.
Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IXJ6}.
Cytoplasm {ECO:0000250|UniProtKB:Q8VDQ8}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriole
{ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:Q8IXJ6}. Midbody
{ECO:0000250|UniProtKB:Q8IXJ6}. Chromosome
{ECO:0000250|UniProtKB:Q8IXJ6}. Perikaryon {ECO:0000250}. Cell
projection {ECO:0000250}. Cell projection, growth cone
{ECO:0000250}. Myelin membrane {ECO:0000250}. Note=Deacetylates
FOXO3 in the cytoplasm. Colocalizes with PLP1 in internodal
regions, at paranodal axoglial junction and Schmidt-Lanterman
incisures of myelin sheat. Colocalizes with CDK5R1 in the
perikaryon, neurites and growth cone of hippocampal neurons.
Colocalizes with alpha-tubulin in neuronal growth cone. Localizes
in the cytoplasm and nucleus of germinal vesicle (GV) stage
oocytes. 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. Colocalizes with PARD3
in internodal region of axons. Colocalizes with acetylated alpha-
tubulin in cell projection processes during primary
oligodendrocyte precursor (OLP) differentiation (By similarity).
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). Colocalizes with KMT5A at mitotic foci.
Colocalizes with CDK1 at centrosome during prophase and splindle
fibers during metaphase. Colocalizes with Aurora kinase AURKA at
centrosome during early prophase and in the centrioles and growing
mitotic spindle throughout metaphase. Colocalizes with Aurora
kinase AURKB during cytokinesis with the midbody. Colocalizes with
microtubules. Detected in perinuclear foci that may be aggresomes
containing misfolded, ubiquitinated proteins. Shuttles between the
cytoplasm and the nucleus through the CRM1 export pathway.
Colocalizes with EP300 in the nucleus (By similarity).
-!- 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 (By similarity).
-!- 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.
-!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q8IXJ6}.
-!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; AB168626; BAE00738.1; -; mRNA.
UniGene; Mfa.8506; -.
ProteinModelPortal; Q4R834; -.
SMR; Q4R834; -.
PRIDE; Q4R834; -.
HOVERGEN; HBG057095; -.
GO; GO:0005814; C:centriole; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005694; C:chromosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0097386; C:glial cell projection; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0044224; C:juxtaparanode region of axon; ISS:UniProtKB.
GO; GO:0043219; C:lateral loop; ISS:UniProtKB.
GO; GO:0072687; C:meiotic spindle; ISS:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0030496; C:midbody; ISS:UniProtKB.
GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
GO; GO:0043209; C:myelin sheath; ISS:UniProtKB.
GO; GO:0005720; C:nuclear heterochromatin; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0033010; C:paranodal junction; ISS:UniProtKB.
GO; GO:0033270; C:paranode region of axon; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
GO; GO:0043220; C:Schmidt-Lanterman incisure; ISS:UniProtKB.
GO; GO:0005819; C:spindle; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; ISS:UniProtKB.
GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
GO; GO:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); ISS:UniProtKB.
GO; GO:0034979; F:NAD-dependent protein deacetylase activity; ISS:UniProtKB.
GO; GO:0033558; F:protein deacetylase activity; ISS:UniProtKB.
GO; GO:0042903; F:tubulin deacetylase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0044242; P:cellular lipid catabolic process; ISS:UniProtKB.
GO; GO:0061433; P:cellular response to caloric restriction; ISS:UniProtKB.
GO; GO:0071872; P:cellular response to epinephrine stimulus; ISS:UniProtKB.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISS:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
GO; GO:0022011; P:myelination in peripheral nervous system; ISS:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:1900425; P:negative regulation of defense response to bacterium; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0070446; P:negative regulation of oligodendrocyte progenitor proliferation; ISS:UniProtKB.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
GO; GO:0034983; P:peptidyl-lysine deacetylation; ISS:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; ISS:UniProtKB.
GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISS:UniProtKB.
GO; GO:0045836; P:positive regulation of meiotic nuclear division; ISS:UniProtKB.
GO; GO:1900195; P:positive regulation of oocyte maturation; ISS:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:2000777; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0006476; P:protein deacetylation; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
GO; GO:0090042; P:tubulin deacetylation; ISS:UniProtKB.
Gene3D; 3.30.1600.10; -; 1.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR003000; Sirtuin.
InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
InterPro; IPR017328; Sirtuin_class_I.
InterPro; IPR026590; Ssirtuin_cat_dom.
Pfam; PF02146; SIR2; 1.
PIRSF; PIRSF037938; SIR2_euk; 1.
SUPFAM; SSF52467; SSF52467; 1.
2: Evidence at transcript level;
Acetylation; Cell cycle; Cell division; Cell membrane;
Cell projection; Chromosome; Cytoplasm; Cytoskeleton; Hydrolase;
Membrane; Metal-binding; Microtubule; Mitosis; NAD; Nucleus;
Phosphoprotein; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q8IXJ6}.
CHAIN 2 389 NAD-dependent protein deacetylase
DOMAIN 65 340 Deacetylase sirtuin-type.
NP_BIND 85 89 NAD. {ECO:0000250|UniProtKB:Q8IXJ6}.
NP_BIND 95 97 NAD. {ECO:0000250|UniProtKB:Q8IXJ6}.
NP_BIND 167 170 NAD. {ECO:0000250|UniProtKB:Q8IXJ6}.
NP_BIND 262 263 NAD. {ECO:0000250|UniProtKB:Q8IXJ6}.
NP_BIND 286 288 NAD. {ECO:0000250|UniProtKB:Q8IXJ6}.
ACT_SITE 187 187 Proton acceptor. {ECO:0000255|PROSITE-
METAL 195 195 Zinc. {ECO:0000255|PROSITE-
METAL 200 200 Zinc. {ECO:0000255|PROSITE-
METAL 221 221 Zinc. {ECO:0000255|PROSITE-
METAL 224 224 Zinc. {ECO:0000255|PROSITE-
BINDING 324 324 NAD; via amide nitrogen.
MOD_RES 2 2 N-acetylalanine.
MOD_RES 23 23 Phosphoserine.
MOD_RES 25 25 Phosphoserine.
MOD_RES 27 27 Phosphoserine.
MOD_RES 53 53 Phosphoserine.
MOD_RES 100 100 Phosphoserine.
MOD_RES 207 207 Phosphoserine.
MOD_RES 368 368 Phosphoserine.
MOD_RES 372 372 Phosphoserine.
SEQUENCE 389 AA; 43222 MW; 97E344998577C506 CRC64;

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