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Protein

NAD-dependent protein deacetylase sirtuin-7

Gene

Sirt7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

NAD-dependent protein deacetylase that specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays selectivity for a single histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors. SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. These data suggest that SIRT7 may play a key role in oncogenic transformation by suppresses expression of tumor suppressor genes by locus-specific deacetylation of H3K18Ac at promoter regions. Also required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis: promotes the association of RNA polymerase I with the rDNA promoter region and coding region. Stimulates transcription activity of the RNA polymerase I complex. May also deacetylate p53/TP53 and promotes cell survival, however such data need additional confirmation (By similarity).By similarity

Catalytic activityi

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.PROSITE-ProRule annotation

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881Proton acceptorPROSITE-ProRule annotation
Metal bindingi196 – 1961ZincPROSITE-ProRule annotation
Metal bindingi199 – 1991ZincPROSITE-ProRule annotation
Metal bindingi226 – 2261ZincPROSITE-ProRule annotation
Metal bindingi229 – 2291ZincPROSITE-ProRule annotation
Binding sitei316 – 3161NAD; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi108 – 12720NADBy similarityAdd
BLAST
Nucleotide bindingi168 – 1714NADBy similarity
Nucleotide bindingi269 – 2713NADBy similarity
Nucleotide bindingi298 – 3003NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent protein deacetylase sirtuin-7 (EC:3.5.1.-)
Alternative name(s):
Regulatory protein SIR2 homolog 7
SIR2-like protein 7
Gene namesi
Name:Sirt7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1305876. Sirt7.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleusnucleolus By similarity

  • Note: Located close to the nuclear membrane when in the cytoplasm. Associated with chromatin. Associated with rDNA promoter and transcribed region. Associated with nucleolar organizer regions during mitosis.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 402402NAD-dependent protein deacetylase sirtuin-7PRO_0000419985Add
BLAST

Post-translational modificationi

Phosphorylated during mitosis.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiB2RZ55.
PeptideAtlasiB2RZ55.

Expressioni

Gene expression databases

GenevisibleiB2RZ55. RN.

Interactioni

Subunit structurei

Interacts with UBTF and the RNA polymerase I complex. Interacts with components of the B-WICH complex, such as MYBBP1A, SMARCA5/SNF2H and BAZ1B/WSTF. Interacts with ELK4, leading to stabilization at target promoters for H3K18Ac deacetylation. Interacts with histone H2A and/or histone H2B (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000051834.

Structurei

3D structure databases

ProteinModelPortaliB2RZ55.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 332242Deacetylase sirtuin-typePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 7567Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the sirtuin family. Class IV subfamily.Curated
Contains 1 deacetylase sirtuin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1905. Eukaryota.
COG0846. LUCA.
GeneTreeiENSGT00530000063706.
HOGENOMiHOG000231240.
HOVERGENiHBG060028.
InParanoidiB2RZ55.
KOiK11417.
OMAiEVCTACT.
OrthoDBiEOG7M98GV.
PhylomeDBiB2RZ55.

Family and domain databases

Gene3Di3.40.50.1220. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 1 hit.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2RZ55-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGGGLSRS ERKAAERVRR LREEQQRERL RQVSRILRKA AAERSAEEGR
60 70 80 90 100
LLAESEDLVT ELQGRSRRRE GLKRRQEEVC DDPEELRRKV RELAGAVRSA
110 120 130 140 150
RHLVVYTGAG ISTAASIPDY RGPNGVWTLL QKGRPVSAAD LSEAEPTLTH
160 170 180 190 200
MSITQLHKHK LVQHVVSQNC DGLHLRSGLP RTAISELHGN MYIEVCTSCI
210 220 230 240 250
PNREYVRVFD VTERTALHRH LTGRTCHKCG TQLRDTIVHF GERGTLGQPL
260 270 280 290 300
NWEAATEAAS KADTILCLGS SLKVLKKYPR LWCMTKPPSR RPKLYIVNLQ
310 320 330 340 350
WTPKDDWAAL KLHGKCDDVM RLLMDELGLE IPVYNRWQDP IFSLATPLRA
360 370 380 390 400
GEEGSHSRKS LCRSREEPPP GDQSAPLASA TPILGGWFGR GCAKRAKRKK

AA
Length:402
Mass (Da):45,113
Last modified:July 1, 2008 - v1
Checksum:i7A1E79AF09204A84
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473948 Genomic DNA. Translation: EDM06872.1.
BC167031 mRNA. Translation: AAI67031.1.
RefSeqiNP_001100543.1. NM_001107073.1.
UniGeneiRn.23064.

Genome annotation databases

EnsembliENSRNOT00000054951; ENSRNOP00000051834; ENSRNOG00000036683.
GeneIDi303745.
KEGGirno:303745.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473948 Genomic DNA. Translation: EDM06872.1.
BC167031 mRNA. Translation: AAI67031.1.
RefSeqiNP_001100543.1. NM_001107073.1.
UniGeneiRn.23064.

3D structure databases

ProteinModelPortaliB2RZ55.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000051834.

Proteomic databases

PaxDbiB2RZ55.
PeptideAtlasiB2RZ55.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000054951; ENSRNOP00000051834; ENSRNOG00000036683.
GeneIDi303745.
KEGGirno:303745.

Organism-specific databases

CTDi51547.
RGDi1305876. Sirt7.

Phylogenomic databases

eggNOGiKOG1905. Eukaryota.
COG0846. LUCA.
GeneTreeiENSGT00530000063706.
HOGENOMiHOG000231240.
HOVERGENiHBG060028.
InParanoidiB2RZ55.
KOiK11417.
OMAiEVCTACT.
OrthoDBiEOG7M98GV.
PhylomeDBiB2RZ55.

Miscellaneous databases

PROiB2RZ55.

Gene expression databases

GenevisibleiB2RZ55. RN.

Family and domain databases

Gene3Di3.40.50.1220. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 1 hit.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.

Entry informationi

Entry nameiSIR7_RAT
AccessioniPrimary (citable) accession number: B2RZ55
Secondary accession number(s): F1LQY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: July 1, 2008
Last modified: July 6, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.