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Q5RJQ4

- SIR2_RAT

UniProt

Q5RJQ4 - SIR2_RAT

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Protein

NAD-dependent protein deacetylase sirtuin-2

Gene

Sirt2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors. 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 with both 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 SETD8 leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression. Deacetylates SETD8 modulating SETD8 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 alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells. Phosphorylation at Ser-330 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. 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. 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.3 Publications

Catalytic activityi

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.PROSITE-ProRule annotation

Cofactori

Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei150 – 1501Proton acceptorPROSITE-ProRule annotation
Metal bindingi158 – 1581ZincPROSITE-ProRule annotation
Metal bindingi163 – 1631ZincPROSITE-ProRule annotation
Metal bindingi184 – 1841ZincPROSITE-ProRule annotation
Metal bindingi187 – 1871ZincPROSITE-ProRule annotation
Binding sitei287 – 2871NAD; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi47 – 6721NADBy similarityAdd
BLAST
Nucleotide bindingi130 – 1334NADBy similarity
Nucleotide bindingi224 – 2263NADBy similarity
Nucleotide bindingi249 – 2513NADBy similarity

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. histone deacetylase activity Source: UniProtKB
  3. NAD+ binding Source: InterPro
  4. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB
  5. NAD-dependent protein deacetylase activity Source: UniProtKB
  6. protein deacetylase activity Source: UniProtKB
  7. tubulin deacetylase activity Source: UniProtKB
  8. zinc ion binding Source: Ensembl

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. cellular lipid catabolic process Source: UniProtKB
  3. cellular response to caloric restriction Source: UniProtKB
  4. cellular response to epinephrine stimulus Source: UniProtKB
  5. cellular response to hepatocyte growth factor stimulus Source: UniProtKB
  6. cellular response to hypoxia Source: UniProtKB
  7. cellular response to molecule of bacterial origin Source: UniProtKB
  8. cellular response to oxidative stress Source: UniProtKB
  9. hepatocyte growth factor receptor signaling pathway Source: UniProtKB
  10. histone H3 deacetylation Source: UniProtKB
  11. histone H4 deacetylation Source: UniProtKB
  12. meiotic nuclear division Source: UniProtKB-KW
  13. mitotic nuclear division Source: UniProtKB-KW
  14. myelination in peripheral nervous system Source: UniProtKB
  15. negative regulation of autophagy Source: UniProtKB
  16. negative regulation of cell proliferation Source: UniProtKB
  17. negative regulation of defense response to bacterium Source: UniProtKB
  18. negative regulation of fat cell differentiation Source: UniProtKB
  19. negative regulation of oligodendrocyte progenitor proliferation Source: UniProtKB
  20. negative regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  21. negative regulation of protein catabolic process Source: UniProtKB
  22. negative regulation of reactive oxygen species metabolic process Source: UniProtKB
  23. negative regulation of striated muscle tissue development Source: Ensembl
  24. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  25. negative regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: UniProtKB
  26. peptidyl-lysine deacetylation Source: UniProtKB
  27. phosphatidylinositol 3-kinase signaling Source: UniProtKB
  28. positive regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
  29. positive regulation of cell division Source: UniProtKB
  30. positive regulation of DNA binding Source: UniProtKB
  31. positive regulation of execution phase of apoptosis Source: UniProtKB
  32. positive regulation of meiosis Source: UniProtKB
  33. positive regulation of oocyte maturation Source: UniProtKB
  34. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  35. positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia Source: UniProtKB
  36. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  37. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  38. protein deacetylation Source: UniProtKB
  39. protein kinase B signaling Source: UniProtKB
  40. regulation of cell cycle Source: UniProtKB
  41. regulation of myelination Source: UniProtKB
  42. ripoptosome assembly involved in necroptotic process Source: Ensembl
  43. substantia nigra development Source: Ensembl
  44. transcription, DNA-templated Source: UniProtKB-KW
  45. tubulin deacetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Autophagy, Cell cycle, Cell division, Differentiation, Meiosis, Mitosis, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent protein deacetylase sirtuin-2 (EC:3.5.1.-)
Alternative name(s):
Regulatory protein SIR2 homolog 2
SIR2-like protein 2
Gene namesi
Name:Sirt2
Synonyms:Sir2l2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi621481. Sirt2.

Subcellular locationi

Nucleus By similarity. Cytoplasm. Cytoplasmperinuclear region. Perikaryon. Myelin membrane. Cell projection. Cytoplasmcytoskeleton. Cell projectiongrowth cone By similarity. Cytoplasmcytoskeletonspindle By similarity. Chromosome By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole By similarity. Midbody By similarity
Note: 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 CDK1 at centrosome during prophase and splindle fibers during metaphase. Colocalizes with Aurora kinase AURKA in centrioles during early prophase and growing mitotic spindle throughout metaphase. Colocalizes with Aurora kinase AURKB during cytokinesis with the midbody. 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. Deacetylates FOXO3 in the cytoplasm. Colocalizes with Aurora kinase AURKA at centrosome. Colocalizes with microtubules. Colocalizes with CDK5R1 in the perikaryon, neurites and growth cone of hippocampal neurons. Colocalizes with alpha-tubulin in neuronal growth cone. Colocalizes with SETD8 at mitotic foci. 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 (By similarity). Colocalizes with PLP1 in internodal regions of myelin sheat, at paranodal axoglial junction and Schmidt-Lanterman (SL) incisures. 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

GO - Cellular componenti

  1. centriole Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. chromosome Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. cytosol Source: UniProtKB
  6. glial cell projection Source: UniProtKB
  7. juxtaparanode region of axon Source: UniProtKB
  8. lateral loop Source: UniProtKB
  9. meiotic spindle Source: UniProtKB
  10. microtubule Source: UniProtKB-KW
  11. midbody Source: UniProtKB
  12. mitotic spindle Source: UniProtKB
  13. myelin sheath Source: UniProtKB
  14. nuclear heterochromatin Source: UniProtKB
  15. nucleus Source: UniProtKB
  16. paranodal junction Source: UniProtKB
  17. paranode region of axon Source: UniProtKB
  18. perikaryon Source: UniProtKB
  19. perinuclear region of cytoplasm Source: UniProtKB
  20. plasma membrane Source: UniProtKB-KW
  21. Schmidt-Lanterman incisure Source: UniProtKB
  22. spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Chromosome, Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311N → A: Reduced deacetylase activity on alpha-tubulin and stimulates oligodendrocyte precursor (OLP) differentiation. 1 Publication
Mutagenesisi133 – 1331D → A: Reduced deacetylase activity on alpha-tubulin. 1 Publication
Mutagenesisi150 – 1501H → A: Reduced deacetylase activity on alpha-tubulin and stimulates oligodendrocyte precursor (OLP) differentiation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350NAD-dependent protein deacetylase sirtuin-2PRO_0000244536Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei330 – 3301Phosphoserine; by CDK2 (in cyclin E-CDK2 complex); by CDK5 (in cyclin p35-CDK5)By similarity
Modified residuei334 – 3341PhosphoserineBy similarity

Post-translational modificationi

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).By similarity
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.By similarity
Ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ5RJQ4.
PRIDEiQ5RJQ4.

PTM databases

PhosphoSiteiQ5RJQ4.

Expressioni

Tissue specificityi

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).2 Publications

Inductioni

In oligodendrocytes during differentiation of CG-4 cells.1 Publication

Gene expression databases

GenevestigatoriQ5RJQ4.

Interactioni

Subunit structurei

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. 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 SETD8; the interaction is direct, stimulates SETD8-mediated methyltransferase activity on histone at 'Lys-20' (H4K20me1) and is increased in a H2O(2)-induced oxidative stress-dependent manner. Interacts with G6PD; the interaction is enhanced by H2O2 treatment. Interacts (via C-terminus region) with EP300. Interacts with a G1/S-specific cyclin E-CDK2 complex. Interacts with AURKA, CDC20, CDK5R1 (p35 form), CDK5, FOXO3, FZR1 and HIF1A. Associates with microtubule in primary cortical mature neurons (By similarity).By similarity

Protein-protein interaction databases

BioGridi262752. 1 interaction.
STRINGi10116.ENSRNOP00000027384.

Structurei

3D structure databases

ProteinModelPortaliQ5RJQ4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 303276Deacetylase sirtuin-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 835Peptide inhibitor bindingBy similarity
Regioni195 – 26470Peptide inhibitor bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi4 – 1411Nuclear export signalBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the sirtuin family. Class I subfamily.Curated
Contains 1 deacetylase sirtuin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0846.
GeneTreeiENSGT00740000115546.
HOGENOMiHOG000085952.
HOVERGENiHBG057095.
InParanoidiQ5RJQ4.
KOiK11412.
OMAiTICHYFM.
OrthoDBiEOG7WX09C.

Family and domain databases

Gene3Di3.40.50.1220. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR017328. Sirtuin_class_I.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 1 hit.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
PIRSFiPIRSF037938. SIR2_euk. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5RJQ4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDFLRNLFTQ TLGLGSQKER LLDELTLEGV TRYMQSERCR RVICLVGAGI
60 70 80 90 100
STSAGIPDFR SPSTGLYANL EKYHLPYPEA IFEISYFKKH PEPFFALAKE
110 120 130 140 150
LYPGQFKPTI CHYFIRLLKE KGLLLRCYTQ NIDTLERVAG LEPQDLVEAH
160 170 180 190 200
GTFYTSHCVN TSCGKEYTMS WMKEKIFSEA TPKCEKCQNV VKPDIVFFGE
210 220 230 240 250
NLPPRFFSCM QSDFSKVDLL IIMGTSLQVQ PFASLISKAP LATPRLLINK
260 270 280 290 300
EKTGQTDPFL GMMMGLGGGM DFDSKKAYRD VAWLGDCDQG CLALADLLGW
310 320 330 340 350
KELEDLVRRE HANIDAQSGS QASNPSATVS PRKSPPPAKE AARTKEKEEH
Length:350
Mass (Da):39,319
Last modified:December 21, 2004 - v1
Checksum:iEA3621A7CCE695FB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC086545 mRNA. Translation: AAH86545.1.
RefSeqiNP_001008369.1. NM_001008368.1.
UniGeneiRn.59887.

Genome annotation databases

EnsembliENSRNOT00000064153; ENSRNOP00000059450; ENSRNOG00000020102.
GeneIDi361532.
KEGGirno:361532.
UCSCiRGD:621481. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC086545 mRNA. Translation: AAH86545.1 .
RefSeqi NP_001008369.1. NM_001008368.1.
UniGenei Rn.59887.

3D structure databases

ProteinModelPortali Q5RJQ4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 262752. 1 interaction.
STRINGi 10116.ENSRNOP00000027384.

PTM databases

PhosphoSitei Q5RJQ4.

Proteomic databases

PaxDbi Q5RJQ4.
PRIDEi Q5RJQ4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000064153 ; ENSRNOP00000059450 ; ENSRNOG00000020102 .
GeneIDi 361532.
KEGGi rno:361532.
UCSCi RGD:621481. rat.

Organism-specific databases

CTDi 22933.
RGDi 621481. Sirt2.

Phylogenomic databases

eggNOGi COG0846.
GeneTreei ENSGT00740000115546.
HOGENOMi HOG000085952.
HOVERGENi HBG057095.
InParanoidi Q5RJQ4.
KOi K11412.
OMAi TICHYFM.
OrthoDBi EOG7WX09C.

Miscellaneous databases

NextBioi 676633.

Gene expression databases

Genevestigatori Q5RJQ4.

Family and domain databases

Gene3Di 3.40.50.1220. 2 hits.
InterProi IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR017328. Sirtuin_class_I.
IPR026590. Ssirtuin_cat_dom.
[Graphical view ]
PANTHERi PTHR11085. PTHR11085. 1 hit.
Pfami PF02146. SIR2. 1 hit.
[Graphical view ]
PIRSFi PIRSF037938. SIR2_euk. 1 hit.
SUPFAMi SSF52467. SSF52467. 1 hit.
PROSITEi PS50305. SIRTUIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  2. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-18; 21-32; 41-116; 176-183; 187-216; 239-245; 302-308 AND 310-332, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  3. "A novel seven transmembrane receptor induced during the early steps of astrocyte differentiation identified by differential expression."
    De Smet C., Nishimori H., Furnari F.B., Boegler O., Huang H.-J.S., Cavenee W.K.
    J. Neurochem. 81:575-588(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  4. "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."
    Li W., Zhang B., Tang J., Cao Q., Wu Y., Wu C., Guo J., Ling E.A., Liang F.
    J. Neurosci. 27:2606-2616(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF ALPHA TUBULIN, FUNCTION AS REGULATOR OF OLIGODENDROCYTE DIFFERENTIATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASN-131; ASP-133 AND HIS-150.
  5. "Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through polarity protein Par-3/atypical protein kinase C (aPKC) signaling."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 108:E952-961(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF PERIPHERAL MYELINATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "SIRT2 is a tumor suppressor that connects aging, acetylome, cell cycle signaling, and carcinogenesis."
    Park S.H., Zhu Y., Ozden O., Kim H.S., Jiang H., Deng C.X., Gius D., Vassilopoulos A.
    Transl. Cancer Res. 1:15-21(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, FUNCTION AS A TUMOR SUPPRESSOR.

Entry informationi

Entry nameiSIR2_RAT
AccessioniPrimary (citable) accession number: Q5RJQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 21, 2004
Last modified: October 29, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Has some ability to deacetylate histones in vitro, but seeing its subcellular location, this is unlikely in vivo.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3