[English
Start Page]
[Deutsche
Startseite]
[Email
Feedback] |
(Last modification: 03. November 2009)
Return to English or German text
Sirtuins: arrangement of pages
Sequences of human SIRT proteins (Note: the databases in several cases contained several entries for the same protein: if possible, I picked the newest entry, usually from 2009)
Return to English or German text
LOCUS NP_036370 747 aa linear PRI 11-OCT-2009 DEFINITION sirtuin 1 isoform a [Homo sapiens]. ACCESSION NP_036370 VERSION NP_036370.2 GI:7657575 DBSOURCE REFSEQ: accession NM_012238.4 KEYWORDS . SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 747) AUTHORS Kakefuda,K., Fujita,Y., Oyagi,A., Hyakkoku,K., Kojima,T., Umemura,K., Tsuruma,K., Shimazawa,M., Ito,M., Nozawa,Y. and Hara,H. TITLE Sirtuin 1 overexpression mice show a reference memory deficit, but not neuroprotection JOURNAL Biochem. Biophys. Res. Commun. 387 (4), 784-788 (2009) PUBMED 19643082 REMARK GeneRIF: These findings suggest that an excessive expression of SIRT1 might induce the memory deficit in mice, but not neuroprotective effects. REFERENCE 2 (residues 1 to 747) AUTHORS Zillikens,M.C., van Meurs,J.B., Rivadeneira,F., Amin,N., Hofman,A., Oostra,B.A., Sijbrands,E.J., Witteman,J.C., Pols,H.A., van Duijn,C.M. and Uitterlinden,A.G. TITLE SIRT1 genetic variation is related to body mass index and risk of obesity JOURNAL Diabetes (2009) In press PUBMED 19741164 REMARK GeneRIF: Observational study of gene-disease association. (HuGE Navigator) Publication Status: Available-Online prior to print REFERENCE 3 (residues 1 to 747) AUTHORS Iwahara,N., Hisahara,S., Hayashi,T. and Horio,Y. TITLE Transcriptional activation of NAD+-dependent protein deacetylase SIRT1 by nuclear receptor TLX JOURNAL Biochem. Biophys. Res. Commun. 386 (4), 671-675 (2009) PUBMED 19555662 REMARK GeneRIF: TLX is an inducer of SIRT1 and may contribute to neurogenesis both as a transactivator and as a repressor. REFERENCE 4 (residues 1 to 747) AUTHORS Zhou,Y., Schmitz,K.M., Mayer,C., Yuan,X., Akhtar,A. and Grummt,I. TITLE Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing JOURNAL Nat. Cell Biol. 11 (8), 1010-1016 (2009) PUBMED 19578370 REMARK GeneRIF: Data show that MOF acetylates TIP5, the largest subunit of NoRC, at a single lysine residue, K633, adjacent to the TIP5 RNA-binding domain, and that SIRT1 (removes the acetyl group from K633. REFERENCE 5 (residues 1 to 747) AUTHORS Halaschek-Wiener,J., Amirabbasi-Beik,M., Monfared,N., Pieczyk,M., Sailer,C., Kollar,A., Thomas,R., Agalaridis,G., Yamada,S., Oliveira,L., Collins,J.A., Meneilly,G., Marra,M.A., Madden,K.M., Le,N.D., Connors,J.M. and Brooks-Wilson,A.R. TITLE Genetic variation in healthy oldest-old JOURNAL PLoS ONE 4 (8), E6641 (2009) PUBMED 19680556 REMARK GeneRIF: Observational study of gene-disease association. (HuGE Navigator) Publication Status: Online-Only REFERENCE 6 (sites) AUTHORS Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E., Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P. TITLE Large-scale characterization of HeLa cell nuclear phosphoproteins JOURNAL Proc. Natl. Acad. Sci. U.S.A. 101 (33), 12130-12135 (2004) PUBMED 15302935 REFERENCE 7 (residues 1 to 747) AUTHORS Langley,E., Pearson,M., Faretta,M., Bauer,U.M., Frye,R.A., Minucci,S., Pelicci,P.G. and Kouzarides,T. TITLE Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence JOURNAL EMBO J. 21 (10), 2383-2396 (2002) PUBMED 12006491 REMARK GeneRIF: the SIRT1 deacetylase as a novel negative regulator of p53 function capable of modulating cellular senescence REFERENCE 8 (residues 1 to 747) AUTHORS Vaziri,H., Dessain,S.K., Ng Eaton,E., Imai,S.I., Frye,R.A., Pandita,T.K., Guarente,L. and Weinberg,R.A. TITLE hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase JOURNAL Cell 107 (2), 149-159 (2001) PUBMED 11672523 REFERENCE 9 (residues 1 to 747) AUTHORS Luo,J., Nikolaev,A.Y., Imai,S., Chen,D., Su,F., Shiloh,A., Guarente,L. and Gu,W. TITLE Negative control of p53 by Sir2alpha promotes cell survival under stress JOURNAL Cell 107 (2), 137-148 (2001) PUBMED 11672522 REMARK GeneRIF: SIRT1(Sir2alpha) deacetylates p53 and promotes survival REFERENCE 10 (residues 1 to 747) AUTHORS Frye,R.A. TITLE Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins JOURNAL Biochem. Biophys. Res. Commun. 273 (2), 793-798 (2000) PUBMED 10873683 REFERENCE 11 (residues 1 to 747) AUTHORS Frye,R.A. TITLE 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 JOURNAL Biochem. Biophys. Res. Commun. 260 (1), 273-279 (1999) PUBMED 10381378 COMMENT VALIDATED REFSEQ: This record has undergone validation or preliminary review. The reference sequence was derived from AF083106.2, AA452304.1 and BC012499.1. On Apr 27, 2000 this sequence version replaced gi:6912658.
Summary: This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Alternative splicing results in multiple transcript variants. [provided by RefSeq].
Transcript Variant: This variant (1) represents the longer transcript and encodes the longer isoform (a).
Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. FEATURES Location/Qualifiers source 1..747 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="10" /map="10q21.3" Protein 1..747 /product="sirtuin 1 isoform a" /note="sir2-like 1; SIR2alpha; sirtuin type 1" /calculated_mol_wt=81550 Site 27 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /citation=[6] Site 47 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /citation=[6] Region 254..489 /region_name="SIRT1" /note="SIRT1: Eukaryotic group (class1) which includes human sirtuins SIRT1-3 and yeast Hst1-4; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2...; cd01408" /db_xref="CDD:29376" Site order(263,265..266,273..274,327,345..346,348,363,440,445, 466..467,481) /site_type="other" /note="NAD+ binding site" /db_xref="CDD:29376" Site order(347,363,412,414..418,444..446) /site_type="other" /note="substrate binding site" /db_xref="CDD:29376" Site order(371,374,395,398) /site_type="other" /note="Zn binding site" /db_xref="CDD:29376" CDS 1..747 /gene="SIRT1" /gene_synonym="SIR2L1" /coded_by="NM_012238.4:54..2297" /note="isoform a is encoded by transcript variant 1" /db_xref="CCDS:CCDS7273.1" /db_xref="GeneID:23411" /db_xref="HGNC:14929" /db_xref="HPRD:08381" /db_xref="MIM:604479" ORIGIN 1 madeaalalq pggspsaaga dreaasspag eplrkrprrd gpglerspge pggaaperev 61 paaargcpga aaaalwreae aeaaaaggeq eaqataaage gdngpglqgp sreppladnl 121 ydeddddege eeeeaaaaai gyrdnllfgd eiitngfhsc esdeedrash asssdwtprp 181 rigpytfvqq hlmigtdprt ilkdllpeti pppelddmtl wqivinilse ppkrkkrkdi 241 ntiedavkll qeckkiivlt gagvsvscgi pdfrsrdgiy arlavdfpdl pdpqamfdie 301 yfrkdprpff kfakeiypgq fqpslchkfi alsdkegkll rnytqnidtl eqvagiqrii 361 qchgsfatas clickykvdc eavrgdifnq vvprcprcpa deplaimkpe ivffgenlpe 421 qfhramkydk devdllivig sslkvrpval ipssiphevp qilinreplp hlhfdvellg 481 dcdviinelc hrlggeyakl ccnpvklsei tekpprtqke laylselppt plhvsedsss 541 pertsppdss vivtlldqaa ksnddldvse skgcmeekpq evqtsrnves iaeqmenpdl 601 knvgsstgek nertsvagtv rkcwpnrvak eqisrrldgn qylflppnry ifhgaevysd 661 seddvlssss cgsnsdsgtc qspsleepme deseieefyn gledepdvpe raggagfgtd 721 gddqeainea isvkqevtdm nypsnks //
Top
LOCUS NP_001135970 452 aa linear PRI 11-OCT-2009 DEFINITION sirtuin 1 isoform b [Homo sapiens]. ACCESSION NP_001135970 VERSION NP_001135970.1 GI:215982798 DBSOURCE REFSEQ: accession NM_001142498.1 KEYWORDS . SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 452) AUTHORS Kakefuda,K., Fujita,Y., Oyagi,A., Hyakkoku,K., Kojima,T., Umemura,K., Tsuruma,K., Shimazawa,M., Ito,M., Nozawa,Y. and Hara,H. TITLE Sirtuin 1 overexpression mice show a reference memory deficit, but not neuroprotection JOURNAL Biochem. Biophys. Res. Commun. 387 (4), 784-788 (2009) PUBMED 19643082 REMARK GeneRIF: These findings suggest that an excessive expression of SIRT1 might induce the memory deficit in mice, but not neuroprotective effects. REFERENCE 2 (residues 1 to 452) AUTHORS Zillikens,M.C., van Meurs,J.B., Rivadeneira,F., Amin,N., Hofman,A., Oostra,B.A., Sijbrands,E.J., Witteman,J.C., Pols,H.A., van Duijn,C.M. and Uitterlinden,A.G. TITLE SIRT1 genetic variation is related to body mass index and risk of obesity JOURNAL Diabetes (2009) In press PUBMED 19741164 REMARK GeneRIF: Observational study of gene-disease association. (HuGE Navigator) Publication Status: Available-Online prior to print REFERENCE 3 (residues 1 to 452) AUTHORS Iwahara,N., Hisahara,S., Hayashi,T. and Horio,Y. TITLE Transcriptional activation of NAD+-dependent protein deacetylase SIRT1 by nuclear receptor TLX JOURNAL Biochem. Biophys. Res. Commun. 386 (4), 671-675 (2009) PUBMED 19555662 REMARK GeneRIF: TLX is an inducer of SIRT1 and may contribute to neurogenesis both as a transactivator and as a repressor. REFERENCE 4 (residues 1 to 452) AUTHORS Zhou,Y., Schmitz,K.M., Mayer,C., Yuan,X., Akhtar,A. and Grummt,I. TITLE Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing JOURNAL Nat. Cell Biol. 11 (8), 1010-1016 (2009) PUBMED 19578370 REMARK GeneRIF: Data show that MOF acetylates TIP5, the largest subunit of NoRC, at a single lysine residue, K633, adjacent to the TIP5 RNA-binding domain, and that SIRT1 (removes the acetyl group from K633. REFERENCE 5 (residues 1 to 452) AUTHORS Halaschek-Wiener,J., Amirabbasi-Beik,M., Monfared,N., Pieczyk,M., Sailer,C., Kollar,A., Thomas,R., Agalaridis,G., Yamada,S., Oliveira,L., Collins,J.A., Meneilly,G., Marra,M.A., Madden,K.M., Le,N.D., Connors,J.M. and Brooks-Wilson,A.R. TITLE Genetic variation in healthy oldest-old JOURNAL PLoS ONE 4 (8), E6641 (2009) PUBMED 19680556 REMARK GeneRIF: Observational study of gene-disease association. (HuGE Navigator) Publication Status: Online-Only REFERENCE 6 (residues 1 to 452) AUTHORS Langley,E., Pearson,M., Faretta,M., Bauer,U.M., Frye,R.A., Minucci,S., Pelicci,P.G. and Kouzarides,T. TITLE Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence JOURNAL EMBO J. 21 (10), 2383-2396 (2002) PUBMED 12006491 REMARK GeneRIF: the SIRT1 deacetylase as a novel negative regulator of p53 function capable of modulating cellular senescence REFERENCE 7 (residues 1 to 452) AUTHORS Vaziri,H., Dessain,S.K., Ng Eaton,E., Imai,S.I., Frye,R.A., Pandita,T.K., Guarente,L. and Weinberg,R.A. TITLE hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase JOURNAL Cell 107 (2), 149-159 (2001) PUBMED 11672523 REFERENCE 8 (residues 1 to 452) AUTHORS Luo,J., Nikolaev,A.Y., Imai,S., Chen,D., Su,F., Shiloh,A., Guarente,L. and Gu,W. TITLE Negative control of p53 by Sir2alpha promotes cell survival under stress JOURNAL Cell 107 (2), 137-148 (2001) PUBMED 11672522 REMARK GeneRIF: SIRT1(Sir2alpha) deacetylates p53 and promotes survival REFERENCE 9 (residues 1 to 452) AUTHORS Frye,R.A. TITLE Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins JOURNAL Biochem. Biophys. Res. Commun. 273 (2), 793-798 (2000) PUBMED 10873683 REFERENCE 10 (residues 1 to 452) AUTHORS Frye,R.A. TITLE 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 JOURNAL Biochem. Biophys. Res. Commun. 260 (1), 273-279 (1999) PUBMED 10381378 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AK289743.1, DB162635.1, AA452304.1 and BC012499.1.
Summary: This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Alternative splicing results in multiple transcript variants. [provided by RefSeq].
Transcript Variant: This variant (2) contains an alternate in-frame exon in the 5' coding region and uses a downstream start codon, compared to variant 1. Isoform b has a shorter N-terminus, compared to isoform a.
Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. FEATURES Location/Qualifiers source 1..452 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="10" /map="10q21.3" Protein 1..452 /product="sirtuin 1 isoform b" /note="sir2-like 1; SIR2alpha; sirtuin type 1" /calculated_mol_wt=50366 Region 1..194 /region_name="SIRT1" /note="SIRT1: Eukaryotic group (class1) which includes human sirtuins SIRT1-3 and yeast Hst1-4; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2...; cd01408" /db_xref="CDD:29376" Site order(32,50..51,53,68,145,150,171..172,186) /site_type="other" /note="NAD+ binding site" /db_xref="CDD:29376" Site order(52,68,117,119..123,149..151) /site_type="other" /note="substrate binding site" /db_xref="CDD:29376" Site order(76,79,100,103) /site_type="other" /note="Zn binding site" /db_xref="CDD:29376" CDS 1..452 /gene="SIRT1" /gene_synonym="SIR2L1" /coded_by="NM_001142498.1:433..1791" /note="isoform b is encoded by transcript variant 2" /db_xref="CCDS:CCDS44412.1" /db_xref="GeneID:23411" /db_xref="HGNC:14929" /db_xref="MIM:604479" ORIGIN 1 mfdieyfrkd prpffkfake iypgqfqpsl chkfialsdk egkllrnytq nidtleqvag 61 iqriiqchgs fatasclick ykvdceavrg difnqvvprc prcpadepla imkpeivffg 121 enlpeqfhra mkydkdevdl livigsslkv rpvalipssi phevpqilin replphlhfd 181 vellgdcdvi inelchrlgg eyaklccnpv klseitekpp rtqkelayls elpptplhvs 241 edsssperts ppdssvivtl ldqaaksndd ldvseskgcm eekpqevqts rnvesiaeqm 301 enpdlknvgs stgeknerts vagtvrkcwp nrvakeqisr rldgnqylfl ppnryifhga 361 evysdseddv lsssscgsns dsgtcqspsl eepmedesei eefynglede pdvperagga 421 gfgtdgddqe aineaisvkq evtdmnypsn ks //
Top
LOCUS NP_036369 389 aa linear PRI 12-JUL-2009 DEFINITION sirtuin 2 isoform 1 [Homo sapiens]. ACCESSION NP_036369 VERSION NP_036369.2 GI:13775600 DBSOURCE REFSEQ: accession NM_012237.2 KEYWORDS . SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 389) AUTHORS Inoue,T., Nakayama,Y., Yamada,H., Li,Y.C., Yamaguchi,S., Osaki,M., Kurimasa,A., Hiratsuka,M., Katoh,M. and Oshimura,M. TITLE SIRT2 downregulation confers resistance to microtubule inhibitors by prolonging chronic mitotic arrest JOURNAL Cell Cycle 8 (8), 1279-1291 (2009) PUBMED 19282667 REMARK GeneRIF: The effects of SIRT2 downregulation on sensitivity to microtubule inhibitors using HCT116 cells, was investigated. REFERENCE 2 (residues 1 to 389) AUTHORS Black,J.C., Mosley,A., Kitada,T., Washburn,M. and Carey,M. TITLE The SIRT2 deacetylase regulates autoacetylation of p300 JOURNAL Mol. Cell 32 (3), 449-455 (2008) PUBMED 18995842 REMARK GeneRIF: p300 undergoes a dynamic cycle of autoacetylation and deacetylation regulated by SIRT2. REFERENCE 3 (residues 1 to 389) AUTHORS Han,Y., Jin,Y.H., Kim,Y.J., Kang,B.Y., Choi,H.J., Kim,D.W., Yeo,C.Y. and Lee,K.Y. TITLE Acetylation of Sirt2 by p300 attenuates its deacetylase activity JOURNAL Biochem. Biophys. Res. Commun. 375 (4), 576-580 (2008) PUBMED 18722353 REMARK GeneRIF: These observations demonstrate that p300 can inactivate Sirt2 by acetylation and that p300 may regulate the activity of p53 indirectly through Sirt2 in addition to its direct modification of p53. REFERENCE 4 (residues 1 to 389) AUTHORS Jin,Y.H., Kim,Y.J., Kim,D.W., Baek,K.H., Kang,B.Y., Yeo,C.Y. and Lee,K.Y. TITLE Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53 JOURNAL Biochem. Biophys. Res. Commun. 368 (3), 690-695 (2008) PUBMED 18249187 REMARK GeneRIF: Therefore, our results suggest that the interaction between Sirt2 and 14-3-3 beta/gamma is a novel mechanism for the negative regulation of p53 beside the well-characterized Mdm2-mediated repression. REFERENCE 5 (residues 1 to 389) AUTHORS Pandithage,R., Lilischkis,R., Harting,K., Wolf,A., Jedamzik,B., Luscher-Firzlaff,J., Vervoorts,J., Lasonder,E., Kremmer,E., Knoll,B. and Luscher,B. TITLE The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility JOURNAL J. Cell Biol. 180 (5), 915-929 (2008) PUBMED 18332217 REMARK GeneRIF: Collectively, our findings identify a posttranslational mechanism that controls SIRT2 function, and they provide evidence for a novel regulatory circuitry involving Cdks, SIRT2, and microtubules. REFERENCE 6 (residues 1 to 389) AUTHORS Finnin,M.S., Donigian,J.R. and Pavletich,N.P. TITLE Structure of the histone deacetylase SIRT2 JOURNAL Nat. Struct. Biol. 8 (7), 621-625 (2001) PUBMED 11427894 REFERENCE 7 (residues 1 to 389) AUTHORS Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X., Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H., Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J., Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M., Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L. TITLE Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning JOURNAL Proc. Natl. Acad. Sci. U.S.A. 97 (17), 9543-9548 (2000) PUBMED 10931946 REFERENCE 8 (residues 1 to 389) AUTHORS Frye,R.A. TITLE Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins JOURNAL Biochem. Biophys. Res. Commun. 273 (2), 793-798 (2000) PUBMED 10873683 REFERENCE 9 (residues 1 to 389) AUTHORS Afshar,G. and Murnane,J.P. TITLE Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2 JOURNAL Gene 234 (1), 161-168 (1999) PUBMED 10393250 REFERENCE 10 (residues 1 to 389) AUTHORS Frye,R.A. TITLE 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 JOURNAL Biochem. Biophys. Res. Commun. 260 (1), 273-279 (1999) PUBMED 10381378 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AF083107.2. On Apr 24, 2001 this sequence version replaced gi:6912656.
Summary: This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Two transcript variants result from alternative splicing of this gene. [provided by RefSeq].
Transcript Variant: This variant (1) contains an additional 47 nt which introduces an earlier in-frame start codon, as compared to transcript variant 2. Isoform 1, encoded by this variant, contains an additional 37 aa in N-terminus.
Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. FEATURES Location/Qualifiers source 1..389 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="19" /map="19q13" Protein 1..389 /product="sirtuin 2 isoform 1" /EC_number="3.5.1.-" /note="silencing information regulator 2-like; sir2-related protein type 2; sirtuin type 2; silent information regulator 2" /calculated_mol_wt=43051 Region 77..337 /region_name="sirtuin core domain" Region 77..331 /region_name="SIRT1" /note="SIRT1: Eukaryotic group (class1) which includes human sirtuins SIRT1-3 and yeast Hst1-4; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2...; cd01408" /db_xref="CDD:29376" Site order(86,88..89,96..97,149,167..168,170,187,261,266, 287..288,323) /site_type="other" /note="NAD+ binding site" /db_xref="CDD:29376" Site order(169,187,233,235..239,265..267) /site_type="other" /note="substrate binding site" /db_xref="CDD:29376" Site order(195,200,221,224) /site_type="other" /note="Zn binding site" /db_xref="CDD:29376" CDS 1..389 /gene="SIRT2" /gene_synonym="SIR2; SIR2L; SIR2L2" /coded_by="NM_012237.2:201..1370" /note="isoform 1 is encoded by transcript variant 1" /db_xref="CCDS:CCDS12523.1" /db_xref="GeneID:22933" /db_xref="HGNC:10886" /db_xref="HPRD:10377" /db_xref="MIM:604480" ORIGIN 1 maepdpshpl etqagkvqea qdsdsdsegg aaggeadmdf lrnlfsqtls lgsqkerlld 61 eltlegvary mqsercrrvi clvgagists agipdfrsps tglydnleky hlpypeaife 121 isyfkkhpep ffalakelyp gqfkptichy fmrllkdkgl llrcytqnid tleriagleq 181 edlveahgtf ytshcvsasc rheyplswmk ekifsevtpk cedcqslvkp divffgeslp 241 arffscmqsd flkvdlllvm gtslqvqpfa sliskaplst prllinkeka gqsdpflgmi 301 mglgggmdfd skkayrdvaw lgecdqgcla laellgwkke ledlvrreha sidaqsgagv 361 pnpstsaspk kspppakdea rtterekpq //
Top
LOCUS NP_085096 352 aa linear PRI 03-SEP-2009 DEFINITION sirtuin 2 isoform 2 [Homo sapiens]. ACCESSION NP_085096 VERSION NP_085096.1 GI:13775602 DBSOURCE REFSEQ: accession NM_030593.1 KEYWORDS . SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 352) AUTHORS Inoue,T., Nakayama,Y., Yamada,H., Li,Y.C., Yamaguchi,S., Osaki,M., Kurimasa,A., Hiratsuka,M., Katoh,M. and Oshimura,M. TITLE SIRT2 downregulation confers resistance to microtubule inhibitors by prolonging chronic mitotic arrest JOURNAL Cell Cycle 8 (8), 1279-1291 (2009) PUBMED 19282667 REMARK GeneRIF: The effects of SIRT2 downregulation on sensitivity to microtubule inhibitors using HCT116 cells, was investigated. REFERENCE 2 (residues 1 to 352) AUTHORS Black,J.C., Mosley,A., Kitada,T., Washburn,M. and Carey,M. TITLE The SIRT2 deacetylase regulates autoacetylation of p300 JOURNAL Mol. Cell 32 (3), 449-455 (2008) PUBMED 18995842 REMARK GeneRIF: p300 undergoes a dynamic cycle of autoacetylation and deacetylation regulated by SIRT2. REFERENCE 3 (residues 1 to 352) AUTHORS Han,Y., Jin,Y.H., Kim,Y.J., Kang,B.Y., Choi,H.J., Kim,D.W., Yeo,C.Y. and Lee,K.Y. TITLE Acetylation of Sirt2 by p300 attenuates its deacetylase activity JOURNAL Biochem. Biophys. Res. Commun. 375 (4), 576-580 (2008) PUBMED 18722353 REMARK GeneRIF: These observations demonstrate that p300 can inactivate Sirt2 by acetylation and that p300 may regulate the activity of p53 indirectly through Sirt2 in addition to its direct modification of p53. REFERENCE 4 (residues 1 to 352) AUTHORS Jin,Y.H., Kim,Y.J., Kim,D.W., Baek,K.H., Kang,B.Y., Yeo,C.Y. and Lee,K.Y. TITLE Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53 JOURNAL Biochem. Biophys. Res. Commun. 368 (3), 690-695 (2008) PUBMED 18249187 REMARK GeneRIF: Therefore, our results suggest that the interaction between Sirt2 and 14-3-3 beta/gamma is a novel mechanism for the negative regulation of p53 beside the well-characterized Mdm2-mediated repression. REFERENCE 5 (residues 1 to 352) AUTHORS Pandithage,R., Lilischkis,R., Harting,K., Wolf,A., Jedamzik,B., Luscher-Firzlaff,J., Vervoorts,J., Lasonder,E., Kremmer,E., Knoll,B. and Luscher,B. TITLE The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility JOURNAL J. Cell Biol. 180 (5), 915-929 (2008) PUBMED 18332217 REMARK GeneRIF: Collectively, our findings identify a posttranslational mechanism that controls SIRT2 function, and they provide evidence for a novel regulatory circuitry involving Cdks, SIRT2, and microtubules. REFERENCE 6 (residues 1 to 352) AUTHORS Finnin,M.S., Donigian,J.R. and Pavletich,N.P. TITLE Structure of the histone deacetylase SIRT2 JOURNAL Nat. Struct. Biol. 8 (7), 621-625 (2001) PUBMED 11427894 REFERENCE 7 (residues 1 to 352) AUTHORS Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X., Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H., Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J., Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M., Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L. TITLE Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning JOURNAL Proc. Natl. Acad. Sci. U.S.A. 97 (17), 9543-9548 (2000) PUBMED 10931946 REFERENCE 8 (residues 1 to 352) AUTHORS Frye,R.A. TITLE Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins JOURNAL Biochem. Biophys. Res. Commun. 273 (2), 793-798 (2000) PUBMED 10873683 REFERENCE 9 (residues 1 to 352) AUTHORS Afshar,G. and Murnane,J.P. TITLE Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2 JOURNAL Gene 234 (1), 161-168 (1999) PUBMED 10393250 REFERENCE 10 (residues 1 to 352) AUTHORS Frye,R.A. TITLE 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 JOURNAL Biochem. Biophys. Res. Commun. 260 (1), 273-279 (1999) PUBMED 10381378 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from BC003012.1.
Summary: This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Two transcript variants result from alternative splicing of this gene. [provided by RefSeq].
Transcript Variant: This variant (2) lacks the additional 47 nt present in the 5' end of the coding region in transcript variant 1. Translation is thought to initiate at a downstream in-frame ATG.
Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. FEATURES Location/Qualifiers source 1..352 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="19" /map="19q13" Protein 1..352 /product="sirtuin 2 isoform 2" /EC_number="3.5.1.-" /note="silencing information regulator 2-like; sir2-related protein type 2; sirtuin type 2; silent information regulator 2" /calculated_mol_wt=39384 Region 40..300 /region_name="sirtuin core domain" Region 40..294 /region_name="SIRT1" /note="SIRT1: Eukaryotic group (class1) which includes human sirtuins SIRT1-3 and yeast Hst1-4; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2...; cd01408" /db_xref="CDD:29376" Site order(49,51..52,59..60,112,130..131,133,150,224,229, 250..251,286) /site_type="other" /note="NAD+ binding site" /db_xref="CDD:29376" Site order(132,150,196,198..202,228..230) /site_type="other" /note="substrate binding site" /db_xref="CDD:29376" Site order(158,163,184,187) /site_type="other" /note="Zn binding site" /db_xref="CDD:29376" CDS 1..352 /gene="SIRT2" /gene_synonym="SIR2; SIR2L; SIR2L2" /coded_by="NM_030593.1:257..1315" /note="isoform 2 is encoded by transcript variant 2" /db_xref="CCDS:CCDS46069.1" /db_xref="GeneID:22933" /db_xref="HGNC:10886" /db_xref="HPRD:10377" /db_xref="MIM:604480" ORIGIN 1 mdflrnlfsq tlslgsqker lldeltlegv arymqsercr rviclvgagi stsagipdfr 61 spstglydnl ekyhlpypea ifeisyfkkh pepffalake lypgqfkpti chyfmrllkd 121 kglllrcytq nidtleriag leqedlveah gtfytshcvs ascrheypls wmkekifsev 181 tpkcedcqsl vkpdivffge slparffscm qsdflkvdll lvmgtslqvq pfasliskap 241 lstprllink ekagqsdpfl gmimglgggm dfdskkayrd vawlgecdqg clalaellgw 301 kkeledlvrr ehasidaqsg agvpnpstsa spkkspppak deartterek pq //
Top
LOCUS NP_036371 399 aa linear PRI 20-SEP-2009 DEFINITION sirtuin 3 isoform a [Homo sapiens]. ACCESSION NP_036371 VERSION NP_036371.1 GI:6912660 DBSOURCE REFSEQ: accession NM_012239.5 KEYWORDS . SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 399) AUTHORS Jin,L., Wei,W., Jiang,Y., Peng,H., Cai,J., Mao,C., Dai,H., Choy,W., Bemis,J.E., Jirousek,M.R., Milne,J.C., Westphal,C.H. and Perni,R.B. TITLE Crystal structures of human SIRT3 displaying substrate-induced conformational changes JOURNAL J. Biol. Chem. 284 (36), 24394-24405 (2009) PUBMED 19535340 REFERENCE 2 (residues 1 to 399) AUTHORS Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A., Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S., Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M., Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A. and Wijmenga,C. TITLE Coeliac disease-associated risk variants in TNFAIP3 and REL implicate altered NF-kappaB signalling JOURNAL Gut 58 (8), 1078-1083 (2009) PUBMED 19240061 REMARK GeneRIF: Observational study of gene-disease association. (HuGE Navigator) REFERENCE 3 (residues 1 to 399) AUTHORS Law,I.K., Liu,L., Xu,A., Lam,K.S., Vanhoutte,P.M., Che,C.M., Leung,P.T. and Wang,Y. TITLE Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins JOURNAL Proteomics 9 (9), 2444-2456 (2009) PUBMED 19343720 REMARK GeneRIF: results show SIRT1 & SIRT3 are localized in different intracellular compartments, mainly nuclei & mitochondria; identified novel SIRT protein interacting partners which may be critically involved in anti-aging & metabolic regulatory activities of sirtuins REFERENCE 4 (residues 1 to 399) AUTHORS Lescai,F., Blanche,H., Nebel,A., Beekman,M., Sahbatou,M., Flachsbart,F., Slagboom,E., Schreiber,S., Sorbi,S., Passarino,G. and Franceschi,C. TITLE Human longevity and 11p15.5: a study in 1321 centenarians JOURNAL Eur. J. Hum. Genet. (2009) In press PUBMED 19367319 REMARK GeneRIF: Observational study and meta-analysis of gene-disease association. (HuGE Navigator) Publication Status: Available-Online prior to print REFERENCE 5 (residues 1 to 399) AUTHORS Halaschek-Wiener,J., Amirabbasi-Beik,M., Monfared,N., Pieczyk,M., Sailer,C., Kollar,A., Thomas,R., Agalaridis,G., Yamada,S., Oliveira,L., Collins,J.A., Meneilly,G., Marra,M.A., Madden,K.M., Le,N.D., Connors,J.M. and Brooks-Wilson,A.R. TITLE Genetic variation in healthy oldest-old JOURNAL PLoS ONE 4 (8), E6641 (2009) PUBMED 19680556 REMARK GeneRIF: Observational study of gene-disease association. (HuGE Navigator) Publication Status: Online-Only REFERENCE 6 (residues 1 to 399) AUTHORS Onyango,P., Celic,I., McCaffery,J.M., Boeke,J.D. and Feinberg,A.P. TITLE SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria JOURNAL Proc. Natl. Acad. Sci. U.S.A. 99 (21), 13653-13658 (2002) PUBMED 12374852 REMARK GeneRIF: the role of SIRT3 in mitochondria involves protein deacetylation REFERENCE 7 (residues 1 to 399) AUTHORS Schwer,B., North,B.J., Frye,R.A., Ott,M. and Verdin,E. TITLE The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase JOURNAL J. Cell Biol. 158 (4), 647-657 (2002) PUBMED 12186850 REMARK GeneRIF: hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. hSIRT3 is proteolytically processed in the mitochondrial matrix to a 28-kD product. REFERENCE 8 (residues 1 to 399) AUTHORS Yang,Y.H., Chen,Y.H., Zhang,C.Y., Nimmakayalu,M.A., Ward,D.C. and Weissman,S. TITLE Cloning and characterization of two mouse genes with homology to the yeast Sir2 gene JOURNAL Genomics 69 (3), 355-369 (2000) PUBMED 11056054 REFERENCE 9 (residues 1 to 399) AUTHORS Frye,R.A. TITLE Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins JOURNAL Biochem. Biophys. Res. Commun. 273 (2), 793-798 (2000) PUBMED 10873683 REFERENCE 10 (residues 1 to 399) AUTHORS Frye,R.A. TITLE 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 JOURNAL Biochem. Biophys. Res. Commun. 260 (1), 273-279 (1999) PUBMED 10381378 COMMENT VALIDATED REFSEQ: This record has undergone validation or preliminary review. The reference sequence was derived from AF083108.2, AL535769.3, BC001042.2, DR762907.1, AI091200.1, AC069287.7 and BM973763.1.
Summary: This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Two alternatively spliced transcript variants that encode different proteins have been described for this gene. [provided by RefSeq].
Transcript Variant: This variant (1) represents the longer transcript and it encodes the longer protein (isoform a).
Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. FEATURES Location/Qualifiers source 1..399 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="11" /map="11p15.5" Protein 1..399 /product="sirtuin 3 isoform a" /note="sir2-like 3; silent mating type information regulation 2, S.cerevisiae, homolog 3; mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase; sirtuin type 3" /calculated_mol_wt=43442 Region 138..373 /region_name="SIRT1" /note="SIRT1: Eukaryotic group (class1) which includes human sirtuins SIRT1-3 and yeast Hst1-4; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2...; cd01408" /db_xref="CDD:29376" Site order(147,149..150,157..158,210,228..229,231,248,319,324, 345..346,365) /site_type="other" /note="NAD+ binding site" /db_xref="CDD:29376" Site order(230,248,292,294..298,323..325) /site_type="other" /note="substrate binding site" /db_xref="CDD:29376" Site order(256,259,280,283) /site_type="other" /note="Zn binding site" /db_xref="CDD:29376" CDS 1..399 /gene="SIRT3" /gene_synonym="SIR2L3" /coded_by="NM_012239.5:35..1234" /note="isoform a is encoded by transcript variant 1" /db_xref="CCDS:CCDS7691.1" /db_xref="GeneID:23410" /db_xref="HGNC:14931" /db_xref="HPRD:06836" /db_xref="MIM:604481" ORIGIN 1 mafwgwraaa alrlwgrvve rveagggvgp fqacgcrlvl ggrddvsagl rgshgargep 61 ldparplqrp prpevprafr rqpraaapsf ffssikggrr sisfsvgass vvgsggssdk 121 gklslqdvae liraracqrv vvmvgagist psgipdfrsp gsglysnlqq ydlpypeaif 181 elpfffhnpk pfftlakely pgnykpnvth yflrllhdkg lllrlytqni dglervsgip 241 asklveahgt fasatctvcq rpfpgedira dvmadrvprc pvctgvvkpd ivffgeplpq 301 rfllhvvdfp madlllilgt slevepfasl teavrssvpr llinrdlvgp lawhprsrdv 361 aqlgdvvhgv eslvellgwt eemrdlvqre tgkldgpdk //
Top
LOCUS NP_001017524 257 aa linear PRI 20-SEP-2009 DEFINITION sirtuin 3 isoform b [Homo sapiens]. ACCESSION NP_001017524 VERSION NP_001017524.1 GI:63054862 DBSOURCE REFSEQ: accession NM_001017524.2 KEYWORDS . SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 257) AUTHORS Jin,L., Wei,W., Jiang,Y., Peng,H., Cai,J., Mao,C., Dai,H., Choy,W., Bemis,J.E., Jirousek,M.R., Milne,J.C., Westphal,C.H. and Perni,R.B. TITLE Crystal structures of human SIRT3 displaying substrate-induced conformational changes JOURNAL J. Biol. Chem. 284 (36), 24394-24405 (2009) PUBMED 19535340 REFERENCE 2 (residues 1 to 257) AUTHORS Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A., Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S., Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M., Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A. and Wijmenga,C. TITLE Coeliac disease-associated risk variants in TNFAIP3 and REL implicate altered NF-kappaB signalling JOURNAL Gut 58 (8), 1078-1083 (2009) PUBMED 19240061 REMARK GeneRIF: Observational study of gene-disease association. (HuGE Navigator) REFERENCE 3 (residues 1 to 257) AUTHORS Law,I.K., Liu,L., Xu,A., Lam,K.S., Vanhoutte,P.M., Che,C.M., Leung,P.T. and Wang,Y. TITLE Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins JOURNAL Proteomics 9 (9), 2444-2456 (2009) PUBMED 19343720 REMARK GeneRIF: results show SIRT1 & SIRT3 are localized in different intracellular compartments, mainly nuclei & mitochondria; identified novel SIRT protein interacting partners which may be critically involved in anti-aging & metabolic regulatory activities of sirtuins REFERENCE 4 (residues 1 to 257) AUTHORS Lescai,F., Blanche,H., Nebel,A., Beekman,M., Sahbatou,M., Flachsbart,F., Slagboom,E., Schreiber,S., Sorbi,S., Passarino,G. and Franceschi,C. TITLE Human longevity and 11p15.5: a study in 1321 centenarians JOURNAL Eur. J. Hum. Genet. (2009) In press PUBMED 19367319 REMARK GeneRIF: Observational study and meta-analysis of gene-disease association. (HuGE Navigator) Publication Status: Available-Online prior to print REFERENCE 5 (residues 1 to 257) AUTHORS Halaschek-Wiener,J., Amirabbasi-Beik,M., Monfared,N., Pieczyk,M., Sailer,C., Kollar,A., Thomas,R., Agalaridis,G., Yamada,S., Oliveira,L., Collins,J.A., Meneilly,G., Marra,M.A., Madden,K.M., Le,N.D., Connors,J.M. and Brooks-Wilson,A.R. TITLE Genetic variation in healthy oldest-old JOURNAL PLoS ONE 4 (8), E6641 (2009) PUBMED 19680556 REMARK GeneRIF: Observational study of gene-disease association. (HuGE Navigator) Publication Status: Online-Only REFERENCE 6 (residues 1 to 257) AUTHORS Onyango,P., Celic,I., McCaffery,J.M., Boeke,J.D. and Feinberg,A.P. TITLE SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria JOURNAL Proc. Natl. Acad. Sci. U.S.A. 99 (21), 13653-13658 (2002) PUBMED 12374852 REMARK GeneRIF: the role of SIRT3 in mitochondria involves protein deacetylation REFERENCE 7 (residues 1 to 257) AUTHORS Schwer,B., North,B.J., Frye,R.A., Ott,M. and Verdin,E. TITLE The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase JOURNAL J. Cell Biol. 158 (4), 647-657 (2002) PUBMED 12186850 REMARK GeneRIF: hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. hSIRT3 is proteolytically processed in the mitochondrial matrix to a 28-kD product. REFERENCE 8 (residues 1 to 257) AUTHORS Yang,Y.H., Chen,Y.H., Zhang,C.Y., Nimmakayalu,M.A., Ward,D.C. and Weissman,S. TITLE Cloning and characterization of two mouse genes with homology to the yeast Sir2 gene JOURNAL Genomics 69 (3), 355-369 (2000) PUBMED 11056054 REFERENCE 9 (residues 1 to 257) AUTHORS Frye,R.A. TITLE Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins JOURNAL Biochem. Biophys. Res. Commun. 273 (2), 793-798 (2000) PUBMED 10873683 REFERENCE 10 (residues 1 to 257) AUTHORS Frye,R.A. TITLE 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 JOURNAL Biochem. Biophys. Res. Commun. 260 (1), 273-279 (1999) PUBMED 10381378 COMMENT VALIDATED REFSEQ: This record has undergone validation or preliminary review. The reference sequence was derived from AF083108.2, AL535769.3, BI755839.1, BC001042.2, DR762907.1, AI091200.1, AC069287.7 and BM973763.1.
Summary: This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Two alternatively spliced transcript variants that encode different proteins have been described for this gene. [provided by RefSeq].
Transcript Variant: This variant (2) uses an alternate splice site in the 5' end which causes the use of a downstream start codon, compared to variant 1. The resulting protein (isoform b) is shorter at the N-terminus compared to isoform a.
Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. FEATURES Location/Qualifiers source 1..257 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="11" /map="11p15.5" Protein 1..257 /product="sirtuin 3 isoform b" /note="sir2-like 3; silent mating type information regulation 2, S.cerevisiae, homolog 3; mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase; sirtuin type 3" /calculated_mol_wt=28436 Region 1..231 /region_name="SIRT1" /note="SIRT1: Eukaryotic group (class1) which includes human sirtuins SIRT1-3 and yeast Hst1-4; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2...; cd01408" /db_xref="CDD:29376" Site order(5,7..8,15..16,68,86..87,89,106,177,182,203..204,223) /site_type="other" /note="NAD+ binding site" /db_xref="CDD:29376" Site order(88,106,150,152..156,181..183) /site_type="other" /note="substrate binding site" /db_xref="CDD:29376" Site order(114,117,138,141) /site_type="other" /note="Zn binding site" /db_xref="CDD:29376" CDS 1..257 /gene="SIRT3" /gene_synonym="SIR2L3" /coded_by="NM_001017524.2:315..1088" /note="isoform b is encoded by transcript variant 2" /db_xref="GeneID:23410" /db_xref="HGNC:14931" /db_xref="MIM:604481" ORIGIN 1 mvgagistps gipdfrspgs glysnlqqyd lpypeaifel pfffhnpkpf ftlakelypg 61 nykpnvthyf lrllhdkgll lrlytqnidg lervsgipas klveahgtfa satctvcqrp 121 fpgediradv madrvprcpv ctgvvkpdiv ffgeplpqrf llhvvdfpma dlllilgtsl 181 evepfaslte avrssvprll inrdlvgpla whprsrdvaq lgdvvhgves lvellgwtee 241 mrdlvqretg kldgpdk //
Top
LOCUS NP_036372 314 aa linear PRI 29-MAR-2009 DEFINITION sirtuin 4 [Homo sapiens]. ACCESSION NP_036372 VERSION NP_036372.1 GI:6912662 DBSOURCE REFSEQ: accession NM_012240.1 KEYWORDS . SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 314) AUTHORS Reiling,E., van Vliet-Ostaptchouk,J.V., van 't Riet,E., van Haeften,T.W., Arp,P.A., Hansen,T., Kremer,D., Groenewoud,M.J., van Hove,E.C., Romijn,J.A., Smit,J.W., Nijpels,G., Heine,R.J., Uitterlinden,A.G., Pedersen,O., Slagboom,P.E., Maassen,J.A., Hofker,M.H., 't Hart,L.M. and Dekker,J.M. TITLE Genetic association analysis of 13 nuclear-encoded mitochondrial candidate genes with type II diabetes mellitus: the DAMAGE study JOURNAL Eur. J. Hum. Genet. (2009) In press PUBMED 19209188 REMARK GeneRIF: Meta-analysis of gene-disease association. (HuGE Navigator) Publication Status: Available-Online prior to print REFERENCE 2 (residues 1 to 314) AUTHORS Ahuja,N., Schwer,B., Carobbio,S., Waltregny,D., North,B.J., Castronovo,V., Maechler,P. and Verdin,E. TITLE Regulation of insulin secretion by SIRT4, a mitochondrial ADP-ribosyltransferase JOURNAL J. Biol. Chem. 282 (46), 33583-33592 (2007) PUBMED 17715127 REMARK GeneRIF: mitochondrial SIRT4 has a role in the regulation of insulin secretion REFERENCE 3 (residues 1 to 314) AUTHORS 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. and Guarente,L. TITLE SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells JOURNAL Cell 126 (5), 941-954 (2006) PUBMED 16959573 REFERENCE 4 (residues 1 to 314) AUTHORS 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., 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. and Gibbs,R.A. CONSRTM Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team TITLE The finished DNA sequence of human chromosome 12 JOURNAL Nature 440 (7082), 346-351 (2006) PUBMED 16541075 REFERENCE 5 (residues 1 to 314) AUTHORS Irobi,J., Van Impe,K., Seeman,P., Jordanova,A., Dierick,I., Verpoorten,N., Michalik,A., De Vriendt,E., Jacobs,A., Van Gerwen,V., Vennekens,K., Mazanec,R., Tournev,I., Hilton-Jones,D., Talbot,K., Kremensky,I., Van Den Bosch,L., Robberecht,W., Van Vandekerckhove,J., Van Broeckhoven,C., Gettemans,J., De Jonghe,P. and Timmerman,V. TITLE Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy JOURNAL Nat. Genet. 36 (6), 597-601 (2004) PUBMED 15122253 REFERENCE 6 (residues 1 to 314) AUTHORS Frye,R.A. TITLE Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins JOURNAL Biochem. Biophys. Res. Commun. 273 (2), 793-798 (2000) PUBMED 10873683 REFERENCE 7 (residues 1 to 314) AUTHORS Frye,R.A. TITLE 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 JOURNAL Biochem. Biophys. Res. Commun. 260 (1), 273-279 (1999) PUBMED 10381378 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AF083109.1.
Summary: This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class IV of the sirtuin family. [provided by RefSeq]. FEATURES Location/Qualifiers source 1..314 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="12" /map="12q" Protein 1..314 /product="sirtuin 4" /note="sir2-like 4; sirtuin type 4" /calculated_mol_wt=35057 Region 47..308 /region_name="SIRT4" /note="SIRT4: Eukaryotic and prokaryotic group (class2) which includes human sirtuin SIRT4 and several bacterial homologs; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein...; cd01409" /db_xref="CDD:29377" Region 55..314 /region_name="sirtuin core domain" Site order(64,66..67,74..75,125,143..144,146,161,260,265, 287..288,307) /site_type="other" /note="NAD+ binding site" /db_xref="CDD:29377" Site order(145,161,232,234..238,264..266) /site_type="other" /note="substrate binding site" /db_xref="CDD:29377" Site order(169,172,220,223) /site_type="other" /note="Zn binding site" /db_xref="CDD:29377" CDS 1..314 /gene="SIRT4" /gene_synonym="MGC130046; MGC130047; MGC57437; SIR2L4" /coded_by="NM_012240.1:21..965" /db_xref="CCDS:CCDS9194.1" /db_xref="GeneID:23409" /db_xref="HGNC:14932" /db_xref="HPRD:06837" /db_xref="MIM:604482" ORIGIN 1 mkmsfaltfr sakgrwianp sqpcskasig lfvpasppld pekvkelqrf itlskrllvm 61 tgagistesg ipdyrsekvg lyartdrrpi qhgdfvrsap irqrywarnf vgwpqfsshq 121 pnpahwalst weklgklywl vtqnvdalht kagsrrltel hgcmdrvlcl dcgeqtprgv 181 lqerfqvlnp twsaeahgla pdgdvflsee qvrsfqvptc vqcgghlkpd vvffgdtvnp 241 dkvdfvhkrv keadsllvvg sslqvysgyr filtawekkl piailnigpt rsddlaclkl 301 nsrcgellpl idpc //
Top
LOCUS NP_036373 310 aa linear PRI 02-AUG-2009 DEFINITION sirtuin 5 isoform 1 [Homo sapiens]. ACCESSION NP_036373 VERSION NP_036373.1 GI:6912664 DBSOURCE REFSEQ: accession NM_012241.3 KEYWORDS . SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 310) AUTHORS Schlicker,C., Gertz,M., Papatheodorou,P., Kachholz,B., Becker,C.F. and Steegborn,C. TITLE Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5 JOURNAL J. Mol. Biol. 382 (3), 790-801 (2008) PUBMED 18680753 REMARK GeneRIF: Results describe the substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. REFERENCE 2 (residues 1 to 310) AUTHORS Chowdari,K.V., Northup,A., Pless,L., Wood,J., Joo,Y.H., Mirnics,K., Lewis,D.A., Levitt,P.R., Bacanu,S.A. and Nimgaonkar,V.L. TITLE DNA pooling: a comprehensive, multi-stage association analysis of ACSL6 and SIRT5 polymorphisms in schizophrenia JOURNAL Genes Brain Behav. 6 (3), 229-239 (2007) PUBMED 16827919 REMARK GeneRIF: Analyses did not yield convincing evidence for associations of schizophrenia with SIRT5. GeneRIF: Observational study of gene-disease association and genetic testing. (HuGE Navigator) REFERENCE 3 (residues 1 to 310) AUTHORS Mahlknecht,U., Ho,A.D., Letzel,S. and Voelter-Mahlknecht,S. TITLE Assignment of the NAD-dependent deacetylase sirtuin 5 gene (SIRT5) to human chromosome band 6p23 by in situ hybridization JOURNAL Cytogenet. Genome Res. 112 (3-4), 208-212 (2006) PUBMED 16484774 REMARK GeneRIF: SIRT5 consists of eight exons and is found in two isoforms, which encode a 310 aa and a 299 aa protein, respectively. REFERENCE 4 (residues 1 to 310) AUTHORS Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L., Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E., Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J., Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O., Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J., Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M., Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K., Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J., Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L., Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P., Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J., Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M., Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L., Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R., Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M., King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J., Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L., McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J., Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K., Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I., Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y., Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K., Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L., Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J., Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S., Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E., Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M., Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Dunham,I., Rogers,J. and Beck,S. TITLE The DNA sequence and analysis of human chromosome 6 JOURNAL Nature 425 (6960), 805-811 (2003) PUBMED 14574404 REFERENCE 5 (residues 1 to 310) AUTHORS Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and Wiemann,S. TITLE Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing JOURNAL EMBO Rep. 1 (3), 287-292 (2000) PUBMED 11256614 REFERENCE 6 (residues 1 to 310) AUTHORS Frye,R.A. TITLE Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins JOURNAL Biochem. Biophys. Res. Commun. 273 (2), 793-798 (2000) PUBMED 10873683 REFERENCE 7 (residues 1 to 310) AUTHORS Frye,R.A. TITLE 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 JOURNAL Biochem. Biophys. Res. Commun. 260 (1), 273-279 (1999) PUBMED 10381378 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from BC000126.1, AF083110.1, DR003695.1, AK094269.1 and AI969140.1.
Summary: This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class III of the sirtuin family. Alternative splicing of this gene results in two transcript variants. [provided by RefSeq].
Transcript Variant: This variant (1) contains a distinct 5' UTR, C-terminal coding region, and 3' UTR as compared to transcript variant 2. This variant encodes isoform 1 which has a longer distinct C-terminus than isoform 2. FEATURES Location/Qualifiers source 1..310 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="6" /map="6p23" Protein 1..310 /product="sirtuin 5 isoform 1" /note="sir2-like 5; silent mating type information regulation 2, S.cerevisiae, homolog 5; sirtuin type 5" /calculated_mol_wt=33750 Region 51..301 /region_name="SIRT5_Af1_CobB" /note="SIRT5_Af1_CobB: Eukaryotic, archaeal and prokaryotic group (class3) which includes human sirtuin SIRT5, Archaeoglobus fulgidus Sir2-Af1, and E. coli CobB; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes...; cd01412" /db_xref="CDD:29380" Site order(60,62..63,70..71,118,140..141,143,158,249,254, 276..277,292) /site_type="other" /note="NAD+ binding site" /db_xref="CDD:29380" Site order(142,158,221,223..227,253..255) /site_type="other" /note="substrate binding site" /db_xref="CDD:29380" Site order(166,169,207,212) /site_type="other" /note="Zn binding site" /db_xref="CDD:29380" CDS 1..310 /gene="SIRT5" /gene_synonym="FLJ36950; SIR2L5" /coded_by="NM_012241.3:297..1229" /note="isoform 1 is encoded by transcript variant 1" /db_xref="CCDS:CCDS4526.1" /db_xref="GeneID:23408" /db_xref="HGNC:14933" /db_xref="HPRD:06838" /db_xref="MIM:604483" ORIGIN 1 mrplqivpsr lisqlycglk ppastrnqic lkmarpsssm adfrkffaka khiviisgag 61 vsaesgvptf rgaggywrkw qaqdlatpla fahnpsrvwe fyhyrrevmg skepnaghra 121 iaecetrlgk qgrrvvvitq nidelhrkag tknlleihgs lfktrctscg vvaenykspi 181 cpalsgkgap epgtqdasip veklprceea gcggllrphv vwfgenldpa ileevdrela 241 hcdlclvvgt ssvvypaamf apqvaargvp vaefntettp atnrfrfhfq gpcgttlpea 301 lachenetvs //
Top
LOCUS NP_112534 299 aa linear PRI 02-AUG-2009 DEFINITION sirtuin 5 isoform 2 [Homo sapiens]. ACCESSION NP_112534 VERSION NP_112534.1 GI:13787215 DBSOURCE REFSEQ: accession NM_031244.2 KEYWORDS . SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 299) AUTHORS Schlicker,C., Gertz,M., Papatheodorou,P., Kachholz,B., Becker,C.F. and Steegborn,C. TITLE Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5 JOURNAL J. Mol. Biol. 382 (3), 790-801 (2008) PUBMED 18680753 REMARK GeneRIF: Results describe the substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. REFERENCE 2 (residues 1 to 299) AUTHORS Chowdari,K.V., Northup,A., Pless,L., Wood,J., Joo,Y.H., Mirnics,K., Lewis,D.A., Levitt,P.R., Bacanu,S.A. and Nimgaonkar,V.L. TITLE DNA pooling: a comprehensive, multi-stage association analysis of ACSL6 and SIRT5 polymorphisms in schizophrenia JOURNAL Genes Brain Behav. 6 (3), 229-239 (2007) PUBMED 16827919 REMARK GeneRIF: Analyses did not yield convincing evidence for associations of schizophrenia with SIRT5. GeneRIF: Observational study of gene-disease association and genetic testing. (HuGE Navigator) REFERENCE 3 (residues 1 to 299) AUTHORS Mahlknecht,U., Ho,A.D., Letzel,S. and Voelter-Mahlknecht,S. TITLE Assignment of the NAD-dependent deacetylase sirtuin 5 gene (SIRT5) to human chromosome band 6p23 by in situ hybridization JOURNAL Cytogenet. Genome Res. 112 (3-4), 208-212 (2006) PUBMED 16484774 REMARK GeneRIF: SIRT5 consists of eight exons and is found in two isoforms, which encode a 310 aa and a 299 aa protein, respectively. REFERENCE 4 (residues 1 to 299) AUTHORS Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L., Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E., Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J., Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O., Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J., Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M., Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K., Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J., Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L., Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P., Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J., Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M., Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L., Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R., Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M., King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J., Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L., McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J., Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K., Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I., Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y., Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K., Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L., Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J., Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S., Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E., Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M., Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Dunham,I., Rogers,J. and Beck,S. TITLE The DNA sequence and analysis of human chromosome 6 JOURNAL Nature 425 (6960), 805-811 (2003) PUBMED 14574404 REFERENCE 5 (residues 1 to 299) AUTHORS Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and Wiemann,S. TITLE Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing JOURNAL EMBO Rep. 1 (3), 287-292 (2000) PUBMED 11256614 REFERENCE 6 (residues 1 to 299) AUTHORS Frye,R.A. TITLE Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins JOURNAL Biochem. Biophys. Res. Commun. 273 (2), 793-798 (2000) PUBMED 10873683 REFERENCE 7 (residues 1 to 299) AUTHORS Frye,R.A. TITLE 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 JOURNAL Biochem. Biophys. Res. Commun. 260 (1), 273-279 (1999) PUBMED 10381378 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from CA406695.1, AK000355.1 and AJ420496.1.
Summary: This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class III of the sirtuin family. Alternative splicing of this gene results in two transcript variants. [provided by RefSeq].
Transcript Variant: This variant (2) contains a distinct 5' UTR, C-terminal coding region, and 3' UTR as compared to transcript variant 1. This variant encodes isoform 2 which has a distinct and shorter C-terminus than isoform 1. FEATURES Location/Qualifiers source 1..299 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="6" /map="6p23" Protein 1..299 /product="sirtuin 5 isoform 2" /note="sir2-like 5; silent mating type information regulation 2, S.cerevisiae, homolog 5; sirtuin type 5" /calculated_mol_wt=32543 Region 51..287 /region_name="SIRT5_Af1_CobB" /note="SIRT5_Af1_CobB: Eukaryotic, archaeal and prokaryotic group (class3) which includes human sirtuin SIRT5, Archaeoglobus fulgidus Sir2-Af1, and E. coli CobB; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes...; cd01412" /db_xref="CDD:29380" Site order(60,62..63,70..71,118,140..141,143,158,249,254, 276..277) /site_type="other" /note="NAD+ binding site" /db_xref="CDD:29380" Site order(142,158,221,223..227,253..255) /site_type="other" /note="substrate binding site" /db_xref="CDD:29380" Site order(166,169,207,212) /site_type="other" /note="Zn binding site" /db_xref="CDD:29380" CDS 1..299 /gene="SIRT5" /gene_synonym="FLJ36950; SIR2L5" /coded_by="NM_031244.2:260..1159" /note="isoform 2 is encoded by transcript variant 2" /db_xref="CCDS:CCDS4527.1" /db_xref="GeneID:23408" /db_xref="HGNC:14933" /db_xref="MIM:604483" ORIGIN 1 mrplqivpsr lisqlycglk ppastrnqic lkmarpsssm adfrkffaka khiviisgag 61 vsaesgvptf rgaggywrkw qaqdlatpla fahnpsrvwe fyhyrrevmg skepnaghra 121 iaecetrlgk qgrrvvvitq nidelhrkag tknlleihgs lfktrctscg vvaenykspi 181 cpalsgkgap epgtqdasip veklprceea gcggllrphv vwfgenldpa ileevdrela 241 hcdlclvvgt ssvvypaamf apqvaargvp vaefntettp atnrfshlis issliiikn //
Top
LOCUS NP_057623 355 aa linear PRI 07-JUN-2009 DEFINITION sirtuin 6 [Homo sapiens]. ACCESSION NP_057623 VERSION NP_057623.1 GI:7706710 DBSOURCE REFSEQ: accession NM_016539.1 KEYWORDS . SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 355) AUTHORS Kawahara,T.L., Michishita,E., Adler,A.S., Damian,M., Berber,E., Lin,M., McCord,R.A., Ongaigui,K.C., Boxer,L.D., Chang,H.Y. and Chua,K.F. TITLE SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span JOURNAL Cell 136 (1), 62-74 (2009) PUBMED 19135889 REFERENCE 2 (residues 1 to 355) AUTHORS Lall,S. TITLE No SIRT6 JOURNAL Nat. Struct. Mol. Biol. 15 (4), 336 (2008) PUBMED 18388907 REMARK GeneRIF: suggests similarities in the molecular mechanisms by which SIRT6 and WRN may prevent premature aging-like phenotypes REFERENCE 3 (residues 1 to 355) AUTHORS Michishita,E., McCord,R.A., Berber,E., Kioi,M., Padilla-Nash,H., Damian,M., Cheung,P., Kusumoto,R., Kawahara,T.L., Barrett,J.C., Chang,H.Y., Bohr,V.A., Ried,T., Gozani,O. and Chua,K.F. TITLE SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin JOURNAL Nature 452 (7186), 492-496 (2008) PUBMED 18337721 REMARK GeneRIF: the first identification of a physiological enzymatic activity of SIRT6 (as histone H3 lysine 9 deacetylase), and linking chromatin regulation by SIRT6 to telomere maintenance and a human premature ageing syndrome REFERENCE 4 (residues 1 to 355) AUTHORS Kanfi,Y., Shalman,R., Peshti,V., Pilosof,S.N., Gozlan,Y.M., Pearson,K.J., Lerrer,B., Moazed,D., Marine,J.C., de Cabo,R. and Cohen,H.Y. TITLE Regulation of SIRT6 protein levels by nutrient availability JOURNAL FEBS Lett. 582 (5), 543-548 (2008) PUBMED 18242175 REMARK GeneRIF: Levels of the mammalian sirtuin, SIRT6, increased upon nutrient deprivation in cultured cells, in mice after fasting, and in rats fed a calorie-restricted diet. REFERENCE 5 (residues 1 to 355) AUTHORS Yamamoto,H., Schoonjans,K. and Auwerx,J. TITLE Sirtuin functions in health and disease JOURNAL Mol. Endocrinol. 21 (8), 1745-1755 (2007) PUBMED 17456799 REMARK Review article REFERENCE 6 (residues 1 to 355) AUTHORS Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H., Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S., Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S., Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B., Birchmeier,W., Lehrach,H. and Wanker,E.E. TITLE A human protein-protein interaction network: a resource for annotating the proteome JOURNAL Cell 122 (6), 957-968 (2005) PUBMED 16169070 REFERENCE 7 (residues 1 to 355) AUTHORS Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J., Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O., Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E., Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C., Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E., Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D., Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M., Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I., Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S., Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K., Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P., Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T., Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I., Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E., Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S., Myers,R.M., Rubin,E.M. and Lucas,S.M. TITLE The DNA sequence and biology of human chromosome 19 JOURNAL Nature 428 (6982), 529-535 (2004) PUBMED 15057824 REFERENCE 8 (residues 1 to 355) AUTHORS Frye,R.A. TITLE Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins JOURNAL Biochem. Biophys. Res. Commun. 273 (2), 793-798 (2000) PUBMED 10873683 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AF233396.1.
Summary: This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class IV of the sirtuin family. [provided by RefSeq]. FEATURES Location/Qualifiers source 1..355 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="19" /map="19p13.3" Protein 1..355 /product="sirtuin 6" /EC_number="2.4.2.31" /note="sir2-related protein type 6; sirtuin type 6" /calculated_mol_wt=38989 Region 45..257 /region_name="SIRT7" /note="SIRT7: Eukaryotic and prokaryotic group (class4) which includes human sirtuin SIRT6, SIRT7, and several bacterial homologs; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent...; cd01410" /db_xref="CDD:29378" Site order(54,56..57,64..65,95,113..114,116,133,214,219, 241..242,257) /site_type="other" /note="NAD+ binding site" /db_xref="CDD:29378" Site order(115,133,186,188..192,218..220) /site_type="other" /note="substrate binding site" /db_xref="CDD:29378" Site order(141,144,166,177) /site_type="other" /note="Zn binding site" /db_xref="CDD:29378" CDS 1..355 /gene="SIRT6" /gene_synonym="SIR2L6" /coded_by="NM_016539.1:61..1128" /db_xref="CCDS:CCDS12122.1" /db_xref="GeneID:51548" /db_xref="HGNC:14934" /db_xref="HPRD:12093" /db_xref="MIM:606211" ORIGIN 1 msvnyaagls pyadkgkcgl peifdppeel erkvwelarl vwqsssvvfh tgagistasg 61 ipdfrgphgv wtmeerglap kfdttfesar ptqthmalvq lervgllrfl vsqnvdglhv 121 rsgfprdkla elhgnmfvee cakcktqyvr dtvvgtmglk atgrlctvak arglracrge 181 lrdtildwed slpdrdlala deasrnadls itlgtslqir psgnlplatk rrggrlvivn 241 lqptkhdrha dlrihgyvde vmtrlmehlg leipawdgpr vleralpplp rpptpklepk 301 eesptrings ipagpkqepc aqhngsepas pkrerptspa phrppkrvka kavps //
Top
LOCUS NP_057622 400 aa linear PRI 26-APR-2009 DEFINITION sirtuin 7 [Homo sapiens]. ACCESSION NP_057622 VERSION NP_057622.1 GI:7706712 DBSOURCE REFSEQ: accession NM_016538.1 KEYWORDS . SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 400) AUTHORS Grob,A., Roussel,P., Wright,J.E., McStay,B., Hernandez-Verdun,D. and Sirri,V. TITLE Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis JOURNAL J. Cell. Sci. 122 (PT 4), 489-498 (2009) PUBMED 19174463 REMARK GeneRIF: associated with NORs during mitosis,interacts with the rDNA transcription factor UBF,phosphorylated via the CDK1-cyclin B pathway during mitosis and dephosphorylated by a phosphatase sensitive to okadaic acid at exit from mitosis GeneRIF: SIRT7 is required for the resumption of rDNA transcription at the exit from mitosis. REFERENCE 2 (residues 1 to 400) AUTHORS Ashraf,N., Zino,S., Macintyre,A., Kingsmore,D., Payne,A.P., George,W.D. and Shiels,P.G. TITLE Altered sirtuin expression is associated with node-positive breast cancer JOURNAL Br. J. Cancer 95 (8), 1056-1061 (2006) PUBMED 17003781 REMARK GeneRIF: Levels of SIRT7 expression were significantly increased in breast cancer REFERENCE 3 (residues 1 to 400) AUTHORS Ford,E., Voit,R., Liszt,G., Magin,C., Grummt,I. and Guarente,L. TITLE Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription JOURNAL Genes Dev. 20 (9), 1075-1080 (2006) PUBMED 16618798 REMARK GeneRIF: SIRT7 is a positive regulator of Pol I transcription and is required for cell viability in mammals. REFERENCE 4 (residues 1 to 400) AUTHORS Voelter-Mahlknecht,S., Letzel,S. and Mahlknecht,U. TITLE Fluorescence in situ hybridization and chromosomal organization of the human Sirtuin 7 gene JOURNAL Int. J. Oncol. 28 (4), 899-908 (2006) PUBMED 16525639 REMARK GeneRIF: Fluorescence in situ hybridization analysis localized the Sirt7 gene to chromosome 17q25.3; a region which is frequently affected by chromosomal alterations in acute leukemias and lymphomas. REFERENCE 5 (residues 1 to 400) AUTHORS De Nigris,F., Cerutti,J., Morelli,C., Califano,D., Chiariotti,L., Viglietto,G., Santelli,G. and Fusco,A. TITLE Isolation of a SIR-like gene, SIR-T8, that is overexpressed in thyroid carcinoma cell lines and tissues JOURNAL Br. J. Cancer 87 (12), 1479 (2002) PUBMED 12454780 REFERENCE 6 (residues 1 to 400) AUTHORS de Nigris,F., Cerutti,J., Morelli,C., Califano,D., Chiariotti,L., Viglietto,G., Santelli,G. and Fusco,A. TITLE Isolation of a SIR-like gene, SIR-T8, that is overexpressed in thyroid carcinoma cell lines and tissues JOURNAL Br. J. Cancer 86 (6), 917-923 (2002) PUBMED 11953824 REMARK Erratum:[Br J Cancer 2002 Dec 2;87(12):1479] REFERENCE 7 (residues 1 to 400) AUTHORS Frye,R.A. TITLE Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins JOURNAL Biochem. Biophys. Res. Commun. 273 (2), 793-798 (2000) PUBMED 10873683 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AF233395.1.
Summary: This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class IV of the sirtuin family. [provided by RefSeq]. FEATURES Location/Qualifiers source 1..400 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="17" /map="17q25" Protein 1..400 /product="sirtuin 7" /note="silent mating type information regulation 2, S.cerevisiae, homolog 7; sir2-related protein type 7; sirtuin type 7" /calculated_mol_wt=44767 Region 100..314 /region_name="SIRT7" /note="SIRT7: Eukaryotic and prokaryotic group (class4) which includes human sirtuin SIRT6, SIRT7, and several bacterial homologs; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent...; cd01410" /db_xref="CDD:29378" Site order(109,111..112,119..120,149,167..168,170,187,268,273, 298..299,314) /site_type="other" /note="NAD+ binding site" /db_xref="CDD:29378" Site order(169,187,237,239..243,272..273,277) /site_type="other" /note="substrate binding site" /db_xref="CDD:29378" Site order(195,198,225,228) /site_type="other" /note="Zn binding site" /db_xref="CDD:29378" CDS 1..400 /gene="SIRT7" /gene_synonym="MGC126840; MGC126842; SIR2L7" /coded_by="NM_016538.1:34..1236" /db_xref="CCDS:CCDS11792.1" /db_xref="GeneID:51547" /db_xref="HGNC:14935" /db_xref="HPRD:12094" /db_xref="MIM:606212" ORIGIN 1 maagglsrse rkaaervrrl reeqqrerlr qvsrilrkaa aersaeegrl laesadlvte 61 lqgrsrrreg lkrrqeevcd dpeelrgkvr elasavrnak ylvvytgagi staasipdyr 121 gpngvwtllq kgrsvsaadl seaeptlthm sitrlheqkl vqhvvsqncd glhlrsglpr 181 taiselhgnm yievctscvp nreyvrvfdv tertalhrhq tgrtchkcgt qlrdtivhfg 241 ergtlgqpln weaateaasr adtilclgss lkvlkkyprl wcmtkppsrr pklyivnlqw 301 tpkddwaalk lhgkcddvmr llmaelglei paysrwqdpi fslatplrag eegshsrksl 361 crsreeappg drgaplssap ilggwfgrgc tkrtkrkkvt //
Top File History:
. |
|
|
