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Q6Q783

- SV422_MOUSE

UniProt

Q6Q783 - SV422_MOUSE

Protein

Histone-lysine N-methyltransferase SUV420H2

Gene

Suv420h2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2).1 Publication

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. histone methyltransferase activity (H4-K20 specific) Source: MGI

    GO - Biological processi

    1. histone H4-K20 trimethylation Source: InterPro
    2. histone methylation Source: MGI
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase SUV420H2 (EC:2.1.1.43)
    Alternative name(s):
    Suppressor of variegation 4-20 homolog 2
    Short name:
    Su(var)4-20 homolog 2
    Short name:
    Suv4-20h2
    Gene namesi
    Name:Suv420h2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:2385262. Suv420h2.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication
    Note: Associated with pericentric heterochromatin. CBX1 and CBX5 are required for the localization to pericentric heterochromatin.

    GO - Cellular componenti

    1. condensed nuclear chromosome, centromeric region Source: MGI
    2. nuclear heterochromatin Source: Ensembl

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 468468Histone-lysine N-methyltransferase SUV420H2PRO_0000281794Add
    BLAST

    Proteomic databases

    PaxDbiQ6Q783.
    PRIDEiQ6Q783.

    PTM databases

    PhosphoSiteiQ6Q783.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6Q783.
    BgeeiQ6Q783.
    GenevestigatoriQ6Q783.

    Interactioni

    Subunit structurei

    Interacts with HP1 proteins CBX1, CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2.3 Publications

    Protein-protein interaction databases

    BioGridi231299. 3 interactions.
    STRINGi10090.ENSMUSP00000104224.

    Structurei

    Secondary structure

    1
    468
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 2114
    Helixi23 – 275
    Helixi45 – 5814
    Helixi61 – 688
    Helixi74 – 774
    Turni78 – 814
    Helixi83 – 9917
    Helixi102 – 1043
    Beta strandi106 – 1116
    Beta strandi118 – 12710
    Beta strandi134 – 14411
    Helixi147 – 1526
    Turni155 – 1573
    Beta strandi160 – 1656
    Turni166 – 1694
    Beta strandi170 – 1767
    Helixi177 – 1804
    Beta strandi188 – 1936
    Beta strandi195 – 20511
    Turni219 – 2224
    Helixi232 – 2376
    Helixi240 – 2434

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AU7X-ray2.07A/B1-246[»]
    ProteinModelPortaliQ6Q783.
    SMRiQ6Q783. Positions 4-246.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini104 – 218115SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni348 – 44194Required for heterochromatin localizationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar4-20 subfamily.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG240704.
    GeneTreeiENSGT00520000055640.
    HOGENOMiHOG000154453.
    HOVERGENiHBG095676.
    InParanoidiQ6Q783.
    KOiK11429.
    OMAiFCAACQP.
    OrthoDBiEOG7MKW6P.
    PhylomeDBiQ6Q783.
    TreeFamiTF106433.

    Family and domain databases

    InterProiIPR025790. Hist-Lys_N-MTase_Suvar4-20.
    IPR001214. SET_dom.
    [Graphical view]
    PfamiPF00856. SET. 1 hit.
    [Graphical view]
    SMARTiSM00317. SET. 1 hit.
    [Graphical view]
    PROSITEiPS51570. SAM_MT43_SUVAR420_2. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6Q783-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPDRVTARE LCENDDLATS LVLDPYLGFR THKMNVSPVP TLRRQHHLRS    50
    ALEAFLRQRD LEAAFRALTL GGWMAHYFQS RAPRQEAALK THIFCYLRAF 100
    LPESGFTILP CTRYSMETNG AKIVSTRAWK KNEKLELLVG CIAELREEDE 150
    DLLRAGENDF SIMYSTRKRS AQLWLGPAAF INHDCKPNCK FVPSDGNTAC 200
    VKVLRDIEPG DEVTCFYGEG FFGEKNEHCE CYTCERKGEG AFRLQPREPE 250
    LRPKPLDKYE LRETKRRLQQ GLVSSQQSLM SRWACSHLSP LRPDPFCAAC 300
    QPSCLLPASP HMDYLPLWLQ RAPQPQPIVP PRKRHRRRRP RIRQASLPPV 350
    LRTACVPLHR WGGCGPHCQL RAEAMVTLHL RPQTRWTPQQ DWYWARRYGL 400
    PSVGRVELTR LAPALPAAPA PAGNPGPVPT PDFIPKQALA FAPFCPPKRL 450
    RLVVSHGSID LDINSGEP 468
    Length:468
    Mass (Da):53,159
    Last modified:July 5, 2004 - v1
    Checksum:iD43D7A25DBDF3BB1
    GO

    Sequence cautioni

    The sequence AAH24816.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH85473.2 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY555193 mRNA. Translation: AAT00540.1.
    AK154848 mRNA. Translation: BAE32874.1.
    BC024816 mRNA. Translation: AAH24816.1. Different initiation.
    BC085473 mRNA. Translation: AAH85473.2. Different initiation.
    CCDSiCCDS20743.2.
    RefSeqiNP_001108490.1. NM_001115018.1.
    NP_666289.2. NM_146177.2.
    XP_006539836.1. XM_006539773.1.
    XP_006539837.1. XM_006539774.1.
    UniGeneiMm.247844.

    Genome annotation databases

    EnsembliENSMUST00000098853; ENSMUSP00000096452; ENSMUSG00000059851.
    ENSMUST00000108582; ENSMUSP00000104223; ENSMUSG00000059851.
    ENSMUST00000108583; ENSMUSP00000104224; ENSMUSG00000059851.
    GeneIDi232811.
    KEGGimmu:232811.
    UCSCiuc009eyi.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY555193 mRNA. Translation: AAT00540.1 .
    AK154848 mRNA. Translation: BAE32874.1 .
    BC024816 mRNA. Translation: AAH24816.1 . Different initiation.
    BC085473 mRNA. Translation: AAH85473.2 . Different initiation.
    CCDSi CCDS20743.2.
    RefSeqi NP_001108490.1. NM_001115018.1.
    NP_666289.2. NM_146177.2.
    XP_006539836.1. XM_006539773.1.
    XP_006539837.1. XM_006539774.1.
    UniGenei Mm.247844.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4AU7 X-ray 2.07 A/B 1-246 [» ]
    ProteinModelPortali Q6Q783.
    SMRi Q6Q783. Positions 4-246.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 231299. 3 interactions.
    STRINGi 10090.ENSMUSP00000104224.

    PTM databases

    PhosphoSitei Q6Q783.

    Proteomic databases

    PaxDbi Q6Q783.
    PRIDEi Q6Q783.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000098853 ; ENSMUSP00000096452 ; ENSMUSG00000059851 .
    ENSMUST00000108582 ; ENSMUSP00000104223 ; ENSMUSG00000059851 .
    ENSMUST00000108583 ; ENSMUSP00000104224 ; ENSMUSG00000059851 .
    GeneIDi 232811.
    KEGGi mmu:232811.
    UCSCi uc009eyi.2. mouse.

    Organism-specific databases

    CTDi 84787.
    MGIi MGI:2385262. Suv420h2.

    Phylogenomic databases

    eggNOGi NOG240704.
    GeneTreei ENSGT00520000055640.
    HOGENOMi HOG000154453.
    HOVERGENi HBG095676.
    InParanoidi Q6Q783.
    KOi K11429.
    OMAi FCAACQP.
    OrthoDBi EOG7MKW6P.
    PhylomeDBi Q6Q783.
    TreeFami TF106433.

    Miscellaneous databases

    ChiTaRSi SUV420H2. mouse.
    NextBioi 381246.
    PROi Q6Q783.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6Q783.
    Bgeei Q6Q783.
    Genevestigatori Q6Q783.

    Family and domain databases

    InterProi IPR025790. Hist-Lys_N-MTase_Suvar4-20.
    IPR001214. SET_dom.
    [Graphical view ]
    Pfami PF00856. SET. 1 hit.
    [Graphical view ]
    SMARTi SM00317. SET. 1 hit.
    [Graphical view ]
    PROSITEi PS51570. SAM_MT43_SUVAR420_2. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin."
      Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., Reinberg D., Jenuwein T.
      Genes Dev. 18:1251-1262(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CBX1; CBX3 AND CBX5.
      Strain: FVB/N.
    2. "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: NOD.
      Tissue: Dendritic cell.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain and Eye.
    4. "Role of the RB1 family in stabilizing histone methylation at constitutive heterochromatin."
      Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M., Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T., Blasco M.A.
      Nat. Cell Biol. 7:420-428(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RB1; RBL1 AND RBL2.
    5. Cited for: INTERACTION WITH RB1; RBL1 AND RBL2.

    Entry informationi

    Entry nameiSV422_MOUSE
    AccessioniPrimary (citable) accession number: Q6Q783
    Secondary accession number(s): Q5RKP6, Q8R1C5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3