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O54864 (SUV91_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Protein existenceEvidence 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 CCAR2 By similarity.

Subunit structure

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. Ref.1 Ref.9 Ref.10 Ref.16 Ref.17

Subcellular location

Nucleus. Nucleus lamina By similarity. Nucleusnucleoplasm By similarity. Chromosomecentromere. 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 class V-like SAM-binding methyltransferase superfamily. 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 processCell cycle
Differentiation
rRNA processing
Transcription
Transcription regulation
   Cellular componentCentromere
Chromosome
Nucleus
   Coding sequence diversityAlternative splicing
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Repressor
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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: Ensembl

histone H3-K9 methylation

Inferred from genetic interaction PubMed 15788566. Source: MGI

histone lysine methylation

Inferred from genetic interaction PubMed 23451023. Source: MGI

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin silencing complex

Inferred from direct assay Ref.9. Source: UniProtKB

chromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

heterochromatin

Inferred from direct assay Ref.14. Source: UniProtKB

nuclear heterochromatin

Traceable author statement Ref.6. Source: MGI

nuclear lamina

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.14. Source: UniProtKB

rDNA heterochromatin

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionhistone methyltransferase activity (H3-K9 specific)

Inferred from direct assay Ref.14. Source: UniProtKB

histone-lysine N-methyltransferase activity

Inferred from direct assay Ref.7. Source: UniProtKB

methyltransferase activity

Inferred from direct assay Ref.7. Source: UniProtKB

protein methyltransferase activity

Traceable author statement Ref.6. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Gfi1bO702372EBI-302230,EBI-4287943
Myod1P100853EBI-302230,EBI-4405734
SIRT1Q96EB64EBI-302230,EBI-1802965From 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 412412Histone-lysine N-methyltransferase SUV39H1
PRO_0000186058

Regions

Domain43 – 10159Chromo
Domain179 – 24062Pre-SET
Domain243 – 366124SET
Domain396 – 41217Post-SET
Region1 – 8989Interaction with SIRT1
Region255 – 377123Mediates interaction with MECOM

Amino acid modifications

Modified residue2661N6-acetyllysine By similarity
Modified residue3911Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 66MAENLK → LKEKVAATRGKRRLSVTVTL SVSTGDAGRGGRSGTDPLLK MGEPATL in isoform 2.
VSP_002208
Alternative sequence277 – 28610IITSEEAERR → VPPGCYLLGK in isoform 3.
VSP_024029
Alternative sequence287 – 412126Missing in isoform 3.
VSP_024030

Experimental info

Sequence conflict3641D → G in BAC40334. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 6B690F4FE7FD997C

FASTA41247,754
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 64BE15984279410B
Show »

FASTA45351,889
Isoform 3 [UniParc].

Checksum: E1BEB67AD19032E1
Show »

FASTA28633,111

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+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.
RefSeqNP_035644.1. NM_011514.2.
UniGeneMm.479743.
Mm.9244.

3D structure databases

ProteinModelPortalO54864.
SMRO54864. Positions 44-100, 115-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203586. 1 interaction.
DIPDIP-32590N.
IntActO54864. 5 interactions.
MINTMINT-256025.

PTM databases

PhosphoSiteO54864.

Proteomic databases

PRIDEO54864.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000115636; ENSMUSP00000111299; ENSMUSG00000039231. [O54864-3]
ENSMUST00000115638; ENSMUSP00000111301; ENSMUSG00000039231. [O54864-1]
GeneID20937.
KEGGmmu:20937.
UCSCuc009snq.2. mouse. [O54864-1]

Organism-specific databases

CTD6839.
MGIMGI:1099440. Suv39h1.

Phylogenomic databases

eggNOGCOG2940.
GeneTreeENSGT00750000117355.
HOGENOMHOG000231244.
HOVERGENHBG055621.
KOK11419.
OrthoDBEOG7RJPR0.
TreeFamTF106452.

Gene expression databases

ArrayExpressO54864.
BgeeO54864.
GenevestigatorO54864.

Family and domain databases

InterProIPR023780. 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]
PfamPF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFPIRSF009343. SUV39_SET. 1 hit.
SMARTSM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
PROSITEPS00598. 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]
ProtoNetSearch...

Other

NextBio299879.
PROO54864.
SOURCESearch...

Entry information

Entry nameSUV91_MOUSE
AccessionPrimary (citable) accession number: O54864
Secondary accession number(s): Q3TEW2 expand/collapse secondary AC list , Q3UT51, Q8C2L3, Q9JLC7, Q9JLP8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot