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NAD-dependent protein deacetylase sirtuin-1 (EC 3.5.1.-)

 SIR1_RAT                Reviewed;         555 AA.
A0A0G2JZ79;
08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
08-JUN-2016, sequence version 2.
27-SEP-2017, entry version 22.
RecName: Full=NAD-dependent protein deacetylase sirtuin-1 {ECO:0000250|UniProtKB:Q923E4};
EC=3.5.1.- {ECO:0000250|UniProtKB:Q96EB6};
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, metobolism,
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
HIST1H1E. 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. Modulates AP-1 transcription factor activity. 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 ACSS2 leading to its activation, and
HMGCS1. Involved in liver and muscle metabolism. Through
deacteylation and activation of PPARGC1A is required to activate
fatty acid oxidation in skeletel 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 faciliting 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. Deacteylates MECOM/EVI1.
Deacetylates PML at 'Lys-487' and this deacetylation promotes PML
control of PER2 nuclear localization. During the neurogenic
transition, repress 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. Involved in the CCAR2-mediated regulation of PCK1 and
NR1D1. Deacetylates CTNB1 at 'Lys-49' (By similarity). In POMC
(pro-opiomelanocortin) neurons, required for leptin-induced
activation of PI3K signaling (By similarity).
{ECO:0000250|UniProtKB:Q923E4, ECO:0000250|UniProtKB:Q96EB6}.
-!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
acetyl-ADP-ribose + a protein. {ECO:0000250|UniProtKB:Q96EB6,
ECO:0000255|PROSITE-ProRule:PRU00236}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ENZYME 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). {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 inhibition of the NAD-
dependent protein deacetylase activity. {ECO:0000250}.
-!- 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 HIST1H1E, deacetylation has been validated only for
HIST1H1E. {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; -.
RGD; 1308542; Sirt1.
PRO; PR:A0A0G2JZ79; -.
Proteomes; UP000002494; Unplaced.
Bgee; ENSRNOG00000051592; -.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IDA:RGD.
GO; GO:0043422; F:protein kinase B binding; IDA:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007569; P:cell aging; IEP:RGD.
GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
GO; GO:1904644; P:cellular response to curcumin; IEP:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP: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:0071303; P:cellular response to vitamin B3; IEP:RGD.
GO; GO:0070932; P:histone H3 deacetylation; IMP:RGD.
GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
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:0043392; P:negative regulation of DNA binding; IMP:RGD.
GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IMP:RGD.
GO; GO:0060125; P:negative regulation of growth hormone secretion; IMP:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
GO; GO:1901984; P:negative regulation of protein acetylation; IMP: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:0032720; P:negative regulation of tumor necrosis factor production; IMP:RGD.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IMP:RGD.
GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:RGD.
GO; GO:0010460; P:positive regulation of heart rate; IMP:RGD.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0090312; P:positive regulation of protein deacetylation; IMP:RGD.
GO; GO:0014858; P:positive regulation of skeletal muscle cell proliferation; IMP:RGD.
GO; GO:2000614; P:positive regulation of thyroid-stimulating hormone secretion; IMP:RGD.
GO; GO:0006476; P:protein deacetylation; IDA:RGD.
GO; GO:2000505; P:regulation of energy homeostasis; IMP:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0045471; P:response to ethanol; IDA:RGD.
GO; GO:1902617; P:response to fluoride; IEP:RGD.
GO; GO:1904373; P:response to kainic acid; IEP:RGD.
GO; GO:0010046; P:response to mycotoxin; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:1904638; P:response to resveratrol; IEP:RGD.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.50.1220; -; 1.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR003000; Sirtuin.
InterPro; IPR026590; Ssirtuin_cat_dom.
Pfam; PF02146; SIR2; 1.
SUPFAM; SSF52467; SSF52467; 1.
PROSITE; PS50305; SIRTUIN; 1.
3: Inferred from homology;
Apoptosis; Biological rhythms; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; Hydrolase; Metal-binding;
Methylation; Myogenesis; NAD; Nucleus; Phosphoprotein;
Reference proteome; rRNA processing; S-nitrosylation; Transcription;
Transcription regulation; Zinc.
CHAIN 1 555 NAD-dependent protein deacetylase
sirtuin-1.
/FTId=PRO_0000436411.
DOMAIN 52 306 Deacetylase sirtuin-type.
{ECO:0000255|PROSITE-ProRule:PRU00236}.
NP_BIND 69 88 NAD. {ECO:0000250}.
NP_BIND 153 156 NAD. {ECO:0000250}.
NP_BIND 248 250 NAD. {ECO:0000250}.
NP_BIND 273 275 NAD. {ECO:0000250}.
REGION 64 67 Required for interaction with the
sumoylated form of CCAR2.
{ECO:0000250|UniProtKB:Q96EB6}.
MOTIF 39 46 Nuclear localization signal.
{ECO:0000250|UniProtKB:Q923E4}.
MOTIF 241 247 Nuclear export signal.
{ECO:0000250|UniProtKB:Q923E4}.
ACT_SITE 171 171 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 179 179 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 182 182 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 203 203 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 206 206 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
BINDING 290 290 NAD; via amide nitrogen. {ECO:0000250}.
MOD_RES 203 203 S-nitrosocysteine.
{ECO:0000250|UniProtKB:Q923E4}.
MOD_RES 206 206 S-nitrosocysteine.
{ECO:0000250|UniProtKB:Q923E4}.
MOD_RES 338 338 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96EB6}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:Q96EB6}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000250|UniProtKB:Q923E4}.
MOD_RES 552 552 Phosphoserine.
{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


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