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NAD-dependent protein deacetylase sirtuin-1 (EC 2 3 1 286) (NAD-dependent protein deacylase sirtuin-1) (EC 2 3 1 -)

 SIR1_RAT                Reviewed;         555 AA.
A0A0G2JZ79;
08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
08-JUN-2016, sequence version 2.
17-JUN-2020, entry version 41.
RecName: Full=NAD-dependent protein deacetylase sirtuin-1 {ECO:0000250|UniProtKB:Q923E4};
EC=2.3.1.286 {ECO:0000250|UniProtKB:Q96EB6};
AltName: Full=NAD-dependent protein deacylase sirtuin-1;
EC=2.3.1.- {ECO:0000250|UniProtKB:Q923E4};
Name=Sirt1 {ECO:0000312|RGD:1308542};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
Mockrin S., Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into mammalian
evolution.";
Nature 428:493-521(2004).
-!- FUNCTION: NAD-dependent protein deacetylase that links transcriptional
regulation directly to intracellular energetics and participates in the
coordination of several separated cellular functions such as cell
cycle, response to DNA damage, metabolism, apoptosis and autophagy. Can
modulate chromatin function through deacetylation of histones and can
promote alterations in the methylation of histones and DNA, leading to
transcriptional repression. Deacetylates a broad range of transcription
factors and coregulators, thereby regulating target gene expression
positively and negatively. Serves as a sensor of the cytosolic ratio of
NAD(+)/NADH which is altered by glucose deprivation and metabolic
changes associated with caloric restriction. Is essential in skeletal
muscle cell differentiation and in response to low nutrients mediates
the inhibitory effect on skeletal myoblast differentiation which also
involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide
phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy-
dependent nucleolar silencing) complex, a complex that mediates
silencing of rDNA in response to intracellular energy status and acts
by recruiting histone-modifying enzymes. The eNoSC complex is able to
sense the energy status of cell: upon glucose starvation, elevation of
NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3
deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by
SUV39H1 and the formation of silent chromatin in the rDNA locus.
Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits
skeletal muscle differentiation by deacetylating PCAF and MYOD1.
Deacetylates H2A and 'Lys-26' of H1-4. Deacetylates 'Lys-16' of histone
H4 (in vitro). Involved in NR0B2/SHP corepression function through
chromatin remodeling: Recruited to LRH1 target gene promoters by
NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading
to transcriptional repression. Proposed to contribute to genomic
integrity via positive regulation of telomere length; however, reports
on localization to pericentromeric heterochromatin are conflicting.
Proposed to play a role in constitutive heterochromatin (CH) formation
and/or maintenance through regulation of the available pool of nuclear
SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation
by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in
SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to
accelerate renewal of the heterochromatin which correlates with greater
genomic integrity during stress response. Deacetylates 'Lys-382' of
p53/TP53 and impairs its ability to induce transcription-dependent
proapoptotic program and modulate cell senescence. Deacetylates TAF1B
and thereby represses rDNA transcription by the RNA polymerase I.
Deacetylates MYC, promotes the association of MYC with MAX and
decreases MYC stability leading to compromised transformational
capability. Deacetylates FOXO3 in response to oxidative stress thereby
increasing its ability to induce cell cycle arrest and resistance to
oxidative stress but inhibiting FOXO3-mediated induction of apoptosis
transcriptional activity; also leading to FOXO3 ubiquitination and
protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4
in regulation of transcriptional activity and apoptosis. Deacetylates
DNMT1; thereby impairs DNMT1 methyltransferase-independent
transcription repressor activity, modulates DNMT1 cell cycle regulatory
function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa-
B p65 thereby inhibiting its transactivating potential and augments
apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1
and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and
enhancement of its transcriptional activity leading to increased
gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and
apoptotic function, possibly by deacetylation. Involved in HES1- and
HEY2-mediated transcriptional repression. In cooperation with MYCN
seems to be involved in transcriptional repression of DUSP6/MAPK3
leading to MYCN stabilization by phosphorylation at 'Ser-62'.
Deacetylates MEF2D. Required for antagonist-mediated transcription
suppression of AR-dependent genes which may be linked to local
deacetylation of histone H3. Represses HNF1A-mediated transcription.
Required for the repression of ESRRG by CREBZF. Deacetylates NR1H3 AND
NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates
transcription of NR1H3:RXR target genes, promotes NR1H3 proteosomal
degradation and results in cholesterol efflux; a promoter clearing
mechanism after reach round of transcription is proposed. Involved in
lipid metabolism. Implicated in regulation of adipogenesis and fat
mobilization in white adipocytes by repression of PPARG which probably
involves association with NCOR1 and SMRT/NCOR2. Deacetylates p300/EP300
and PRMT1. Deacetylates ACSS2 leading to its activation, and HMGCS1
deacetylation. Involved in liver and muscle metabolism. Through
deacetylation and activation of PPARGC1A is required to activate fatty
acid oxidation in skeletal muscle under low-glucose conditions and is
involved in glucose homeostasis. Involved in regulation of PPARA and
fatty acid beta-oxidation in liver. Involved in positive regulation of
insulin secretion in pancreatic beta cells in response to glucose; the
function seems to imply transcriptional repression of UCP2. Proposed to
deacetylate IRS2 thereby facilitating its insulin-induced tyrosine
phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby
decreasing its stability and transactivation in lipogenic gene
expression. Involved in DNA damage response by repressing genes which
are involved in DNA repair, such as XPC and TP73, deacetylating
XRCC6/Ku70, and facilitating recruitment of additional factors to sites
of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to
initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2.
Also involved in DNA repair of DNA double-strand breaks by homologous
recombination and specifically single-strand annealing independently of
XRCC6/Ku70 and NBN. Transcriptional suppression of XPC probably
involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT)
signaling. Transcriptional suppression of TP73 probably involves E2F4
and PCAF. Deacetylates WRN thereby regulating its helicase and
exonuclease activities and regulates WRN nuclear translocation in
response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and
stimulates cellular AP endonuclease activity by promoting the
association of APEX1 to XRCC1. Increases p53/TP53-mediated
transcription-independent apoptosis by blocking nuclear translocation
of cytoplasmic p53/TP53 and probably redirecting it to mitochondria.
Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to
sequester BAX away from mitochondria thereby inhibiting stress-induced
apoptosis. Is involved in autophagy, presumably by deacetylating ATG5,
ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced
binding of AKT1 and PDK1 to PIP3 and promotes their activation.
Proposed to play role in regulation of STK11/LBK1-dependent AMPK
signaling pathways implicated in cellular senescence which seems to
involve the regulation of the acetylation status of STK11/LBK1. Can
deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic
localization and association with STRAD; however, the relevance of such
activity in normal cells is unclear. In endothelial cells is shown to
inhibit STK11/LBK1 activity and to promote its degradation.
Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its
degradation. Deacetylates CIITA and augments its MHC class II
transactivation and contributes to its stability. Deacetylates
MECOM/EVI1. Deacetylates PML at 'Lys-487' and this deacetylation
promotes PML control of PER2 nuclear localization. During the
neurogenic transition, represses selective NOTCH1-target genes through
histone deacetylation in a BCL6-dependent manner and leading to
neuronal differentiation. Regulates the circadian expression of several
core clock genes, including ARNTL/BMAL1, RORC, PER2 and CRY1 and plays
a critical role in maintaining a controlled rhythmicity in histone
acetylation, thereby contributing to circadian chromatin remodeling.
Deacetylates ARNTL/BMAL1 and histones at the circadian gene promoters
in order to facilitate repression by inhibitory components of the
circadian oscillator. Deacetylates PER2, facilitating its
ubiquitination and degradation by the proteosome. Protects
cardiomyocytes against palmitate-induced apoptosis. Deacetylates XBP1
isoform 2; deacetylation decreases protein stability of XBP1 isoform 2
and inhibits its transcriptional activity. Deacetylates PCK1 and
directs its activity toward phosphoenolpyruvate production promoting
gluconeogenesis. Involved in the CCAR2-mediated regulation of PCK1 and
NR1D1. Deacetylates CTNB1 at 'Lys-49'. In POMC (pro-opiomelanocortin)
neurons, required for leptin-induced activation of PI3K signaling. In
addition to protein deacetylase activity, also acts as protein-lysine
deacylase: acts as a protein depropionylase by mediating
depropionylation of Osterix (SP7). Deacetylates SOX9; promoting SOX9
nuclear localization and transactivation activity.
{ECO:0000250|UniProtKB:Q923E4, ECO:0000250|UniProtKB:Q96EB6}.
-!- CATALYTIC ACTIVITY:
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;
EC=2.3.1.286; Evidence={ECO:0000250|UniProtKB:Q96EB6,
ECO:0000255|PROSITE-ProRule:PRU00236};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + N(6)-propanoyl-L-lysyl-[protein] + NAD(+) = 3''-O-
propanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
Xref=Rhea:RHEA:23500, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13758,
ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
ChEBI:CHEBI:57540, ChEBI:CHEBI:138019, ChEBI:CHEBI:145015;
Evidence={ECO:0000250|UniProtKB:Q923E4};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23501;
Evidence={ECO:0000250|UniProtKB:Q923E4};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q8IXJ6};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q8IXJ6};
-!- ACTIVITY REGULATION: Inhibited by nicotinamide. Activated by
resveratrol (3,5,4'-trihydroxy-trans-stilbene), butein (3,4,2',4'-
tetrahydroxychalcone), piceatannol (3,5,3',4'-tetrahydroxy-trans-
stilbene), Isoliquiritigenin (4,2',4'-trihydroxychalcone), fisetin
(3,7,3',4'-tetrahydroxyflavone) and quercetin (3,5,7,3',4'-
pentahydroxyflavone). MAPK8/JNK1 and RPS19BP1/AROS act as positive
regulators of deacetylation activity. Negatively regulated by CCAR2.
{ECO:0000250|UniProtKB:Q96EB6}.
-!- SUBUNIT: Interacts with XBP1 isoform 2 (By similarity). Found in a
complex with PCAF and MYOD1. Interacts with FOXO1; the interaction
deacetylates FOXO1, resulting in its nuclear retention and promotion of
its transcriptional activity Component of the eNoSC complex, composed
of SIRT1, SUV39H1 and RRP8. Interacts with HES1, HEY2 and PML.
Interacts with RPS19BP1/AROS. Interacts with CCAR2 (via N-terminus);
the interaction disrupts the interaction between SIRT1 and p53/TP53.
Interacts with SETD7; the interaction induces the dissociation of SIRT1
from p53/TP53 and increases p53/TP53 activity. Interacts with MYCN,
NR1I2, CREBZF, TSC2, TLE1, FOS, JUN, NR0B2, PPARG, NCOR, IRS1, IRS2 and
NMNAT1. Interacts with HNF1A; the interaction occurs under nutrient
restriction. Interacts with SUZ12; the interaction mediates the
association with the PRC4 histone methylation complex which is specific
as an association with PCR2 and PCR3 complex variants is not found.
Interacts with HIV-1 tat. Interacts with BCL6; leads to a epigenetic
repression of specific target genes. Interacts with CLOCK, ARNTL/BMAL1
and PER2 (By similarity). Interacts with PPARA; the interaction seems
to be modulated by NAD(+) levels. Interacts with NR1H3 and this
interaction is inhibited in the presence of CCAR2. Interacts with
CHEK2. Interacts with p53/TP53. Exhibits a preferential interaction
with sumoylated CCAR2 over its unmodified form (By similarity).
Interacts with PACS2 (By similarity). Interacts with SIRT7 (By
similarity). {ECO:0000250|UniProtKB:Q923E4,
ECO:0000250|UniProtKB:Q96EB6}.
-!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250|UniProtKB:Q96EB6}.
Cytoplasm {ECO:0000250|UniProtKB:Q96EB6}. Nucleus
{ECO:0000250|UniProtKB:Q96EB6}. Note=Recruited to the nuclear bodies
via its interaction with PML. Colocalized with APEX1 in the nucleus.
May be found in nucleolus, nuclear euchromatin, heterochromatin and
inner membrane (By similarity). Shuttles between nucleus and cytoplasm
(By similarity). Colocalizes in the nucleus with XBP1 isoform 2 (By
similarity). {ECO:0000250|UniProtKB:Q923E4,
ECO:0000250|UniProtKB:Q96EB6}.
-!- PTM: Methylated on multiple lysine residues; methylation is enhanced
after DNA damage and is dispensable for deacetylase activity toward
p53/TP53. {ECO:0000250|UniProtKB:Q96EB6}.
-!- PTM: Phosphorylated. Phosphorylated by STK4/MST1, resulting in
inhibition of SIRT1-mediated p53/TP53 deacetylation. Phosphorylation by
MAPK8/JNK1 at Thr-338 leads to increased nuclear localization and
enzymatic activity. Phosphorylation at Thr-338 by DYRK1A and DYRK3
activates deacetylase activity and promotes cell survival.
Phosphorylated by CaMK2, leading to increased p53/TP53 and NF-kappa-B
p65/RELA deacetylation activity (By similarity).
{ECO:0000250|UniProtKB:Q923E4, ECO:0000250|UniProtKB:Q96EB6}.
-!- PTM: S-nitrosylated by GAPDH, leading to inhibit the NAD-dependent
protein deacetylase activity. {ECO:0000250|UniProtKB:Q923E4}.
-!- PTM: Acetylated at various Lys residues. Deacetylated via an
autocatalytic mechanism. Autodeacetylation at Lys-46 promotes its
protein deacetylase activity. {ECO:0000250|UniProtKB:Q923E4}.
-!- MISCELLANEOUS: Red wine, which contains resveratrol, may participate in
activation of sirtuin proteins, and may therefore contribute to an
extended lifespan as has been observed in yeast.
{ECO:0000250|UniProtKB:Q96EB6}.
-!- MISCELLANEOUS: Calf histone H1 is used as substrate in the in vitro
deacetylation assay. As, in vivo, interaction occurs between SIRT1 with
H1-4, deacetylation has been validated only for H1-4.
{ECO:0000250|UniProtKB:Q96EB6}.
-!- MISCELLANEOUS: The reported ADP-ribosyltransferase activity of sirtuins
is likely to be an inefficient side reaction of the deacetylase
activity and may not be physiologically relevant.
{ECO:0000250|UniProtKB:Q96EB6}.
-!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
{ECO:0000305}.
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EMBL; AABR07044925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
SMR; A0A0G2JZ79; -.
STRING; 10116.ENSRNOP00000000427; -.
PaxDb; A0A0G2JZ79; -.
RGD; 1308542; Sirt1.
PRO; PR:A0A0G2JZ79; -.
Proteomes; UP000002494; Unplaced.
Bgee; ENSRNOG00000051592; Expressed in lung and 8 other tissues.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0000785; C:chromatin; ISO:RGD.
GO; GO:0005677; C:chromatin silencing complex; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0005739; C:mitochondrion; ISO:RGD.
GO; GO:0000790; C:nuclear chromatin; ISO:RGD.
GO; GO:0005635; C:nuclear envelope; ISO:RGD.
GO; GO:0005719; C:nuclear euchromatin; ISO:RGD.
GO; GO:0005720; C:nuclear heterochromatin; ISO:RGD.
GO; GO:0005637; C:nuclear inner membrane; ISO:RGD.
GO; GO:0005730; C:nucleolus; ISO:RGD.
GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0016605; C:PML body; ISO:RGD.
GO; GO:0033553; C:rDNA heterochromatin; ISO:RGD.
GO; GO:0043425; F:bHLH transcription factor binding; ISO:RGD.
GO; GO:0019213; F:deacetylase activity; ISO:RGD.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0042393; F:histone binding; ISO:RGD.
GO; GO:0004407; F:histone deacetylase activity; ISO:RGD.
GO; GO:0043398; F:HLH domain binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:1990254; F:keratin filament binding; ISO:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:RGD.
GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IDA:RGD.
GO; GO:0046969; F:NAD-dependent histone deacetylase activity (H3-K9 specific); ISO:RGD.
GO; GO:0034979; F:NAD-dependent protein deacetylase activity; ISO:RGD.
GO; GO:0035257; F:nuclear hormone receptor binding; ISO:RGD.
GO; GO:0002039; F:p53 binding; ISO:RGD.
GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
GO; GO:0033558; F:protein deacetylase activity; ISO:RGD.
GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
GO; GO:0043422; F:protein kinase B binding; IDA:RGD.
GO; GO:0106231; F:protein-propionyllysine depropionylase activity; ISS:UniProtKB.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
GO; GO:0008134; F:transcription factor binding; ISO:RGD.
GO; GO:0001525; P:angiogenesis; ISO:RGD.
GO; GO:0042595; P:behavioral response to starvation; ISO:RGD.
GO; GO:0007569; P:cell aging; IEP:RGD.
GO; GO:0001678; P:cellular glucose homeostasis; ISO:RGD.
GO; GO:1904646; P:cellular response to amyloid-beta; IMP:ARUK-UCL.
GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
GO; GO:1904644; P:cellular response to curcumin; IEP:RGD.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
GO; GO:0071479; P:cellular response to ionizing radiation; ISO:RGD.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:1904648; P:cellular response to rotenone; IEP:RGD.
GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD.
GO; GO:0071303; P:cellular response to vitamin B3; IEP:RGD.
GO; GO:0035356; P:cellular triglyceride homeostasis; ISO:RGD.
GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
GO; GO:0006325; P:chromatin organization; ISO:RGD.
GO; GO:0000183; P:chromatin silencing at rDNA; ISO:RGD.
GO; GO:0032922; P:circadian regulation of gene expression; ISO:RGD.
GO; GO:0007623; P:circadian rhythm; ISO:RGD.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISO:RGD.
GO; GO:0006343; P:establishment of chromatin silencing; ISO:RGD.
GO; GO:0055089; P:fatty acid homeostasis; ISO:RGD.
GO; GO:0016575; P:histone deacetylation; ISO:RGD.
GO; GO:0070932; P:histone H3 deacetylation; IMP:RGD.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
GO; GO:0033210; P:leptin-mediated signaling pathway; ISO:RGD.
GO; GO:0010934; P:macrophage cytokine production; ISO:RGD.
GO; GO:0030225; P:macrophage differentiation; ISO:RGD.
GO; GO:0006344; P:maintenance of chromatin silencing; ISO:RGD.
GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; ISO:RGD.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:RGD.
GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
GO; GO:2000655; P:negative regulation of cellular response to testosterone stimulus; ISO:RGD.
GO; GO:2000773; P:negative regulation of cellular senescence; ISO:RGD.
GO; GO:0043392; P:negative regulation of DNA binding; IMP:RGD.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISO:RGD.
GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:RGD.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IMP:RGD.
GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
GO; GO:0060125; P:negative regulation of growth hormone secretion; IMP:RGD.
GO; GO:0051097; P:negative regulation of helicase activity; ISO:RGD.
GO; GO:0071441; P:negative regulation of histone H3-K14 acetylation; ISO:RGD.
GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; ISO:RGD.
GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; ISO:RGD.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:ARUK-UCL.
GO; GO:1901215; P:negative regulation of neuron death; ISO:RGD.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:2000757; P:negative regulation of peptidyl-lysine acetylation; ISO:RGD.
GO; GO:0042326; P:negative regulation of phosphorylation; ISO:RGD.
GO; GO:0031393; P:negative regulation of prostaglandin biosynthetic process; ISO:RGD.
GO; GO:1901984; P:negative regulation of protein acetylation; IMP:RGD.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:RGD.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:RGD.
GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:RGD.
GO; GO:0032007; P:negative regulation of TOR signaling; ISO:RGD.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:RGD.
GO; GO:0001542; P:ovulation from ovarian follicle; ISO:RGD.
GO; GO:0018394; P:peptidyl-lysine acetylation; ISO:RGD.
GO; GO:0034983; P:peptidyl-lysine deacetylation; ISO:RGD.
GO; GO:0002821; P:positive regulation of adaptive immune response; ISO:RGD.
GO; GO:1904179; P:positive regulation of adipose tissue development; ISO:RGD.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IMP:RGD.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; ISO:RGD.
GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
GO; GO:2000774; P:positive regulation of cellular senescence; ISO:RGD.
GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:RGD.
GO; GO:0031937; P:positive regulation of chromatin silencing; ISO:RGD.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
GO; GO:0045739; P:positive regulation of DNA repair; ISO:RGD.
GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD.
GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:RGD.
GO; GO:0010460; P:positive regulation of heart rate; IMP:RGD.
GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; ISO:RGD.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:RGD.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
GO; GO:0016239; P:positive regulation of macroautophagy; ISO:RGD.
GO; GO:2000111; P:positive regulation of macrophage apoptotic process; ISO:RGD.
GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; ISO:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
GO; GO:0090312; P:positive regulation of protein deacetylation; IMP:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
GO; GO:0014858; P:positive regulation of skeletal muscle cell proliferation; IMP:RGD.
GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; ISO:RGD.
GO; GO:2000614; P:positive regulation of thyroid-stimulating hormone secretion; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
GO; GO:0006476; P:protein deacetylation; IDA:RGD.
GO; GO:0106230; P:protein depropionylation; ISS:UniProtKB.
GO; GO:0031648; P:protein destabilization; ISO:RGD.
GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
GO; GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; ISO:RGD.
GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
GO; GO:0070857; P:regulation of bile acid biosynthetic process; ISO:RGD.
GO; GO:0090335; P:regulation of brown fat cell differentiation; ISO:RGD.
GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
GO; GO:0032071; P:regulation of endodeoxyribonuclease activity; ISO:RGD.
GO; GO:0010906; P:regulation of glucose metabolic process; ISO:RGD.
GO; GO:0010883; P:regulation of lipid storage; ISO:RGD.
GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:RGD.
GO; GO:0035358; P:regulation of peroxisome proliferator activated receptor signaling pathway; ISO:RGD.
GO; GO:0071900; P:regulation of protein serine/threonine kinase activity; ISO:RGD.
GO; GO:0034391; P:regulation of smooth muscle cell apoptotic process; ISO:RGD.
GO; GO:0045471; P:response to ethanol; IDA:RGD.
GO; GO:1902617; P:response to fluoride; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; ISO:RGD.
GO; GO:0032868; P:response to insulin; ISO:RGD.
GO; GO:1904373; P:response to kainic acid; IEP:RGD.
GO; GO:0044321; P:response to leptin; ISO:RGD.
GO; GO:0010046; P:response to mycotoxin; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
GO; GO:1904638; P:response to resveratrol; IEP:RGD.
GO; GO:0000012; P:single strand break repair; ISO:RGD.
GO; GO:0007283; P:spermatogenesis; ISO:RGD.
GO; GO:0090400; P:stress-induced premature senescence; ISO:RGD.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
GO; GO:0006642; P:triglyceride mobilization; ISO:RGD.
GO; GO:0070914; P:UV-damage excision repair; ISO:RGD.
GO; GO:0050872; P:white fat cell differentiation; ISO:RGD.
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; IPR026590; Ssirtuin_cat_dom.
Pfam; PF02146; SIR2; 1.
SUPFAM; SSF52467; SSF52467; 1.
PROSITE; PS50305; SIRTUIN; 1.
3: Inferred from homology;
Acetylation; Apoptosis; Biological rhythms; Cytoplasm;
Developmental protein; Differentiation; Metal-binding; Methylation;
Myogenesis; NAD; Nucleus; Phosphoprotein; Reference proteome;
S-nitrosylation; Transcription; Transcription regulation; Transferase;
Zinc.
CHAIN 1..555
/note="NAD-dependent protein deacetylase sirtuin-1"
/id="PRO_0000436411"
DOMAIN 52..306
/note="Deacetylase sirtuin-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
NP_BIND 69..88
/note="NAD"
/evidence="ECO:0000250|UniProtKB:Q8IXJ6"
NP_BIND 153..156
/note="NAD"
/evidence="ECO:0000250|UniProtKB:Q8IXJ6"
NP_BIND 248..250
/note="NAD"
/evidence="ECO:0000250|UniProtKB:Q8IXJ6"
NP_BIND 273..275
/note="NAD"
/evidence="ECO:0000250|UniProtKB:Q8IXJ6"
REGION 64..67
/note="Required for interaction with the sumoylated form of
CCAR2"
/evidence="ECO:0000250|UniProtKB:Q96EB6"
MOTIF 39..46
/note="Nuclear localization signal"
/evidence="ECO:0000250|UniProtKB:Q923E4"
MOTIF 241..247
/note="Nuclear export signal"
/evidence="ECO:0000250|UniProtKB:Q923E4"
ACT_SITE 171
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
METAL 179
/note="Zinc"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
METAL 182
/note="Zinc"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
METAL 203
/note="Zinc"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
METAL 206
/note="Zinc"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
BINDING 290
/note="NAD; via amide nitrogen"
/evidence="ECO:0000250"
MOD_RES 46
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q923E4"
MOD_RES 185
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q923E4"
MOD_RES 203
/note="S-nitrosocysteine"
/evidence="ECO:0000250|UniProtKB:Q923E4"
MOD_RES 206
/note="S-nitrosocysteine"
/evidence="ECO:0000250|UniProtKB:Q923E4"
MOD_RES 238
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q923E4"
MOD_RES 321
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q923E4"
MOD_RES 338
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q96EB6"
MOD_RES 343
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q96EB6"
MOD_RES 352
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q96EB6"
MOD_RES 417
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q923E4"
MOD_RES 466
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q923E4"
MOD_RES 468
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q96EB6"
MOD_RES 552
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q96EB6"
SEQUENCE 555 AA; 62059 MW; A408C8A746AB812F CRC64;
MIGTDPRTIL KDLLPETIPP PELDDMTLWQ IVINILSEPP KRKKRKDINT IEDAVKLLQE
CKKIIVLTGA GVSVSCGIPD FRSRDGIYAR LAVDFPDLPD PQAMFDIEYF RKDPRPFFKF
AKEIYPGQFQ PSLCHKFIAL SDKEGKLLRN YTQNIDTLEQ VAGIQRIIQC HGSFATASCL
ICKYKVDCEA VRGDIFNQVV PRCPRCPADE PLAIMKPEIV FFGENLPEQF HRAMKYDKDE
VDLLIVIGSS LKVRPVALIP SSIPHEVPQI LINREPLPHL HFDVELLGDC DVIINELCHR
LGGEYAKLCC NPVKLSEITE KPPRTQKELV HLSELPPTPL HISEDSSSPE RTVPQDSSVI
ATLVDQTIKN KVDDLEVSEP KSCVEEKSQE VQTYRNVESI NVENPDFKAV GSSTGDKNER
TSVAETVRKC WPNRLAKEQI SKRLDGNQYL FVPPNRYIFH GAEVYSDSED DALSSSSCGS
NSDSGTCQSP SLEEPLEDES EIEEFYNGLE DDADRPECAG GSGADGGDQE AVNEAIAMKQ
ELTDVNCTPD KSEHY


Related products :

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ER1338 NAD-dependent protein deacetylase sirtuin-1 Elisa Kit 96T
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YHB0761Ra Rat NAD-dependent protein deacetylase sirtuin-1 (SIRT1)ELISA Kit 96T
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EIAAB38516 Mouse,Mus musculus,NAD-dependent deacetylase sirtuin-7,Sir2l7,SIR2-like protein 7,Sirt7
E0430r ELISA NAD-dependent deacetylase sirtuin-2,Rat,Rattus norvegicus,Sir2l2,SIR2-like protein 2,Sirt2 96T
E0430r ELISA kit NAD-dependent deacetylase sirtuin-2,Rat,Rattus norvegicus,Sir2l2,SIR2-like protein 2,Sirt2 96T
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EIAAB38511 Homo sapiens,Human,NAD-dependent deacetylase sirtuin-5,SIR2L5,SIR2-like protein 5,SIRT5
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U0430m CLIA Mouse,mSIR2L2,Mus musculus,NAD-dependent deacetylase sirtuin-2,Sir2l2,SIR2-like protein 2,Sirt2 96T
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Pathways :
WP1672: Mismatch repair
WP1676: Non-homologous end-joining
WP1493: Carbon assimilation C4 pathway
WP1678: Nucleotide excision repair
WP1625: Base excision repair
WP1619: Amino sugar and nucleotide sugar metabolism
WP232: G Protein Signaling Pathways
WP1049: G Protein Signaling Pathways
WP1694: Pyrimidine metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP1661: Glyoxylate and dicarboxylate metabolism
WP2371: Parkinsons Disease Pathway
WP1371: G Protein Signaling Pathways
WP1714: Tyrosine metabolism
WP1502: Mitochondrial biogenesis
WP1909: Signal regulatory protein (SIRP) family interactions
WP525: Mitochondrial Unfolded-Protein Response
WP73: G Protein Signaling Pathways
WP1613: 1,4-Dichlorobenzene degradation
WP210: Cytoplasmic Ribosomal Proteins
WP1624: Bacterial secretion system
WP2203: TSLP Signaling Pathway
WP1689: Porphyrin and chlorophyll metabolism
WP1693: Purine metabolism
WP1650: Fluorobenzoate degradation

Related Genes :
[SIRT1 SIR2L1] NAD-dependent protein deacetylase sirtuin-1 (hSIRT1) (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 1) (SIR2-like protein 1) (hSIR2) [Cleaved into: SirtT1 75 kDa fragment (75SirT1)]
[Sirt1 Sir2l1] NAD-dependent protein deacetylase sirtuin-1 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 1) (SIR2-like protein 1) (SIR2alpha) (Sir2) (mSIR2a) [Cleaved into: SirtT1 75 kDa fragment (75SirT1)]
[SIRT7 SIR2L7] NAD-dependent protein deacetylase sirtuin-7 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-7) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 7) (SIR2-like protein 7)
[Sirt7 Sir2l7] NAD-dependent protein deacetylase sirtuin-7 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-7) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 7) (SIR2-like protein 7)
[Sirt7] NAD-dependent protein deacetylase sirtuin-7 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-7) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 7) (SIR2-like protein 7)
[SIRT7] NAD-dependent protein deacetylase sirtuin-7 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-7) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 7) (SIR2-like protein 7)
[Sirt1] NAD-dependent protein deacetylase sirtuin-1 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-)
[Sirt2 Sir2l2] NAD-dependent protein deacetylase sirtuin-2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2) (mSIR2L2)
[SIRT3 SIR2L3] NAD-dependent protein deacetylase sirtuin-3, mitochondrial (hSIRT3) (EC 2.3.1.286) (Regulatory protein SIR2 homolog 3) (SIR2-like protein 3)
[Sirt3 Sir2l3] NAD-dependent protein deacetylase sirtuin-3 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 3) (SIR2-like protein 3) (mSIR2L3)
[SIRT2 SIR2L SIR2L2] NAD-dependent protein deacetylase sirtuin-2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2)
[Sirt2 Sir2l2] NAD-dependent protein deacetylase sirtuin-2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2)
[SIRT2 QtsA-13614] NAD-dependent protein deacetylase sirtuin-2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2)
[SIRT2] NAD-dependent protein deacetylase sirtuin-2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2)
[Sirt5 Sir2l5] NAD-dependent protein deacylase sirtuin-5, mitochondrial (EC 2.3.1.-) (Regulatory protein SIR2 homolog 5) (SIR2-like protein 5)
[HST3 YOR025W OR26.15] NAD-dependent histone deacetylase HST3 (EC 2.3.1.286) (Homologous to SIR2 protein 3) (Regulatory protein SIR2 homolog 3)
[sir2 cobB npdA MSMEG_5175 MSMEI_5041] NAD-dependent protein deacylase Sir2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog)
[HST2 YPL015C LPA2C] NAD-dependent protein deacetylase HST2 (EC 2.3.1.286) (Homologous to SIR2 protein 2) (Regulatory protein SIR2 homolog 2)
[sir-2.1 R11A8.4] NAD-dependent protein deacetylase sir-2.1 (EC 2.3.1.286) (Protein sir-2.1) (Regulatory protein SIR2 homolog 1)
[SIR2 MAR1 YDL042C D2714] NAD-dependent histone deacetylase SIR2 (EC 2.3.1.286) (Regulatory protein SIR2) (Silent information regulator 2)
[yjeF nnrD nnrE A6V01_16625 A9X72_22835 AC789_1c45800 ACN002_4392 AW106_17115 AWB10_23600 BB545_04070 BHJ80_02460 BN17_41441 BOH76_10905 BON72_19710 BON76_04155 BON95_14955 BTQ06_07255 BVL39_04290 C5N07_07145 C6669_06565 C7235_22665 C7B02_22745 C9162_14280 C9306_16010 C9Z28_08925 C9Z37_19300 C9Z69_17100 C9Z89_19770 CA593_04975 CIG45_09950 CMR93_01155 CO706_20770 COD30_21525 CR538_23135 CRD98_04165 CRM83_17370 D0X26_12915 D2184_07750 D4628_06615 D4636_22485 D5H35_20705 D6004_16440 D6T60_21965 D6T98_03825 D6X36_01235 D7Z75_22435 D9610_19255 D9F87_11835 D9G95_09255 D9J44_09440 D9K48_15185 D9S45_09270 DAH18_07435 DAH32_17635 DBQ99_23525 DEN97_13975 DEO19_11825 DIV22_15595 DL479_09745 DL530_20050 DL705_08080 DL800_29085 DLU50_02155 DLU67_01070 DLW60_20515 DM155_20490 DM267_22125 DM296_19440 DM820_22760 DN660_14005 DN700_22785 DN808_26000 DND79_22955 DOY67_18795 DP277_02605 DQF36_19900 DQF57_15735 DQF71_21295 DQF72_18940 DQP61_08520 DRW19_23395 DS143_20990 DS732_02620 DVB38_20810 E4K55_08625 EA223_01085 EAM59_16370 EAN77_04060 EAX79_02935 EB476_05880 EBM08_18815 ED600_08260 EG075_07990 EG599_16930 EG796_08825 EH412_13985 EHD79_20055 EHH55_18965 EHJ36_13975 EI028_05185 EJ366_20605 EJC75_20595 EKI52_12685 EYD11_20595 EYY78_08665 F7F00_14745 F7F18_09875 F7F23_18595 F7F26_20125 FQ915_09945 FQZ46_21935 GP664_20690 GP666_16320 GP935_18145 GP946_15695 GQN16_16290] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMA87_25350 BMT91_24760 BON76_21885 BvCmsC61A_00149 BvCmsKSNP120_04693 BvCmsKSP026_03873 BvCmsKSP076_04891 C7B08_25495 C9Z39_20510 CR538_10415 D3Y67_22910 D4023_08350 D9G42_11130 D9I97_22010 D9J11_25195 D9J52_16665 DJ503_24045 DLX40_18195 DM267_05215 DN627_18690 DP258_02540 DQE91_25240 EC3234A_36c00010 EC382_21100 ECTO6_01955 EHH55_07135 FORC82_1921 FV293_07100 GHR40_13690 GKE15_01795 GKE22_01795 GKE24_01795 GKE26_01795 GKE29_19015 GKE31_01795 GKE39_01795 GKE46_01795 GKE58_00235 GKE60_01795 GKE64_01795 GKE77_01800 GKE87_19180 GKE93_04790 GKF00_12775 GKF03_06100 GKF74_23075 GKF86_23585 GKF89_24720 GKG12_21690 GP700_02420 GP720_02430 GP727_01495 GP912_03195 NCTC12650_02300 NCTC8500_02249 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[cobB sir2 TM_0490] NAD-dependent protein deacetylase (EC 2.3.1.286) (Regulatory protein SIR2 homolog) (Sir2Tm)
[nnrD nnrE BHS81_24940 BMA87_06210 BON75_25135 BUE81_24185 BW690_00535 C5P01_11605 C9114_00800 C9141_20385 C9160_20005 C9201_17640 C9Z03_11025 C9Z39_09990 CF006_04810 CG692_00180 CI641_014360 CI693_12780 COD46_22200 CWS33_03515 D2185_07770 D3821_07085 D3O91_01535 D3Y67_00680 D4011_02210 D4638_06395 D6W00_07670 D6X63_00505 D7W70_13040 D8Y65_09515 D9D20_08295 D9D44_05795 D9G29_02235 D9H68_15720 D9H94_06330 D9I18_04405 D9J11_13510 D9J52_05810 D9J63_13405 DAH30_09295 DAH34_17710 DAH37_06235 DEN89_23315 DEO04_15015 DK132_00975 DL292_04305 DL326_12595 DLU82_19955 DM973_03315 DMC44_08050 DMY83_06260 DNW42_15620 DOY22_05310 DOY61_22135 DQE91_09055 DT034_15395 E0I42_01095 E2119_06500 E5P22_06605 E5S42_20000 EA213_12050 EAI42_08035 EAI42_19730 EAI46_08330 ED307_02425 EEP23_07485 EH186_16255 EI021_09655 EI041_04975 EIZ86_02830 EL75_3998 EL79_4176 EL80_4091 ELT20_09170 EPT01_09990 EXX24_09350 EXX78_19455 F1E13_09470 F1E19_03510 FQ022_21765 FQR64_20885 FRV13_14670 FV293_00830 GHR40_02625 GKF89_03420 GNZ03_04915 GP654_08840 GP689_08305 GQE30_17865 GQE34_01730 GQE51_12505 GQE64_09140 GQL64_02225 GRW80_01300 RK56_012375] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[hchA A8C65_13880 A9R57_25255 AMK83_16550 AWB10_10580 AWG90_013200 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BON65_01250 BON66_15955 BON86_06490 BON95_14610 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP047_03567 BvCmsSINP011_04162 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 C9Z23_21970 C9Z37_00915 C9Z43_06360 C9Z78_05610 CDC27_10055 CDL37_00765 CI693_17820 CI694_25210 CIG45_02340 COD46_23180 CQP61_17160 CRD98_26150 D2188_01360 D4628_09465 D6T98_10515 D6X36_17295 D9D20_21030 D9D43_06110 D9G29_20785 D9G69_01560 D9H68_20750 D9H70_25730 D9I87_15275 D9J58_04360 D9S45_22925 DEN89_24995 DEO04_05510 DL705_18425 DL800_09215 DLU50_17670 DLW88_16170 DLY44_04800 DND16_20085 DNR35_16895 DQE83_22775 DQP61_11280 DTL43_21780 DTZ20_09315 DU321_04440 DXT73_20690 E2134_24005 E2135_17195 E2855_02503 E2863_02392 E4K55_17625 E4K61_03800 E5P22_21380 E5S46_06650 EA213_19000 EA225_13320 EAX79_27320 EC95NR1_00961 ED648_25045 EG796_17135 EHD79_18540 EI028_00085 ELT20_21515 ELV08_24970 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 ExPECSC019_03873 ExPECSC038_01920 EXX71_02385 EXX78_21815 EYD11_09165 F7F11_20115 F7F18_11615 F7F29_22635 FNJ83_13175 FQ915_04255 FQR64_09390 FQZ46_21375 FWK02_18105 FZ043_14730 GIY13_02485 GNZ00_15670 GNZ02_11235 GNZ03_00440 GP712_09450 GQE64_12165 GQL64_10635 GQM17_02800 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC10974_02300 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13216_04667 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PGD_01271 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[nnrD nnrE AM465_02020 B9N33_15780 CCZ14_19830 CCZ17_16420 CRT43_25115 CUB99_10555 D3M98_16440 DMZ50_17425 E0L04_15155 EA159_10695 EA167_13135 EA191_15140 EA203_13015 EA232_12620 EA435_16485 EA834_13380 EGT48_17755 ELT34_11260 ELT48_15265 ELU82_07770 ELU96_21535 ELV13_19730 ELV24_17300 ELX79_17045 ELX83_07080 ELY23_03690 ELY24_03230 ELY50_08410 EPS76_03600 FNJ67_23970 GJ638_00690 GQE47_08805 GQS26_11015] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[nnrD nnrE AWE53_001910 AWF59_005750 B6V57_24370 BON91_13100 C4K41_15875 CT146_11325 DL251_17220 DL979_11485 DNR41_18350 DS966_08145 DU333_08330 EA189_18095 EA200_16470 EA222_17945 EA231_14430 EA242_18875 EA245_16610 EA250_13620 EA410_11490 EA429_17170 EA434_08485 ELT23_15105 ELT33_15080 EPS94_17855 EWK56_08710 EYX99_04120 GFU40_15060 GFU47_18670 GKE92_06870 GQE58_16030] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[nnrE nnrD A6581_03005 BON65_22485 BTQ04_18255 BWP17_13485 C5P44_18675 C9E67_27615 C9Z29_19790 CDC27_22640 CRE06_02245 CVH05_06805 D4074_23045 D4660_23100 D4L91_22960 D4M06_23395 D4U85_22780 D5I97_22295 D6C36_22900 D6D43_22980 D6X76_08950 D7K33_08105 D7K63_02170 D7K66_01520 D9H70_08725 D9L89_02165 D9X77_21450 D9X97_13480 DAH26_05170 DAH43_08760 DL455_22110 DLT82_15085 DLY44_22375 DM962_21215 DMI04_22175 DMI53_04255 DMO02_24530 DN703_23710 DNB37_06865 DNJ62_09625 DNK12_21320 DOE35_23455 DOS18_22575 DOT81_15665 DOU81_22350 DOY56_08285 DRP48_15945 DS721_07085 DTL90_17285 DXX80_015190 EB509_04120 EB510_02725 EB515_02120 EBA84_09245 EBJ06_01180 ECs5142 ED225_08520 ED607_06855 ED611_08790 ED903_07005 ED944_02120 EEA45_03685 EF173_02115 EGC26_01575 EGU87_19925 EHD63_02120 EHJ66_01180 EHV81_18940 EHV90_18430 EHW09_20350 EHX09_21145 EO241_14890 EXM29_20650 EXX06_20710 EXX23_19010 EXX53_17380 EXX55_21245 EXX87_19040 F7G01_00660 F7G03_07050 FE846_00250 GIY19_13310 GJD97_24935 GN312_12090] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[MJ0917] Bifunctional NADP phosphatase/NAD kinase [Includes: NAD kinase (EC 2.7.1.23) (ATP-dependent NAD kinase) (Poly(P)-dependent NAD kinase) (PPNK); NADP phosphatase (NADPase) (pNPPase) (EC 3.1.3.-)]
[nnrE nnrD AWG90_025805 B9M99_07915 D2188_20860 D3P01_12890 D9J60_12150 DND16_20500 DU321_10380 E0L12_16180 EA225_21040 EA233_14165 EHD45_05020 EQ830_14685 FNJ83_25735 GIY13_02560 GKE15_09400 GKE22_10415 GKE24_11540 GKE26_10895 GKE29_08435 GKE31_09680 GKE39_09275 GKE46_09075 GKE58_08910 GKE60_08975 GKE64_21185 GKE77_09955 GKE87_04180 GKE93_00770 GNZ00_20320 GNZ02_08865 GP712_07970 HMPREF3040_03054] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]

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