HUMAN:SIR4

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	No Information Provided. (synonyms: SIR2L4)
Protein Name(s)	NAD-dependent protein lipoamidase sirtuin-4, mitochondrial (ECO:0000255 with HAMAP-Rule:MF_03161, ECO:0000303 with PMID:25525879^[1]) NAD-dependent ADP-ribosyltransferase sirtuin-4 (ECO:0000255 with HAMAP-Rule:MF_03161) NAD-dependent protein deacetylase sirtuin-4 (ECO:0000255 with HAMAP-Rule:MF_03161) Regulatory protein SIR2 homolog 4 (ECO:0000255 with HAMAP-Rule:MF_03161) SIR2-like protein 4 (ECO:0000255 with HAMAP-Rule:MF_03161)
External Links
UniProt	Q9Y6E7
EMBL	AF083109 AC003982 BC109319 BC109320
CCDS	CCDS9194.1
RefSeq	NP_036372.1 XP_006719371.1 XP_006719372.1
UniGene	Hs.50861
ProteinModelPortal	Q9Y6E7
SMR	Q9Y6E7
BioGrid	116981
IntAct	Q9Y6E7
STRING	9606.ENSP00000202967
ChEMBL	CHEMBL2163185
PhosphoSite	Q9Y6E7
BioMuta	SIRT4
DMDM	38258657
PaxDb	Q9Y6E7
PRIDE	Q9Y6E7
Ensembl	ENST00000202967
GeneID	23409
KEGG	hsa:23409
UCSC	uc001tyc.3
CTD	23409
GeneCards	SIRT4
HGNC	HGNC:14932
HPA	HPA029691 HPA029692
MIM	604482
neXtProt	NX_Q9Y6E7
PharmGKB	PA37937
eggNOG	COG0846
GeneTree	ENSGT00740000115330
HOGENOM	HOG000085953
HOVERGEN	HBG059577
InParanoid	Q9Y6E7
KO	K11414
OMA	CSKASIG
PhylomeDB	Q9Y6E7
TreeFam	TF106182
GeneWiki	SIRT4
GenomeRNAi	23409
NextBio	45593
PRO	PR:Q9Y6E7
Proteomes	UP000005640
Bgee	Q9Y6E7
CleanEx	HS_SIRT4
ExpressionAtlas	Q9Y6E7
Genevisible	Q9Y6E7
GO	GO:0005743 GO:0005759 GO:0005739 GO:0047708 GO:0061690 GO:0003950 GO:0070403 GO:0008270 GO:0006974 GO:0071456 GO:0006342 GO:0006541 GO:0010667 GO:0046322 GO:0046676 GO:1903217 GO:0034983 GO:0046889 GO:0006471 GO:0000820 GO:1904182 GO:0072350
Gene3D	3.30.1600.10 3.40.50.1220
HAMAP	MF_01967
InterPro	IPR029035 IPR003000 IPR026591 IPR026587 IPR026590
PANTHER	PTHR11085
Pfam	PF02146
SUPFAM	SSF52467
PROSITE	PS50305

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0046322	negative regulation of fatty acid oxidation	PMID:24043310^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1904182	regulation of pyruvate dehydrogenase activity	PMID:25525879^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0061690	lipoamidase activity	PMID:25525879^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0047708	biotinidase activity	PMID:25525879^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0072350	tricarboxylic acid metabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8R216	P	Seeded From UniProt	complete
involved_in	GO:0046889	positive regulation of lipid biosynthetic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8R216	P	Seeded From UniProt	complete
involved_in	GO:0046676	negative regulation of insulin secretion	PMID:17715127^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0046322	negative regulation of fatty acid oxidation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8R216	P	Seeded From UniProt	complete
involved_in	GO:0034983	peptidyl-lysine deacetylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8R216	P	Seeded From UniProt	complete
NOT\|enables	GO:0034979	NAD-dependent protein deacetylase activity	PMID:17715127^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8R216	P	Seeded From UniProt	complete
involved_in	GO:0006541	glutamine metabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8R216	P	Seeded From UniProt	complete
involved_in	GO:0006471	protein ADP-ribosylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8R216	P	Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	PMID:16959573^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	PMID:17715127^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:16079181^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003950	NAD+ ADP-ribosyltransferase activity	PMID:17715127^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003950	NAD+ ADP-ribosyltransferase activity	PMID:16959573^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003950	NAD+ ADP-ribosyltransferase activity	PMID:16959573^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:1903217	negative regulation of protein processing involved in protein targeting to mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V641 ensembl:ENSRNOP00000001523	P	Seeded From UniProt	complete
involved_in	GO:0071456	cellular response to hypoxia	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V641 ensembl:ENSRNOP00000001523	P	Seeded From UniProt	complete
involved_in	GO:0010667	negative regulation of cardiac muscle cell apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V641 ensembl:ENSRNOP00000001523	P	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:G3V641 ensembl:ENSRNOP00000001523	C	Seeded From UniProt	complete
involved_in	GO:1904182	regulation of pyruvate dehydrogenase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	P	Seeded From UniProt	complete
involved_in	GO:0072350	tricarboxylic acid metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	P	Seeded From UniProt	complete
enables	GO:0061690	lipoamidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	F	Seeded From UniProt	complete
involved_in	GO:0046889	positive regulation of lipid biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	P	Seeded From UniProt	complete
involved_in	GO:0046676	negative regulation of insulin secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	P	Seeded From UniProt	complete
involved_in	GO:0046322	negative regulation of fatty acid oxidation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	P	Seeded From UniProt	complete
involved_in	GO:0034983	peptidyl-lysine deacetylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	P	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	P	Seeded From UniProt	complete
involved_in	GO:0006541	glutamine metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	P	Seeded From UniProt	complete
involved_in	GO:0006471	protein ADP-ribosylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	P	Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	C	Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	C	Seeded From UniProt	complete
enables	GO:0003950	NAD+ ADP-ribosyltransferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	F	Seeded From UniProt	complete
involved_in	GO:0000820	regulation of glutamine family amino acid metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R216 ensembl:ENSMUSP00000107697	P	Seeded From UniProt	complete
enables	GO:0070403	NAD+ binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003000	F	Seeded From UniProt	complete
enables	GO:0003950	NAD+ ADP-ribosyltransferase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000376616	F	Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000376616	C	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000376616	F	Seeded From UniProt	complete
enables	GO:0070403	NAD+ binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000376616	F	Seeded From UniProt	complete
involved_in	GO:0006476	protein deacetylation	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000376616	P	Seeded From UniProt	complete
involved_in	GO:0006471	protein ADP-ribosylation	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000376616	P	Seeded From UniProt	complete
involved_in	GO:0006471	protein ADP-ribosylation	PMID:10381378^[6] PMID:17456799^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006342	chromatin silencing	PMID:10381378^[6]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003950	NAD+ ADP-ribosyltransferase activity	PMID:10381378^[6] PMID:17456799^[7] Reactome:R-HSA-5688276	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	Reactome:R-HSA-1592230	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	Reactome:R-HSA-5688276	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496	C	Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0170	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Mathias, RA et al. (2014) Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity. Cell 159 1615-25 PubMed GONUTS page
↑ Laurent, G et al. (2013) SIRT4 represses peroxisome proliferator-activated receptor α activity to suppress hepatic fat oxidation. Mol. Cell. Biol. 33 4552-61 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Ahuja, N et al. (2007) Regulation of insulin secretion by SIRT4, a mitochondrial ADP-ribosyltransferase. J. Biol. Chem. 282 33583-92 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Haigis, MC et al. (2006) SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 126 941-54 PubMed GONUTS page
↑ Michishita, E et al. (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell 16 4623-35 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Frye, RA (1999) Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res. Commun. 260 273-9 PubMed GONUTS page
↑ ^7.0 ^7.1 Yamamoto, H et al. (2007) Sirtuin functions in health and disease. Mol. Endocrinol. 21 1745-55 PubMed GONUTS page

[PMID:25525879-1] 1.0 ^1.1 ^1.2 ^1.3 Mathias, RA et al. (2014) Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity. Cell 159 1615-25 PubMed GONUTS page

[PMID:24043310-2] Laurent, G et al. (2013) SIRT4 represses peroxisome proliferator-activated receptor α activity to suppress hepatic fat oxidation. Mol. Cell. Biol. 33 4552-61 PubMed GONUTS page

[PMID:17715127-3] 3.0 ^3.1 ^3.2 ^3.3 Ahuja, N et al. (2007) Regulation of insulin secretion by SIRT4, a mitochondrial ADP-ribosyltransferase. J. Biol. Chem. 282 33583-92 PubMed GONUTS page

[PMID:16959573-4] 4.0 ^4.1 ^4.2 Haigis, MC et al. (2006) SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 126 941-54 PubMed GONUTS page

[PMID:16079181-5] Michishita, E et al. (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell 16 4623-35 PubMed GONUTS page

[PMID:10381378-6] 6.0 ^6.1 ^6.2 Frye, RA (1999) Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res. Commun. 260 273-9 PubMed GONUTS page

[PMID:17456799-7] 7.0 ^7.1 Yamamoto, H et al. (2007) Sirtuin functions in health and disease. Mol. Endocrinol. 21 1745-55 PubMed GONUTS page

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HUMAN:SIR4

Contents

Annotations

Notes

References

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