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Q9NRC8

- SIR7_HUMAN

UniProt

Q9NRC8 - SIR7_HUMAN

Protein

NAD-dependent protein deacetylase sirtuin-7

Gene

SIRT7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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.3 Publications

    Catalytic activityi

    NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.1 PublicationPROSITE-ProRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei187 – 1871Proton acceptor
    Metal bindingi195 – 1951ZincPROSITE-ProRule annotation
    Metal bindingi198 – 1981ZincPROSITE-ProRule annotation
    Metal bindingi225 – 2251ZincPROSITE-ProRule annotation
    Metal bindingi228 – 2281ZincPROSITE-ProRule annotation
    Binding sitei315 – 3151NAD; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi107 – 12620NADBy similarityAdd
    BLAST
    Nucleotide bindingi167 – 1704NADBy similarity
    Nucleotide bindingi268 – 2703NADBy similarity
    Nucleotide bindingi297 – 2993NADBy similarity

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. NAD+ binding Source: InterPro
    4. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. histone H3 deacetylation Source: UniProtKB
    2. histone H4 deacetylation Source: GOC
    3. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    4. positive regulation of transcription on exit from mitosis Source: UniProtKB
    5. rRNA transcription Source: UniProtKB

    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
    Synonyms:SIR2L7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:14935. SIRT7.

    Subcellular locationi

    Cytoplasm. Nucleusnucleolus
    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleolus Source: UniProtKB
    3. nucleolus organizer region Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi111 – 1111S → A: Abolishes activation of pre-rRNA synthesis. 2 Publications
    Mutagenesisi187 – 1871H → Y: Abolishes deacetylase activity and activation of pre-rRNA synthesis. 2 Publications

    Organism-specific databases

    PharmGKBiPA37940.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 400400NAD-dependent protein deacetylase sirtuin-7PRO_0000110271Add
    BLAST

    Post-translational modificationi

    Phosphorylated during mitosis.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NRC8.
    PaxDbiQ9NRC8.
    PRIDEiQ9NRC8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NRC8.
    BgeeiQ9NRC8.
    CleanExiHS_SIRT7.
    GenevestigatoriQ9NRC8.

    Organism-specific databases

    HPAiCAB037261.

    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.4 Publications

    Protein-protein interaction databases

    BioGridi119602. 661 interactions.
    DIPiDIP-59906N.
    IntActiQ9NRC8. 2 interactions.
    MINTiMINT-1424083.
    STRINGi9606.ENSP00000329466.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRC8.
    SMRiQ9NRC8. Positions 77-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini90 – 331242Deacetylase sirtuin-typePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi8 – 7467Arg-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0846.
    HOGENOMiHOG000231240.
    HOVERGENiHBG060028.
    InParanoidiQ9NRC8.
    KOiK11417.
    OMAiWFGRGCA.
    OrthoDBiEOG7M98GV.
    PhylomeDBiQ9NRC8.
    TreeFamiTF106184.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NRC8-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAAGGLSRSE RKAAERVRRL REEQQRERLR QVSRILRKAA AERSAEEGRL    50
    LAESADLVTE LQGRSRRREG LKRRQEEVCD DPEELRGKVR ELASAVRNAK 100
    YLVVYTGAGI STAASIPDYR GPNGVWTLLQ KGRSVSAADL SEAEPTLTHM 150
    SITRLHEQKL VQHVVSQNCD GLHLRSGLPR TAISELHGNM YIEVCTSCVP 200
    NREYVRVFDV TERTALHRHQ TGRTCHKCGT QLRDTIVHFG ERGTLGQPLN 250
    WEAATEAASR ADTILCLGSS LKVLKKYPRL WCMTKPPSRR PKLYIVNLQW 300
    TPKDDWAALK LHGKCDDVMR LLMAELGLEI PAYSRWQDPI FSLATPLRAG 350
    EEGSHSRKSL CRSREEAPPG DRGAPLSSAP ILGGWFGRGC TKRTKRKKVT 400
    Length:400
    Mass (Da):44,898
    Last modified:October 1, 2000 - v1
    Checksum:i55D7736A864AFE6F
    GO
    Isoform 2 (identifier: Q9NRC8-2) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:183
    Mass (Da):20,404
    Checksum:iEC211D79031585C2
    GO
    Isoform 3 (identifier: Q9NRC8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-30: MAAGGLSRSERKAAERVRRLREEQQRERLR → MPGPRRRSPSACP
         336-400: WQDPIFSLATPLRAGEEGSHSRKSLCRSREEAPPGDRGAPLSSAPILGGWFGRGCTKRTKRKKVT → VL

    Note: No experimental confirmation available.

    Show »
    Length:320
    Mass (Da):35,851
    Checksum:iC0E80615256EEA7A
    GO

    Sequence cautioni

    The sequence CAB70848.2 differs from that shown. Reason:

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711L → Q in BAG52860. (PubMed:14702039)Curated
    Sequence conflicti384 – 3841G → S in BAF82954. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3030MAAGG…RERLR → MPGPRRRSPSACP in isoform 3. 1 PublicationVSP_044396Add
    BLAST
    Alternative sequencei162 – 18322QHVVS…PRTAI → RALGGWYTCQGPGRAPWCPV GN in isoform 2. 1 PublicationVSP_008736Add
    BLAST
    Alternative sequencei184 – 400217Missing in isoform 2. 1 PublicationVSP_008737Add
    BLAST
    Alternative sequencei336 – 40065WQDPI…RKKVT → VL in isoform 3. 1 PublicationVSP_044397Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF233395 mRNA. Translation: AAF43431.1.
    AK002027 mRNA. Translation: BAA92044.1.
    AK094326 mRNA. Translation: BAG52860.1.
    AK290265 mRNA. Translation: BAF82954.1.
    AC145207 Genomic DNA. No translation available.
    BC017305 mRNA. Translation: AAH17305.1.
    BC101791 mRNA. Translation: AAI01792.1.
    BC101793 mRNA. Translation: AAI01794.1.
    AL137626 mRNA. Translation: CAB70848.2. Sequence problems.
    CCDSiCCDS11792.1. [Q9NRC8-1]
    PIRiT46324.
    RefSeqiNP_057622.1. NM_016538.2. [Q9NRC8-1]
    UniGeneiHs.514636.

    Genome annotation databases

    EnsembliENST00000328666; ENSP00000329466; ENSG00000187531. [Q9NRC8-1]
    GeneIDi51547.
    KEGGihsa:51547.
    UCSCiuc002kcj.2. human. [Q9NRC8-1]

    Polymorphism databases

    DMDMi38258650.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF233395 mRNA. Translation: AAF43431.1 .
    AK002027 mRNA. Translation: BAA92044.1 .
    AK094326 mRNA. Translation: BAG52860.1 .
    AK290265 mRNA. Translation: BAF82954.1 .
    AC145207 Genomic DNA. No translation available.
    BC017305 mRNA. Translation: AAH17305.1 .
    BC101791 mRNA. Translation: AAI01792.1 .
    BC101793 mRNA. Translation: AAI01794.1 .
    AL137626 mRNA. Translation: CAB70848.2 . Sequence problems.
    CCDSi CCDS11792.1. [Q9NRC8-1 ]
    PIRi T46324.
    RefSeqi NP_057622.1. NM_016538.2. [Q9NRC8-1 ]
    UniGenei Hs.514636.

    3D structure databases

    ProteinModelPortali Q9NRC8.
    SMRi Q9NRC8. Positions 77-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119602. 661 interactions.
    DIPi DIP-59906N.
    IntActi Q9NRC8. 2 interactions.
    MINTi MINT-1424083.
    STRINGi 9606.ENSP00000329466.

    Chemistry

    ChEMBLi CHEMBL2163184.

    Polymorphism databases

    DMDMi 38258650.

    Proteomic databases

    MaxQBi Q9NRC8.
    PaxDbi Q9NRC8.
    PRIDEi Q9NRC8.

    Protocols and materials databases

    DNASUi 51547.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328666 ; ENSP00000329466 ; ENSG00000187531 . [Q9NRC8-1 ]
    GeneIDi 51547.
    KEGGi hsa:51547.
    UCSCi uc002kcj.2. human. [Q9NRC8-1 ]

    Organism-specific databases

    CTDi 51547.
    GeneCardsi GC17M079869.
    HGNCi HGNC:14935. SIRT7.
    HPAi CAB037261.
    MIMi 606212. gene.
    neXtProti NX_Q9NRC8.
    PharmGKBi PA37940.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0846.
    HOGENOMi HOG000231240.
    HOVERGENi HBG060028.
    InParanoidi Q9NRC8.
    KOi K11417.
    OMAi WFGRGCA.
    OrthoDBi EOG7M98GV.
    PhylomeDBi Q9NRC8.
    TreeFami TF106184.

    Miscellaneous databases

    ChiTaRSi SIRT7. human.
    GeneWikii SIRT7.
    GenomeRNAii 51547.
    NextBioi 35463912.
    PROi Q9NRC8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRC8.
    Bgeei Q9NRC8.
    CleanExi HS_SIRT7.
    Genevestigatori Q9NRC8.

    Family and domain databases

    Gene3Di 3.40.50.1220. 2 hits.
    InterProi IPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR003000. Sirtuin.
    IPR026590. Ssirtuin_cat_dom.
    [Graphical view ]
    PANTHERi PTHR11085. PTHR11085. 1 hit.
    Pfami PF02146. SIR2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52467. SSF52467. 1 hit.
    PROSITEi PS50305. SIRTUIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Phylogenetic classification of prokaryotic and eukaryotic Sir-2 like proteins."
      Frye R.A.
      Biochem. Biophys. Res. Commun. 273:793-798(2000) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Cerebellum, Colon and Placenta.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Liver and Lymph.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-400 (ISOFORM 1).
      Tissue: Testis.
    6. "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] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "'SIRT8' expressed in thyroid cancer is actually SIRT7."
      Frye R.A.
      Br. J. Cancer 87:1479-1479(2002) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UBTF, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    11. "Functional proteomics establishes the interaction of SIRT7 with chromatin remodeling complexes and expands its role in regulation of RNA polymerase I transcription."
      Tsai Y.C., Greco T.M., Boonmee A., Miteva Y., Cristea I.M.
      Mol. Cell. Proteomics 11:M111.015156.01-M111.015156.17(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MYBBP1A; SMARCA5 AND BAZ1B, MUTAGENESIS OF SER-111.
    12. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH ELK4, MUTAGENESIS OF HIS-187.

    Entry informationi

    Entry nameiSIR7_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRC8
    Secondary accession number(s): A8K2K0
    , B3KSU8, Q3MIK4, Q9NSZ6, Q9NUS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Miscellaneous

    Overexpressed in human thyroid carcinoma cell lines and tissues, but not in adenomas.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3