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Entry version 183 (31 Jul 2019)
Sequence version 2 (31 Oct 2003)
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Protein

NAD-dependent protein deacetylase sirtuin-2

Gene

SIRT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (PubMed:24177535, PubMed:12620231, PubMed:16648462, PubMed:18249187, PubMed:18332217, PubMed:18995842, PubMed:20587414, PubMed:21081649, PubMed:20543840, PubMed:22014574, PubMed:21726808, PubMed:21949390, PubMed:22771473, PubMed:23468428, PubMed:23908241, PubMed:24940000, PubMed:24769394, PubMed:24681946). 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 (PubMed:23468428). Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response (PubMed:23468428). Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition. Upon bacterium Listeria monocytogenes infection, deacetylates 'Lys-18' of histone H3 in a receptor tyrosine kinase MET- and PI3K/Akt-dependent manner, thereby inhibiting transcriptional activity and promoting late stages of listeria infection (PubMed:23908241). 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 (PubMed:24940000). 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 (PubMed:20543840). 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 (PubMed:24681946). Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300 (PubMed:18249187). Deacetylates also EIF5A (PubMed:22771473). Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions. Plays a role as tumor suppressor (PubMed:22014574).By similarity28 Publications
Isoform 1: Deacetylates EP300, alpha-tubulin and histone H3 and H4.1 Publication
Isoform 2: Deacetylates EP300, alpha-tubulin and histone H3 and H4.1 Publication
Isoform 5: Lacks deacetylation activity.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by Sirtinol, A3 and M15 small molecules (PubMed:11483616). Inhibited by nicotinamide. Inhibited by a macrocyclic peptide inhibitor S2iL5 (PubMed:24389023). Inhibited by EP300-induced acetylation (PubMed:18722353).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei187Proton acceptorCurated1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi195ZincPROSITE-ProRule annotation4 Publications1
Metal bindingi200ZincPROSITE-ProRule annotation4 Publications1
Metal bindingi221ZincPROSITE-ProRule annotation4 Publications1
Metal bindingi224ZincPROSITE-ProRule annotation4 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei324NAD; via amide nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi85 – 89NADCombined sources1 Publication5
Nucleotide bindingi95 – 97NADCombined sources1 Publication3
Nucleotide bindingi167 – 170NADCombined sources1 Publication4
Nucleotide bindingi262 – 263NADCombined sources1 Publication2
Nucleotide bindingi286 – 288NADCombined sources1 Publication3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processAutophagy, Cell cycle, Cell division, Differentiation, Immunity, Innate immunity, Meiosis, Mitosis, Neurogenesis, Transcription, Transcription regulation
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
Q8IXJ6

SIGNOR Signaling Network Open Resource

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SIGNORi
Q8IXJ6

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
NAD-dependent protein deacetylase sirtuin-2 (EC:3.5.1.-7 Publications)
Alternative name(s):
Regulatory protein SIR2 homolog 2
SIR2-like protein 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SIRT2
Synonyms:SIR2L, SIR2L2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:10886 SIRT2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
604480 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q8IXJ6

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi53S → A: Reduces deacetylase activity. 1 Publication1
Mutagenesisi97R → A: No effect on deacetylase activity. 1 Publication1
Mutagenesisi98S → A: Inhibits deacetylase activity. 1 Publication1
Mutagenesisi100S → A: Reduces deacetylase activity. 1 Publication1
Mutagenesisi116E → A: Reduces binding for the peptide inhibitor S2iL5. 1 Publication1
Mutagenesisi120E → A: Reduces binding for the peptide inhibitor S2iL5. 1 Publication1
Mutagenesisi167Q → A: Reduces deacetylase activity. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-168 and A-187. 2 Publications1
Mutagenesisi168N → A: Abolishes deacetylation of alpha-tubulin. Inhibits deacetylation of histone H3 at 'Lys-18'. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-167 and A-187. 5 Publications1
Mutagenesisi170D → A or N: Reduces deacetylase activity. 1 Publication1
Mutagenesisi187H → Y or A: Inhibits deacetylase activity toward histone, alpha-tubulin, FZR1 and CDC20. No effect on CDK2-dependent phosphorylation. Does not inhibit interaction with alpha-tubulin, HDAC6, HIF1A and the cyclin E-CDK2 complex. Inhibits interaction with BEX4 and KMT5A. Abolishes deacetylation, dimeric formation and enzymatic activity increase of G6PD. Prevents histone H4 methylation at 'Lys-20'(H4K20me1) in metaphase chromosomes. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-167 and A-168. 12 Publications1
Mutagenesisi244F → A: Reduces strongly binding for the peptide inhibitor S2iL5. 1 Publication1
Mutagenesisi265Q → A: Reduces binding for the peptide inhibitor S2iL5. 1 Publication1
Mutagenesisi271S → A: Reduces binding for the peptide inhibitor S2iL5. 1 Publication1
Mutagenesisi279S → A: Reduces deacetylase activity. 1 Publication1
Mutagenesisi280T → A: Reduces deacetylase activity. 1 Publication1
Mutagenesisi294D → A: Reduces binding for the peptide inhibitor S2iL5. 1 Publication1
Mutagenesisi311S → A: Reduces deacetylase activity. 1 Publication1
Mutagenesisi315Y → A: Reduces deacetylase activity. 1 Publication1
Mutagenesisi364S → A: Abolishes CDK2-dependent phosphorylation. 1 Publication1
Mutagenesisi368S → A: Does not affect deacetylase activity. Abolishes CDK2-dependent phosphorylation. Inhibits cellular proliferation delay in the early metaphase to prevent chromosomal instability. Does not inhibit interaction with a cyclin E-CDK2 complex. Does not inhibit interaction with HDAC6 and ubiquitination. Inhibits cell adhesion and migration and neurite outgrowth. Inhibits deacetylase activity; when associated with A-372. 3 Publications1
Mutagenesisi368S → D: Abolishes CDK2-dependent phosphorylation. Inhibits interaction with a cyclin E-CDK2 complex. Reduces strongly histone deacetylation activity. 3 Publications1
Mutagenesisi368S → E: Abolishes CDK2-dependent phosphorylation. 3 Publications1
Mutagenesisi372S → A: Reduces phosphorylation. Does not inhibit interaction with HDAC6, ubiquitination and deacetylase activity. Inhibits deacetylase activity; when associated with A-368. 1 Publication1

Keywords - Diseasei

Neurodegeneration

Organism-specific databases

DisGeNET

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DisGeNETi
22933

Open Targets

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OpenTargetsi
ENSG00000068903

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA35786

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4462

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2708

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
SIRT2

Domain mapping of disease mutations (DMDM)

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DMDMi
38258608

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001102582 – 389NAD-dependent protein deacetylase sirtuin-2Add BLAST388

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Modified residuei25PhosphoserineCombined sources1
Modified residuei27PhosphoserineCombined sources1
Modified residuei53PhosphoserineBy similarity1
Modified residuei100PhosphoserineBy similarity1
Modified residuei207PhosphoserineBy similarity1
Modified residuei368Phosphoserine; by CDK2 and CDK5Combined sources3 Publications1
Modified residuei372Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated at phosphoserine and phosphothreonine. Phosphorylated at Ser-368 by a mitotic kinase CDK1/cyclin B at the G2/M transition; phosphorylation regulates the delay in cell-cycle progression. Phosphorylated at Ser-368 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-368 by CDC14A and CDC14B around early anaphase.4 Publications
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.1 Publication
Ubiquitinated.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q8IXJ6

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q8IXJ6

MaxQB - The MaxQuant DataBase

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MaxQBi
Q8IXJ6

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q8IXJ6

PeptideAtlas

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PeptideAtlasi
Q8IXJ6

PRoteomics IDEntifications database

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PRIDEi
Q8IXJ6

ProteomicsDB human proteome resource

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ProteomicsDBi
71008 [Q8IXJ6-1]
71009 [Q8IXJ6-2]
71010 [Q8IXJ6-3]
71011 [Q8IXJ6-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q8IXJ6

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q8IXJ6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Isoform 1 is expressed in heart, liver and skeletal muscle, weakly expressed in the cortex. Isoform 2 is strongly expressed in the cortex, weakly expressed in heart and liver. Weakly expressed in several malignancies including breast, liver, brain, kidney and prostate cancers compared to normal tissues. Weakly expressed in glioma cell lines compared to normal brain tissues (at protein level). Widely expressed. Highly expressed in heart, brain and skeletal muscle, while it is weakly expressed in placenta and lung. Down-regulated in many gliomas suggesting that it may act as a tumor suppressor gene in human gliomas possibly through the regulation of microtubule network.6 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Peaks during mitosis. After mitosis, it is probably degraded by the 26S proteasome.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in response to low levels of glucose and anoxia-reoxygenation stress. Up-regulated by trichostatin A. Down-regulated in response to high levels of glucose. Down-regulated by histone deacetylation in several tumors.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000068903 Expressed in 230 organ(s), highest expression level in C1 segment of cervical spinal cord

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q8IXJ6 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q8IXJ6 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004573
HPA011165

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with CDC20, FOXO3 and FZR1. Associates with microtubules in primary cortical mature neurons (By similarity). Homotrimer. Isoform 1 and isoform 2 interact (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 KMT5A isoform 2; the interaction is direct, stimulates KMT5A-mediated methyltransferase activity on histone at 'Lys-20' (H4K20me1) and is increased in a H2O2-induced oxidative stress-dependent manner.

Interacts with G6PD; the interaction is enhanced by H2O2 treatment.

Interacts with a G1/S-specific cyclin E-CDK2 complex.

Interacts with AURKA, CDK5R1 (p35 form) and CDK5 and HIF1A. Isoform 1, isoform 2 and isoform 5 interact (via C-terminus region) with EP300 (PubMed:24177535).

Interacts with the tRNA ligase SARS; recruited to the VEGFA promoter via interaction with SARS (PubMed:24940000).

Interacts with BEX4; negatively regulates alpha-tubulin deacetylation by SIRT2 (PubMed:27512957).

By similarity20 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
116593, 68 interactors

Database of interacting proteins

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DIPi
DIP-33350N

Protein interaction database and analysis system

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IntActi
Q8IXJ6, 27 interactors

Molecular INTeraction database

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MINTi
Q8IXJ6

STRING: functional protein association networks

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STRINGi
9606.ENSP00000249396

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q8IXJ6

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1389
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q8IXJ6

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q8IXJ6

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini65 – 340Deacetylase sirtuin-typePROSITE-ProRule annotationAdd BLAST276

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni116 – 120Peptide inhibitor binding5
Regioni232 – 301Peptide inhibitor bindingAdd BLAST70

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi41 – 51Nuclear export signalAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the sirtuin family. Class I subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2682 Eukaryota
COG0846 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157514

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q8IXJ6

KEGG Orthology (KO)

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KOi
K11412

Database of Orthologous Groups

More...
OrthoDBi
973532at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8IXJ6

TreeFam database of animal gene trees

More...
TreeFami
TF106181

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.1600.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029035 DHS-like_NAD/FAD-binding_dom
IPR003000 Sirtuin
IPR026591 Sirtuin_cat_small_dom_sf
IPR017328 Sirtuin_class_I
IPR026590 Ssirtuin_cat_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02146 SIR2, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF037938 SIR2_euk, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52467 SSF52467, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50305 SIRTUIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 11 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8IXJ6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAEPDPSHPL ETQAGKVQEA QDSDSDSEGG AAGGEADMDF LRNLFSQTLS
60 70 80 90 100
LGSQKERLLD ELTLEGVARY MQSERCRRVI CLVGAGISTS AGIPDFRSPS
110 120 130 140 150
TGLYDNLEKY HLPYPEAIFE ISYFKKHPEP FFALAKELYP GQFKPTICHY
160 170 180 190 200
FMRLLKDKGL LLRCYTQNID TLERIAGLEQ EDLVEAHGTF YTSHCVSASC
210 220 230 240 250
RHEYPLSWMK EKIFSEVTPK CEDCQSLVKP DIVFFGESLP ARFFSCMQSD
260 270 280 290 300
FLKVDLLLVM GTSLQVQPFA SLISKAPLST PRLLINKEKA GQSDPFLGMI
310 320 330 340 350
MGLGGGMDFD SKKAYRDVAW LGECDQGCLA LAELLGWKKE LEDLVRREHA
360 370 380
SIDAQSGAGV PNPSTSASPK KSPPPAKDEA RTTEREKPQ
Length:389
Mass (Da):43,182
Last modified:October 31, 2003 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA392442A8F6316F1
GO
Isoform 2 (identifier: Q8IXJ6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: Missing.

Show »
Length:352
Mass (Da):39,515
Checksum:iFFED07DEF9E3416A
GO
Isoform 3 (identifier: Q8IXJ6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADM → MPLAECPSCRCLSSFRSV

Note: No experimental confirmation available.
Show »
Length:369
Mass (Da):41,353
Checksum:i0805580CAAB59A51
GO
Isoform 4 (identifier: Q8IXJ6-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     266-271: VQPFAS → GRGLAG
     272-389: Missing.

Note: No experimental confirmation available.
Show »
Length:271
Mass (Da):30,379
Checksum:iFF4641368029BD94
GO
Isoform 5 (identifier: Q8IXJ6-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     6-76: PSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERC → R

Note: Lacks deacetylase activity, at least toward known SIRT2 targets.
Show »
Length:319
Mass (Da):35,654
Checksum:i78A23E5456789A9D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 11 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WYM3A0A087WYM3_HUMAN
NAD-dependent protein deacetylase
SIRT2
389Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0A0MRF5A0A0A0MRF5_HUMAN
NAD-dependent protein deacetylase s...
SIRT2
234Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EWX6E7EWX6_HUMAN
NAD-dependent protein deacetylase s...
SIRT2
237Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B5MCS1B5MCS1_HUMAN
NAD-dependent protein deacetylase s...
SIRT2
169Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8WCF4F8WCF4_HUMAN
NAD-dependent protein deacetylase s...
SIRT2
111Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JZQ0C9JZQ0_HUMAN
NAD-dependent protein deacetylase s...
SIRT2
130Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JR33C9JR33_HUMAN
NAD-dependent protein deacetylase s...
SIRT2
73Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9J3U7C9J3U7_HUMAN
NAD-dependent protein deacetylase s...
SIRT2
78Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8WF57F8WF57_HUMAN
NAD-dependent protein deacetylase s...
SIRT2
39Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8WDM4F8WDM4_HUMAN
NAD-dependent protein deacetylase s...
SIRT2
52Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There is more potential isoformShow all

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD45971 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAF67015 differs from that shown. Reason: Frameshift at several positions.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti199S → N (PubMed:10931946).Curated1
Sequence conflicti219P → L in CAD43717 (Ref. 5) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0087261 – 38MAEPD…GEADM → MPLAECPSCRCLSSFRSV in isoform 3. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_0087241 – 37Missing in isoform 2. 5 PublicationsAdd BLAST37
Alternative sequenceiVSP_0553286 – 76PSHPL…QSERC → R in isoform 5. 1 PublicationAdd BLAST71
Alternative sequenceiVSP_008727266 – 271VQPFAS → GRGLAG in isoform 4. 1 Publication6
Alternative sequenceiVSP_008728272 – 389Missing in isoform 4. 1 PublicationAdd BLAST118

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF083107 mRNA Translation: AAD40850.2
AF095714 mRNA Translation: AAD45971.1 Different initiation.
AY030277 mRNA Translation: AAK51133.1
KF032391 mRNA Translation: AGZ02589.1
AJ505014 mRNA Translation: CAD43717.1
AF160214 mRNA Translation: AAF67015.1 Frameshift.
AK290716 mRNA Translation: BAF83405.1
AK314492 mRNA Translation: BAG37092.1
CH471126 Genomic DNA Translation: EAW56833.1
CH471126 Genomic DNA Translation: EAW56835.1
BC003012 mRNA Translation: AAH03012.1
BC003547 mRNA Translation: AAH03547.1
AF131800 mRNA Translation: AAD20046.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS12523.1 [Q8IXJ6-1]
CCDS46069.1 [Q8IXJ6-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001180215.1, NM_001193286.1
NP_036369.2, NM_012237.3 [Q8IXJ6-1]
NP_085096.1, NM_030593.2 [Q8IXJ6-2]
XP_006723174.1, XM_006723111.1 [Q8IXJ6-2]
XP_011524956.1, XM_011526654.1 [Q8IXJ6-2]
XP_011524957.1, XM_011526655.1 [Q8IXJ6-5]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000249396; ENSP00000249396; ENSG00000068903 [Q8IXJ6-1]
ENST00000392081; ENSP00000375931; ENSG00000068903 [Q8IXJ6-2]
ENST00000634533; ENSP00000489602; ENSG00000283100 [Q8IXJ6-1]
ENST00000635478; ENSP00000488940; ENSG00000283100 [Q8IXJ6-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
22933

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:22933

UCSC genome browser

More...
UCSCi
uc002ojt.3 human [Q8IXJ6-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF083107 mRNA Translation: AAD40850.2
AF095714 mRNA Translation: AAD45971.1 Different initiation.
AY030277 mRNA Translation: AAK51133.1
KF032391 mRNA Translation: AGZ02589.1
AJ505014 mRNA Translation: CAD43717.1
AF160214 mRNA Translation: AAF67015.1 Frameshift.
AK290716 mRNA Translation: BAF83405.1
AK314492 mRNA Translation: BAG37092.1
CH471126 Genomic DNA Translation: EAW56833.1
CH471126 Genomic DNA Translation: EAW56835.1
BC003012 mRNA Translation: AAH03012.1
BC003547 mRNA Translation: AAH03547.1
AF131800 mRNA Translation: AAD20046.1
CCDSiCCDS12523.1 [Q8IXJ6-1]
CCDS46069.1 [Q8IXJ6-2]
RefSeqiNP_001180215.1, NM_001193286.1
NP_036369.2, NM_012237.3 [Q8IXJ6-1]
NP_085096.1, NM_030593.2 [Q8IXJ6-2]
XP_006723174.1, XM_006723111.1 [Q8IXJ6-2]
XP_011524956.1, XM_011526654.1 [Q8IXJ6-2]
XP_011524957.1, XM_011526655.1 [Q8IXJ6-5]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J8FX-ray1.70A/B/C34-356[»]
3ZGOX-ray1.63A/B/C34-356[»]
3ZGVX-ray2.27A/B34-356[»]
4L3OX-ray2.52A/B/C/D55-356[»]
4R8MX-ray2.10A/B38-356[»]
4RMGX-ray1.88A56-356[»]
4RMHX-ray1.42A56-356[»]
4RMIX-ray1.45A56-356[»]
4RMJX-ray1.87A/B56-356[»]
4X3OX-ray1.50A52-355[»]
4X3PX-ray1.80A52-355[»]
4Y6LX-ray1.60A/B52-356[»]
4Y6OX-ray1.60A/B52-356[»]
4Y6QX-ray1.90A/B/C/D52-356[»]
5D7OX-ray1.63A/B50-356[»]
5D7PX-ray1.76A/B56-356[»]
5D7QX-ray2.01A/B56-356[»]
5DY4X-ray1.77A56-356[»]
5DY5X-ray1.95A56-356[»]
5FYQX-ray3.00A/B1-356[»]
5G4CX-ray2.10A/B34-356[»]
5MARX-ray1.89A/B56-356[»]
5MATX-ray2.07A/C56-356[»]
5Y0ZX-ray2.00A/B52-356[»]
5Y5NX-ray2.30A32-356[»]
5YQLX-ray1.60A56-356[»]
5YQMX-ray1.74A56-356[»]
5YQNX-ray1.60A56-356[»]
5YQOX-ray1.48A56-356[»]
SMRiQ8IXJ6
ModBaseiSearch...

Protein-protein interaction databases

BioGridi116593, 68 interactors
DIPiDIP-33350N
IntActiQ8IXJ6, 27 interactors
MINTiQ8IXJ6
STRINGi9606.ENSP00000249396

Chemistry databases

BindingDBiQ8IXJ6
ChEMBLiCHEMBL4462
GuidetoPHARMACOLOGYi2708

PTM databases

iPTMnetiQ8IXJ6
PhosphoSitePlusiQ8IXJ6

Polymorphism and mutation databases

BioMutaiSIRT2
DMDMi38258608

Proteomic databases

EPDiQ8IXJ6
jPOSTiQ8IXJ6
MaxQBiQ8IXJ6
PaxDbiQ8IXJ6
PeptideAtlasiQ8IXJ6
PRIDEiQ8IXJ6
ProteomicsDBi71008 [Q8IXJ6-1]
71009 [Q8IXJ6-2]
71010 [Q8IXJ6-3]
71011 [Q8IXJ6-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
22933
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249396; ENSP00000249396; ENSG00000068903 [Q8IXJ6-1]
ENST00000392081; ENSP00000375931; ENSG00000068903 [Q8IXJ6-2]
ENST00000634533; ENSP00000489602; ENSG00000283100 [Q8IXJ6-1]
ENST00000635478; ENSP00000488940; ENSG00000283100 [Q8IXJ6-2]
GeneIDi22933
KEGGihsa:22933
UCSCiuc002ojt.3 human [Q8IXJ6-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
22933
DisGeNETi22933

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SIRT2
HGNCiHGNC:10886 SIRT2
HPAiCAB004573
HPA011165
MIMi604480 gene
neXtProtiNX_Q8IXJ6
OpenTargetsiENSG00000068903
PharmGKBiPA35786

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2682 Eukaryota
COG0846 LUCA
GeneTreeiENSGT00940000157514
InParanoidiQ8IXJ6
KOiK11412
OrthoDBi973532at2759
PhylomeDBiQ8IXJ6
TreeFamiTF106181

Enzyme and pathway databases

SABIO-RKiQ8IXJ6
SIGNORiQ8IXJ6

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
SIRT2 human
EvolutionaryTraceiQ8IXJ6

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
SIRT2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
22933

Protein Ontology

More...
PROi
PR:Q8IXJ6

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000068903 Expressed in 230 organ(s), highest expression level in C1 segment of cervical spinal cord
ExpressionAtlasiQ8IXJ6 baseline and differential
GenevisibleiQ8IXJ6 HS

Family and domain databases

Gene3Di3.30.1600.10, 1 hit
InterProiView protein in InterPro
IPR029035 DHS-like_NAD/FAD-binding_dom
IPR003000 Sirtuin
IPR026591 Sirtuin_cat_small_dom_sf
IPR017328 Sirtuin_class_I
IPR026590 Ssirtuin_cat_dom
PfamiView protein in Pfam
PF02146 SIR2, 1 hit
PIRSFiPIRSF037938 SIR2_euk, 1 hit
SUPFAMiSSF52467 SSF52467, 1 hit
PROSITEiView protein in PROSITE
PS50305 SIRTUIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSIR2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8IXJ6
Secondary accession number(s): A8K3V1
, B2RB45, O95889, Q924Y7, Q9P0G8, Q9UNT0, Q9Y6E9, U5TP13
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 31, 2003
Last modified: July 31, 2019
This is version 183 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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