Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 SIR2_RAT                Reviewed;         350 AA.
Q5RJQ4;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
22-NOV-2017, entry version 113.
RecName: Full=NAD-dependent protein deacetylase sirtuin-2;
EC=3.5.1.-;
AltName: Full=Regulatory protein SIR2 homolog 2;
AltName: Full=SIR2-like protein 2;
Name=Sirt2; Synonyms=Sir2l2;
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 MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
PROTEIN SEQUENCE OF 6-18; 21-32; 41-116; 176-183; 187-216; 239-245;
302-308 AND 310-332, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[3]
INDUCTION.
PubMed=12065666; DOI=10.1046/j.1471-4159.2002.00847.x;
De Smet C., Nishimori H., Furnari F.B., Boegler O., Huang H.-J.S.,
Cavenee W.K.;
"A novel seven transmembrane receptor induced during the early steps
of astrocyte differentiation identified by differential expression.";
J. Neurochem. 81:575-588(2002).
[4]
FUNCTION IN DEACETYLATION OF ALPHA TUBULIN, FUNCTION AS REGULATOR OF
OLIGODENDROCYTE DIFFERENTIATION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF ASN-131; ASP-133 AND HIS-150.
PubMed=17344398; DOI=10.1523/JNEUROSCI.4181-06.2007;
Li W., Zhang B., Tang J., Cao Q., Wu Y., Wu C., Guo J., Ling E.A.,
Liang F.;
"Sirtuin 2, a mammalian homolog of yeast silent information regulator-
2 longevity regulator, is an oligodendroglial protein that decelerates
cell differentiation through deacetylating alpha-tubulin.";
J. Neurosci. 27:2606-2616(2007).
[5]
FUNCTION IN REGULATION OF PERIPHERAL MYELINATION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=21949390; DOI=10.1073/pnas.1104969108;
Beirowski B., Gustin J., Armour S.M., Yamamoto H., Viader A.,
North B.J., Michan S., Baloh R.H., Golden J.P., Schmidt R.E.,
Sinclair D.A., Auwerx J., Milbrandt J.;
"Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through
polarity protein Par-3/atypical protein kinase C (aPKC) signaling.";
Proc. Natl. Acad. Sci. U.S.A. 108:E952-961(2011).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-63; SER-170 AND
SER-330, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[7]
REVIEW, AND FUNCTION AS A TUMOR SUPPRESSOR.
PubMed=22943040;
Park S.H., Zhu Y., Ozden O., Kim H.S., Jiang H., Deng C.X., Gius D.,
Vassilopoulos A.;
"SIRT2 is a tumor suppressor that connects aging, acetylome, cell
cycle signaling, and carcinogenesis.";
Transl. Cancer Res. 1:15-21(2012).
-!- FUNCTION: NAD-dependent protein deacetylase, which deacetylates
internal lysines on histone and alpha-tubulin as well as many
other proteins such as key transcription factors
(PubMed:17344398). Participates in the modulation of multiple and
diverse biological processes such as cell cycle control, genomic
integrity, microtubule dynamics, cell differentiation, metabolic
networks, and autophagy. Plays a major role in the control of cell
cycle progression and genomic stability. Functions in the
antephase checkpoint preventing precocious mitotic entry in
response to microtubule stress agents, and hence allowing proper
inheritance of chromosomes. Positively regulates the anaphase
promoting complex/cyclosome (APC/C) ubiquitin ligase complex
activity by deacetylating CDC20 and FZR1, then allowing
progression through mitosis. Associates both with chromatin at
transcriptional start sites (TSSs) and enhancers of active genes.
Plays a role in cell cycle and chromatin compaction through
epigenetic modulation of the regulation of histone H4 'Lys-20'
methylation (H4K20me1) during early mitosis. Specifically
deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M
transition and metaphase enabling H4K20me1 deposition by KMT5A
leading to ulterior levels of H4K20me2 and H4K20me3 deposition
throughout cell cycle, and mitotic S-phase progression.
Deacetylates KMT5A modulating KMT5A chromatin localization during
the mitotic stress response. Deacetylates also histone H3 at 'Lys-
57' (H3K56ac) during the mitotic G2/M transition. During oocyte
meiosis progression, may deacetylate histone H4 at 'Lys-16'
(H4K16ac) and alpha-tubulin, regulating spindle assembly and
chromosome alignment by influencing microtubule dynamics and
kinetochore function. Deacetylates histone H4 at 'Lys-16'
(H4K16ac) at the VEGFA promoter and thereby contributes to
regulate expression of VEGFA, a key regulator of angiogenesis.
Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal
motility, oligodendroglial cell arbor projection processes and
proliferation of non-neuronal cells. Phosphorylation at Ser-368 by
a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated
alpha-tubulin deacetylation, negatively regulating cell adhesion,
cell migration and neurite outgrowth during neuronal
differentiation. Deacetylates PARD3 and participates in the
regulation of Schwann cell peripheral myelination formation during
early postnatal development and during postinjury remyelination.
Involved in several cellular metabolic pathways. Plays a role in
the regulation of blood glucose homeostasis by deacetylating and
stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in
response to low nutrient availability. Acts as a key regulator in
the pentose phosphate pathway (PPP) by deacetylating and
activating the glucose-6-phosphate G6PD enzyme, and therefore,
stimulates the production of cytosolic NADPH to counteract
oxidative damage. Maintains energy homeostasis in response to
nutrient deprivation as well as energy expenditure by inhibiting
adipogenesis and promoting lipolysis. Attenuates adipocyte
differentiation by deacetylating and promoting FOXO1 interaction
to PPARG and subsequent repression of PPARG-dependent
transcriptional activity. Plays a role in the regulation of
lysosome-mediated degradation of protein aggregates by autophagy
in neuronal cells. Deacetylates FOXO1 in response to oxidative
stress or serum deprivation, thereby negatively regulating FOXO1-
mediated autophagy (By similarity). Deacetylates a broad range of
transcription factors and co-regulators regulating target gene
expression. Deacetylates transcriptional factor FOXO3 stimulating
the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and
degradation (By similarity). Deacetylates HIF1A and therefore
promotes HIF1A degradation and inhibition of HIF1A transcriptional
activity in tumor cells in response to hypoxia. Deacetylates RELA
in the cytoplasm inhibiting NF-kappaB-dependent transcription
activation upon TNF-alpha stimulation. Inhibits transcriptional
activation by deacetylating p53/TP53 and EP300. Deacetylates also
EIF5A. Functions as a negative regulator on oxidative stress-
tolerance in response to anoxia-reoxygenation conditions. Plays a
role as tumor suppressor (By similarity).
{ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8,
ECO:0000269|PubMed:17344398, ECO:0000269|PubMed:21949390,
ECO:0000269|PubMed:22943040}.
-!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
acetyl-ADP-ribose + a protein. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q8IXJ6};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q8IXJ6};
-!- ENZYME REGULATION: Inhibited by Sirtinol, A3 and M15 small
molecules. Inhibited by nicotinamide. Inhibited by a macrocyclic
peptide inhibitor S2iL5. Inhibited by EP300-induced acetylation
(By similarity). {ECO:0000250|UniProtKB:Q8IXJ6}.
-!- SUBUNIT: Interacts with CDC20, FOXO3 and FZR1 (By similarity).
Associates with microtubules in primary cortical mature neurons
(By similarity). Homotrimer. Interacts (via both phosphorylated,
unphosphorylated, active or inactive forms) with HDAC6; the
interaction is necessary for the complex to interact with alpha-
tubulin, suggesting that these proteins belong to a large complex
that deacetylates the cytoskeleton. Interacts with FOXO1; the
interaction is disrupted upon serum-starvation or oxidative
stress, leading to increased level of acetylated FOXO1 and
induction of autophagy (By similarity). Interacts with RELA; the
interaction occurs in the cytoplasm and is increased in a TNF-
alpha-dependent manner. Interacts with HOXA10; the interaction is
direct. Interacts with YWHAB and YWHAG; the interactions occur in
a AKT-dependent manner and increase SIRT2-dependent TP53
deacetylation. Interacts with MAPK1/ERK2 and MAPK3/ERK1; the
interactions increase SIRT2 stability and deacetylation activity.
Interacts (phosphorylated form) with KMT5A isoform 2; the
interaction is direct, stimulates KMT5A-mediated methyltransferase
activity on histone at 'Lys-20' (H4K20me1) and is increased in a
H(2)O(2)-induced oxidative stress-dependent manner. Interacts with
G6PD; the interaction is enhanced by H(2)O(2) treatment. Interacts
with a G1/S-specific cyclin E-CDK2 complex. Interacts with AURKA,
CDK5R1 (p35 form) and CDK5 and HIF1A. Interacts with the tRNA
ligase SARS; recruited to the VEGFA promoter via interaction with
SARS (By similarity). Interacts with BEX4; negatively regulates
alpha-tubulin deacetylation by SIRT2 (By similarity).
{ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8VDQ8}.
Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IXJ6}.
Cytoplasm {ECO:0000250|UniProtKB:Q8VDQ8}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriole
{ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:Q8IXJ6}. Midbody
{ECO:0000250|UniProtKB:Q8IXJ6}. Chromosome
{ECO:0000250|UniProtKB:Q8IXJ6}. Perikaryon {ECO:0000250}. Cell
projection {ECO:0000250}. Cell projection, growth cone
{ECO:0000250}. Myelin membrane {ECO:0000250}. Note=Deacetylates
FOXO3 in the cytoplasm. Colocalizes with PLP1 in internodal
regions, at paranodal axoglial junction and Schmidt-Lanterman
incisures of myelin sheat. Colocalizes with CDK5R1 in the
perikaryon, neurites and growth cone of hippocampal neurons.
Colocalizes with alpha-tubulin in neuronal growth cone. Localizes
in the cytoplasm and nucleus of germinal vesicle (GV) stage
oocytes. Colocalizes with alpha-tubulin on the meiotic spindle as
the oocytes enter into metaphase, and also during meiotic anaphase
and telophase, especially with the midbody. Colocalizes with PARD3
in internodal region of axons. Colocalizes with acetylated alpha-
tubulin in cell projection processes during primary
oligodendrocyte precursor (OLP) differentiation (By similarity).
Localizes in the cytoplasm during most of the cell cycle except in
the G2/M transition and during mitosis, where it is localized in
association with chromatin and induces deacetylation of histone at
'Lys-16' (H4K16ac). Colocalizes with KMT5A at mitotic foci.
Colocalizes with CDK1 at centrosome during prophase and splindle
fibers during metaphase. Colocalizes with Aurora kinase AURKA at
centrosome during early prophase and in the centrioles and growing
mitotic spindle throughout metaphase. Colocalizes with Aurora
kinase AURKB during cytokinesis with the midbody. Colocalizes with
microtubules. Detected in perinuclear foci that may be aggresomes
containing misfolded, ubiquitinated proteins. Shuttles between the
cytoplasm and the nucleus through the CRM1 export pathway.
Colocalizes with EP300 in the nucleus (By similarity).
{ECO:0000250|UniProtKB:Q8IXJ6}.
-!- TISSUE SPECIFICITY: Expressed in the cerebellum, cerebral cortex
and cervival spinal cord. Expressed in Purkinje cells,
oligodendrocytes and Schwann cells (at protein level). Expressed
in the central nervous system (CNS). {ECO:0000269|PubMed:17344398,
ECO:0000269|PubMed:21949390}.
-!- INDUCTION: In oligodendrocytes during differentiation of CG-4
cells. {ECO:0000269|PubMed:12065666}.
-!- PTM: Phosphorylated at phosphoserine and phosphothreonine.
Phosphorylated at Ser-330 by a mitotic kinase CDK1/cyclin B at the
G2/M transition; phosphorylation regulates the delay in cell-cycle
progression. Phosphorylated at Ser-330 by a mitotic kinase G1/S-
specific cyclin E/Cdk2 complex; phosphorylation inactivates SIRT2-
mediated alpha-tubulin deacetylation and thereby negatively
regulates cell adhesion, cell migration and neurite outgrowth
during neuronal differentiation. Phosphorylated by cyclin A/Cdk2
and p35-Cdk5 complexes and to a lesser extent by the cyclin
D3/Cdk4 and cyclin B/Cdk1, in vitro. Dephosphorylated at Ser-330
by CDC14A and CDC14B around early anaphase (By similarity).
{ECO:0000250|UniProtKB:Q8IXJ6}.
-!- PTM: Acetylated by EP300; acetylation leads both to the decreased
of SIRT2-mediated alpha-tubulin deacetylase activity and SIRT2-
mediated down-regulation of TP53 transcriptional activity.
{ECO:0000250|UniProtKB:Q8IXJ6}.
-!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q8IXJ6}.
-!- MISCELLANEOUS: Has some ability to deacetylate histones in vitro,
but seeing its subcellular location, this is unlikely in vivo.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; BC086545; AAH86545.1; -; mRNA.
RefSeq; NP_001008369.1; NM_001008368.1.
UniGene; Rn.59887; -.
ProteinModelPortal; Q5RJQ4; -.
SMR; Q5RJQ4; -.
BioGrid; 262752; 1.
STRING; 10116.ENSRNOP00000059450; -.
ChEMBL; CHEMBL3232690; -.
iPTMnet; Q5RJQ4; -.
PhosphoSitePlus; Q5RJQ4; -.
PaxDb; Q5RJQ4; -.
PRIDE; Q5RJQ4; -.
Ensembl; ENSRNOT00000064153; ENSRNOP00000059450; ENSRNOG00000020102.
GeneID; 361532; -.
KEGG; rno:361532; -.
UCSC; RGD:621481; rat.
CTD; 22933; -.
RGD; 621481; Sirt2.
eggNOG; KOG2682; Eukaryota.
eggNOG; COG0846; LUCA.
GeneTree; ENSGT00870000136486; -.
HOGENOM; HOG000085952; -.
HOVERGEN; HBG057095; -.
InParanoid; Q5RJQ4; -.
KO; K11412; -.
PRO; PR:Q5RJQ4; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000020102; -.
ExpressionAtlas; Q5RJQ4; baseline and differential.
Genevisible; Q5RJQ4; RN.
GO; GO:0005814; C:centriole; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005694; C:chromosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0097386; C:glial cell projection; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
GO; GO:0043219; C:lateral loop; IDA:UniProtKB.
GO; GO:0072687; C:meiotic spindle; ISS:UniProtKB.
GO; GO:0005874; C:microtubule; ISO:RGD.
GO; GO:0030496; C:midbody; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISO:RGD.
GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0035748; C:myelin sheath abaxonal region; IDA:RGD.
GO; GO:0005720; C:nuclear heterochromatin; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0033010; C:paranodal junction; IDA:UniProtKB.
GO; GO:0033270; C:paranode region of axon; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:UniProtKB.
GO; GO:0005819; C:spindle; ISS:UniProtKB.
GO; GO:0097456; C:terminal loop; IDA:RGD.
GO; GO:0048487; F:beta-tubulin binding; ISO:RGD.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:RGD.
GO; GO:0004407; F:histone deacetylase activity; ISS:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
GO; GO:0070403; F:NAD+ binding; ISO:RGD.
GO; GO:0017136; F:NAD-dependent histone deacetylase activity; ISO:RGD.
GO; GO:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); ISS:UniProtKB.
GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IDA:UniProtKB.
GO; GO:0033558; F:protein deacetylase activity; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; ISO:RGD.
GO; GO:0042903; F:tubulin deacetylase activity; IDA:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
GO; GO:0008270; F:zinc ion binding; ISO:RGD.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0044242; P:cellular lipid catabolic process; ISS:UniProtKB.
GO; GO:0061433; P:cellular response to caloric restriction; ISS:UniProtKB.
GO; GO:0071872; P:cellular response to epinephrine stimulus; ISS:UniProtKB.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISS:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
GO; GO:0007417; P:central nervous system development; IEP:RGD.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0016575; P:histone deacetylation; ISO:RGD.
GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0022011; P:myelination in peripheral nervous system; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:1900425; P:negative regulation of defense response to bacterium; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; ISO:RGD.
GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IMP:RGD.
GO; GO:0070446; P:negative regulation of oligodendrocyte progenitor proliferation; IMP:UniProtKB.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0045843; P:negative regulation of striated muscle tissue development; ISO:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0034983; P:peptidyl-lysine deacetylation; ISS:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; ISS:UniProtKB.
GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISS:UniProtKB.
GO; GO:0045836; P:positive regulation of meiotic nuclear division; ISS:UniProtKB.
GO; GO:1900195; P:positive regulation of oocyte maturation; ISS:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:2000777; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0006476; P:protein deacetylation; IMP:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
GO; GO:0045598; P:regulation of fat cell differentiation; ISO:RGD.
GO; GO:0031641; P:regulation of myelination; IMP:UniProtKB.
GO; GO:1901026; P:ripoptosome assembly involved in necroptotic process; ISO:RGD.
GO; GO:0021762; P:substantia nigra development; ISO:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0090042; P:tubulin deacetylation; IDA:UniProtKB.
Gene3D; 3.40.50.1220; -; 1.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR003000; Sirtuin.
InterPro; IPR017328; Sirtuin_class_I.
InterPro; IPR026590; Ssirtuin_cat_dom.
Pfam; PF02146; SIR2; 1.
PIRSF; PIRSF037938; SIR2_euk; 1.
SUPFAM; SSF52467; SSF52467; 1.
PROSITE; PS50305; SIRTUIN; 1.
1: Evidence at protein level;
Autophagy; Cell cycle; Cell division; Cell membrane; Cell projection;
Chromosome; Complete proteome; Cytoplasm; Cytoskeleton;
Differentiation; Direct protein sequencing; Hydrolase; Meiosis;
Membrane; Metal-binding; Microtubule; Mitosis; NAD; Neurogenesis;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 350 NAD-dependent protein deacetylase
sirtuin-2.
/FTId=PRO_0000244536.
DOMAIN 28 303 Deacetylase sirtuin-type.
{ECO:0000255|PROSITE-ProRule:PRU00236}.
NP_BIND 48 52 NAD. {ECO:0000250|UniProtKB:Q8IXJ6}.
NP_BIND 58 60 NAD. {ECO:0000250|UniProtKB:Q8IXJ6}.
NP_BIND 130 133 NAD. {ECO:0000250|UniProtKB:Q8IXJ6}.
NP_BIND 225 226 NAD. {ECO:0000250|UniProtKB:Q8IXJ6}.
NP_BIND 249 251 NAD. {ECO:0000250|UniProtKB:Q8IXJ6}.
REGION 79 83 Peptide inhibitor binding. {ECO:0000250}.
REGION 195 264 Peptide inhibitor binding. {ECO:0000250}.
MOTIF 4 14 Nuclear export signal. {ECO:0000250}.
ACT_SITE 150 150 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 158 158 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 163 163 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 184 184 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 187 187 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
BINDING 287 287 NAD; via amide nitrogen.
{ECO:0000250|UniProtKB:Q8IXJ6}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 334 334 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IXJ6}.
MUTAGEN 131 131 N->A: Reduced deacetylase activity on
alpha-tubulin and stimulates
oligodendrocyte precursor (OLP)
differentiation.
{ECO:0000269|PubMed:17344398}.
MUTAGEN 133 133 D->A: Reduced deacetylase activity on
alpha-tubulin.
{ECO:0000269|PubMed:17344398}.
MUTAGEN 150 150 H->A: Reduced deacetylase activity on
alpha-tubulin and stimulates
oligodendrocyte precursor (OLP)
differentiation.
{ECO:0000269|PubMed:17344398}.
SEQUENCE 350 AA; 39319 MW; EA3621A7CCE695FB CRC64;
MDFLRNLFTQ TLGLGSQKER LLDELTLEGV TRYMQSERCR RVICLVGAGI STSAGIPDFR
SPSTGLYANL EKYHLPYPEA IFEISYFKKH PEPFFALAKE LYPGQFKPTI CHYFIRLLKE
KGLLLRCYTQ NIDTLERVAG LEPQDLVEAH GTFYTSHCVN TSCGKEYTMS WMKEKIFSEA
TPKCEKCQNV VKPDIVFFGE NLPPRFFSCM QSDFSKVDLL IIMGTSLQVQ PFASLISKAP
LATPRLLINK EKTGQTDPFL GMMMGLGGGM DFDSKKAYRD VAWLGDCDQG CLALADLLGW
KELEDLVRRE HANIDAQSGS QASNPSATVS PRKSPPPAKE AARTKEKEEH


Related products :

Catalog number Product name Quantity
18-003-43078 NAD-dependent deacetylase sirtuin-2 - EC 3.5.1.-; SIR2-like; SIR2-like protein 2 Polyclonal 0.05 mg Aff Pur
18-003-43078 NAD-dependent deacetylase sirtuin-2 - EC 3.5.1.-; SIR2-like; SIR2-like protein 2 Polyclonal 0.1 mg Protein A
EIAAB38504 Mouse,mSIR2a,Mus musculus,NAD-dependent deacetylase sirtuin-1,Sir2,SIR2alpha,Sir2l1,SIR2-like protein 1,Sirt1
18-003-43079 NAD-dependent deacetylase sirtuin-1 - EC 3.5.1.-; hSIRT1; hSIR2; SIR2-like protein 1 Polyclonal 0.1 mg Protein A
18-003-43079 NAD-dependent deacetylase sirtuin-1 - EC 3.5.1.-; hSIRT1; hSIR2; SIR2-like protein 1 Polyclonal 0.05 mg Aff Pur
18-003-43080 NAD-dependent deacetylase sirtuin-3. mitochondrial - EC 3.5.1.-; SIR2-like protein 3; hSIRT3 Polyclonal 0.1 mg Protein A
18-003-43080 NAD-dependent deacetylase sirtuin-3. mitochondrial - EC 3.5.1.-; SIR2-like protein 3; hSIRT3 Polyclonal 0.05 mg Aff Pur
EIAAB38513 Mouse,Mus musculus,NAD-dependent deacetylase sirtuin-6,Sir2l6,SIR2-like protein 6,Sirt6
EIAAB38516 Mouse,Mus musculus,NAD-dependent deacetylase sirtuin-7,Sir2l7,SIR2-like protein 7,Sirt7
EIAAB38510 Mouse,Mus musculus,NAD-dependent deacetylase sirtuin-5,Sir2l5,SIR2-like protein 5,Sirt5
E0430r ELISA kit NAD-dependent deacetylase sirtuin-2,Rat,Rattus norvegicus,Sir2l2,SIR2-like protein 2,Sirt2 96T
EIAAB38511 Homo sapiens,Human,NAD-dependent deacetylase sirtuin-5,SIR2L5,SIR2-like protein 5,SIRT5
E0430r ELISA NAD-dependent deacetylase sirtuin-2,Rat,Rattus norvegicus,Sir2l2,SIR2-like protein 2,Sirt2 96T
EIAAB38514 Homo sapiens,Human,NAD-dependent deacetylase sirtuin-6,SIR2L6,SIR2-like protein 6,SIRT6
EIAAB38515 Homo sapiens,Human,NAD-dependent deacetylase sirtuin-7,SIR2L7,SIR2-like protein 7,SIRT7
U0430r CLIA NAD-dependent deacetylase sirtuin-2,Rat,Rattus norvegicus,Sir2l2,SIR2-like protein 2,Sirt2 96T
E2135m ELISA kit Mouse,mSIR2L3,Mus musculus,NAD-dependent deacetylase sirtuin-3,Sir2l3,SIR2-like protein 3,Sirt3 96T
U0430m CLIA Mouse,mSIR2L2,Mus musculus,NAD-dependent deacetylase sirtuin-2,Sir2l2,SIR2-like protein 2,Sirt2 96T
E0430m ELISA kit Mouse,mSIR2L2,Mus musculus,NAD-dependent deacetylase sirtuin-2,Sir2l2,SIR2-like protein 2,Sirt2 96T
E2135m ELISA Mouse,mSIR2L3,Mus musculus,NAD-dependent deacetylase sirtuin-3,Sir2l3,SIR2-like protein 3,Sirt3 96T
U2135m CLIA kit Mouse,mSIR2L3,Mus musculus,NAD-dependent deacetylase sirtuin-3,Sir2l3,SIR2-like protein 3,Sirt3 96T
U2135m CLIA Mouse,mSIR2L3,Mus musculus,NAD-dependent deacetylase sirtuin-3,Sir2l3,SIR2-like protein 3,Sirt3 96T
E0430m ELISA Mouse,mSIR2L2,Mus musculus,NAD-dependent deacetylase sirtuin-2,Sir2l2,SIR2-like protein 2,Sirt2 96T
U0430h CLIA Homo sapiens,Human,NAD-dependent deacetylase sirtuin-2,SIR2L,SIR2L2,SIR2-like protein 2,SIRT2 96T
E0430h ELISA kit Homo sapiens,Human,NAD-dependent deacetylase sirtuin-2,SIR2L,SIR2L2,SIR2-like protein 2,SIRT2 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur