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NAD-dependent protein lipoamidase sirtuin-4, mitochondrial (EC 3.5.1.-) (NAD-dependent ADP-ribosyltransferase sirtuin-4) (EC 2.4.2.-) (NAD-dependent protein deacetylase sirtuin-4) (EC 3.5.1.-) (Regulatory protein SIR2 homolog 4) (SIR2-like protein 4)

 SIR4_HUMAN              Reviewed;         314 AA.
Q9Y6E7; O43346; Q32M33;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
28-FEB-2018, entry version 140.
RecName: Full=NAD-dependent protein lipoamidase sirtuin-4, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000303|PubMed:25525879};
EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000305|PubMed:25525879};
AltName: Full=NAD-dependent ADP-ribosyltransferase sirtuin-4 {ECO:0000255|HAMAP-Rule:MF_03161};
EC=2.4.2.- {ECO:0000255|HAMAP-Rule:MF_03161};
AltName: Full=NAD-dependent protein deacetylase sirtuin-4 {ECO:0000255|HAMAP-Rule:MF_03161};
EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_03161};
AltName: Full=Regulatory protein SIR2 homolog 4 {ECO:0000255|HAMAP-Rule:MF_03161};
AltName: Full=SIR2-like protein 4 {ECO:0000255|HAMAP-Rule:MF_03161};
Flags: Precursor;
Name=SIRT4 {ECO:0000255|HAMAP-Rule:MF_03161,
ECO:0000312|HGNC:HGNC:14932}; Synonyms=SIR2L4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=10381378; DOI=10.1006/bbrc.1999.0897;
Frye R.A.;
"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. 260:273-279(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, INTERACTION WITH GLUD1, AND
SUBCELLULAR LOCATION.
PubMed=16959573; DOI=10.1016/j.cell.2006.06.057;
Haigis M.C., Mostoslavsky R., Haigis K.M., Fahie K.,
Christodoulou D.C., Murphy A.J., Valenzuela D.M., Yancopoulos G.D.,
Karow M., Blander G., Wolberger C., Prolla T.A., Weindruch R.,
Alt F.W., Guarente L.;
"SIRT4 inhibits glutamate dehydrogenase and opposes the effects of
calorie restriction in pancreatic beta cells.";
Cell 126:941-954(2006).
[5]
PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBCELLULAR LOCATION, AND
INTERACTION WITH IDE AND SLC25A5.
PubMed=17715127; DOI=10.1074/jbc.M705488200;
Ahuja N., Schwer B., Carobbio S., Waltregny D., North B.J.,
Castronovo V., Maechler P., Verdin E.;
"Regulation of insulin secretion by SIRT4, a mitochondrial ADP-
ribosyltransferase.";
J. Biol. Chem. 282:33583-33592(2007).
[6]
SUBCELLULAR LOCATION.
PubMed=16079181; DOI=10.1091/mbc.E05-01-0033;
Michishita E., Park J.Y., Burneskis J.M., Barrett J.C., Horikawa I.;
"Evolutionarily conserved and nonconserved cellular localizations and
functions of human SIRT proteins.";
Mol. Biol. Cell 16:4623-4635(2005).
[7]
FUNCTION AS A TUMOR SUPPRESSOR.
PubMed=23562301; DOI=10.1016/j.ccr.2013.02.024;
Jeong S.M., Xiao C., Finley L.W., Lahusen T., Souza A.L., Pierce K.,
Li Y.H., Wang X., Laurent G., German N.J., Xu X., Li C., Wang R.H.,
Lee J., Csibi A., Cerione R., Blenis J., Clish C.B., Kimmelman A.,
Deng C.X., Haigis M.C.;
"SIRT4 has tumor-suppressive activity and regulates the cellular
metabolic response to DNA damage by inhibiting mitochondrial glutamine
metabolism.";
Cancer Cell 23:450-463(2013).
[8]
FUNCTION AS A TUMOR SUPPRESSOR.
PubMed=23663782; DOI=10.1016/j.cell.2013.04.023;
Csibi A., Fendt S.M., Li C., Poulogiannis G., Choo A.Y., Chapski D.J.,
Jeong S.M., Dempsey J.M., Parkhitko A., Morrison T., Henske E.P.,
Haigis M.C., Cantley L.C., Stephanopoulos G., Yu J., Blenis J.;
"The mTORC1 pathway stimulates glutamine metabolism and cell
proliferation by repressing SIRT4.";
Cell 153:840-854(2013).
[9]
FUNCTION, AND INTERACTION WITH PCCA; MCCC1 AND PC.
PubMed=23438705; DOI=10.1016/j.mito.2013.02.002;
Wirth M., Karaca S., Wenzel D., Ho L., Tishkoff D., Lombard D.B.,
Verdin E., Urlaub H., Jedrusik-Bode M., Fischle W.;
"Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and
mammals interact with pyruvate carboxylase and other acetylated
biotin-dependent carboxylases.";
Mitochondrion 13:705-720(2013).
[10]
FUNCTION.
PubMed=24043310; DOI=10.1128/MCB.00087-13;
Laurent G., de Boer V.C., Finley L.W., Sweeney M., Lu H., Schug T.T.,
Cen Y., Jeong S.M., Li X., Sauve A.A., Haigis M.C.;
"SIRT4 represses peroxisome proliferator-activated receptor alpha
activity to suppress hepatic fat oxidation.";
Mol. Cell. Biol. 33:4552-4561(2013).
[11]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH DLAT AND
PDHX, MUTAGENESIS OF HIS-161, AND INDUCTION BY GLUTAMINE.
PubMed=25525879; DOI=10.1016/j.cell.2014.11.046;
Mathias R.A., Greco T.M., Oberstein A., Budayeva H.G., Chakrabarti R.,
Rowland E.A., Kang Y., Shenk T., Cristea I.M.;
"Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex
activity.";
Cell 159:1615-1625(2014).
-!- FUNCTION: Acts as NAD-dependent protein lipoamidase, ADP-ribosyl
transferase and deacetylase. Catalyzes more efficiently removal of
lipoyl- and biotinyl- than acetyl-lysine modifications. 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. 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. 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. Impairs SIRT1:PPARA interaction
probably through the regulation of NAD(+) levels
(PubMed:24043310). Down-regulates insulin secretion.
{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:25525879}.
-!- CATALYTIC ACTIVITY: NAD(+) + a protein = nicotinamide + an N-(ADP-
D-ribosyl)-protein. {ECO:0000255|HAMAP-Rule:MF_03161}.
-!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
acetyl-ADP-ribose + a protein. {ECO:0000255|HAMAP-Rule:MF_03161}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_03161};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_03161};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=719 uM for a peptide of H3 biotinylated at 'Lys-9'
{ECO:0000269|PubMed:25525879};
KM=814 uM for a peptide of H3 lipoylated at 'Lys-9'
{ECO:0000269|PubMed:25525879};
KM=239 uM for a peptide of DLAT lipoylated at 'Lys-259'
{ECO:0000269|PubMed:25525879};
Note=kcat is 0.0019 sec(-1) for the delipoylation of H3 'Lys-9'.
kcat is 0.0005 sec(-1) for the debiotinylation of H3 'Lys-9'.
kcat is 0.0018 sec(-1) for the delipoylation of DLAT 'Lys-259'.
{ECO:0000269|PubMed:25525879};
-!- SUBUNIT: Interacts with GLUD1, IDE and SLC25A5 (PubMed:16959573,
PubMed:17715127). Interacts with DLAT and PDHX (PubMed:25525879).
Interacts with MCCC1 (via the biotin carboxylation domain)
(PubMed:23438705). Interacts with PCCA and PC (PubMed:23438705).
{ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:16959573,
ECO:0000269|PubMed:17715127, ECO:0000269|PubMed:23438705,
ECO:0000269|PubMed:25525879}.
-!- INTERACTION:
P10515:DLAT; NbExp=6; IntAct=EBI-2606540, EBI-2959723;
O00330:PDHX; NbExp=4; IntAct=EBI-2606540, EBI-751566;
P05141:SLC25A5; NbExp=2; IntAct=EBI-2606540, EBI-355133;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
Rule:MF_03161, ECO:0000269|PubMed:16079181,
ECO:0000269|PubMed:16959573, ECO:0000269|PubMed:17715127}.
-!- TISSUE SPECIFICITY: Detected in vascular smooth muscle and
striated muscle. Detected in insulin-producing beta-cells in
pancreas islets of Langerhans (at protein level). Widely
expressed. Weakly expressed in leukocytes and fetal thymus.
{ECO:0000269|PubMed:10381378}.
-!- INDUCTION: Induced by glutamine (at protein level).
{ECO:0000269|PubMed:25525879}.
-!- MISCELLANEOUS: Expression is down-regulated in a number of
cancers, while overexpression reduces cell proliferation,
transformation, and tumor development (PubMed:23562301,
PubMed:23663782). {ECO:0000305|PubMed:23562301,
ECO:0000305|PubMed:23663782}.
-!- MISCELLANEOUS: According to some authors, ADP-ribosyltransferase
activity of sirtuins may be an inefficient side reaction of the
deacetylase activity and may not be physiologically relevant.
{ECO:0000255|HAMAP-Rule:MF_03161}.
-!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
{ECO:0000255|HAMAP-Rule:MF_03161}.
-!- SEQUENCE CAUTION:
Sequence=AAB95634.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF083109; AAD40852.1; -; mRNA.
EMBL; AC003982; AAB95634.1; ALT_SEQ; Genomic_DNA.
EMBL; BC109319; AAI09320.1; -; mRNA.
EMBL; BC109320; AAI09321.1; -; mRNA.
CCDS; CCDS9194.1; -.
RefSeq; NP_036372.1; NM_012240.2.
RefSeq; XP_006719371.1; XM_006719308.2.
RefSeq; XP_006719372.1; XM_006719309.3.
UniGene; Hs.50861; -.
ProteinModelPortal; Q9Y6E7; -.
SMR; Q9Y6E7; -.
BioGrid; 116981; 10.
IntAct; Q9Y6E7; 109.
STRING; 9606.ENSP00000202967; -.
ChEMBL; CHEMBL2163185; -.
iPTMnet; Q9Y6E7; -.
PhosphoSitePlus; Q9Y6E7; -.
BioMuta; SIRT4; -.
DMDM; 38258657; -.
PaxDb; Q9Y6E7; -.
PeptideAtlas; Q9Y6E7; -.
PRIDE; Q9Y6E7; -.
Ensembl; ENST00000202967; ENSP00000202967; ENSG00000089163.
GeneID; 23409; -.
KEGG; hsa:23409; -.
UCSC; uc001tyc.4; human.
CTD; 23409; -.
DisGeNET; 23409; -.
EuPathDB; HostDB:ENSG00000089163.4; -.
GeneCards; SIRT4; -.
HGNC; HGNC:14932; SIRT4.
HPA; HPA029691; -.
HPA; HPA029692; -.
MIM; 604482; gene.
neXtProt; NX_Q9Y6E7; -.
OpenTargets; ENSG00000089163; -.
PharmGKB; PA37937; -.
eggNOG; KOG2683; Eukaryota.
eggNOG; COG0846; LUCA.
GeneTree; ENSGT00870000136443; -.
HOGENOM; HOG000085953; -.
HOVERGEN; HBG059577; -.
InParanoid; Q9Y6E7; -.
KO; K11414; -.
OMA; ARQRYWA; -.
OrthoDB; EOG091G0DTB; -.
PhylomeDB; Q9Y6E7; -.
TreeFam; TF106182; -.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
GeneWiki; SIRT4; -.
GenomeRNAi; 23409; -.
PRO; PR:Q9Y6E7; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000089163; -.
CleanEx; HS_SIRT4; -.
ExpressionAtlas; Q9Y6E7; baseline and differential.
Genevisible; Q9Y6E7; HS.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0047708; F:biotinidase activity; IDA:UniProtKB.
GO; GO:0061690; F:lipoamidase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0006342; P:chromatin silencing; TAS:ProtInc.
GO; GO:0006541; P:glutamine metabolic process; ISS:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0046322; P:negative regulation of fatty acid oxidation; IMP:UniProtKB.
GO; GO:0046676; P:negative regulation of insulin secretion; IMP:UniProtKB.
GO; GO:1903217; P:negative regulation of protein processing involved in protein targeting to mitochondrion; IEA:Ensembl.
GO; GO:0034983; P:peptidyl-lysine deacetylation; ISS:UniProtKB.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0006471; P:protein ADP-ribosylation; ISS:UniProtKB.
GO; GO:0000820; P:regulation of glutamine family amino acid metabolic process; IEA:Ensembl.
GO; GO:1904182; P:regulation of pyruvate dehydrogenase activity; IDA:UniProtKB.
GO; GO:0072350; P:tricarboxylic acid metabolic process; ISS:UniProtKB.
Gene3D; 3.30.1600.10; -; 2.
HAMAP; MF_01967; Sirtuin_ClassII; 1.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR003000; Sirtuin.
InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
InterPro; IPR026587; Sirtuin_class_II.
InterPro; IPR026590; Ssirtuin_cat_dom.
Pfam; PF02146; SIR2; 1.
SUPFAM; SSF52467; SSF52467; 1.
PROSITE; PS50305; SIRTUIN; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; DNA damage; Hydrolase;
Metal-binding; Mitochondrion; NAD; Reference proteome; Transferase;
Transit peptide; Tumor suppressor; Zinc.
TRANSIT 1 28 Mitochondrion. {ECO:0000255|HAMAP-
Rule:MF_03161,
ECO:0000269|PubMed:16959573,
ECO:0000269|PubMed:17715127}.
CHAIN 29 314 NAD-dependent protein lipoamidase
sirtuin-4, mitochondrial.
/FTId=PRO_0000110264.
DOMAIN 45 314 Deacetylase sirtuin-type.
{ECO:0000255|HAMAP-Rule:MF_03161}.
NP_BIND 62 82 NAD. {ECO:0000255|HAMAP-Rule:MF_03161}.
NP_BIND 143 146 NAD. {ECO:0000255|HAMAP-Rule:MF_03161}.
NP_BIND 260 262 NAD. {ECO:0000255|HAMAP-Rule:MF_03161}.
NP_BIND 286 288 NAD. {ECO:0000255|HAMAP-Rule:MF_03161}.
ACT_SITE 161 161 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03161}.
METAL 169 169 Zinc. {ECO:0000255|HAMAP-Rule:MF_03161}.
METAL 172 172 Zinc. {ECO:0000255|HAMAP-Rule:MF_03161}.
METAL 220 220 Zinc. {ECO:0000255|HAMAP-Rule:MF_03161}.
METAL 223 223 Zinc. {ECO:0000255|HAMAP-Rule:MF_03161}.
BINDING 304 304 NAD; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_03161}.
MUTAGEN 161 161 H->Y: Abolishes inhibition of PDH complex
activity. {ECO:0000269|PubMed:25525879}.
SEQUENCE 314 AA; 35188 MW; 2B76963AD2C3B354 CRC64;
MKMSFALTFR SAKGRWIANP SQPCSKASIG LFVPASPPLD PEKVKELQRF ITLSKRLLVM
TGAGISTESG IPDYRSEKVG LYARTDRRPI QHGDFVRSAP IRQRYWARNF VGWPQFSSHQ
PNPAHWALST WEKLGKLYWL VTQNVDALHT KAGSRRLTEL HGCMDRVLCL DCGEQTPRGV
LQERFQVLNP TWSAEAHGLA PDGDVFLSEE QVRSFQVPTC VQCGGHLKPD VVFFGDTVNP
DKVDFVHKRV KEADSLLVVG SSLQVYSGYR FILTAWEKKL PIAILNIGPT RSDDLACLKL
NSRCGELLPL IDPC


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18-003-43079 NAD-dependent deacetylase sirtuin-1 - EC 3.5.1.-; hSIRT1; hSIR2; SIR2-like protein 1 Polyclonal 0.05 mg Aff Pur
EIAAB38510 Mouse,Mus musculus,NAD-dependent deacetylase sirtuin-5,Sir2l5,SIR2-like protein 5,Sirt5
EIAAB38513 Mouse,Mus musculus,NAD-dependent deacetylase sirtuin-6,Sir2l6,SIR2-like protein 6,Sirt6
EIAAB38516 Mouse,Mus musculus,NAD-dependent deacetylase sirtuin-7,Sir2l7,SIR2-like protein 7,Sirt7
E0430r ELISA NAD-dependent deacetylase sirtuin-2,Rat,Rattus norvegicus,Sir2l2,SIR2-like protein 2,Sirt2 96T
EIAAB38511 Homo sapiens,Human,NAD-dependent deacetylase sirtuin-5,SIR2L5,SIR2-like protein 5,SIRT5
EIAAB38514 Homo sapiens,Human,NAD-dependent deacetylase sirtuin-6,SIR2L6,SIR2-like protein 6,SIRT6
EIAAB38515 Homo sapiens,Human,NAD-dependent deacetylase sirtuin-7,SIR2L7,SIR2-like protein 7,SIRT7
E0430r ELISA kit NAD-dependent deacetylase sirtuin-2,Rat,Rattus norvegicus,Sir2l2,SIR2-like protein 2,Sirt2 96T
U0430r CLIA NAD-dependent deacetylase sirtuin-2,Rat,Rattus norvegicus,Sir2l2,SIR2-like protein 2,Sirt2 96T
E2135m ELISA Mouse,mSIR2L3,Mus musculus,NAD-dependent deacetylase sirtuin-3,Sir2l3,SIR2-like protein 3,Sirt3 96T
U0430m CLIA Mouse,mSIR2L2,Mus musculus,NAD-dependent deacetylase sirtuin-2,Sir2l2,SIR2-like protein 2,Sirt2 96T
E0430m ELISA kit Mouse,mSIR2L2,Mus musculus,NAD-dependent deacetylase sirtuin-2,Sir2l2,SIR2-like protein 2,Sirt2 96T


 

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