SIRT4
entrez
23409
canonical
uniprot
Q9Y6E7
canonical
ensembl
ENSG00000089163
resolver
ensp
ENSP00000202967
resolver
ensp
ENSP00000521005
resolver
ensp
ENSP00000521592
resolver
ensp
ENSP00000521593
resolver
ensp
ENSP00000521594
resolver
ensp
ENSP00000632743
resolver
enst
ENST00000202967
resolver
enst
ENST00000850925
resolver
enst
ENST00000851533
resolver
enst
ENST00000851534
resolver
enst
ENST00000851535
resolver
enst
ENST00000962684
resolver
genesymbol
SIRT4
resolver
genesymbol_syn
SIR2L4
resolver
hgnc
HGNC:14932
resolver
uniprot
A0ABJ7H8K5
resolver
uniprot
O43346
resolver
uniprot
Q32M33
resolver
uniprot_entry
A0ABJ7H8K5_HUMAN
resolver
uniprot_entry
SIR4_HUMAN
resolver
uniprot_sec
O43346
resolver
uniprot_sec
Q32M33
resolver
amino_acid_sequence
MKMSFALTFRSAKGRWIANPSQPCSKASIGLFVPASPPLDPEKVKELQRFITLSKRLLVMTGAGISTESGIPDYRSEKVGLYARTDRRPIQHGDFVRSAPIRQRYWARNFVGWPQFSSHQPNPAHWALSTWEKLGKLYWLVTQNVDALHTKAGSRRLTELHGCMDRVLCLDCGEQTPRGVLQERFQVLNPTWSAEAHGLAPDGDVFLSEEQVRSFQVPTCVQCGGHLKPDVVFFGDTVNPDKVDFVHKRVKEADSLLVVGSSLQVYSGYRFILTAWEKKLPIAILNIGPTRSDDLACLKLNSRCGELLPLIDPC
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.286
uniprot
proteins
ec_number
2.3.1.313
uniprot
proteins
ec_number
2.4.2.-
uniprot
proteins
function
FUNCTION: Acts as a NAD-dependent protein lipoamidase, biotinylase, deacetylase and ADP-ribosyl transferase (PubMed:16959573, PubMed:17715127, PubMed:24052263, PubMed:25525879). Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications (PubMed:24052263, PubMed:25525879). Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner (PubMed:25525879). Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity (PubMed:16959573, PubMed:17715127). Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest (PubMed:16959573, PubMed:17715127). In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation (PubMed:23663782). Acts as a tumor suppressor (PubMed:23562301, PubMed:23663782). Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis (By similarity). Does not seem to deacetylate PC (PubMed:23438705). Controls fatty acid oxidation by inhibiting PPARA transcriptional activation (PubMed:24043310). Impairs SIRT1-PPARA interaction probably through the regulation of NAD(+) levels (PubMed:24043310). Down-regulates insulin secretion (PubMed:17715127). {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:16959573, ECO:0000269|PubMed:17715127, ECO:0000269|PubMed:23438705, ECO:0000269|PubMed:23562301, ECO:0000269|PubMed:23663782, ECO:0000269|PubMed:24043310, ECO:0000269|PubMed:24052263, ECO:0000269|PubMed:25525879}.
uniprot
proteins
mass_dalton
35188
uniprot
proteins
mutagenesis
MUTAGEN 161; /note="H->Y: Abolishes inhibition of PDH complex activity."; /evidence="ECO:0000269|PubMed:25525879
uniprot
proteins
protein_family
Class II subfamily
uniprot
proteins
protein_family
Sirtuin family
uniprot
proteins
pubmed
10381378
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16079181
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16959573
uniprot
proteins
pubmed
17715127
uniprot
proteins
pubmed
23438705
uniprot
proteins
pubmed
23562301
uniprot
proteins
pubmed
23663782
uniprot
proteins
pubmed
24043310
uniprot
proteins
pubmed
24052263
uniprot
proteins
pubmed
25525879
uniprot
proteins
sequence_length
314
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:16959573, ECO:0000269|PubMed:17715127}.
uniprot
proteins