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Q8VHL1

- SETD7_MOUSE

UniProt

Q8VHL1 - SETD7_MOUSE

Protein

Histone-lysine N-methyltransferase SETD7

Gene

Setd7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (05 Feb 2008)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.1 Publication

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei245 – 2451SubstrateBy similarity
    Binding sitei317 – 3171SubstrateBy similarity
    Binding sitei335 – 3351Substrate; via carbonyl oxygenBy similarity
    Binding sitei356 – 3561S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation

    GO - Molecular functioni

    1. histone-lysine N-methyltransferase activity Source: UniProtKB
    2. protein-lysine N-methyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. peptidyl-lysine dimethylation Source: UniProtKB
    2. peptidyl-lysine monomethylation Source: UniProtKB
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase SETD7 (EC:2.1.1.43)
    Alternative name(s):
    Histone H3-K4 methyltransferase SETD7
    Short name:
    H3-K4-HMTase SETD7
    SET domain-containing protein 7
    SET7/9
    Gene namesi
    Name:Setd7
    Synonyms:Kiaa1717, Set7, Set9
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1920501. Setd7.

    Subcellular locationi

    Nucleus By similarity. Chromosome By similarity

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 366366Histone-lysine N-methyltransferase SETD7PRO_0000186055Add
    BLAST

    Proteomic databases

    MaxQBiQ8VHL1.
    PaxDbiQ8VHL1.
    PRIDEiQ8VHL1.

    PTM databases

    PhosphoSiteiQ8VHL1.

    Expressioni

    Developmental stagei

    Expressed during all pre-implementation stages in both male and female embryos.1 Publication

    Gene expression databases

    BgeeiQ8VHL1.
    GenevestigatoriQ8VHL1.

    Interactioni

    Subunit structurei

    Interacts with IPF1/PDX-1.By similarity

    Protein-protein interaction databases

    BioGridi215865. 1 interaction.
    IntActiQ8VHL1. 1 interaction.
    MINTiMINT-4114741.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VHL1.
    SMRiQ8VHL1. Positions 52-344.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati36 – 5823MORN 1Add
    BLAST
    Repeati59 – 8123MORN 2Add
    BLAST
    Repeati106 – 12823MORN 3Add
    BLAST
    Domaini214 – 336123SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni226 – 2283S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
    Regioni256 – 2583Substrate bindingBy similarity
    Regioni266 – 2683Substrate bindingBy similarity
    Regioni296 – 2972S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi51 – 544Poly-Phe

    Domaini

    The SET domain is necessary but not sufficient for histone methyltransferase activity.By similarity

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET7 subfamily.PROSITE-ProRule annotation
    Contains 3 MORN repeats.Curated
    Contains 1 SET domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG4642.
    GeneTreeiENSGT00390000004827.
    HOGENOMiHOG000074731.
    HOVERGENiHBG028309.
    InParanoidiQ8VHL1.
    KOiK11431.
    OMAiGSSVYHF.
    OrthoDBiEOG7M98G8.
    PhylomeDBiQ8VHL1.
    TreeFamiTF106392.

    Family and domain databases

    InterProiIPR017155. Hist-Lys_N-MeTrfase_SET.
    IPR003409. MORN.
    IPR001214. SET_dom.
    [Graphical view]
    PfamiPF02493. MORN. 4 hits.
    PF00856. SET. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037249. Histone_Lys_mtfrase_SET. 1 hit.
    SMARTiSM00317. SET. 1 hit.
    [Graphical view]
    PROSITEiPS51577. SAM_MT43_SET7. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8VHL1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSDDEVVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK    50
    FFFFDGSTLE GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDS 100
    DGRLIFKGQY KDNNRHGVCW IHYPDGGSLV GEVNEDGEMT GEKIAYVYPD 150
    QRTALYGKFI DGEMLEGKLA TLMATEEGRP HFEVTSGSSV YHFDKSTSSC 200
    ISSDALLPDP YESERVYVAD SLISSAGEGL FSKVAVGPNT VMSFYNGVRI 250
    THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT 300
    PNCVYDLFVH PRFGPIKCIR TLRAVEAEEE LTVAYGYDHS PPGKSGPEAP 350
    EWYQVELKAF QATQQK 366
    Length:366
    Mass (Da):40,506
    Last modified:February 5, 2008 - v2
    Checksum:iC826EAFCB4B9D345
    GO

    Sequence cautioni

    The sequence BAC98238.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771E → V in AAH50190. (PubMed:15489334)Curated
    Sequence conflicti165 – 1651L → I in AAL56578. (PubMed:11779497)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF448509 mRNA. Translation: AAL56578.1.
    AK129428 mRNA. Translation: BAC98238.1. Different initiation.
    AK048924 mRNA. Translation: BAC33493.1.
    AK147422 mRNA. Translation: BAE27903.1.
    AK147413 mRNA. Translation: BAE27897.1.
    AK147667 mRNA. Translation: BAE28059.1.
    AK170161 mRNA. Translation: BAE41607.1.
    BC050190 mRNA. Translation: AAH50190.1.
    CCDSiCCDS17341.1.
    RefSeqiNP_542983.3. NM_080793.5.
    UniGeneiMm.192111.

    Genome annotation databases

    EnsembliENSMUST00000037141; ENSMUSP00000043492; ENSMUSG00000037111.
    GeneIDi73251.
    KEGGimmu:73251.
    UCSCiuc008peb.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF448509 mRNA. Translation: AAL56578.1 .
    AK129428 mRNA. Translation: BAC98238.1 . Different initiation.
    AK048924 mRNA. Translation: BAC33493.1 .
    AK147422 mRNA. Translation: BAE27903.1 .
    AK147413 mRNA. Translation: BAE27897.1 .
    AK147667 mRNA. Translation: BAE28059.1 .
    AK170161 mRNA. Translation: BAE41607.1 .
    BC050190 mRNA. Translation: AAH50190.1 .
    CCDSi CCDS17341.1.
    RefSeqi NP_542983.3. NM_080793.5.
    UniGenei Mm.192111.

    3D structure databases

    ProteinModelPortali Q8VHL1.
    SMRi Q8VHL1. Positions 52-344.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 215865. 1 interaction.
    IntActi Q8VHL1. 1 interaction.
    MINTi MINT-4114741.

    PTM databases

    PhosphoSitei Q8VHL1.

    Proteomic databases

    MaxQBi Q8VHL1.
    PaxDbi Q8VHL1.
    PRIDEi Q8VHL1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000037141 ; ENSMUSP00000043492 ; ENSMUSG00000037111 .
    GeneIDi 73251.
    KEGGi mmu:73251.
    UCSCi uc008peb.1. mouse.

    Organism-specific databases

    CTDi 80854.
    MGIi MGI:1920501. Setd7.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG4642.
    GeneTreei ENSGT00390000004827.
    HOGENOMi HOG000074731.
    HOVERGENi HBG028309.
    InParanoidi Q8VHL1.
    KOi K11431.
    OMAi GSSVYHF.
    OrthoDBi EOG7M98G8.
    PhylomeDBi Q8VHL1.
    TreeFami TF106392.

    Miscellaneous databases

    ChiTaRSi SETD7. mouse.
    NextBioi 337766.
    PROi Q8VHL1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8VHL1.
    Genevestigatori Q8VHL1.

    Family and domain databases

    InterProi IPR017155. Hist-Lys_N-MeTrfase_SET.
    IPR003409. MORN.
    IPR001214. SET_dom.
    [Graphical view ]
    Pfami PF02493. MORN. 4 hits.
    PF00856. SET. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037249. Histone_Lys_mtfrase_SET. 1 hit.
    SMARTi SM00317. SET. 1 hit.
    [Graphical view ]
    PROSITEi PS51577. SAM_MT43_SET7. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase."
      Wang H., Cao R., Xia L., Erdjument-Bromage H., Borchers C., Tempst P., Zhang Y.
      Mol. Cell 8:1207-1217(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pancreas.
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryonic tail.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6 and NOD.
      Tissue: Brain and Cerebellum.
    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].
      Strain: 129/Sv X 129SvCp.
      Tissue: Embryonic stem cell.
    5. "Covalent histone modifications underlie the developmental regulation of insulin gene transcription in pancreatic beta cells."
      Chakrabarti S.K., Francis J., Ziesmann S.M., Garmey J.C., Mirmira R.G.
      J. Biol. Chem. 278:23617-23623(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The analysis of X-chromosome inactivation-related gene expression from single mouse embryo with sex-determination."
      Jeong K.S., Park J.H., Lee S.
      Biochem. Biophys. Res. Commun. 333:803-807(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiSETD7_MOUSE
    AccessioniPrimary (citable) accession number: Q8VHL1
    Secondary accession number(s): Q6ZPJ6, Q80UU3, Q8C7Y6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 103 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3