O54864 (SUV91_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Suv39h1
Synonyms:	Suv39h

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.7
Enzyme regulation	Negatively regulated by KIAA1967/DBC1 By similarity.
Subunit structure	Interacts with KIAA1967/DBC1 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. Ref.1 Ref.9 Ref.10 Ref.15
Subcellular location	Nucleus. Chromosome › centromere. Note: Associates with centromeric constitutive heterochromatin. Ref.1 Ref.14
Tissue specificity	Widely expressed. Ref.1 Ref.6
Developmental stage	Expression present throughout embryogenesis. Higher expression between E9.5 and E13.
Domain	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.
Post-translational modification	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.
Disruption phenotype	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. Ref.8
Sequence similarities	Belongs to the histone-lysine methyltransferase family. Suvar3-9 subfamily. Contains 1 chromo domain. Contains 1 post-SET domain. Contains 1 pre-SET domain. Contains 1 SET domain.
Sequence caution	Isoform 2: The sequence AAF60970.1 differs from that shown. Reason: Frameshift at position 35.

Ontologies

Keywords
Biological process	Cell cycle Differentiation Transcription Transcription regulation rRNA processing
Cellular component	Centromere Chromosome Nucleus
Coding sequence diversity	Alternative splicing
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Repressor Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA packaging Traceable author statement Ref.6. Source: MGI cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW chromatin silencing Traceable author statement Ref.9. Source: UniProtKB chromatin silencing at rDNA Inferred from electronic annotation. Source: Compara rRNA processing Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromatin silencing complex Inferred from direct assay Ref.9. Source: UniProtKB chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear heterochromatin Traceable author statement Ref.6. Source: MGI rDNA heterochromatin Inferred from electronic annotation. Source: Compara
Molecular_function	histone methyltransferase activity (H3-K9 specific) Inferred from direct assay Ref.14. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SIRT1	Q96EB6	4	EBI-302230,EBI-1802965	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O54864-1)

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.

Isoform 2 (identifier: O54864-2)

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

Note: Incomplete sequence.

Isoform 3 (identifier: O54864-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 412	412	Histone-lysine N-methyltransferase SUV39H1		PRO_0000186058
Regions
	Domain	43 – 101	59	Chromo
	Domain	179 – 240	62	Pre-SET
	Domain	242 – 370	129	SET
	Domain	396 – 412	17	Post-SET
	Region	1 – 89	89	Interaction with SIRT1
	Region	255 – 377	123	Mediates interaction with MECOM
Amino acid modifications
	Modified residue	266	1	N6-acetyllysine By similarity
	Modified residue	391	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 6	6	MAENLK → LKEKVAATRGKRRLSVTVTL SVSTGDAGRGGRSGTDPLLK MGEPATL in isoform 2.		VSP_002208
	Alternative sequence	277 – 286	10	IITSEEAERR → VPPGCYLLGK in isoform 3.		VSP_024029
	Alternative sequence	287 – 412	126	Missing in isoform 3.		VSP_024030
Experimental info
	Sequence conflict	364	1	D → G in BAC40334. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 6B690F4FE7FD997C	FASTA	412	47,754
	10 20 30 40 50 60 MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGVSKKNL YDFEVEYLCD YKKIREQEYY 70 80 90 100 110 120 LVKWRGYPDS ENTWEPRQNL KCIRVLKQFH KDLERELVRR HRRSKPPRHL DPNLANYLVQ 130 140 150 160 170 180 KAKQRRALQR WEQELNAKRS HLGRITVENE VDLDGPPRSF VYINEYRVGE GITLNQVAVG 190 200 210 220 230 240 CECQDCLLAP TGGCCPGASL HKFAYNDQGQ VRLKAGQPIY ECNSRCCCGY DCPNRVVQKG 250 260 270 280 290 300 IRYDLCIFRT NDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD 310 320 330 340 350 360 LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF ATRTIWAGEE 370 380 390 400 410 LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC KCGTTACRKY LF
	Isoform 2 [UniParc]. Checksum: 64BE15984279410B	FASTA	453	51,889
	10 20 30 40 50 60 LKEKVAATRG KRRLSVTVTL SVSTGDAGRG GRSGTDPLLK MGEPATLGCS VCCKSSWNQL 70 80 90 100 110 120 QDLCRLAKLS CPALGVSKKN LYDFEVEYLC DYKKIREQEY YLVKWRGYPD SENTWEPRQN 130 140 150 160 170 180 LKCIRVLKQF HKDLERELVR RHRRSKPPRH LDPNLANYLV QKAKQRRALQ RWEQELNAKR 190 200 210 220 230 240 SHLGRITVEN EVDLDGPPRS FVYINEYRVG EGITLNQVAV GCECQDCLLA PTGGCCPGAS 250 260 270 280 290 300 LHKFAYNDQG QVRLKAGQPI YECNSRCCCG YDCPNRVVQK GIRYDLCIFR TNDGRGWGVR 310 320 330 340 350 360 TLEKIRKNSF VMEYVGEIIT SEEAERRGQI YDRQGATYLF DLDYVEDVYT VDAAYYGNIS 370 380 390 400 410 420 HFVNHSCDPN LQVYNVFIDN LDERLPRIAF FATRTIWAGE ELTFDYNMQV DPVDMESTRM 430 440 450 DSNFGLAGLP GSPKKRVRIE CKCGTTACRK YLF
	Isoform 3 [UniParc]. Checksum: E1BEB67AD19032E1	FASTA	286	33,111
	10 20 30 40 50 60 MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGVSKKNL YDFEVEYLCD YKKIREQEYY 70 80 90 100 110 120 LVKWRGYPDS ENTWEPRQNL KCIRVLKQFH KDLERELVRR HRRSKPPRHL DPNLANYLVQ 130 140 150 160 170 180 KAKQRRALQR WEQELNAKRS HLGRITVENE VDLDGPPRSF VYINEYRVGE GITLNQVAVG 190 200 210 220 230 240 CECQDCLLAP TGGCCPGASL HKFAYNDQGQ VRLKAGQPIY ECNSRCCCGY DCPNRVVQKG 250 260 270 280 IRYDLCIFRT NDGRGWGVRT LEKIRKNSFV MEYVGEVPPG CYLLGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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]	"Partitioning and plasticity of repressive histone methylation states in mammalian chromatin." Peters A.H.F.M., Kubicek S., Mechtler K., O'Sullivan R.J., Derijck A.A., Perez-Burgos L., Kohlmaier A., Opravil S., Tachibana M., Shinkai Y., Martens J.H.A., Jenuwein T. Mol. Cell 12:1577-1589(2003) [PubMed] [Europe PMC] [Abstract] 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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00124116. IPI00776368. IPI00970272.
RefSeq	NP_035644.1. NM_011514.2.
UniGene	Mm.479743. Mm.9244.
3D structure databases
ProteinModelPortal	O54864.
SMR	O54864. Positions 44-100, 115-411.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32590N.
IntAct	O54864. 8 interactions.
MINT	MINT-256025.
PTM databases
PhosphoSite	O54864.
Proteomic databases
PRIDE	O54864.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000115636; ENSMUSP00000111299; ENSMUSG00000039231. ENSMUST00000115638; ENSMUSP00000111301; ENSMUSG00000039231.
GeneID	20937.
KEGG	mmu:20937.
UCSC	uc009snq.2. mouse.
Organism-specific databases
CTD	6839.
MGI	MGI:1099440. Suv39h1.
Phylogenomic databases
eggNOG	COG2940.
GeneTree	ENSGT00690000101898.
HOGENOM	HOG000231244.
HOVERGEN	HBG055621.
KO	K11419.
OrthoDB	EOG4SXNCF.
Gene expression databases
ArrayExpress	O54864.
Bgee	O54864.
Genevestigator	O54864.
GermOnline	ENSMUSG00000039231. Mus musculus.
Family and domain databases
InterPro	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]
Pfam	PF00385. Chromo. 1 hit. PF05033. Pre-SET. 1 hit. PF00856. SET. 1 hit. [Graphical view]
PIRSF	PIRSF009343. SUV39_SET. 1 hit.
SMART	SM00298. CHROMO. 1 hit. SM00508. PostSET. 1 hit. SM00468. PreSET. 1 hit. SM00317. SET. 1 hit. [Graphical view]
SUPFAM	SSF54160. Chromodomain-like. 1 hit.
PROSITE	PS00598. CHROMO_1. 1 hit. PS50013. CHROMO_2. 1 hit. PS50868. POST_SET. 1 hit. PS50867. PRE_SET. 1 hit. PS50280. SET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	299879.
SOURCE	Search...

Entry information

Entry name

SUV91_MOUSE

Accession

Primary (citable) accession number: O54864
Secondary accession number(s): Q3TEW2 , Q3UT51, Q8C2L3, Q9JLC7, Q9JLP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	June 1, 1998
Last modified:	April 3, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program