Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone-lysine N-methyltransferase SETD7

Gene

SETD7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.6 Publications

Catalytic activityi

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

Kineticsi

  1. KM=29 µM for histone H31 Publication
  2. KM=12 µM for TAF101 Publication
  3. KM=69 µM for p53/TP531 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei245 – 2451Substrate
    Binding sitei317 – 3171Substrate
    Binding sitei335 – 3351Substrate; via carbonyl oxygen
    Binding sitei356 – 3561S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation2 Publications

    GO - Molecular functioni

    • chromatin binding Source: Ensembl
    • histone-lysine N-methyltransferase activity Source: UniProtKB
    • p53 binding Source: UniProtKB
    • protein-lysine N-methyltransferase activity Source: UniProtKB

    GO - Biological processi

    • cellular response to DNA damage stimulus Source: MGI
    • chromatin modification Source: UniProtKB
    • chromatin organization Source: Reactome
    • heterochromatin organization Source: MGI
    • negative regulation of transferase activity Source: Ensembl
    • peptidyl-lysine dimethylation Source: UniProtKB
    • peptidyl-lysine monomethylation Source: UniProtKB
    • positive regulation of transcription, DNA-templated Source: Ensembl
    • regulation of histone H3-K9 methylation Source: Ensembl
    • response to ethanol Source: Ensembl
    • transcription, DNA-templated Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi2.1.1.43. 2681.
    ReactomeiREACT_268728. PKMTs methylate histone lysines.

    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
    Lysine N-methyltransferase 7
    SET domain-containing protein 7
    SET7/9
    Gene namesi
    Name:SETD7
    Synonyms:KIAA1717, KMT7, SET7, SET9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:30412. SETD7.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi220 – 2201E → A: Increases near-attack conformations. 1 Publication
    Mutagenesisi228 – 2281E → A: Increases near-attack conformations. 1 Publication
    Mutagenesisi245 – 2451Y → A: Significantly reduces the monomethyltransferase activity but increases the dimethyltransferase activity. 2 Publications
    Mutagenesisi294 – 2941K → A: Significantly reduces the catalytic activity. 1 Publication
    Mutagenesisi297 – 2971H → A or G: Abolishes methyltransferase activity. 5 Publications
    Mutagenesisi317 – 3171K → A: Induces a reduction in methyltransferase activity toward TAF10 but an increased methyltransferase activity for H3 and p53/TP53. 1 Publication

    Organism-specific databases

    PharmGKBiPA143485615.

    Polymorphism and mutation databases

    BioMutaiSETD7.
    DMDMi25091217.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 366366Histone-lysine N-methyltransferase SETD7PRO_0000186054Add
    BLAST

    Proteomic databases

    MaxQBiQ8WTS6.
    PaxDbiQ8WTS6.
    PeptideAtlasiQ8WTS6.
    PRIDEiQ8WTS6.

    PTM databases

    PhosphoSiteiQ8WTS6.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in pancreatic islets.

    Gene expression databases

    BgeeiQ8WTS6.
    CleanExiHS_SETD7.
    ExpressionAtlasiQ8WTS6. baseline and differential.
    GenevisibleiQ8WTS6. HS.

    Organism-specific databases

    HPAiHPA058111.

    Interactioni

    Subunit structurei

    Interacts with IPF1/PDX-1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Foxo3Q9WVH45EBI-1268586,EBI-6127038From a different organism.
    HIST1H3DP684314EBI-1268586,EBI-79722
    Hist1h3iP684332EBI-1268586,EBI-79743From a different organism.
    RB1P064004EBI-1268586,EBI-491274
    RELAQ0420610EBI-1268586,EBI-73886
    RelaQ042072EBI-1268586,EBI-644400From a different organism.
    SERTAD1Q9UHV22EBI-1268586,EBI-748601
    TAF10Q129622EBI-1268586,EBI-708376
    TP53P046376EBI-1268586,EBI-366083

    Protein-protein interaction databases

    BioGridi123332. 32 interactions.
    DIPiDIP-29045N.
    IntActiQ8WTS6. 14 interactions.
    MINTiMINT-6615937.
    STRINGi9606.ENSP00000274031.

    Structurei

    Secondary structure

    1
    366
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi54 – 563Combined sources
    Beta strandi61 – 644Combined sources
    Beta strandi67 – 759Combined sources
    Beta strandi81 – 877Combined sources
    Beta strandi90 – 989Combined sources
    Beta strandi100 – 1023Combined sources
    Beta strandi104 – 1118Combined sources
    Helixi114 – 1163Combined sources
    Beta strandi119 – 1224Combined sources
    Beta strandi128 – 1314Combined sources
    Beta strandi135 – 1373Combined sources
    Beta strandi141 – 1477Combined sources
    Beta strandi151 – 16010Combined sources
    Beta strandi163 – 17614Combined sources
    Beta strandi179 – 1846Combined sources
    Beta strandi186 – 1883Combined sources
    Turni203 – 2064Combined sources
    Helixi210 – 2134Combined sources
    Beta strandi216 – 2205Combined sources
    Turni224 – 2263Combined sources
    Beta strandi228 – 2347Combined sources
    Beta strandi241 – 2455Combined sources
    Beta strandi248 – 2503Combined sources
    Helixi252 – 2565Combined sources
    Helixi260 – 2623Combined sources
    Beta strandi266 – 2683Combined sources
    Beta strandi270 – 2723Combined sources
    Beta strandi274 – 2763Combined sources
    Turni279 – 2824Combined sources
    Turni284 – 2863Combined sources
    Helixi292 – 2943Combined sources
    Beta strandi295 – 3006Combined sources
    Beta strandi302 – 3109Combined sources
    Turni311 – 3133Combined sources
    Beta strandi314 – 32310Combined sources
    Beta strandi330 – 3334Combined sources
    Beta strandi338 – 3403Combined sources
    Beta strandi344 – 3463Combined sources
    Helixi351 – 36313Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H3IX-ray2.10A/B52-344[»]
    1MT6X-ray2.20A58-337[»]
    1MUFX-ray2.26A81-337[»]
    1N6AX-ray1.70A108-366[»]
    1N6CX-ray2.30A70-366[»]
    1O9SX-ray1.75A/B108-366[»]
    1XQHX-ray1.75A/E108-366[»]
    2F69X-ray1.30A110-366[»]
    3CBMX-ray1.69A111-366[»]
    3CBOX-ray1.65A111-366[»]
    3CBPX-ray1.42A111-366[»]
    3M53X-ray1.85A110-366[»]
    3M54X-ray1.60A110-366[»]
    3M55X-ray1.55A110-366[»]
    3M56X-ray1.65A110-366[»]
    3M57X-ray1.70A110-366[»]
    3M58X-ray1.40A110-366[»]
    3M59X-ray1.70A110-366[»]
    3M5AX-ray1.75A110-366[»]
    3OS5X-ray1.69A111-366[»]
    3VUZX-ray2.50A111-366[»]
    3VV0X-ray2.00A111-366[»]
    4E47X-ray2.00A/B/C/D109-366[»]
    4J7FX-ray1.59A110-366[»]
    4J7IX-ray2.56A110-366[»]
    4J83X-ray1.70A110-366[»]
    4J8OX-ray1.63A110-366[»]
    4JDSX-ray1.70A/B/C/D109-366[»]
    4JLGX-ray1.90A/B109-366[»]
    ProteinModelPortaliQ8WTS6.
    SMRiQ8WTS6. Positions 52-344.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8WTS6.

    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 binding
    Regioni256 – 2583Substrate binding
    Regioni266 – 2683Substrate binding
    Regioni296 – 2972S-adenosyl-L-methionine binding

    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.

    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.
    InParanoidiQ8WTS6.
    KOiK11431.
    OMAiGSSVYHF.
    PhylomeDBiQ8WTS6.
    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.

    Q8WTS6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDSDDEMVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK
    60 70 80 90 100
    FFFFDGSTLE GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDT
    110 120 130 140 150
    DGRLIFKGQY KDNIRHGVCW IYYPDGGSLV GEVNEDGEMT GEKIAYVYPD
    160 170 180 190 200
    ERTALYGKFI DGEMIEGKLA TLMSTEEGRP HFELMPGNSV YHFDKSTSSC
    210 220 230 240 250
    ISTNALLPDP YESERVYVAE SLISSAGEGL FSKVAVGPNT VMSFYNGVRI
    260 270 280 290 300
    THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT
    310 320 330 340 350
    PNCIYDMFVH PRFGPIKCIR TLRAVEADEE LTVAYGYDHS PPGKSGPEAP
    360
    EWYQVELKAF QATQQK
    Length:366
    Mass (Da):40,721
    Last modified:March 1, 2002 - v1
    Checksum:i73A1217079E3BA13
    GO

    Sequence cautioni

    The sequence BAB21808.1 differs from that shown. Reason: Erroneous initiation. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF448510 mRNA. Translation: AAL56579.1.
    AF462150 mRNA. Translation: AAL69901.1.
    AB051504 mRNA. Translation: BAB21808.1. Different initiation.
    AC112236 Genomic DNA. No translation available.
    AC114743 Genomic DNA. Translation: AAY40937.1.
    BC121055 mRNA. Translation: AAI21056.1.
    BC121056 mRNA. Translation: AAI21057.1.
    CCDSiCCDS3748.1.
    RefSeqiNP_001293128.1. NM_001306199.1.
    NP_085151.1. NM_030648.3.
    UniGeneiHs.480792.

    Genome annotation databases

    EnsembliENST00000274031; ENSP00000274031; ENSG00000145391.
    GeneIDi80854.
    KEGGihsa:80854.
    UCSCiuc003ihw.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF448510 mRNA. Translation: AAL56579.1.
    AF462150 mRNA. Translation: AAL69901.1.
    AB051504 mRNA. Translation: BAB21808.1. Different initiation.
    AC112236 Genomic DNA. No translation available.
    AC114743 Genomic DNA. Translation: AAY40937.1.
    BC121055 mRNA. Translation: AAI21056.1.
    BC121056 mRNA. Translation: AAI21057.1.
    CCDSiCCDS3748.1.
    RefSeqiNP_001293128.1. NM_001306199.1.
    NP_085151.1. NM_030648.3.
    UniGeneiHs.480792.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H3IX-ray2.10A/B52-344[»]
    1MT6X-ray2.20A58-337[»]
    1MUFX-ray2.26A81-337[»]
    1N6AX-ray1.70A108-366[»]
    1N6CX-ray2.30A70-366[»]
    1O9SX-ray1.75A/B108-366[»]
    1XQHX-ray1.75A/E108-366[»]
    2F69X-ray1.30A110-366[»]
    3CBMX-ray1.69A111-366[»]
    3CBOX-ray1.65A111-366[»]
    3CBPX-ray1.42A111-366[»]
    3M53X-ray1.85A110-366[»]
    3M54X-ray1.60A110-366[»]
    3M55X-ray1.55A110-366[»]
    3M56X-ray1.65A110-366[»]
    3M57X-ray1.70A110-366[»]
    3M58X-ray1.40A110-366[»]
    3M59X-ray1.70A110-366[»]
    3M5AX-ray1.75A110-366[»]
    3OS5X-ray1.69A111-366[»]
    3VUZX-ray2.50A111-366[»]
    3VV0X-ray2.00A111-366[»]
    4E47X-ray2.00A/B/C/D109-366[»]
    4J7FX-ray1.59A110-366[»]
    4J7IX-ray2.56A110-366[»]
    4J83X-ray1.70A110-366[»]
    4J8OX-ray1.63A110-366[»]
    4JDSX-ray1.70A/B/C/D109-366[»]
    4JLGX-ray1.90A/B109-366[»]
    ProteinModelPortaliQ8WTS6.
    SMRiQ8WTS6. Positions 52-344.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi123332. 32 interactions.
    DIPiDIP-29045N.
    IntActiQ8WTS6. 14 interactions.
    MINTiMINT-6615937.
    STRINGi9606.ENSP00000274031.

    Chemistry

    BindingDBiQ8WTS6.
    ChEMBLiCHEMBL5523.
    GuidetoPHARMACOLOGYi2703.

    PTM databases

    PhosphoSiteiQ8WTS6.

    Polymorphism and mutation databases

    BioMutaiSETD7.
    DMDMi25091217.

    Proteomic databases

    MaxQBiQ8WTS6.
    PaxDbiQ8WTS6.
    PeptideAtlasiQ8WTS6.
    PRIDEiQ8WTS6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000274031; ENSP00000274031; ENSG00000145391.
    GeneIDi80854.
    KEGGihsa:80854.
    UCSCiuc003ihw.3. human.

    Organism-specific databases

    CTDi80854.
    GeneCardsiGC04M140417.
    HGNCiHGNC:30412. SETD7.
    HPAiHPA058111.
    MIMi606594. gene.
    neXtProtiNX_Q8WTS6.
    PharmGKBiPA143485615.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG4642.
    GeneTreeiENSGT00390000004827.
    HOGENOMiHOG000074731.
    HOVERGENiHBG028309.
    InParanoidiQ8WTS6.
    KOiK11431.
    OMAiGSSVYHF.
    PhylomeDBiQ8WTS6.
    TreeFamiTF106392.

    Enzyme and pathway databases

    BRENDAi2.1.1.43. 2681.
    ReactomeiREACT_268728. PKMTs methylate histone lysines.

    Miscellaneous databases

    ChiTaRSiSETD7. human.
    EvolutionaryTraceiQ8WTS6.
    GeneWikiiSETD7.
    GenomeRNAii80854.
    NextBioi71300.
    PROiQ8WTS6.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8WTS6.
    CleanExiHS_SETD7.
    ExpressionAtlasiQ8WTS6. baseline and differential.
    GenevisibleiQ8WTS6. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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], PROTEIN SEQUENCE OF 35-44; 108-115; 144-152; 234-258 AND 345-358, MUTAGENESIS OF HIS-297.
      Tissue: Brain.
    2. "Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation."
      Nishioka K., Chuikov S., Sarma K., Erdjument-Bromage H., Allis C.D., Tempst P., Reinberg D.
      Genes Dev. 16:479-489(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-45; 104-115; 144-152; 159-169; 201-250 AND 324-358, MUTAGENESIS OF HIS-297.
      Tissue: Cervix carcinoma.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "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].
    6. "Cascade of distinct histone modifications during collagenase gene activation."
      Martens J.H., Verlaan M., Kalkhoven E., Zantema A.
      Mol. Cell. Biol. 23:1808-1816(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Gene-specific modulation of TAF10 function by SET9-mediated methylation."
      Kouskouti A., Scheer E., Staub A., Tora L., Talianidis I.
      Mol. Cell 14:175-182(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF HIS-297.
    8. "Pdx-1 links histone H3-Lys-4 methylation to RNA polymerase II elongation during activation of insulin transcription."
      Francis J., Chakrabarti S.K., Garmey J.C., Mirmira R.G.
      J. Biol. Chem. 280:36244-36253(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IPF1, MUTAGENESIS OF HIS-297.
    9. Cited for: FUNCTION.
    10. "Catalytic mechanism and product specificity of the histone lysine methyltransferase SET7/9: an ab initio QM/MM-FE study with multiple initial structures."
      Hu P., Zhang Y.
      J. Am. Chem. Soc. 128:1272-1278(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-220; GLU-228; TYR-245 AND LYS-294.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "Crystal structure and functional analysis of the histone methyltransferase SET7/9."
      Wilson J., Jing C., Walker P., Martin S., Howell S., Blackburn G., Gamblin S., Xiao B.
      Cell 111:105-115(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 52-344.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    15. "Structure and catalytic mechanism of the human histone methyltransferase SET7/9."
      Xiao B., Jing C., Wilson J.R., Walker P.A., Vasisht N., Kelly G., Howell S., Taylor I.A., Blackburn G.M., Gamblin S.J.
      Nature 421:652-656(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 108-366 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND HISTONE PEPTIDE, FUNCTION, MUTAGENESIS OF TYR-245.
    16. "Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet."
      Kwon T., Chang J.H., Kwak E., Lee C.W., Joachimiak A., Kim Y.C., Lee J., Cho Y.
      EMBO J. 22:292-303(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 70-366 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 108-366, FUNCTION, MUTAGENESIS OF HIS-297.
    18. "Structural basis for the methylation site specificity of SET7/9."
      Couture J.-F., Collazo E., Hauk G., Trievel R.C.
      Nat. Struct. Mol. Biol. 13:140-146(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 110-366, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-317.

    Entry informationi

    Entry nameiSETD7_HUMAN
    AccessioniPrimary (citable) accession number: Q8WTS6
    Secondary accession number(s): B5WWL3
    , Q0VAH3, Q4W5A9, Q9C0E6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: March 1, 2002
    Last modified: July 22, 2015
    This is version 140 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

    Monomethyltransferase activity is achieved by disrupting the formation at near-attack conformations for the dimethylation reaction.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.