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O54864

- SUV91_MOUSE

UniProt

O54864 - SUV91_MOUSE

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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

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 methyltransferase activity Source: MGI
  5. transcription regulatory region sequence-specific DNA binding Source: UniProtKB
  6. 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
Complete GO annotation...

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-KW
  3. heterochromatin Source: UniProtKB
  4. nuclear heterochromatin Source: MGI
  5. nucleus Source: UniProtKB
  6. rDNA heterochromatin Source: Ensembl
Complete GO annotation...

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

MaxQBiO54864.
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

BgeeiO54864.
ExpressionAtlasiO54864. baseline and differential.
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.
GeneTreeiENSGT00760000118855.
HOGENOMiHOG000231244.
HOVERGENiHBG055621.
InParanoidiO54864.
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

        10         20         30         40         50
MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGVSKKNL YDFEVEYLCD
60 70 80 90 100
YKKIREQEYY LVKWRGYPDS ENTWEPRQNL KCIRVLKQFH KDLERELVRR
110 120 130 140 150
HRRSKPPRHL DPNLANYLVQ KAKQRRALQR WEQELNAKRS HLGRITVENE
160 170 180 190 200
VDLDGPPRSF VYINEYRVGE GITLNQVAVG CECQDCLLAP TGGCCPGASL
210 220 230 240 250
HKFAYNDQGQ VRLKAGQPIY ECNSRCCCGY DCPNRVVQKG IRYDLCIFRT
260 270 280 290 300
NDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD
310 320 330 340 350
LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF
360 370 380 390 400
ATRTIWAGEE LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC
410
KCGTTACRKY LF
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

MaxQBi O54864.
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 ENSGT00760000118855.
HOGENOMi HOG000231244.
HOVERGENi HBG055621.
InParanoidi O54864.
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

Bgeei O54864.
ExpressionAtlasi O54864. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 139 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