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O54864

- SUV91_MOUSE

UniProt

O54864 - SUV91_MOUSE

Protein

Histone-lysine N-methyltransferase SUV39H1

Gene

Suv39h1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD+/NADP+ ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.7 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Negatively regulated by CCAR2.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi181 – 1811Zinc 1By similarity
    Metal bindingi181 – 1811Zinc 2By similarity
    Metal bindingi183 – 1831Zinc 1By similarity
    Metal bindingi186 – 1861Zinc 1By similarity
    Metal bindingi186 – 1861Zinc 3By similarity
    Metal bindingi194 – 1941Zinc 1By similarity
    Metal bindingi195 – 1951Zinc 1By similarity
    Metal bindingi195 – 1951Zinc 2By similarity
    Metal bindingi222 – 2221Zinc 2By similarity
    Metal bindingi222 – 2221Zinc 3By similarity
    Metal bindingi226 – 2261Zinc 2By similarity
    Metal bindingi228 – 2281Zinc 3By similarity
    Metal bindingi232 – 2321Zinc 3By similarity
    Binding sitei297 – 2971S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi326 – 3261Zinc 4By similarity
    Metal bindingi400 – 4001Zinc 4By similarity
    Metal bindingi402 – 4021Zinc 4By similarity
    Metal bindingi407 – 4071Zinc 4By similarity

    GO - Molecular functioni

    1. histone-lysine N-methyltransferase activity Source: UniProtKB
    2. histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
    3. methyltransferase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein methyltransferase activity Source: MGI
    6. transcription regulatory region sequence-specific DNA binding Source: UniProtKB
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW
    3. chromatin silencing Source: UniProtKB
    4. chromatin silencing at rDNA Source: Ensembl
    5. DNA packaging Source: MGI
    6. histone H3-K9 dimethylation Source: UniProtKB
    7. histone H3-K9 methylation Source: MGI
    8. histone H3-K9 trimethylation Source: UniProtKB
    9. histone lysine methylation Source: MGI
    10. negative regulation of circadian rhythm Source: UniProtKB
    11. negative regulation of transcription, DNA-templated Source: UniProtKB
    12. rhythmic process Source: UniProtKB-KW
    13. rRNA processing Source: UniProtKB-KW
    14. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    Biological rhythms, Cell cycle, Differentiation, rRNA processing, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, S-adenosyl-L-methionine, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_224328. SIRT1 negatively regulates rRNA Expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase SUV39H1 (EC:2.1.1.43)
    Alternative name(s):
    Histone H3-K9 methyltransferase 1
    Short name:
    H3-K9-HMTase 1
    Position-effect variegation 3-9 homolog
    Suppressor of variegation 3-9 homolog 1
    Short name:
    Su(var)3-9 homolog 1
    Gene namesi
    Name:Suv39h1
    Synonyms:Suv39h
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1099440. Suv39h1.

    Subcellular locationi

    Nucleus. Nucleus lamina By similarity. Nucleusnucleoplasm By similarity. Chromosomecentromere
    Note: Associates with centromeric constitutive heterochromatin.

    GO - Cellular componenti

    1. chromatin silencing complex Source: UniProtKB
    2. chromosome, centromeric region Source: UniProtKB-SubCell
    3. heterochromatin Source: UniProtKB
    4. nuclear heterochromatin Source: MGI
    5. nuclear lamina Source: UniProtKB-SubCell
    6. nucleoplasm Source: UniProtKB-SubCell
    7. nucleus Source: UniProtKB
    8. rDNA heterochromatin Source: Ensembl

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice lacking Suv39h1 and Suv39h2 display severely impaired viability and chromosomal instabilities that are associated with an increased tumor risk and perturbed chromosome interactions during male meiosis. They also show a higher level of histone H3 with phosphorylated 'Ser-10' and a reduced number of cells in G1 phase and an increased portion of cells with aberrant nuclear morphologies.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 412412Histone-lysine N-methyltransferase SUV39H1PRO_0000186058Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei266 – 2661N6-acetyllysineBy similarity
    Modified residuei391 – 3911Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on serine residues, and to a lesser degree, on threonine residues.By similarity
    Acetylated at Lys-266, leading to inhibition of enzyme activity. SIRT1-mediated deacetylation relieves this inhibition By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiO54864.

    PTM databases

    PhosphoSiteiO54864.

    Expressioni

    Tissue specificityi

    Widely expressed.2 Publications

    Developmental stagei

    Expression present throughout embryogenesis. Higher expression between E9.5 and E13.

    Gene expression databases

    ArrayExpressiO54864.
    BgeeiO54864.
    GenevestigatoriO54864.

    Interactioni

    Subunit structurei

    Interacts with CCAR2 and GFI1B. Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8 By similarity. Interacts with H3 and H4 histones. Interacts with DNMT3B, CBX1, CBX4, MBD1, RUNX1, RUNX3, MYOD1, SMAD5 and RB1. Interacts with SBF1 through the SET domain. Interacts with HDAC1 and HDAC2 through the N-terminus and associates with the core histone deacetylase complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. Interacts (via SET domain) with MECOM; enhances MECOM transcriptional repression activity. Interacts with LMNA; the interaction increases stability of SUV39H1. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Gfi1bO702372EBI-302230,EBI-4287943
    Myod1P100853EBI-302230,EBI-4405734
    SIRT1Q96EB64EBI-302230,EBI-1802965From a different organism.

    Protein-protein interaction databases

    BioGridi203586. 1 interaction.
    DIPiDIP-32590N.
    IntActiO54864. 5 interactions.
    MINTiMINT-256025.

    Structurei

    3D structure databases

    ProteinModelPortaliO54864.
    SMRiO54864. Positions 44-100, 115-411.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 10159ChromoPROSITE-ProRule annotationAdd
    BLAST
    Domaini179 – 24062Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini243 – 366124SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini396 – 41217Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 8989Interaction with SIRT1Add
    BLAST
    Regioni254 – 2563S-adenosyl-L-methionine bindingBy similarity
    Regioni255 – 377123Mediates interaction with MECOMAdd
    BLAST
    Regioni323 – 3242S-adenosyl-L-methionine bindingBy similarity

    Domaini

    Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates to stable binding to heterochromatin.
    In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.By similarity

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
    Contains 1 chromo domain.PROSITE-ProRule annotation
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 pre-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2940.
    GeneTreeiENSGT00750000117355.
    HOGENOMiHOG000231244.
    HOVERGENiHBG055621.
    KOiK11419.
    OrthoDBiEOG7RJPR0.
    TreeFamiTF106452.

    Family and domain databases

    InterProiIPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    IPR011381. Histone_H3-K9_MeTrfase.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    [Graphical view]
    PfamiPF00385. Chromo. 1 hit.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view]
    PIRSFiPIRSF009343. SUV39_SET. 1 hit.
    SMARTiSM00298. CHROMO. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00468. PreSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view]
    SUPFAMiSSF54160. SSF54160. 1 hit.
    PROSITEiPS00598. CHROMO_1. 1 hit.
    PS50013. CHROMO_2. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50867. PRE_SET. 1 hit.
    PS51579. SAM_MT43_SUVAR39_3. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O54864-1) [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

    MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGVSKKNL YDFEVEYLCD    50
    YKKIREQEYY LVKWRGYPDS ENTWEPRQNL KCIRVLKQFH KDLERELVRR 100
    HRRSKPPRHL DPNLANYLVQ KAKQRRALQR WEQELNAKRS HLGRITVENE 150
    VDLDGPPRSF VYINEYRVGE GITLNQVAVG CECQDCLLAP TGGCCPGASL 200
    HKFAYNDQGQ VRLKAGQPIY ECNSRCCCGY DCPNRVVQKG IRYDLCIFRT 250
    NDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD 300
    LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF 350
    ATRTIWAGEE LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC 400
    KCGTTACRKY LF 412
    Length:412
    Mass (Da):47,754
    Last modified:June 1, 1998 - v1
    Checksum:i6B690F4FE7FD997C
    GO
    Isoform 2 (identifier: O54864-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MAENLK → LKEKVAATRGKRRLSVTVTLSVSTGDAGRGGRSGTDPLLKMGEPATL

    Note: Incomplete sequence.Curated

    Show »
    Length:453
    Mass (Da):51,889
    Checksum:i64BE15984279410B
    GO
    Isoform 3 (identifier: O54864-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         277-286: IITSEEAERR → VPPGCYLLGK
         287-412: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:286
    Mass (Da):33,111
    Checksum:iE1BEB67AD19032E1
    GO

    Sequence cautioni

    Isoform 2 : The sequence AAF60970.1 differs from that shown. Reason: Frameshift at position 35.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti364 – 3641D → G in BAC40334. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 66MAENLK → LKEKVAATRGKRRLSVTVTL SVSTGDAGRGGRSGTDPLLK MGEPATL in isoform 2. CuratedVSP_002208
    Alternative sequencei277 – 28610IITSEEAERR → VPPGCYLLGK in isoform 3. 1 PublicationVSP_024029
    Alternative sequencei287 – 412126Missing in isoform 3. 1 PublicationVSP_024030Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF019969 mRNA. Translation: AAB92225.1.
    AF193861 mRNA. Translation: AAF60969.1.
    AF193862 mRNA. Translation: AAF60970.1. Frameshift.
    AK088405 mRNA. Translation: BAC40334.1.
    AK139757 mRNA. Translation: BAE24129.1.
    AK169389 mRNA. Translation: BAE41136.1.
    AL663032 Genomic DNA. Translation: CAM19494.1.
    AL663032 Genomic DNA. Translation: CAM19495.1.
    BC023860 mRNA. Translation: AAH23860.1.
    AF149203 Genomic DNA. Translation: AAF73151.1.
    CCDSiCCDS40846.1. [O54864-1]
    RefSeqiNP_001277645.1. NM_001290716.1.
    NP_035644.1. NM_011514.2. [O54864-1]
    UniGeneiMm.479743.
    Mm.9244.

    Genome annotation databases

    EnsembliENSMUST00000115636; ENSMUSP00000111299; ENSMUSG00000039231. [O54864-3]
    ENSMUST00000115638; ENSMUSP00000111301; ENSMUSG00000039231. [O54864-1]
    GeneIDi20937.
    KEGGimmu:20937.
    UCSCiuc009snq.2. mouse. [O54864-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF019969 mRNA. Translation: AAB92225.1 .
    AF193861 mRNA. Translation: AAF60969.1 .
    AF193862 mRNA. Translation: AAF60970.1 . Frameshift.
    AK088405 mRNA. Translation: BAC40334.1 .
    AK139757 mRNA. Translation: BAE24129.1 .
    AK169389 mRNA. Translation: BAE41136.1 .
    AL663032 Genomic DNA. Translation: CAM19494.1 .
    AL663032 Genomic DNA. Translation: CAM19495.1 .
    BC023860 mRNA. Translation: AAH23860.1 .
    AF149203 Genomic DNA. Translation: AAF73151.1 .
    CCDSi CCDS40846.1. [O54864-1 ]
    RefSeqi NP_001277645.1. NM_001290716.1.
    NP_035644.1. NM_011514.2. [O54864-1 ]
    UniGenei Mm.479743.
    Mm.9244.

    3D structure databases

    ProteinModelPortali O54864.
    SMRi O54864. Positions 44-100, 115-411.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203586. 1 interaction.
    DIPi DIP-32590N.
    IntActi O54864. 5 interactions.
    MINTi MINT-256025.

    PTM databases

    PhosphoSitei O54864.

    Proteomic databases

    PRIDEi O54864.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000115636 ; ENSMUSP00000111299 ; ENSMUSG00000039231 . [O54864-3 ]
    ENSMUST00000115638 ; ENSMUSP00000111301 ; ENSMUSG00000039231 . [O54864-1 ]
    GeneIDi 20937.
    KEGGi mmu:20937.
    UCSCi uc009snq.2. mouse. [O54864-1 ]

    Organism-specific databases

    CTDi 6839.
    MGIi MGI:1099440. Suv39h1.

    Phylogenomic databases

    eggNOGi COG2940.
    GeneTreei ENSGT00750000117355.
    HOGENOMi HOG000231244.
    HOVERGENi HBG055621.
    KOi K11419.
    OrthoDBi EOG7RJPR0.
    TreeFami TF106452.

    Enzyme and pathway databases

    Reactomei REACT_224328. SIRT1 negatively regulates rRNA Expression.

    Miscellaneous databases

    NextBioi 299879.
    PROi O54864.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O54864.
    Bgeei O54864.
    Genevestigatori O54864.

    Family and domain databases

    InterProi IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    IPR011381. Histone_H3-K9_MeTrfase.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    [Graphical view ]
    Pfami PF00385. Chromo. 1 hit.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF009343. SUV39_SET. 1 hit.
    SMARTi SM00298. CHROMO. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00468. PreSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54160. SSF54160. 1 hit.
    PROSITEi PS00598. CHROMO_1. 1 hit.
    PS50013. CHROMO_2. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50867. PRE_SET. 1 hit.
    PS51579. SAM_MT43_SUVAR39_3. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31."
      Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G., Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G., Jenuwein T.
      EMBO J. 18:1923-1938(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH CBX1.
      Tissue: Brain.
    2. "Molecular and genetic analysis of the mouse homolog of the Drosophila suppressor of position-effect variegation 3-9 gene."
      Bultman S., Magnuson T.
      Mamm. Genome 11:251-254(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Embryo.
    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] (ISOFORMS 1 AND 3).
      Strain: C57BL/6J and NOD.
      Tissue: Egg, Liver and Thymus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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 1).
      Strain: FVB/N.
      Tissue: Mammary gland.
    6. "Isolation and characterization of Suv39h2, a second histone H3 methyltransferase gene that displays testis-specific expression."
      O'Carroll D., Scherthan H., Peters A.H.F.M., Opravil S., Haynes A.R., Laible G., Rea S., Schmid M., Lebersorger A., Jerratsch M., Sattler L., Mattei M.-G., Denny P., Brown S.D.M., Schweizer D., Jenuwein T.
      Mol. Cell. Biol. 20:9423-9433(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-276, TISSUE SPECIFICITY.
      Strain: C57BL/6J.
    7. "Regulation of chromatin structure by site-specific histone H3 methyltransferases."
      Rea S., Eisenhaber F., O'Carroll D., Strahl B.D., Sun Z.-W., Schmid M., Opravil S., Mechtler K., Ponting C.P., Allis C.D., Jenuwein T.
      Nature 406:593-599(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY.
    8. "Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability."
      Peters A.H.F.M., O'Carroll D., Scherthan H., Mechtler K., Sauer S., Schofer C., Weipoltshammer K., Pagani M., Lachner M., Kohlmaier A., Opravil S., Doyle M., Sibilia M., Jenuwein T.
      Cell 107:323-337(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    9. "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases."
      Vaute O., Nicolas E., Vandel L., Trouche D.
      Nucleic Acids Res. 30:475-481(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HISTONE DEACETYLASE COMPLEX.
    10. "Suv39h-mediated histone H3 lysine 9 methylation directs DNA methylation to major satellite repeats at pericentric heterochromatin."
      Lehnertz B., Ueda Y., Derijck A.A.H.A., Braunschweig U., Perez-Burgos L., Kubicek S., Chen T., Li E., Jenuwein T., Peters A.H.F.M.
      Curr. Biol. 13:1192-1200(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DNMT3B.
    11. Cited for: FUNCTION.
    12. "Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains."
      Rice J.C., Briggs S.D., Ueberheide B., Barber C.M., Shabanowitz J., Hunt D.F., Shinkai Y., Allis C.D.
      Mol. Cell 12:1591-1598(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Epigenetic regulation of telomere length in mammalian cells by the Suv39h1 and Suv39h2 histone methyltransferases."
      Garcia-Cao M., O'Sullivan R., Peters A.H.F.M., Jenuwein T., Blasco M.A.
      Nat. Genet. 36:94-99(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation."
      Vaquero A., Scher M., Erdjument-Bromage H., Tempst P., Serrano L., Reinberg D.
      Nature 450:440-444(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model."
      Liu B., Wang Z., Zhang L., Ghosh S., Zheng H., Zhou Z.
      Nat. Commun. 4:1868-1868(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LMNA.
    17. "A novel interaction between the proto-oncogene Evi1 and histone methyltransferases, SUV39H1 and G9a."
      Spensberger D., Delwel R.
      FEBS Lett. 582:2761-2767(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MECOM.
    18. "Temporal orchestration of repressive chromatin modifiers by circadian clock Period complexes."
      Duong H.A., Weitz C.J.
      Nat. Struct. Mol. Biol. 21:126-132(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN RHYTHMS, IDENTIFIACTION IN A LARGE PER COMPLEX.

    Entry informationi

    Entry nameiSUV91_MOUSE
    AccessioniPrimary (citable) accession number: O54864
    Secondary accession number(s): Q3TEW2
    , Q3UT51, Q8C2L3, Q9JLC7, Q9JLP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 138 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

    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