Sirt1
entrez
93759
canonical
uniprot
Q923E4
canonical
ensembl
ENSMUSG00000020063
resolver
ensp
ENSMUSP00000020257
resolver
ensp
ENSMUSP00000101082
resolver
enst
ENSMUST00000105442
resolver
genesymbol
Sirt1
resolver
genesymbol_syn
Sir2l1
resolver
uniprot
F7DFF9
resolver
uniprot
Q3UNI1
resolver
uniprot
Q3USJ2
resolver
uniprot
Q3USY7
resolver
uniprot
Q53Z05
resolver
uniprot
Q9QXG8
resolver
uniprot_entry
F7DFF9_MOUSE
resolver
uniprot_entry
Q3UNI1_MOUSE
resolver
uniprot_entry
Q3USJ2_MOUSE
resolver
uniprot_entry
Q3USY7_MOUSE
resolver
uniprot_entry
Q53Z05_MOUSE
resolver
uniprot_entry
SIR1_MOUSE
resolver
uniprot_sec
Q9QXG8
resolver
activity_regulation
ACTIVITY REGULATION: Activated by TULP3 in response to calorie restriction (PubMed:39695235). MAPK8/JNK1 and RPS19BP1/AROS act as positive regulators of deacetylation activity (By similarity). Inhibited by nicotinamide. Negatively regulated by CCAR2 (By similarity). 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) (By similarity). {ECO:0000250|UniProtKB:Q96EB6, ECO:0000269|PubMed:39695235}.
uniprot
proteins
amino_acid_sequence
MADEVALALQAAGSPSAAAAMEAASQPADEPLRKRPRRDGPGLGRSPGEPSAAVAPAAAGCEAASAAAPAALWREAAGAAASAEREAPATAVAGDGDNGSGLRREPRAADDFDDDEGEEEDEAAAAAAAAAIGYRDNLLLTDGLLTNGFHSCESDDDDRTSHASSSDWTPRPRIGPYTFVQQHLMIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDINTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIEYFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRILQCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLGDCDVIINELCHRLGGEYAKLCCNPVKLSEITEKPPRPQKELVHLSELPPTPLHISEDSSSPERTVPQDSSVIATLVDQATNNNVNDLEVSESSCVEEKPQEVQTSRNVENINVENPDFKAVGSSTADKNERTSVAETVRKCWPNRLAKEQISKRLEGNQYLFVPPNRYIFHGAEVYSDSEDDVLSSSSCGSNSDSGTCQSPSLEEPLEDESEIEEFYNGLEDDTERPECAGGSGFGADGGDQEVVNEAIATRQELTDVNYPSDKS
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.286
uniprot
proteins
function
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 (PubMed:11250901, PubMed:11672522, PubMed:12651913, PubMed:12887892, PubMed:12960381, PubMed:15175761, PubMed:15220471, PubMed:15632193, PubMed:15744310, PubMed:15788402, PubMed:16098828, PubMed:16366736, PubMed:16790548, PubMed:16892051, PubMed:17098745, PubMed:17347648, PubMed:17620057, PubMed:17901049, PubMed:17936707, PubMed:18004385, PubMed:18296641, PubMed:18371449, PubMed:18477450, PubMed:18662546, PubMed:18662547, PubMed:18687677, PubMed:19299583, PubMed:19356714, PubMed:20167603, PubMed:20817729, PubMed:21176092, PubMed:21187328, PubMed:21189328, PubMed:21622680, PubMed:23160044, PubMed:28883095). Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression (By similarity). Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively (By similarity). Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction (By similarity). 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) (PubMed:12887892, PubMed:18477450). 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 (By similarity). 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 (PubMed:18004385). Deacetylates 'Lys-266' of SUV39H1, leading to its activation (By similarity). Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1 (PubMed:12887892). Deacetylates H2A and 'Lys-26' of H1-4 (By similarity). Deacetylates 'Lys-16' of histone H4 (in vitro) (By similarity). 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 (By similarity). Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting (PubMed:21187328). Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1 (By similarity). Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2 (By similarity). 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 (By similarity). Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence (PubMed:11672522, PubMed:12960381). Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I (PubMed:11250901). Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability (By similarity). 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 (By similarity). Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis (By similarity). Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing (By similarity). Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF (By similarity). Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1 (PubMed:17620057). Deacetylates FOXO1, which increases its DNA binding ability and enhances its transcriptional activity leading to increased gluconeogenesis in liver (PubMed:15220471, PubMed:15788402). Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation (PubMed:16892051). Involved in HES1- and HEY2-mediated transcriptional repression (By similarity). In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62' (By similarity). Deacetylates MEF2D (By similarity). Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3 (By similarity). Represses HNF1A-mediated transcription (PubMed:21176092). Required for the repression of ESRRG by CREBZF (By similarity). Deacetylates NR1H3 and NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteasomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed (PubMed:17936707). Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis (By similarity). Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2 (PubMed:15175761). Deacetylates p300/EP300 and PRMT1 (PubMed:15632193, PubMed:28883095). Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation (PubMed:16790548). Involved in liver and muscle metabolism (By similarity). 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 (PubMed:15716268, PubMed:15744310, PubMed:17347648, PubMed:23142079). Involved in regulation of PPARA and fatty acid beta-oxidation in liver (PubMed:19356714). Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2 (PubMed:16098828, PubMed:16366736, PubMed:17901049). Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation (PubMed:17901049). Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression (By similarity). 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 (By similarity). Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN (By similarity). Promotes DNA double-strand breaks by mediating deacetylation of SIRT6 (By similarity). Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling (By similarity). Transcriptional suppression of TP73 probably involves E2F4 and PCAF (By similarity). Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage (By similarity). Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1 (By similarity). Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER) (By similarity). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria (By similarity). Deacetylates XRCC6/Ku70 at 'Lys-537' and 'Lys-540' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis (By similarity). Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8 (PubMed:18296641, PubMed:21189328). Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation (By similarity). Acts as a regulator of AMPK activity in response to calorie restriction: deacetylates the ATP6V1E1 subunit of the V-ATPase complex following activation by TULP3, leading to (1) V-ATPase complex inhibition on lysosomes and (2) AMPK activation via the AXIN1-STK11/LKB1 axis (PubMed:39695235). 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 (PubMed:18687677). 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 (By similarity). In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation (By similarity). Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation (PubMed:17098745). Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability (By similarity). Deacetylates MECOM/EVI1 (By similarity). Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization (By similarity). During the neurogenic transition, represses selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation (By similarity). Regulates the circadian expression of several core clock genes, including BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling (PubMed:18662546, PubMed:18662547, PubMed:19299583). Deacetylates BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator (PubMed:18662546, PubMed:18662547, PubMed:19299583). Deacetylates PER2, facilitating its ubiquitination and degradation by the proteasome (PubMed:18662546). Protects cardiomyocytes against palmitate-induced apoptosis (PubMed:21622680). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (By similarity). Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis (PubMed:30193097). Involved in the CCAR2-mediated regulation of PCK1 and NR1D1 (By similarity). Deacetylates CTNB1 at 'Lys-49' (By similarity). In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling (PubMed:20620997). Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity (PubMed:26910618). Involved in the regulation of centrosome duplication: Deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly (By similarity). Deacetylates NDC80/HEC1 (By similarity). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by mediating protein delactylation, depropionylation and decrotonylation (PubMed:30026585). Mediates depropionylation of Osterix (SP7) (PubMed:30026585). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase (By similarity). Mediates protein delactylation of TEAD1 and YAP1 (By similarity). {ECO:0000250|UniProtKB:Q96EB6, ECO:0000269|PubMed:11250901, ECO:0000269|PubMed:11672522, ECO:0000269|PubMed:12651913, ECO:0000269|PubMed:12887892, ECO:0000269|PubMed:12960381, ECO:0000269|PubMed:15175761, ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:15632193, ECO:0000269|PubMed:15716268, ECO:0000269|PubMed:15744310, ECO:0000269|PubMed:15788402, ECO:0000269|PubMed:16098828, ECO:0000269|PubMed:16366736, ECO:0000269|PubMed:16790548, ECO:0000269|PubMed:16892051, ECO:0000269|PubMed:17098745, ECO:0000269|PubMed:17347648, ECO:0000269|PubMed:17620057, ECO:0000269|PubMed:17901049, ECO:0000269|PubMed:17936707, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:18296641, ECO:0000269|PubMed:18371449, ECO:0000269|PubMed:18477450, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:18662547, ECO:0000269|PubMed:18687677, ECO:0000269|PubMed:19299583, ECO:0000269|PubMed:19356714, ECO:0000269|PubMed:20167603, ECO:0000269|PubMed:20620997, ECO:0000269|PubMed:20817729, ECO:0000269|PubMed:21176092, ECO:0000269|PubMed:21187328, ECO:0000269|PubMed:21189328, ECO:0000269|PubMed:21622680, ECO:0000269|PubMed:23142079, ECO:0000269|PubMed:23160044, ECO:0000269|PubMed:26910618, ECO:0000269|PubMed:28883095, ECO:0000269|PubMed:30026585, ECO:0000269|PubMed:30193097, ECO:0000269|PubMed:39695235}.; FUNCTION: [Isoform 2]: Deacetylates 'Lys-382' of p53/TP53, however with lower activity than isoform 1. In combination, the two isoforms exert an additive effect. Isoform 2 regulates p53/TP53 expression and cellular stress response and is in turn repressed by p53/TP53 presenting a SIRT1 isoform-dependent auto-regulatory loop. {ECO:0000250|UniProtKB:Q96EB6}.; FUNCTION: [SirtT1 75 kDa fragment]: Catalytically inactive 75SirT1 may be involved in regulation of apoptosis. May be involved in protecting chondrocytes from apoptotic death by associating with cytochrome C and interfering with apoptosome assembly. {ECO:0000250|UniProtKB:Q96EB6}.
uniprot
proteins
mass_dalton
80372
uniprot
proteins
mutagenesis
MUTAGEN 37..38; /note="RR->AA: Abolishes nuclear localization; when associated with A-227; A-228; A-229 and A-230."; MUTAGEN 138..145; /note="LLLTDGLL->AAATGAA: Abolishes nuclear export; when associated with A-425; A-427; A-428; A-429; A-430 and A-431."; /evidence="ECO:0000269|PubMed:17197703"; MUTAGEN 154; /note="S->A: Abolishes in vitro phosphorylation by CaMK2; when associated with A-649; A-651 and A-683."; /evidence="ECO:0000269|PubMed:19680552"; MUTAGEN 222; /note="E->K: Abolished NAD-dependent protein deacetylase activity."; /evidence="ECO:0000269|PubMed:39695235"; MUTAGEN 227..230; /note="KKRK->AAAA: Abolishes nuclear localization; when associated with A-37 and A-38."; /evidence="ECO:0000269|PubMed:17197703"; MUTAGEN 230; /note="K->R: Decreased acetylation, leading to increased protein deacetylase activity."; /evidence="ECO:0000269|PubMed:28923965"; MUTAGEN 261; /note="G->A: Abolished ADP-ribosyltransferase activity in vitro without affecting the NAD-dependent protein deacetylase activity."; /evidence="ECO:0000269|PubMed:15716268"; MUTAGEN 355; /note="H->Y: Loss of deacetylation activity. Loss of inhibition of E2F1 and loss of coactivation of FOXO1-mediated transcription."; /evidence="ECO:0000269|PubMed:11672522, ECO:0000269|PubMed:12887892, ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:16892051"; MUTAGEN 363; /note="C->S: Does not affect S-nitrosylation."; /evidence="ECO:0000269|PubMed:20972425"; MUTAGEN 366; /note="C->S: Does not affect S-nitrosylation."; /evidence="ECO:0000269|PubMed:20972425"; MUTAGEN 369; /note="K->R: Does not affect protein deacetylase activity."; /evidence="ECO:0000269|PubMed:28923965"; MUTAGEN 387; /note="C->S: Impairs S-nitrosylation. Abolishes S-nitrosylation; when associated with S-390."; /evidence="ECO:0000269|PubMed:20972425"; MUTAGEN 390; /note="C->S: Impairs S-nitrosylation. Abolishes S-nitrosylation; when associated with S-387."; /evidence="ECO:0000269|PubMed:20972425"; MUTAGEN 425..431; /note="VDLLIVI->ADAAAAA: Abolishes nuclear export; when associated with A-138; A-139; A-140; A-144 and A-145."; /evidence="ECO:0000269|PubMed:17197703"; MUTAGEN 505; /note="K->R: Does not affect protein deacetylase activity."; /evidence="ECO:0000269|PubMed:28923965"; MUTAGEN 522; /note="T->D: Increased deacetylase activity toward p53/TP53 and increases resistance to genotoxic stress (mimicks residue phosphorylation)."; /evidence="ECO:0000269|PubMed:20167603"; MUTAGEN 522; /note="T->V: Reduces phosphorylation. Impairs deacetylase activity toward p53/TP53 and decreases resistance to genotoxic stress. Does not change nuclear localization."; /evidence="ECO:0000269|PubMed:20167603"; MUTAGEN 600; /note="K->R: Does not affect protein deacetylase activity."; /evidence="ECO:0000269|PubMed:28923965"; MUTAGEN 649; /note="S->A: Abolishes in vitro phosphorylation by CaMK2; when associated with A-154; A-651 and A-683."; /evidence="ECO:0000269|PubMed:19680552"; MUTAGEN 651; /note="S->A: Abolishes in vitro phosphorylation by CaMK2; when associated with A-154; A-649 and A-683."; /evidence="ECO:0000269|PubMed:19680552"; MUTAGEN 683; /note="S->A: Abolishes in vitro phosphorylation by CaMK2; when associated with A-154; A-649 and A-651."; /evidence="ECO:0000269|PubMed:19680552
uniprot
proteins
post_translational_modification
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 Ser-46 and Thr-522 leads to increased nuclear localization and enzymatic activity. Phosphorylation at Thr-522 by DYRK1A and DYRK3 activates deacetylase activity and promotes cell survival (PubMed:20167603). Phosphorylation by mammalian target of rapamycin complex 1 (mTORC1) at Ser-46 inhibits deacetylation activity. Phosphorylated by CaMK2, leading to increased p53/TP53 and NF-kappa-B p65/RELA deacetylation activity (By similarity). {ECO:0000250|UniProtKB:Q96EB6, ECO:0000269|PubMed:20167603}.; PTM: Proteolytically cleaved by cathepsin B upon TNF treatment to yield catalytic inactive but stable SirtT1 75 kDa fragment (75SirT1). {ECO:0000250|UniProtKB:Q96EB6}.; PTM: S-nitrosylated by GAPDH, leading to inhibit the NAD-dependent protein deacetylase activity. {ECO:0000269|PubMed:20972425}.; PTM: Acetylated at various Lys residues (PubMed:28923965). Deacetylated via an autocatalytic mechanism (PubMed:28923965). Autodeacetylation at Lys-230 promotes its protein deacetylase activity (PubMed:28923965). {ECO:0000269|PubMed:28923965}.; PTM: Ubiquitinated; leading to degradation. Deubiquitinated by USP22; leading to stabilization. {ECO:0000250|UniProtKB:Q96EB6}.
uniprot
proteins
protein_family
Class I subfamily
uniprot
proteins
protein_family
Sirtuin family
uniprot
proteins
pubmed
10693811
uniprot
proteins
pubmed
11250901
uniprot
proteins
pubmed
11672522
uniprot
proteins
pubmed
12482959
uniprot
proteins
pubmed
12651913
uniprot
proteins
pubmed
12887892
uniprot
proteins
pubmed
12960381
uniprot
proteins
pubmed
15175761
uniprot
proteins
pubmed
15220471
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15632193
uniprot
proteins
pubmed
15716268
uniprot
proteins
pubmed
15744310
uniprot
proteins
pubmed
15788402
uniprot
proteins
pubmed
16098828
uniprot
proteins
pubmed
16224023
uniprot
proteins
pubmed
16269335
uniprot
proteins
pubmed
16366736
uniprot
proteins
pubmed
16790548
uniprot
proteins
pubmed
16892051
uniprot
proteins
pubmed
17098745
uniprot
proteins
pubmed
17197703
uniprot
proteins
pubmed
17347648
uniprot
proteins
pubmed
17620057
uniprot
proteins
pubmed
17901049
uniprot
proteins
pubmed
17936707
uniprot
proteins
pubmed
18004385
uniprot
proteins
pubmed
18270565
uniprot
proteins
pubmed
18296641
uniprot
proteins
pubmed
18371449
uniprot
proteins
pubmed
18477450
uniprot
proteins
pubmed
18662546
uniprot
proteins
pubmed
18662547
uniprot
proteins
pubmed
18687325
uniprot
proteins
pubmed
18687677
uniprot
proteins
pubmed
19299583
uniprot
proteins
pubmed
19356714
uniprot
proteins
pubmed
19478080
uniprot
proteins
pubmed
19680552
uniprot
proteins
pubmed
20167603
uniprot
proteins
pubmed
20620997
uniprot
proteins
pubmed
20668652
uniprot
proteins
pubmed
20817729
uniprot
proteins
pubmed
20955178
uniprot
proteins
pubmed
20972425
uniprot
proteins
pubmed
20975832
uniprot
proteins
pubmed
21176092
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21187328
uniprot
proteins
pubmed
21189328
uniprot
proteins
pubmed
21622680
uniprot
proteins
pubmed
22510882
uniprot
proteins
pubmed
23142079
uniprot
proteins
pubmed
23160044
uniprot
proteins
pubmed
26910618
uniprot
proteins
pubmed
28842251
uniprot
proteins
pubmed
28883095
uniprot
proteins
pubmed
28923965
uniprot
proteins
pubmed
30026585
uniprot
proteins
pubmed
30193097
uniprot
proteins
pubmed
39695235
uniprot
proteins
sequence_length
737
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250|UniProtKB:Q96EB6}. Cytoplasm {ECO:0000269|PubMed:17197703, ECO:0000269|PubMed:17901049}. Nucleus {ECO:0000269|PubMed:17197703, ECO:0000269|PubMed:17901049, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:20955178}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q96EB6}. Note=Colocalizes in the nucleus with XBP1 isoform 2. 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 (PubMed:17197703). {ECO:0000250|UniProtKB:Q96EB6, ECO:0000269|PubMed:17197703}.; SUBCELLULAR LOCATION: [SirtT1 75 kDa fragment]: Cytoplasm {ECO:0000250|UniProtKB:Q96EB6}. Mitochondrion {ECO:0000250|UniProtKB:Q96EB6}.
uniprot
proteins