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Q6Q783 (SV422_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 76. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase SUV420H2
EC=2.1.1.43
Alternative name(s):
Suppressor of variegation 4-20 homolog 2
Short name=Su(var)4-20 homolog 2
Short name=Suv4-20h2
Gene names
Name:Suv420h2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Interacts with HP1 proteins CBX1, CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2. Ref.1 Ref.4 Ref.5

Subcellular location

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

Sequence similarities

Belongs to the histone-lysine methyltransferase family. Suvar4-20 subfamily.

Contains 1 SET domain.

Sequence caution

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 468468Histone-lysine N-methyltransferase SUV420H2
PRO_0000281794

Regions

Domain103 – 222120SET
Region348 – 44194Required for heterochromatin localization

Sequences

Sequence LengthMass (Da)Tools
Q6Q783 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D43D7A25DBDF3BB1

FASTA46853,159
        10         20         30         40         50         60 
MGPDRVTARE LCENDDLATS LVLDPYLGFR THKMNVSPVP TLRRQHHLRS ALEAFLRQRD 

        70         80         90        100        110        120 
LEAAFRALTL GGWMAHYFQS RAPRQEAALK THIFCYLRAF LPESGFTILP CTRYSMETNG 

       130        140        150        160        170        180 
AKIVSTRAWK KNEKLELLVG CIAELREEDE DLLRAGENDF SIMYSTRKRS AQLWLGPAAF 

       190        200        210        220        230        240 
INHDCKPNCK FVPSDGNTAC VKVLRDIEPG DEVTCFYGEG FFGEKNEHCE CYTCERKGEG 

       250        260        270        280        290        300 
AFRLQPREPE LRPKPLDKYE LRETKRRLQQ GLVSSQQSLM SRWACSHLSP LRPDPFCAAC 

       310        320        330        340        350        360 
QPSCLLPASP HMDYLPLWLQ RAPQPQPIVP PRKRHRRRRP RIRQASLPPV LRTACVPLHR 

       370        380        390        400        410        420 
WGGCGPHCQL RAEAMVTLHL RPQTRWTPQQ DWYWARRYGL PSVGRVELTR LAPALPAAPA 

       430        440        450        460 
PAGNPGPVPT PDFIPKQALA FAPFCPPKRL RLVVSHGSID LDINSGEP

« Hide

References

« Hide 'large scale' references
[1]"A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin."
Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., Reinberg D., Jenuwein T.
Genes Dev. 18:1251-1262(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CBX1; CBX3 AND CBX5.
Strain: FVB/N.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. 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].
Strain: NOD.
Tissue: Dendritic cell.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain and Eye.
[4]"Role of the RB1 family in stabilizing histone methylation at constitutive heterochromatin."
Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M., Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T., Blasco M.A.
Nat. Cell Biol. 7:420-428(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RB1; RBL1 AND RBL2.
[5]"The retinoblastoma protein regulates pericentric heterochromatin."
Isaac C.E., Francis S.M., Martens A.L., Julian L.M., Seifried L.A., Erdmann N., Binne U.K., Harrington L., Sicinski P., Berube N.G., Dyson N.J., Dick F.A.
Mol. Cell. Biol. 26:3659-3671(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RB1; RBL1 AND RBL2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY555193 mRNA. Translation: AAT00540.1.
AK154848 mRNA. Translation: BAE32874.1.
BC024816 mRNA. Translation: AAH24816.1. Different initiation.
BC085473 mRNA. Translation: AAH85473.2. Different initiation.
IPIIPI00454188.
RefSeqNP_001108490.1. NM_001115018.1.
NP_666289.2. NM_146177.2.
UniGeneMm.247844.

3D structure databases

ProteinModelPortalQ6Q783.
SMRQ6Q783. Positions 4-243.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000104224.

PTM databases

PhosphoSiteQ6Q783.

Proteomic databases

PaxDbQ6Q783.
PRIDEQ6Q783.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000098853; ENSMUSP00000096452; ENSMUSG00000059851.
ENSMUST00000108582; ENSMUSP00000104223; ENSMUSG00000059851.
ENSMUST00000108583; ENSMUSP00000104224; ENSMUSG00000059851.
GeneID232811.
KEGGmmu:232811.
UCSCuc009eyi.2. mouse.

Organism-specific databases

CTD84787.
MGIMGI:2385262. Suv420h2.

Phylogenomic databases

eggNOGNOG240704.
GeneTreeENSGT00520000055640.
HOGENOMHOG000154453.
HOVERGENHBG095676.
InParanoidQ6Q783.
KOK11429.
OMASTRAWKK.
OrthoDBEOG437RDW.

Gene expression databases

ArrayExpressQ6Q783.
BgeeQ6Q783.
GenevestigatorQ6Q783.

Family and domain databases

InterProIPR025790. Hist-Lys_N-MTase_Suvar4-20.
IPR001214. SET_dom.
[Graphical view]
PfamPF00856. SET. 1 hit.
[Graphical view]
SMARTSM00317. SET. 1 hit.
[Graphical view]
PROSITEPS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSUV420H2. mouse.
NextBio381246.
SOURCESearch...

Entry information

Entry nameSV422_MOUSE
AccessionPrimary (citable) accession number: Q6Q783
Secondary accession number(s): Q5RKP6, Q8R1C5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 5, 2004
Last modified: April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents