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Q9NQR1

- SETD8_HUMAN

UniProt

Q9NQR1 - SETD8_HUMAN

Protein

N-lysine methyltransferase SETD8

Gene

SETD8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (15 Nov 2002)
      Previous versions | rss
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    Functioni

    Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration.8 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].3 PublicationsPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei312 – 3121S-adenosyl-L-methionine

    GO - Molecular functioni

    1. histone-lysine N-methyltransferase activity Source: UniProtKB
    2. p53 binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein-lysine N-methyltransferase activity Source: UniProtKB
    5. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. histone lysine methylation Source: GOC
    2. mitotic cell cycle Source: Reactome
    3. mitotic nuclear division Source: UniProtKB-KW
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    6. peptidyl-lysine monomethylation Source: UniProtKB
    7. regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi2.1.1.43. 2681.
    ReactomeiREACT_172744. Condensation of Prophase Chromosomes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-lysine methyltransferase SETD8 (EC:2.1.1.-)
    Alternative name(s):
    H4-K20-HMTase SETD8
    Histone-lysine N-methyltransferase SETD8 (EC:2.1.1.43)
    Lysine N-methyltransferase 5A
    PR/SET domain-containing protein 07
    Short name:
    PR-Set7
    Short name:
    PR/SET07
    SET domain-containing protein 8
    Gene namesi
    Name:SETD8
    Synonyms:KMT5A, PRSET7, SET07, SET8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:29489. SETD8.

    Subcellular locationi

    Nucleus. Chromosome
    Note: Specifically localizes to mitotic chromosomes. Colocalized with SIRT2 at mitotic foci. Associates with chromosomes during mitosis; association is increased in a H2O(2)-induced oxidative stress-dependent manner. Associates with silent chromatin on euchromatic arms. Not associated with constitutive heterochromatin.

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. nucleolus Source: HPA
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi172 – 1721K → Q: Inhibits the interaction with SIRT2. Increases the number of mitotic foci formation. Does not change methyltransferase activity. 1 Publication
    Mutagenesisi172 – 1721K → R: Increases the interaction with SIRT2. Reduces the number of mitotic foci formation. Does not change methyltransferase activity. 1 Publication
    Mutagenesisi286 – 2861Y → A or F: Strongly reduces affinity for histone H4 and abolishes methyltransferase activity. 1 Publication
    Mutagenesisi300 – 3001E → A: Strongly reduces affinity for histone H4. 1 Publication
    Mutagenesisi311 – 3111C → A: Strongly reduces affinity for histone H4. 1 Publication
    Mutagenesisi336 – 3361R → G: Abolishes methyltransferase activity. 2 Publications
    Mutagenesisi340 – 3401H → A: Strongly decreases methyltransferase activity. 1 Publication
    Mutagenesisi375 – 3751Y → A: Strongly reduces affinity for histone H4 and methyltransferase activity. 1 Publication
    Mutagenesisi375 – 3751Y → F: Alters methyltransferase activity, so that both monomethylation and dimethylation take place. 1 Publication
    Mutagenesisi379 – 3791D → A or N: Abolishes histone H4 binding and methyltransferase activity. 4 Publications
    Mutagenesisi385 – 3939Missing: Abolishes methyltransferase activity.
    Mutagenesisi388 – 3881H → A or E: Strongly reduces affinity for histone H4. 1 Publication
    Mutagenesisi388 – 3881H → F: Increases affinity for histone H4. 1 Publication

    Organism-specific databases

    PharmGKBiPA143485616.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 393393N-lysine methyltransferase SETD8PRO_0000186081Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei100 – 1001Phosphoserine2 Publications
    Modified residuei172 – 1721N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylated at Lys-172; does not change methyltransferase activity. Deacetylated at Lys-172 by SIRT2; does not change methyltransferase activity.1 Publication
    Ubiquitinated and degraded by the DCX(DTL) complex.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NQR1.
    PaxDbiQ9NQR1.
    PRIDEiQ9NQR1.

    PTM databases

    PhosphoSiteiQ9NQR1.

    Expressioni

    Developmental stagei

    Not detected during G1 phase. First detected during S through G2 phases, and peaks during mitosis (at protein level).1 Publication

    Inductioni

    By HCFC1 C-terminal chain, independently of HCFC1 N-terminal chain. Transiently induced by TGF-beta and during the cell cycle.2 Publications

    Gene expression databases

    ArrayExpressiQ9NQR1.
    BgeeiQ9NQR1.
    CleanExiHS_SETD8.
    GenevestigatoriQ9NQR1.

    Organism-specific databases

    HPAiHPA053747.

    Interactioni

    Subunit structurei

    Interacts with L3MBTL1. Isoform 2 interacts with SIRT2 (phosphorylated form); the interaction is direct, stimulates SETD8-mediated methyltransferase activity at histone H4 'Lys-20' (H4K20me1) and is increased in a H2O(2)-induced oxidative stress-dependent manner.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST2H4BP628055EBI-1268946,EBI-302023
    TWIST1Q156725EBI-1268946,EBI-1797287

    Protein-protein interaction databases

    BioGridi132490. 25 interactions.
    DIPiDIP-39133N.
    IntActiQ9NQR1. 3 interactions.
    MINTiMINT-3072203.
    STRINGi9606.ENSP00000332995.

    Structurei

    Secondary structure

    1
    393
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi236 – 25318
    Beta strandi259 – 2646
    Turni265 – 2673
    Beta strandi268 – 2758
    Beta strandi282 – 2854
    Beta strandi288 – 2925
    Helixi293 – 30311
    Helixi306 – 3094
    Helixi310 – 3123
    Beta strandi313 – 3186
    Beta strandi321 – 3266
    Helixi335 – 3373
    Beta strandi345 – 3539
    Beta strandi356 – 36510
    Helixi382 – 3876
    Helixi389 – 3924

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZKKX-ray1.45A/B/C/D231-393[»]
    2BQZX-ray1.50A/E233-393[»]
    3F9WX-ray1.60A/B/C/D232-393[»]
    3F9XX-ray1.25A/B/C/D232-393[»]
    3F9YX-ray1.50A/B232-393[»]
    3F9ZX-ray1.60A/B/C/D232-393[»]
    4IJ8X-ray2.00A/B232-393[»]
    ProteinModelPortaliQ9NQR1.
    SMRiQ9NQR1. Positions 233-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NQR1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini257 – 378122SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni267 – 2693S-adenosyl-L-methionine binding
    Regioni339 – 3402S-adenosyl-L-methionine binding

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili134 – 16330Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi6 – 6762Ala-richAdd
    BLAST
    Compositional biasi29 – 324Poly-Arg

    Domaini

    Although the SET domain contains the active site of enzymatic activity, both sequences upstream and downstream of the SET domain are required for methyltransferase activity.

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. PR/SET subfamily.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG2940.
    HOGENOMiHOG000020818.
    HOVERGENiHBG067546.
    InParanoidiQ9NQR1.
    KOiK11428.
    OMAiCSGMRSP.
    OrthoDBiEOG70KGRN.
    PhylomeDBiQ9NQR1.
    TreeFamiTF335181.

    Family and domain databases

    InterProiIPR016858. Hist_H4-K20_MeTrfase.
    IPR001214. SET_dom.
    [Graphical view]
    PfamiPF00856. SET. 1 hit.
    [Graphical view]
    PIRSFiPIRSF027717. Histone_H4-K20_mtfrase. 1 hit.
    SMARTiSM00317. SET. 1 hit.
    [Graphical view]
    PROSITEiPS51571. SAM_MT43_PR_SET. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NQR1-1) [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

    MGEGGAAAAL VAAAAAAAAA AAAVVAGQRR RRLGRRARCH GPGRAAGGKM    50
    SKPCAVEAAA AAVAATAPGP EMVERRGPGR PRTDGENVFT GQSKIYSYMS 100
    PNKCSGMRFP LQEENSVTHH EVKCQGKPLA GIYRKREEKR NAGNAVRSAM 150
    KSEEQKIKDA RKGPLVPFPN QKSEAAEPPK TPPSSCDSTN AAIAKQALKK 200
    PIKGKQAPRK KAQGKTQQNR KLTDFYPVRR SSRKSKAELQ SEERKRIDEL 250
    IESGKEEGMK IDLIDGKGRG VIATKQFSRG DFVVEYHGDL IEITDAKKRE 300
    ALYAQDPSTG CYMYYFQYLS KTYCVDATRE TNRLGRLINH SKCGNCQTKL 350
    HDIDGVPHLI LIASRDIAAG EELLYDYGDR SKASIEAHPW LKH 393
    Length:393
    Mass (Da):42,890
    Last modified:November 15, 2002 - v3
    Checksum:i2DCD9B697834B5BD
    GO
    Isoform 2 (identifier: Q9NQR1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: Missing.
         42-57: PGRAAGGKMSKPCAVE → MARGRKMSKPRAVEAA

    Show »
    Length:352
    Mass (Da):39,223
    Checksum:iE0DA1AB9881EE4E6
    GO

    Sequence cautioni

    The sequence AAL40879.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1632KG → RR in AAF97812. 1 PublicationCurated
    Sequence conflicti281 – 2811D → A in AAF97812. 1 PublicationCurated
    Sequence conflicti343 – 3431C → R in AAF97812. 1 PublicationCurated
    Sequence conflicti357 – 3571P → R in AAH50346. (PubMed:15489334)Curated
    Sequence conflicti373 – 3731L → P in AAF97812. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4141Missing in isoform 2. 3 PublicationsVSP_002226Add
    BLAST
    Alternative sequencei42 – 5716PGRAA…PCAVE → MARGRKMSKPRAVEAA in isoform 2. 3 PublicationsVSP_002227Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY064546 mRNA. Translation: AAL40879.1. Different initiation.
    AY102937 mRNA. Translation: AAM47033.1.
    AF287261 mRNA. Translation: AAF97812.2.
    AK292645 mRNA. Translation: BAF85334.1.
    BC050346 mRNA. Translation: AAH50346.1.
    CCDSiCCDS9247.1. [Q9NQR1-2]
    RefSeqiNP_065115.3. NM_020382.3. [Q9NQR1-2]
    UniGeneiHs.443735.
    Hs.572262.

    Genome annotation databases

    EnsembliENST00000330479; ENSP00000332995; ENSG00000183955. [Q9NQR1-2]
    ENST00000402868; ENSP00000384629; ENSG00000183955. [Q9NQR1-2]
    GeneIDi387893.
    KEGGihsa:387893.
    UCSCiuc001uew.3. human. [Q9NQR1-2]

    Polymorphism databases

    DMDMi25091219.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY064546 mRNA. Translation: AAL40879.1 . Different initiation.
    AY102937 mRNA. Translation: AAM47033.1 .
    AF287261 mRNA. Translation: AAF97812.2 .
    AK292645 mRNA. Translation: BAF85334.1 .
    BC050346 mRNA. Translation: AAH50346.1 .
    CCDSi CCDS9247.1. [Q9NQR1-2 ]
    RefSeqi NP_065115.3. NM_020382.3. [Q9NQR1-2 ]
    UniGenei Hs.443735.
    Hs.572262.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZKK X-ray 1.45 A/B/C/D 231-393 [» ]
    2BQZ X-ray 1.50 A/E 233-393 [» ]
    3F9W X-ray 1.60 A/B/C/D 232-393 [» ]
    3F9X X-ray 1.25 A/B/C/D 232-393 [» ]
    3F9Y X-ray 1.50 A/B 232-393 [» ]
    3F9Z X-ray 1.60 A/B/C/D 232-393 [» ]
    4IJ8 X-ray 2.00 A/B 232-393 [» ]
    ProteinModelPortali Q9NQR1.
    SMRi Q9NQR1. Positions 233-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 132490. 25 interactions.
    DIPi DIP-39133N.
    IntActi Q9NQR1. 3 interactions.
    MINTi MINT-3072203.
    STRINGi 9606.ENSP00000332995.

    Chemistry

    BindingDBi Q9NQR1.
    ChEMBLi CHEMBL1795176.
    GuidetoPHARMACOLOGYi 2704.

    PTM databases

    PhosphoSitei Q9NQR1.

    Polymorphism databases

    DMDMi 25091219.

    Proteomic databases

    MaxQBi Q9NQR1.
    PaxDbi Q9NQR1.
    PRIDEi Q9NQR1.

    Protocols and materials databases

    DNASUi 387893.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330479 ; ENSP00000332995 ; ENSG00000183955 . [Q9NQR1-2 ]
    ENST00000402868 ; ENSP00000384629 ; ENSG00000183955 . [Q9NQR1-2 ]
    GeneIDi 387893.
    KEGGi hsa:387893.
    UCSCi uc001uew.3. human. [Q9NQR1-2 ]

    Organism-specific databases

    CTDi 387893.
    GeneCardsi GC12P123868.
    H-InvDB HIX0037637.
    HGNCi HGNC:29489. SETD8.
    HPAi HPA053747.
    MIMi 607240. gene.
    neXtProti NX_Q9NQR1.
    PharmGKBi PA143485616.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOGENOMi HOG000020818.
    HOVERGENi HBG067546.
    InParanoidi Q9NQR1.
    KOi K11428.
    OMAi CSGMRSP.
    OrthoDBi EOG70KGRN.
    PhylomeDBi Q9NQR1.
    TreeFami TF335181.

    Enzyme and pathway databases

    BRENDAi 2.1.1.43. 2681.
    Reactomei REACT_172744. Condensation of Prophase Chromosomes.

    Miscellaneous databases

    EvolutionaryTracei Q9NQR1.
    GeneWikii SETD8.
    GenomeRNAii 387893.
    NextBioi 101711.
    PROi Q9NQR1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NQR1.
    Bgeei Q9NQR1.
    CleanExi HS_SETD8.
    Genevestigatori Q9NQR1.

    Family and domain databases

    InterProi IPR016858. Hist_H4-K20_MeTrfase.
    IPR001214. SET_dom.
    [Graphical view ]
    Pfami PF00856. SET. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF027717. Histone_H4-K20_mtfrase. 1 hit.
    SMARTi SM00317. SET. 1 hit.
    [Graphical view ]
    PROSITEi PS51571. SAM_MT43_PR_SET. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin."
      Nishioka K., Rice J.C., Sarma K., Erdjument-Bromage H., Werner J., Wang Y., Chuikov S., Valenzuela P., Tempst P., Steward R., Lis J.T., Allis C.D., Reinberg D.
      Mol. Cell 9:1201-1213(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 108-131; 220-231 AND 349-393, FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-336.
      Tissue: Cervix carcinoma.
    2. "Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase."
      Fang J., Feng Q., Ketel C.S., Wang H., Cao R., Xia L., Erdjument-Bromage H., Tempst P., Simon J.A., Zhang Y.
      Curr. Biol. 12:1086-1099(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 83-103; 109-134; 141-151; 162-172; 221-230; 245-260; 280-297 AND 350-393, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-340 AND 385-ILE--HIS-393.
    3. "A novel PR/SET domain-containing gene, SET07, as a candidate tumor suppressor."
      Tain F., Huang S.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "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] (ISOFORM 2).
      Tissue: Thymus.
    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] (ISOFORM 2).
      Tissue: Testis.
    6. "Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes."
      Rice J.C., Nishioka K., Sarma K., Steward R., Reinberg D., Allis C.D.
      Genes Dev. 16:2225-2230(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    7. "A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1."
      Julien E., Herr W.
      Mol. Cell 14:713-725(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    8. "SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20."
      Yin Y., Liu C., Tsai S.N., Zhou B., Ngai S.M., Zhu G.
      J. Biol. Chem. 280:30025-30031(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    9. "A trans-tail histone code defined by monomethylated H4 Lys-20 and H3 Lys-9 demarcates distinct regions of silent chromatin."
      Sims J.K., Houston S.I., Magazinnik T., Rice J.C.
      J. Biol. Chem. 281:12760-12766(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Modulation of p53 function by SET8-mediated methylation at lysine 382."
      Shi X., Kachirskaia I., Yamaguchi H., West L.E., Wen H., Wang E.W., Dutta S., Appella E., Gozani O.
      Mol. Cell 27:636-646(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-379.
    11. "Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1."
      Kalakonda N., Fischle W., Boccuni P., Gurvich N., Hoya-Arias R., Zhao X., Miyata Y., Macgrogan D., Zhang J., Sims J.K., Rice J.C., Nimer S.D.
      Oncogene 27:4293-4304(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH L3MBTL1.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "The MBT repeats of L3MBTL1 link SET8-mediated p53 methylation at lysine 382 to target gene repression."
      West L.E., Roy S., Lachmi-Weiner K., Hayashi R., Shi X., Appella E., Kutateladze T.G., Gozani O.
      J. Biol. Chem. 285:37725-37732(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-379.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation."
      Serrano L., Martinez-Redondo P., Marazuela-Duque A., Vazquez B.N., Dooley S.J., Voigt P., Beck D.B., Kane-Goldsmith N., Tong Q., Rabanal R.M., Fondevila D., Munoz P., Kruger M., Tischfield J.A., Vaquero A.
      Genes Dev. 27:639-653(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-172, DEACETYLATION AT LYS-172 BY SIRT2, INTERACTION WITH SIRT2, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-172, MASS SPECTROMETRY (ISOFORM 2).
    16. "CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration."
      Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.
      Mol. Cell 49:1147-1158(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, UBIQUITINATION, MUTAGENESIS OF ARG-336 AND ASP-379.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 233-393 IN COMPLEX WITH HISTONE H4 AND S-ADENOSYLMETHIONINE, FUNCTION.
    18. "Structural and functional analysis of SET8, a histone H4 'Lys-20' methyltransferase."
      Couture J.-F., Collazo E., Brunzelle J.S., Trievel R.C.
      Genes Dev. 19:1455-1465(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 231-393 IN COMPLEX WITH HISTONE H4 AND S-ADENOSYLMETHIONINE, FUNCTION, MUTAGENESIS OF TYR-286; GLU-300; CYS-311; TYR-375; ASP-379 AND HIS-388.

    Entry informationi

    Entry nameiSETD8_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQR1
    Secondary accession number(s): A8K9D0, Q86W83, Q8TD09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: November 15, 2002
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 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

    Caution

    It is uncertain whether Met-1 or Met-72 is the initiator.Curated

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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