Sequence of SIR4_HUMAN
EC Number:2.3.1.286
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
[protein]-N6-acetyl-L-lysine + NAD+ + H2O = [protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
Other sequences found for EC No. 2.3.1.286
General information:
Sequence
0 MKMSFALTFR SAKGRWIANP SQPCSKASIG LFVPASPPLD PEKVKELQRF ITLSKRLLVM
60 TGAGISTESG IPDYRSEKVG LYARTDRRPI QHGDFVRSAP IRQRYWARNF VGWPQFSSHQ
120 PNPAHWALST WEKLGKLYWL VTQNVDALHT KAGSRRLTEL HGCMDRVLCL DCGEQTPRGV
180 LQERFQVLNP TWSAEAHGLA PDGDVFLSEE QVRSFQVPTC VQCGGHLKPD VVFFGDTVNP
240 DKVDFVHKRV KEADSLLVVG SSLQVYSGYR FILTAWEKKL PIAILNIGPT RSDDLACLKL
300 NSRCGELLPL IDPC
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
865931
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
865932
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
865933
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
865934
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
865935
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
865936
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
865937
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
865938
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
865939
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
865940
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
865941
Feldman J.L.,Baeza J.,Denu J.M.
Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins.
J. Biol. Chem.
288
31350-31356
2013
865942
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
