SIR2_MACFA
ID SIR2_MACFA Reviewed; 389 AA.
AC Q4R834;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=NAD-dependent protein deacetylase sirtuin-2;
DE EC=2.3.1.286 {ECO:0000250|UniProtKB:Q8IXJ6};
DE AltName: Full=NAD-dependent protein defatty-acylase sirtuin-2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q8IXJ6};
DE AltName: Full=Regulatory protein SIR2 homolog 2;
DE AltName: Full=SIR2-like protein 2;
GN Name=SIRT2; ORFNames=QtsA-13614;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NAD-dependent protein deacetylase, which deacetylates
CC internal lysines on histone and alpha-tubulin as well as many other
CC proteins such as key transcription factors. Participates in the
CC modulation of multiple and diverse biological processes such as cell
CC cycle control, genomic integrity, microtubule dynamics, cell
CC differentiation, metabolic networks, and autophagy. Plays a major role
CC in the control of cell cycle progression and genomic stability.
CC Functions in the antephase checkpoint preventing precocious mitotic
CC entry in response to microtubule stress agents, and hence allowing
CC proper inheritance of chromosomes. Positively regulates the anaphase
CC promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity
CC by deacetylating CDC20 and FZR1, then allowing progression through
CC mitosis. Associates both with chromatin at transcriptional start sites
CC (TSSs) and enhancers of active genes. Plays a role in cell cycle and
CC chromatin compaction through epigenetic modulation of the regulation of
CC histone H4 'Lys-20' methylation (H4K20me1) during early mitosis.
CC Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the
CC G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A
CC leading to ulterior levels of H4K20me2 and H4K20me3 deposition
CC throughout cell cycle, and mitotic S-phase progression. Deacetylates
CC KMT5A modulating KMT5A chromatin localization during the mitotic stress
CC response. Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the
CC mitotic G2/M transition. During oocyte meiosis progression, may
CC deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin,
CC regulating spindle assembly and chromosome alignment by influencing
CC microtubule dynamics and kinetochore function. Deacetylates histone H4
CC at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to
CC regulate expression of VEGFA, a key regulator of angiogenesis.
CC Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal
CC motility, oligodendroglial cell arbor projection processes and
CC proliferation of non-neuronal cells. Phosphorylation at Ser-368 by a
CC G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha-
CC tubulin deacetylation, negatively regulating cell adhesion, cell
CC migration and neurite outgrowth during neuronal differentiation.
CC Deacetylates PARD3 and participates in the regulation of Schwann cell
CC peripheral myelination formation during early postnatal development and
CC during postinjury remyelination. Involved in several cellular metabolic
CC pathways. Plays a role in the regulation of blood glucose homeostasis
CC by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1
CC activity in response to low nutrient availability. Acts as a key
CC regulator in the pentose phosphate pathway (PPP) by deacetylating and
CC activating the glucose-6-phosphate G6PD enzyme, and therefore,
CC stimulates the production of cytosolic NADPH to counteract oxidative
CC damage. Maintains energy homeostasis in response to nutrient
CC deprivation as well as energy expenditure by inhibiting adipogenesis
CC and promoting lipolysis. Attenuates adipocyte differentiation by
CC deacetylating and promoting FOXO1 interaction to PPARG and subsequent
CC repression of PPARG-dependent transcriptional activity. Plays a role in
CC the regulation of lysosome-mediated degradation of protein aggregates
CC by autophagy in neuronal cells. Deacetylates FOXO1 in response to
CC oxidative stress or serum deprivation, thereby negatively regulating
CC FOXO1-mediated autophagy (By similarity). Deacetylates a broad range of
CC transcription factors and co-regulators regulating target gene
CC expression. Deacetylates transcriptional factor FOXO3 stimulating the
CC ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and
CC degradation (By similarity). Deacetylates HIF1A and therefore promotes
CC HIF1A degradation and inhibition of HIF1A transcriptional activity in
CC tumor cells in response to hypoxia. Deacetylates RELA in the cytoplasm
CC inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha
CC stimulation. Inhibits transcriptional activation by deacetylating
CC p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a negative
CC regulator on oxidative stress-tolerance in response to anoxia-
CC reoxygenation conditions. Plays a role as tumor suppressor (By
CC similarity). In addition to protein deacetylase activity, also has
CC activity toward long-chain fatty acyl groups and mediates protein-
CC lysine demyristoylation and depalmitoylation of target proteins, such
CC as ARF6 and KRAS, thereby regulating their association with membranes
CC (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6,
CC ECO:0000250|UniProtKB:Q8VDQ8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-tetradecanoyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC tetradecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:70567, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15437,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:141129, ChEBI:CHEBI:189674;
CC Evidence={ECO:0000250|UniProtKB:Q8IXJ6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70568;
CC Evidence={ECO:0000250|UniProtKB:Q8IXJ6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-hexadecanoyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC hexadecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:70563, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14175,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:138936, ChEBI:CHEBI:189673;
CC Evidence={ECO:0000250|UniProtKB:Q8IXJ6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70564;
CC Evidence={ECO:0000250|UniProtKB:Q8IXJ6};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8IXJ6};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q8IXJ6};
CC -!- ACTIVITY REGULATION: Inhibited by Sirtinol, A3 and M15 small molecules.
CC Inhibited by nicotinamide (By similarity).
CC {ECO:0000250|UniProtKB:Q8IXJ6}.
CC -!- SUBUNIT: Interacts with CDC20, FOXO3 and FZR1 (By similarity).
CC Associates with microtubules in primary cortical mature neurons (By
CC similarity). Homotrimer. Interacts (via both phosphorylated,
CC unphosphorylated, active or inactive forms) with HDAC6; the interaction
CC is necessary for the complex to interact with alpha-tubulin, suggesting
CC that these proteins belong to a large complex that deacetylates the
CC cytoskeleton. Interacts with FOXO1; the interaction is disrupted upon
CC serum-starvation or oxidative stress, leading to increased level of
CC acetylated FOXO1 and induction of autophagy (By similarity). Interacts
CC with RELA; the interaction occurs in the cytoplasm and is increased in
CC a TNF-alpha-dependent manner. Interacts with HOXA10; the interaction is
CC direct. Interacts with YWHAB and YWHAG; the interactions occur in a
CC AKT-dependent manner and increase SIRT2-dependent TP53 deacetylation.
CC Interacts with MAPK1/ERK2 and MAPK3/ERK1; the interactions increase
CC SIRT2 stability and deacetylation activity. Interacts (phosphorylated
CC form) with KMT5A isoform 2; the interaction is direct, stimulates
CC KMT5A-mediated methyltransferase activity on histone at 'Lys-20'
CC (H4K20me1) and is increased in a H(2)O(2)-induced oxidative stress-
CC dependent manner. Interacts with G6PD; the interaction is enhanced by
CC H(2)O(2) treatment. Interacts with a G1/S-specific cyclin E-CDK2
CC complex. Interacts with AURKA, CDK5R1 (p35 form) and CDK5 and HIF1A.
CC Interacts with the tRNA ligase SARS1; recruited to the VEGFA promoter
CC via interaction with SARS1 (By similarity). Interacts with BEX4;
CC negatively regulates alpha-tubulin deacetylation by SIRT2 (By
CC similarity). {ECO:0000250|UniProtKB:Q8IXJ6,
CC ECO:0000250|UniProtKB:Q8VDQ8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IXJ6}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8VDQ8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q8IXJ6}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250|UniProtKB:Q8IXJ6}. Midbody
CC {ECO:0000250|UniProtKB:Q8IXJ6}. Chromosome
CC {ECO:0000250|UniProtKB:Q8IXJ6}. Perikaryon
CC {ECO:0000250|UniProtKB:Q8VDQ8}. Cell projection
CC {ECO:0000250|UniProtKB:Q8VDQ8}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q8VDQ8}. Myelin membrane
CC {ECO:0000250|UniProtKB:Q8VDQ8}. Note=Localizes in the cytoplasm during
CC most of the cell cycle except in the G2/M transition and during
CC mitosis, where it is localized in association with chromatin and
CC induces deacetylation of histone at 'Lys-16' (H4K16ac). Colocalizes
CC with KMT5A at mitotic foci. Colocalizes with CDK1 at centrosome during
CC prophase and splindle fibers during metaphase. Colocalizes with Aurora
CC kinase AURKA at centrosome during early prophase and in the centrioles
CC and growing mitotic spindle throughout metaphase. Colocalizes with
CC Aurora kinase AURKB during cytokinesis with the midbody. Colocalizes
CC with microtubules (By similarity). Detected in perinuclear foci that
CC may be aggresomes containing misfolded, ubiquitinated proteins (By
CC similarity). Shuttles between the cytoplasm and the nucleus through the
CC CRM1 export pathway. Colocalizes with EP300 in the nucleus.
CC Translocates to the nucleus and chromatin upon bacterium Listeria
CC monocytogenes infection in interphase cells (By similarity).
CC Deacetylates FOXO3 in the cytoplasm. Colocalizes with PLP1 in
CC internodal regions, at paranodal axoglial junction and Schmidt-
CC Lanterman incisures of myelin sheat. Colocalizes with CDK5R1 in the
CC perikaryon, neurites and growth cone of hippocampal neurons.
CC Colocalizes with alpha-tubulin in neuronal growth cone. Localizes in
CC the cytoplasm and nucleus of germinal vesicle (GV) stage oocytes.
CC Colocalizes with alpha-tubulin on the meiotic spindle as the oocytes
CC enter into metaphase, and also during meiotic anaphase and telophase,
CC especially with the midbody. Colocalizes with PARD3 in internodal
CC region of axons (By similarity). Colocalizes with acetylated alpha-
CC tubulin in cell projection processes during primary oligodendrocyte
CC precursor (OLP) differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8}.
CC -!- PTM: Phosphorylated at phosphoserine and phosphothreonine.
CC Phosphorylated at Ser-368 by a mitotic kinase CDK1/cyclin B at the G2/M
CC transition; phosphorylation regulates the delay in cell-cycle
CC progression. Phosphorylated at Ser-368 by a mitotic kinase G1/S-
CC specific cyclin E/Cdk2 complex; phosphorylation inactivates SIRT2-
CC mediated alpha-tubulin deacetylation and thereby negatively regulates
CC cell adhesion, cell migration and neurite outgrowth during neuronal
CC differentiation. Phosphorylated by cyclin A/Cdk2 and p35-Cdk5 complexes
CC and to a lesser extent by the cyclin D3/Cdk4 and cyclin B/Cdk1, in
CC vitro. Dephosphorylated at Ser-368 by CDC14A and CDC14B around early
CC anaphase (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6}.
CC -!- PTM: Acetylated by EP300; acetylation leads both to the decreased of
CC SIRT2-mediated alpha-tubulin deacetylase activity and SIRT2-mediated
CC down-regulation of TP53 transcriptional activity.
CC {ECO:0000250|UniProtKB:Q8IXJ6}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q8IXJ6}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000305}.
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DR EMBL; AB168626; BAE00738.1; -; mRNA.
DR AlphaFoldDB; Q4R834; -.
DR SMR; Q4R834; -.
DR STRING; 9541.XP_005589202.1; -.
DR eggNOG; KOG2682; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097386; C:glial cell projection; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR GO; GO:0044224; C:juxtaparanode region of axon; ISS:UniProtKB.
DR GO; GO:0043219; C:lateral loop; ISS:UniProtKB.
DR GO; GO:0072687; C:meiotic spindle; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0033010; C:paranodal junction; ISS:UniProtKB.
DR GO; GO:0033270; C:paranode region of axon; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); ISS:UniProtKB.
DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; ISS:UniProtKB.
DR GO; GO:0140773; F:NAD-dependent protein demyristoylase activity; ISS:UniProtKB.
DR GO; GO:0140774; F:NAD-dependent protein depalmitoylase activity; ISS:UniProtKB.
DR GO; GO:0033558; F:protein lysine deacetylase activity; ISS:UniProtKB.
DR GO; GO:0042903; F:tubulin deacetylase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044242; P:cellular lipid catabolic process; ISS:UniProtKB.
DR GO; GO:0061433; P:cellular response to caloric restriction; ISS:UniProtKB.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; ISS:UniProtKB.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
DR GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISS:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0070446; P:negative regulation of oligodendrocyte progenitor proliferation; ISS:UniProtKB.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
DR GO; GO:0034983; P:peptidyl-lysine deacetylation; ISS:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; ISS:UniProtKB.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISS:UniProtKB.
DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:1900195; P:positive regulation of oocyte maturation; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:2000777; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006476; P:protein deacetylation; ISS:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
DR GO; GO:0090042; P:tubulin deacetylation; ISS:UniProtKB.
DR Gene3D; 3.30.1600.10; -; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR017328; Sirtuin_class_I.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR PIRSF; PIRSF037938; SIR2_euk; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Cell membrane; Cell projection;
KW Chromosome; Cytoplasm; Cytoskeleton; Membrane; Metal-binding; Microtubule;
KW Mitosis; NAD; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT CHAIN 2..389
FT /note="NAD-dependent protein deacetylase sirtuin-2"
FT /id="PRO_0000244535"
FT DOMAIN 65..340
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 85..89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT BINDING 95..97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT BINDING 167..170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 262..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT BINDING 286..288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT BINDING 324
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJQ4"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJQ4"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJQ4"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXJ6"
SQ SEQUENCE 389 AA; 43222 MW; 97E344998577C506 CRC64;
MAEPDPSHPL ETQAGKVQEA QDSDSDSEGG AAGGEADMDF LRNLFSQTLS LGSQKERLLD
ELTLEGVARY MQSERCRRVI CLVGAGISTS AGIPDFRSPS TGLYDNLEKY HLPYPEAIFE
ISYFKKHPEP FFALAKELYP GQFKPTICHY FMRLLKDKGL LLRCYTQNID TLERIAGLEQ
EDLVEAHGTF YTSHCVSASC RHEYPLSWMK EKIFSEVTPK CEDCQSLVKP DIVFFGESLP
ARFFSCMQSD FLKVDLLLVM GTSLQVQPFA SLISKAPLST PRLLINKEKA GQSDPFLGMI
LGLGGGMDFD SKKAYRDVAW LGDCDQGCLA LAELLGWKKE LEDLVRREHA SIDAQSGAEA
PNPSTSASPR KSPPPAQDEA RTTEREKPQ
