Q8IXJ6 · SIR2_HUMAN
- ProteinNAD-dependent protein deacetylase sirtuin-2
- GeneSIRT2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids389 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 (PubMed:12620231, PubMed:16648462, PubMed:18249187, PubMed:18332217, PubMed:18995842, PubMed:20543840, PubMed:20587414, PubMed:21081649, PubMed:21726808, PubMed:21949390, PubMed:22014574, PubMed:22771473, PubMed:23468428, PubMed:23908241, PubMed:24177535, PubMed:24681946, PubMed:24769394, PubMed:24940000).
Plays a major role in the control of cell cycle progression and genomic stability (PubMed:12697818, PubMed:16909107, PubMed:17488717, PubMed:17726514, PubMed:19282667, PubMed:23468428).
Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes (PubMed:12697818, PubMed:16909107, PubMed:17488717, PubMed:17726514, PubMed:19282667, PubMed:23468428).
Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis (PubMed:22014574).
Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes (PubMed:23468428).
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 (PubMed:23468428).
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 (PubMed:20587414).
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 (PubMed:24940000).
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 (PubMed:18332217, PubMed:18995842).
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 (PubMed:17488717).
Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination (PubMed:21949390).
Involved in several cellular metabolic pathways (PubMed:20543840, PubMed:21726808, PubMed:24769394).
Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability (PubMed:21726808).
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 (PubMed:24769394).
Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis (PubMed:20543840).
Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity (PubMed:20543840).
Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells (PubMed:20543840).
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 (PubMed:21081649).
Inhibits transcriptional activation by deacetylating p53/TP53 and EP300 (PubMed:18249187, PubMed:18995842).
Deacetylates also EIF5A (PubMed:22771473).
Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions (PubMed:24769394).
Plays a role as tumor suppressor (PubMed:22014574).
In addition to protein deacetylase activity, also has activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as ARF6 and KRAS, thereby regulating their association with membranes (PubMed:25704306, PubMed:29239724, PubMed:32103017).
Isoform 1
Isoform 2
Isoform 5
Catalytic activity
- H2O + N6-acetyl-L-lysyl-[protein] + NAD+ = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
- H2O + N6-tetradecanoyl-L-lysyl-[protein] + NAD+ = 2''-O-tetradecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamideThis reaction proceeds in the forward direction.
- H2O + N6-hexadecanoyl-L-lysyl-[protein] + NAD+ = 2''-O-hexadecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamideThis reaction proceeds in the forward direction.
Cofactor
Activity regulation
Inhibited by nicotinamide. Inhibited by a macrocyclic peptide inhibitor S2iL5 (PubMed:24389023).
Inhibited by EP300-induced acetylation (PubMed:18722353).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
19 μM | an peptide acetylated on lysine | |||||
0.24 μM | an peptide myristoylated on lysine |
kcat is 0.018 sec-1 with a peptide myristoylated on lysine as substrate (PubMed:25704306).
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 85-89 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: AGIST | ||||||
Binding site | 95-97 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DFR | ||||||
Binding site | 167-170 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QNID | ||||||
Active site | 187 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 195 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 200 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 221 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 224 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 262-263 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TS | ||||||
Binding site | 286-288 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: NKE | ||||||
Binding site | 324 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD-dependent protein deacetylase sirtuin-2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8IXJ6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Colocalizes with KMT5A at mitotic foci (PubMed:23468428).
Colocalizes with CDK1 at centrosome during prophase and splindle fibers during metaphase (PubMed:17488717).
Colocalizes with Aurora kinase AURKA at centrosome during early prophase and in the centrioles and growing mitotic spindle throughout metaphase (PubMed:17488717).
Colocalizes with Aurora kinase AURKB during cytokinesis with the midbody (PubMed:17488717).
Colocalizes with microtubules (PubMed:12620231).
Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (By similarity).
Shuttles between the cytoplasm and the nucleus through the CRM1 export pathway (PubMed:17726514).
Colocalizes with EP300 in the nucleus (PubMed:24177535).
Translocates to the nucleus and chromatin upon bacterium Listeria monocytogenes infection in interphase cells (PubMed:23908241).
Deacetylates FOXO3 in the cytoplasm (By similarity).
Colocalizes with PLP1 in internodal regions, at paranodal axoglial junction and Schmidt-Lanterman incisures of myelin sheath (By similarity).
Colocalizes with CDK5R1 in the perikaryon, neurites and growth cone of hippocampal neurons (By similarity).
Colocalizes with alpha-tubulin in neuronal growth cone (By similarity).
Localizes in the cytoplasm and nucleus of germinal vesicle (GV) stage oocytes (By similarity).
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 PARD3 in internodal region of axons (By similarity).
Colocalizes with acetylated alpha-tubulin in cell projection processes during primary oligodendrocyte precursor (OLP) differentiation (By similarity).
Isoform 1
Isoform 2
Isoform 5
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 53 | Reduces deacetylase activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 97 | No effect on deacetylase activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 98 | Inhibits deacetylase activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 100 | Reduces deacetylase activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 116 | Reduces binding for the peptide inhibitor S2iL5. | ||||
Sequence: E → A | ||||||
Mutagenesis | 120 | Reduces binding for the peptide inhibitor S2iL5. | ||||
Sequence: E → A | ||||||
Mutagenesis | 167 | 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. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 168 | 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. | ||||
Sequence: N → A | ||||||
Mutagenesis | 170 | Reduces deacetylase activity. | ||||
Sequence: D → A or N | ||||||
Mutagenesis | 187 | 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. Strongly reduced activity toward long-chain fatty acyl groups. | ||||
Sequence: H → Y or A | ||||||
Mutagenesis | 244 | Strongly reduces binding for the peptide inhibitor S2iL5. | ||||
Sequence: F → A | ||||||
Mutagenesis | 265 | Reduces binding for the peptide inhibitor S2iL5. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 271 | Reduces binding for the peptide inhibitor S2iL5. | ||||
Sequence: S → A | ||||||
Mutagenesis | 279 | Reduces deacetylase activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 280 | Reduces deacetylase activity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 294 | Reduces binding for the peptide inhibitor S2iL5. | ||||
Sequence: D → A | ||||||
Mutagenesis | 311 | Reduces deacetylase activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 315 | Reduces deacetylase activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 364 | Abolishes CDK2-dependent phosphorylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 368 | 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. | ||||
Sequence: S → A | ||||||
Mutagenesis | 368 | Abolishes CDK2-dependent phosphorylation. Inhibits interaction with a cyclin E-CDK2 complex. Reduces strongly histone deacetylation activity. | ||||
Sequence: S → D | ||||||
Mutagenesis | 368 | Abolishes CDK2-dependent phosphorylation. | ||||
Sequence: S → E | ||||||
Mutagenesis | 372 | Reduces phosphorylation. Does not inhibit interaction with HDAC6, ubiquitination and deacetylase activity. Inhibits deacetylase activity; when associated with A-368. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 734 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000110258 | 2-389 | UniProt | NAD-dependent protein deacetylase sirtuin-2 | |||
Sequence: AEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASIDAQSGAGVPNPSTSASPKKSPPPAKDEARTTEREKPQ | |||||||
Modified residue | 23 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 25 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 27 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 53 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 53 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 100 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 207 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 365 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 366 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 368 | UniProt | Phosphoserine; by CDK2 and CDK5 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 368 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 372 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 372 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Developmental stage
Gene expression databases
Organism-specific databases
Interaction
Subunit
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 SARS1; recruited to the VEGFA promoter via interaction with SARS1 (PubMed:24940000).
Interacts with BEX4; negatively regulates alpha-tubulin deacetylation by SIRT2 (PubMed:27512957).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8IXJ6 | BUB1B O60566 | 3 | EBI-477232, EBI-1001438 | |
BINARY | Q8IXJ6 | CDC14B O60729 | 2 | EBI-477232, EBI-970231 | |
BINARY | Q8IXJ6 | G6PD P11413 | 3 | EBI-477232, EBI-4289891 | |
BINARY | Q8IXJ6 | KAT2B Q92831 | 4 | EBI-477232, EBI-477430 | |
BINARY | Q8IXJ6 | RELA Q04206 | 2 | EBI-477232, EBI-73886 | |
BINARY | Q8IXJ6 | SHANK3 Q9BYB0 | 2 | EBI-477232, EBI-1752330 | |
BINARY | Q8IXJ6-2 | CDC20 Q12834 | 2 | EBI-5240785, EBI-367462 | |
BINARY | Q8IXJ6-2 | FZR1 Q9UM11 | 2 | EBI-5240785, EBI-724997 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-34 | Disordered | ||||
Sequence: MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGG | ||||||
Motif | 41-51 | Nuclear export signal | ||||
Sequence: LRNLFSQTLSL | ||||||
Domain | 57-338 | Deacetylase sirtuin-type | ||||
Sequence: RLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWK | ||||||
Region | 351-389 | Disordered | ||||
Sequence: SIDAQSGAGVPNPSTSASPKKSPPPAKDEARTTEREKPQ | ||||||
Compositional bias | 374-389 | Basic and acidic residues | ||||
Sequence: PPAKDEARTTEREKPQ |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q8IXJ6-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length389
- Mass (Da)43,182
- Last updated2003-10-31 v2
- ChecksumA392442A8F6316F1
Q8IXJ6-2
- Name2
- Differences from canonical
- 1-37: Missing
Q8IXJ6-3
- Name3
- Differences from canonical
- 1-38: MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADM → MPLAECPSCRCLSSFRSV
Q8IXJ6-4
- Name4
Q8IXJ6-5
- Name5
- Differences from canonical
- 6-76: PSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERC → R
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J3U7 | C9J3U7_HUMAN | SIRT2 | 78 | ||
E7EWX6 | E7EWX6_HUMAN | SIRT2 | 237 | ||
F8WF57 | F8WF57_HUMAN | SIRT2 | 39 | ||
F8WCF4 | F8WCF4_HUMAN | SIRT2 | 111 | ||
F8WDM4 | F8WDM4_HUMAN | SIRT2 | 52 | ||
F8WBT6 | F8WBT6_HUMAN | SIRT2 | 96 | ||
C9JZQ0 | C9JZQ0_HUMAN | SIRT2 | 130 | ||
C9JR33 | C9JR33_HUMAN | SIRT2 | 73 | ||
B5MCS1 | B5MCS1_HUMAN | SIRT2 | 169 | ||
A0A0A0MRF5 | A0A0A0MRF5_HUMAN | SIRT2 | 234 | ||
A0AAG2T947 | A0AAG2T947_HUMAN | SIRT2 | 389 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_008724 | 1-37 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008726 | 1-38 | in isoform 3 | |||
Sequence: MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADM → MPLAECPSCRCLSSFRSV | ||||||
Alternative sequence | VSP_055328 | 6-76 | in isoform 5 | |||
Sequence: PSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERC → R | ||||||
Sequence conflict | 199 | in Ref. 6 | ||||
Sequence: S → N | ||||||
Sequence conflict | 219 | in Ref. 5; CAD43717 | ||||
Sequence: P → L | ||||||
Alternative sequence | VSP_008727 | 266-271 | in isoform 4 | |||
Sequence: VQPFAS → GRGLAG | ||||||
Alternative sequence | VSP_008728 | 272-389 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 374-389 | Basic and acidic residues | ||||
Sequence: PPAKDEARTTEREKPQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF083107 EMBL· GenBank· DDBJ | AAD40850.2 EMBL· GenBank· DDBJ | mRNA | ||
AF095714 EMBL· GenBank· DDBJ | AAD45971.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY030277 EMBL· GenBank· DDBJ | AAK51133.1 EMBL· GenBank· DDBJ | mRNA | ||
KF032391 EMBL· GenBank· DDBJ | AGZ02589.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ505014 EMBL· GenBank· DDBJ | CAD43717.1 EMBL· GenBank· DDBJ | mRNA | ||
AF160214 EMBL· GenBank· DDBJ | AAF67015.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK290716 EMBL· GenBank· DDBJ | BAF83405.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314492 EMBL· GenBank· DDBJ | BAG37092.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471126 EMBL· GenBank· DDBJ | EAW56833.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471126 EMBL· GenBank· DDBJ | EAW56835.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003012 EMBL· GenBank· DDBJ | AAH03012.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003547 EMBL· GenBank· DDBJ | AAH03547.1 EMBL· GenBank· DDBJ | mRNA | ||
AF131800 EMBL· GenBank· DDBJ | AAD20046.1 EMBL· GenBank· DDBJ | mRNA |