SIRT5
entrez
23408
canonical
uniprot
Q9NXA8
canonical
ensembl
ENSG00000124523
resolver
ensp
ENSP00000352830
resolver
ensp
ENSP00000368564
resolver
ensp
ENSP00000380509
resolver
ensp
ENSP00000476228
resolver
ensp
ENSP00000505086
resolver
ensp
ENSP00000505415
resolver
ensp
ENSP00000505469
resolver
ensp
ENSP00000505496
resolver
ensp
ENSP00000505733
resolver
ensp
ENSP00000506431
resolver
ensp
ENSP00000558630
resolver
ensp
ENSP00000558631
resolver
ensp
ENSP00000558633
resolver
ensp
ENSP00000558634
resolver
ensp
ENSP00000558636
resolver
ensp
ENSP00000558638
resolver
ensp
ENSP00000558639
resolver
ensp
ENSP00000558640
resolver
ensp
ENSP00000558641
resolver
ensp
ENSP00000558643
resolver
ensp
ENSP00000652345
resolver
ensp
ENSP00000652350
resolver
ensp
ENSP00000652351
resolver
ensp
ENSP00000652353
resolver
ensp
ENSP00000652357
resolver
ensp
ENSP00000692649
resolver
ensp
ENSP00000692656
resolver
ensp
ENSP00000692657
resolver
ensp
ENSP00000785744
resolver
ensp
ENSP00000797095
resolver
enst
ENST00000680402
resolver
enst
ENST00000681012
resolver
enst
ENST00000681243
resolver
genesymbol
SIRT5
resolver
genesymbol_syn
SIR2L5
resolver
hgnc
HGNC:14933
resolver
uniprot
A0A7P0T9N1
resolver
uniprot
A0A7P0Z4N6
resolver
uniprot
B4DFM4
resolver
uniprot
B4DYJ5
resolver
uniprot
F5H5Z9
resolver
uniprot
Q5T294
resolver
uniprot
Q5T295
resolver
uniprot
Q9Y6E6
resolver
uniprot_entry
A0A7P0T9N1_HUMAN
resolver
uniprot_entry
A0A7P0Z4N6_HUMAN
resolver
uniprot_entry
SIR5_HUMAN
resolver
uniprot_sec
B4DFM4
resolver
uniprot_sec
B4DYJ5
resolver
uniprot_sec
F5H5Z9
resolver
uniprot_sec
Q5T294
resolver
uniprot_sec
Q5T295
resolver
uniprot_sec
Q9Y6E6
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by suramin. NAD-dependent lysine desuccinylase activity is inhibited by physiological nicotinamide concentrations, while deacetylase activity is not. In contrast, resveratrol activates deacetylase activity, while inhibiting desuccinylase activity. {ECO:0000269|PubMed:17355872, ECO:0000269|PubMed:23028781, ECO:0000269|PubMed:23185430}.
uniprot
proteins
amino_acid_sequence
MRPLQIVPSRLISQLYCGLKPPASTRNQICLKMARPSSSMADFRKFFAKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPLAFAHNPSRVWEFYHYRREVMGSKEPNAGHRAIAECETRLGKQGRRVVVITQNIDELHRKAGTKNLLEIHGSLFKTRCTSCGVVAENYKSPICPALSGKGAPEPGTQDASIPVEKLPRCEEAGCGGLLRPHVVWFGENLDPAILEEVDRELAHCDLCLVVGTSSVVYPAAMFAPQVAARGVPVAEFNTETTPATNRFRFHFQGPCGTTLPEALACHENETVS
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
function
FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:21908771, PubMed:22076378, PubMed:24703693, PubMed:29180469). Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting (PubMed:22076378, PubMed:24703693). Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (PubMed:24140062). Activates SHMT2 by mediating its desuccinylation (PubMed:29180469). Modulates ketogenesis through the desuccinylation and activation of HMGCS2 (By similarity). Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX. {ECO:0000250|UniProtKB:Q8K2C6, ECO:0000269|PubMed:18680753, ECO:0000269|PubMed:21908771, ECO:0000269|PubMed:22076378, ECO:0000269|PubMed:24140062, ECO:0000269|PubMed:24703693, ECO:0000269|PubMed:29180469}.
uniprot
proteins
mass_dalton
33881
uniprot
proteins
mutagenesis
MUTAGEN 69; /note="T->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:23028781"; MUTAGEN 102; /note="Y->F: Increases the KM for desuccinylation."; /evidence="ECO:0000269|PubMed:22076378"; MUTAGEN 105; /note="R->M: Increases the KM for desuccinylation. Does not affect deacetylase activity."; /evidence="ECO:0000269|PubMed:22076378, ECO:0000269|PubMed:23028781"; MUTAGEN 158; /note="H->A: Abolishes desuccinylation and deglutarylation activity."; /evidence="ECO:0000269|PubMed:21908771, ECO:0000269|PubMed:22076378, ECO:0000269|PubMed:24703693, ECO:0000269|PubMed:29180469
uniprot
proteins
protein_family
Class III subfamily
uniprot
proteins
protein_family
Sirtuin family
uniprot
proteins
pubmed
10381378
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16079181
uniprot
proteins
pubmed
17355872
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18680753
uniprot
proteins
pubmed
21143562
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21908771
uniprot
proteins
pubmed
22076378
uniprot
proteins
pubmed
22767592
uniprot
proteins
pubmed
22849721
uniprot
proteins
pubmed
23028781
uniprot
proteins
pubmed
23185430
uniprot
proteins
pubmed
23438705
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24140062
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24703693
uniprot
proteins
pubmed
29180469
uniprot
proteins
sequence_length
310
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion intermembrane space. Cytoplasm, cytosol. Nucleus. Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:21143562}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03160, ECO:0000269|PubMed:21143562}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03160, ECO:0000269|PubMed:21143562}.
uniprot
proteins