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Protein

Histone-lysine N-methyltransferase SUV420H2

Gene

Suv420h2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

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

GO - Molecular functioni

  1. histone methyltransferase activity (H4-K20 specific) Source: MGI

GO - Biological processi

  1. histone H4-K20 trimethylation Source: InterPro
  2. histone methylation Source: MGI
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Suv420h2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:2385262. Suv420h2.

Subcellular locationi

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

GO - Cellular componenti

  1. condensed nuclear chromosome, centromeric region Source: MGI
  2. nuclear heterochromatin Source: MGI
  3. nucleoplasm Source: MGI
  4. pericentric heterochromatin Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Histone-lysine N-methyltransferase SUV420H2PRO_0000281794Add
BLAST

Proteomic databases

MaxQBiQ6Q783.
PaxDbiQ6Q783.
PRIDEiQ6Q783.

PTM databases

PhosphoSiteiQ6Q783.

Expressioni

Gene expression databases

BgeeiQ6Q783.
ExpressionAtlasiQ6Q783. baseline and differential.
GenevestigatoriQ6Q783.

Interactioni

Subunit structurei

Interacts with HP1 proteins CBX1, CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2.3 Publications

Protein-protein interaction databases

BioGridi231299. 3 interactions.
STRINGi10090.ENSMUSP00000104224.

Structurei

Secondary structure

1
468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2114Combined sources
Helixi23 – 275Combined sources
Helixi45 – 5814Combined sources
Helixi61 – 688Combined sources
Helixi74 – 774Combined sources
Turni78 – 814Combined sources
Helixi83 – 9917Combined sources
Helixi102 – 1043Combined sources
Beta strandi106 – 1116Combined sources
Beta strandi118 – 12710Combined sources
Beta strandi134 – 14411Combined sources
Helixi147 – 1526Combined sources
Turni155 – 1573Combined sources
Beta strandi160 – 1656Combined sources
Turni166 – 1694Combined sources
Beta strandi170 – 1767Combined sources
Helixi177 – 1804Combined sources
Beta strandi188 – 1936Combined sources
Beta strandi195 – 20511Combined sources
Turni219 – 2224Combined sources
Helixi232 – 2376Combined sources
Helixi240 – 2434Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AU7X-ray2.07A/B1-246[»]
ProteinModelPortaliQ6Q783.
SMRiQ6Q783. Positions 4-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 218115SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni348 – 44194Required for heterochromatin localizationAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar4-20 subfamily.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG240704.
GeneTreeiENSGT00520000055640.
HOGENOMiHOG000154453.
HOVERGENiHBG095676.
InParanoidiQ6Q783.
KOiK11429.
OMAiFCAACQP.
OrthoDBiEOG7MKW6P.
PhylomeDBiQ6Q783.
TreeFamiTF106433.

Family and domain databases

InterProiIPR025790. Hist-Lys_N-MTase_Suvar4-20.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51570. SAM_MT43_SUVAR420_2. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6Q783-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPDRVTARE LCENDDLATS LVLDPYLGFR THKMNVSPVP TLRRQHHLRS
60 70 80 90 100
ALEAFLRQRD LEAAFRALTL GGWMAHYFQS RAPRQEAALK THIFCYLRAF
110 120 130 140 150
LPESGFTILP CTRYSMETNG AKIVSTRAWK KNEKLELLVG CIAELREEDE
160 170 180 190 200
DLLRAGENDF SIMYSTRKRS AQLWLGPAAF INHDCKPNCK FVPSDGNTAC
210 220 230 240 250
VKVLRDIEPG DEVTCFYGEG FFGEKNEHCE CYTCERKGEG AFRLQPREPE
260 270 280 290 300
LRPKPLDKYE LRETKRRLQQ GLVSSQQSLM SRWACSHLSP LRPDPFCAAC
310 320 330 340 350
QPSCLLPASP HMDYLPLWLQ RAPQPQPIVP PRKRHRRRRP RIRQASLPPV
360 370 380 390 400
LRTACVPLHR WGGCGPHCQL RAEAMVTLHL RPQTRWTPQQ DWYWARRYGL
410 420 430 440 450
PSVGRVELTR LAPALPAAPA PAGNPGPVPT PDFIPKQALA FAPFCPPKRL
460
RLVVSHGSID LDINSGEP
Length:468
Mass (Da):53,159
Last modified:July 5, 2004 - v1
Checksum:iD43D7A25DBDF3BB1
GO

Sequence cautioni

The sequence AAH24816.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH85473.2 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY555193 mRNA. Translation: AAT00540.1.
AK154848 mRNA. Translation: BAE32874.1.
BC024816 mRNA. Translation: AAH24816.1. Different initiation.
BC085473 mRNA. Translation: AAH85473.2. Different initiation.
CCDSiCCDS20743.2.
RefSeqiNP_001108490.1. NM_001115018.1.
NP_666289.2. NM_146177.2.
XP_006539836.1. XM_006539773.1.
XP_006539837.1. XM_006539774.1.
UniGeneiMm.247844.

Genome annotation databases

EnsembliENSMUST00000098853; ENSMUSP00000096452; ENSMUSG00000059851.
ENSMUST00000108582; ENSMUSP00000104223; ENSMUSG00000059851.
ENSMUST00000108583; ENSMUSP00000104224; ENSMUSG00000059851.
GeneIDi232811.
KEGGimmu:232811.
UCSCiuc009eyi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY555193 mRNA. Translation: AAT00540.1.
AK154848 mRNA. Translation: BAE32874.1.
BC024816 mRNA. Translation: AAH24816.1. Different initiation.
BC085473 mRNA. Translation: AAH85473.2. Different initiation.
CCDSiCCDS20743.2.
RefSeqiNP_001108490.1. NM_001115018.1.
NP_666289.2. NM_146177.2.
XP_006539836.1. XM_006539773.1.
XP_006539837.1. XM_006539774.1.
UniGeneiMm.247844.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AU7X-ray2.07A/B1-246[»]
ProteinModelPortaliQ6Q783.
SMRiQ6Q783. Positions 4-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231299. 3 interactions.
STRINGi10090.ENSMUSP00000104224.

PTM databases

PhosphoSiteiQ6Q783.

Proteomic databases

MaxQBiQ6Q783.
PaxDbiQ6Q783.
PRIDEiQ6Q783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098853; ENSMUSP00000096452; ENSMUSG00000059851.
ENSMUST00000108582; ENSMUSP00000104223; ENSMUSG00000059851.
ENSMUST00000108583; ENSMUSP00000104224; ENSMUSG00000059851.
GeneIDi232811.
KEGGimmu:232811.
UCSCiuc009eyi.2. mouse.

Organism-specific databases

CTDi84787.
MGIiMGI:2385262. Suv420h2.

Phylogenomic databases

eggNOGiNOG240704.
GeneTreeiENSGT00520000055640.
HOGENOMiHOG000154453.
HOVERGENiHBG095676.
InParanoidiQ6Q783.
KOiK11429.
OMAiFCAACQP.
OrthoDBiEOG7MKW6P.
PhylomeDBiQ6Q783.
TreeFamiTF106433.

Miscellaneous databases

ChiTaRSiSuv420h2. mouse.
NextBioi381246.
PROiQ6Q783.
SOURCEiSearch...

Gene expression databases

BgeeiQ6Q783.
ExpressionAtlasiQ6Q783. baseline and differential.
GenevestigatoriQ6Q783.

Family and domain databases

InterProiIPR025790. Hist-Lys_N-MTase_Suvar4-20.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51570. SAM_MT43_SUVAR420_2. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: INTERACTION WITH RB1; RBL1 AND RBL2.

Entry informationi

Entry nameiSV422_MOUSE
AccessioniPrimary (citable) accession number: Q6Q783
Secondary accession number(s): Q5RKP6, Q8R1C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 5, 2004
Last modified: March 4, 2015
This is version 92 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.