Q9NRC8 (SIRT7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NAD-dependent deacetylase sirtuin-7
EC=3.5.1.-

Alternative name(s):
SIR2-like protein 7

Gene names

Name:	SIRT7
Synonyms:	SIR2L7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	NAD-dependent protein deacetylase. 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. Ref.9 Ref.10
Catalytic activity	NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Interacts with UBTF and the RNA polymerase I complex. Interacts with histone H2A and/or histone H2B. Ref.9 Ref.10
Subcellular location	Cytoplasm. Nucleus › nucleolus. 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. Ref.5 Ref.8 Ref.9 Ref.10
Post-translational modification	Phosphorylated during mitosis Probable. Ref.10
Miscellaneous	Overexpressed in human thyroid carcinoma cell lines and tissues, but not in adenomas.
Sequence similarities	Belongs to the sirtuin family. Contains 1 deacetylase sirtuin-type domain.
Caution	Was originally (Ref.5) termed SIR-T8/SIRT8. This was later (Ref.6) retracted. See also Ref.7.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding NAD Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of transcription on exit from mitosis Inferred from mutant phenotype Ref.10. Source: UniProtKB protein deacetylation Inferred from electronic annotation. Source: InterPro rRNA transcription Inferred from mutant phenotype Ref.10. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus organizer region Inferred from direct assay Ref.10. Source: UniProtKB
Molecular function	NAD+ binding Inferred from electronic annotation. Source: InterPro hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.10. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NRC8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NRC8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     162-183: QHVVSQNCDGLHLRSGLPRTAI → RALGGWYTCQGPGRAPWCPVGN
     184-400: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 400	400	NAD-dependent deacetylase sirtuin-7		PRO_0000110271
Regions
	Domain	90 – 331	242	Deacetylase sirtuin-type
	Nucleotide binding	107 – 126	20	NAD By similarity
	Nucleotide binding	167 – 171	5	NAD By similarity
	Compositional bias	8 – 74	67	Arg-rich
Sites
	Active site	187	1	Proton acceptor By similarity
	Metal binding	195	1	Zinc By similarity
	Metal binding	198	1	Zinc By similarity
	Metal binding	225	1	Zinc By similarity
	Metal binding	228	1	Zinc By similarity
Natural variations
	Alternative sequence	162 – 183	22	QHVVS…PRTAI → RALGGWYTCQGPGRAPWCPV GN in isoform 2.		VSP_008736
	Alternative sequence	184 – 400	217	Missing in isoform 2.		VSP_008737
Experimental info
	Mutagenesis	111	1	S → A: Abolishes activation of pre-rRNA synthesis. Ref.9
	Mutagenesis	187	1	H → Y: Abolishes activation of pre-rRNA synthesis. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 55D7736A864AFE6F	FASTA	400	44,898
	10 20 30 40 50 60 MAAGGLSRSE RKAAERVRRL REEQQRERLR QVSRILRKAA AERSAEEGRL LAESADLVTE 70 80 90 100 110 120 LQGRSRRREG LKRRQEEVCD DPEELRGKVR ELASAVRNAK YLVVYTGAGI STAASIPDYR 130 140 150 160 170 180 GPNGVWTLLQ KGRSVSAADL SEAEPTLTHM SITRLHEQKL VQHVVSQNCD GLHLRSGLPR 190 200 210 220 230 240 TAISELHGNM YIEVCTSCVP NREYVRVFDV TERTALHRHQ TGRTCHKCGT QLRDTIVHFG 250 260 270 280 290 300 ERGTLGQPLN WEAATEAASR ADTILCLGSS LKVLKKYPRL WCMTKPPSRR PKLYIVNLQW 310 320 330 340 350 360 TPKDDWAALK LHGKCDDVMR LLMAELGLEI PAYSRWQDPI FSLATPLRAG EEGSHSRKSL 370 380 390 400 CRSREEAPPG DRGAPLSSAP ILGGWFGRGC TKRTKRKKVT
	Isoform 2 [UniParc]. Checksum: EC211D79031585C2	FASTA	183	20,404
	10 20 30 40 50 60 MAAGGLSRSE RKAAERVRRL REEQQRERLR QVSRILRKAA AERSAEEGRL LAESADLVTE 70 80 90 100 110 120 LQGRSRRREG LKRRQEEVCD DPEELRGKVR ELASAVRNAK YLVVYTGAGI STAASIPDYR 130 140 150 160 170 180 GPNGVWTLLQ KGRSVSAADL SEAEPTLTHM SITRLHEQKL VRALGGWYTC QGPGRAPWCP VGN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phylogenetic classification of prokaryotic and eukaryotic Sir-2 like proteins." Frye R.A. Biochem. Biophys. Res. Commun. 273:793-798(2000) [PubMed: 10873683] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Spleen.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Placenta.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Liver and Lymph.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-400 (ISOFORM 1). Tissue: Testis.
[5]	"Isolation of a SIR-like gene, SIR-T8, that is overexpressed in thyroid carcinoma cell lines and tissues." de Nigris F., Cerutti J., Morelli C., Califano D., Chiariotti L., Viglietto G., Santelli G., Fusco A. Br. J. Cancer 86:917-923(2002) [PubMed: 11953824] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	Erratum De Nigris F., Cerutti J., Morelli C., Califano D., Chiariotti L., Viglietto G., Santelli G., Fusco A. Br. J. Cancer 87:1479-1479(2002) [PubMed: 12454780] [Abstract]
[7]	"'SIRT8' expressed in thyroid cancer is actually SIRT7." Frye R.A. Br. J. Cancer 87:1479-1479(2002) [PubMed: 12454781] [Abstract] Cited for: SHOWS THAT SIR-T8 IS SIRT7.
[8]	"Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins." Michishita E., Park J.Y., Burneskis J.M., Barrett J.C., Horikawa I. Mol. Biol. Cell 16:4623-4635(2005) [PubMed: 16079181] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription." Ford E., Voit R., Liszt G., Magin C., Grummt I., Guarente L. Genes Dev. 20:1075-1080(2006) [PubMed: 16618798] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE I COMPLEX, INTERACTION WITH HISTONE H2A AND/OR HISTONE H2B, MUTAGENESIS OF SER-111 AND HIS-187, SUBCELLULAR LOCATION.
[10]	"Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis." Grob A., Roussel P., Wright J.E., McStay B., Hernandez-Verdun D., Sirri V. J. Cell Sci. 122:489-498(2009) [PubMed: 19174463] [Abstract] Cited for: FUNCTION, INTERACTION WITH UBTF, PHOSPHORYLATION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF233395 mRNA. Translation: AAF43431.1. AK002027 mRNA. Translation: BAA92044.1. BC017305 mRNA. Translation: AAH17305.1. BC101791 mRNA. Translation: AAI01792.1. BC101793 mRNA. Translation: AAI01794.1. AL137626 mRNA. Translation: CAB70848.2. Sequence problems.
IPI	IPI00334648. IPI00383601.
PIR	T46324.
RefSeq	NP_057622.1. NM_016538.2.
UniGene	Hs.514636.
3D structure databases
ProteinModelPortal	Q9NRC8.
SMR	Q9NRC8. Positions 88-329.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NRC8. 2 interactions.
MINT	MINT-1424083.
STRING	Q9NRC8.
Polymorphism databases
DMDM	38258650.
Proteomic databases
PRIDE	Q9NRC8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000328666; ENSP00000329466; ENSG00000187531.
GeneID	51547.
KEGG	hsa:51547.
UCSC	uc002kcj.1. human.
Organism-specific databases
CTD	51547.
GeneCards	GC17M079869.
H-InvDB	HIX0202414.
HGNC	HGNC:14935. SIRT7.
HPA	CAB037261.
MIM	606212. gene.
neXtProt	NX_Q9NRC8.
PharmGKB	PA37940.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15680.
GeneTree	ENSGT00530000063706.
HOGENOM	HBG596746.
HOVERGEN	HBG060028.
InParanoid	Q9NRC8.
OMA	HQTGRAC.
OrthoDB	EOG4FN4HW.
PhylomeDB	Q9NRC8.
Enzyme and pathway databases
Pathway_Interaction_DB	hdac_classi_pathway. Signaling events mediated by HDAC Class I. hdac_classiii_pathway. Signaling events mediated by HDAC Class III.
Gene expression databases
ArrayExpress	Q9NRC8.
Bgee	Q9NRC8.
CleanEx	HS_SIRT7.
Genevestigator	Q9NRC8.
GermOnline	ENSG00000187531. Homo sapiens.
Family and domain databases
InterPro	IPR003000. NAD-dep_deAcase_sirtuin. [Graphical view]
KO	K11417.
PANTHER	PTHR11085. SIR2. 1 hit.
Pfam	PF02146. SIR2. 1 hit. [Graphical view]
PROSITE	PS50305. SIRTUIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	55323.
SOURCE	Search...

Entry information

Entry name

SIRT7_HUMAN

Accession

Primary (citable) accession number: Q9NRC8
Secondary accession number(s): Q3MIK4, Q9NSZ6, Q9NUS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.