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Q3U8K7 (SV421_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase SUV420H1

EC=2.1.1.43
Alternative name(s):
Suppressor of variegation 4-20 homolog 1
Short name=Su(var)4-20 homolog 1
Short name=Suv4-20h1
Gene names
Name:Suv420h1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length883 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 class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar4-20 subfamily.

Contains 1 SET domain.

Sequence caution

The sequence AAH11214.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAT00539.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC39834.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE23934.1 differs from that shown. Reason: Erroneous termination at position 3. Translated as Trp.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3U8K7-1)

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: Q3U8K7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     393-394: TS → SK
     395-883: Missing.
Isoform 3 (identifier: Q3U8K7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     104-126: Missing.
Isoform 4 (identifier: Q3U8K7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     328-883: Missing.
Isoform 5 (identifier: Q3U8K7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     104-126: Missing.
     831-883: EGEEEEEDCEDDFDDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA → SGKAAEANCW
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 883883Histone-lysine N-methyltransferase SUV420H1
PRO_0000281788

Regions

Domain194 – 309116SET

Natural variations

Alternative sequence104 – 12623Missing in isoform 3 and isoform 5.
VSP_024053
Alternative sequence328 – 883556Missing in isoform 4.
VSP_024054
Alternative sequence393 – 3942TS → SK in isoform 2.
VSP_024055
Alternative sequence395 – 883489Missing in isoform 2.
VSP_024056
Alternative sequence831 – 88353EGEEE…LRLNA → SGKAAEANCW in isoform 5.
VSP_024057

Experimental info

Sequence conflict531S → N in AAH75709. Ref.3
Sequence conflict1531K → E in AAH11214. Ref.2
Sequence conflict2921V → L in BAC39834. Ref.1
Sequence conflict3281R → Q in BAE31010. Ref.2
Sequence conflict4281P → A in AAH75709. Ref.3
Sequence conflict4721E → G in BAC38817. Ref.1
Sequence conflict5211N → S in AAH75709. Ref.3
Sequence conflict5901P → H in BAC38817. Ref.1
Sequence conflict5951R → G in BAE31010. Ref.2
Sequence conflict6641H → Y in AAH75709. Ref.3
Sequence conflict6781A → T in AAH75709. Ref.3

Secondary structure

..................................... 883
Helix Strand Turn

Details...

Sequences

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

Last modified April 3, 2007. Version 2.
Checksum: 2B24461F582CC5F1

FASTA88398,580
        10         20         30         40         50         60 
MKWLGDSKNM VVNGRRNGGK LSNDHQQNQS KLQQHSGKDT LKTGRNAVER RSSRCHGNSG 

        70         80         90        100        110        120 
FEGQSRYVPS SGMSAKELCE NDDLATSLVL DPYLGFQTHK MNTSAFPSRS SRHISKADSF 

       130        140        150        160        170        180 
SHNNPVRFRP IKGRQEELKE VIERFKKDEH LEKAFKCLTS GEWARHYFLN KNKMQEKLFK 

       190        200        210        220        230        240 
EHVFIYLRMF ATDSGFEILP CNRYSSEQNG AKIVATKEWK RNDKIELLVG CIAELSEIEE 

       250        260        270        280        290        300 
NMLLRHGEND FSVMYSTRKN CAQLWLGPAA FINHDCRPNC KFVSTGRDTA CVKALRDIEP 

       310        320        330        340        350        360 
GEEISCYYGD GFFGENNEFC ECYTCERRGT GAFKSRVGLP APAPVINSKY GLRETDKRLN 

       370        380        390        400        410        420 
RLKKLGDSSK NSDSQSVSSN TDADTTQEKD NATSNRKSSV GVKKSSKSRA LTRPSMPRVP 

       430        440        450        460        470        480 
AASNSTSPKL VHTNNPRVPK KLRKPAKPLL SKIRLRNHCK RLDQKSASRK LEMGSLVLKE 

       490        500        510        520        530        540 
PKVVLYKNLP IKKEREPEGP AHAAVGSGCL TRHAAREHRQ NHGRGAHSQG DSLPCTYTTR 

       550        560        570        580        590        600 
RSLRTRTGLK ETTDIKLEPS PLDGYKNGIL EPCPDSGQQP TPEVLEELAP ETAHREEASQ 

       610        620        630        640        650        660 
ECPKNDSCLS RKKFRQVKPV KHLAKTEDCS PEHSFPGKDG LPDLPGSHPD QGEPSGTVRV 

       670        680        690        700        710        720 
PVSHTDSAPS PVGCSVVAPD SFTKDSFRTA QSKKKRRVTR YDAQLILENS SGIPKLTLRR 

       730        740        750        760        770        780 
RHDSSSKTND HESDGVNSSK ISIKLSKDHD SDSNLYVAKL SNGVSAGPGS SSTKLKIQLK 

       790        800        810        820        830        840 
RDEESRGPCA EGLHENGVCC SDPLSLLESQ MEVDDYSQYE EDSTDESSSS EGEEEEEDCE 

       850        860        870        880 
DDFDDDFIPL PPAKRLRLIV GKDSIDIDIS SRRREDQSLR LNA 

« Hide

Isoform 2 [UniParc].

Checksum: 1425ECDBE1F767D7
Show »

FASTA39444,723
Isoform 3 [UniParc].

Checksum: 2EEE457CEE91A890
Show »

FASTA86096,070
Isoform 4 [UniParc].

Checksum: 6400D6AAEEA26B99
Show »

FASTA32737,546
Isoform 5 [UniParc].

Checksum: 478C772F2EAFDEC4
Show »

FASTA81790,944

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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CBX1; CBX3 AND CBX5.
Strain: C57BL/6.
[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] (ISOFORMS 1; 2; 3 AND 4).
Strain: C57BL/6J.
Tissue: Bone marrow, Cerebellum, Hippocampus, Lung, Oviduct and Vagina.
[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] (ISOFORMS 4 AND 5).
Strain: Czech II and FVB/N.
Tissue: Mammary tumor and Salivary gland.
[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
AY555192 mRNA. Translation: AAT00539.1. Different initiation.
AK036880 mRNA. Translation: BAC29617.1.
AK054093 mRNA. Translation: BAC35652.1.
AK082660 mRNA. Translation: BAC38565.1.
AK083227 mRNA. Translation: BAC38817.1.
AK087267 mRNA. Translation: BAC39834.1. Different initiation.
AK139255 mRNA. Translation: BAE23934.1. Sequence problems.
AK152179 mRNA. Translation: BAE31010.1.
BC011214 mRNA. Translation: AAH11214.1. Different initiation.
BC075709 mRNA. Translation: AAH75709.1.
RefSeqNP_001161356.1. NM_001167884.1.
NP_001161357.1. NM_001167885.1.
NP_001161358.1. NM_001167886.1.
NP_001161359.1. NM_001167887.1.
NP_001161360.1. NM_001167888.1.
NP_001161361.1. NM_001167889.1.
NP_659120.3. NM_144871.4.
XP_006531790.1. XM_006531727.1.
XP_006531791.1. XM_006531728.1.
XP_006531794.1. XM_006531731.1.
UniGeneMm.278578.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BUPX-ray2.17A/B70-336[»]
ProteinModelPortalQ3U8K7.
SMRQ3U8K7. Positions 72-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230441. 3 interactions.

PTM databases

PhosphoSiteQ3U8K7.

Proteomic databases

PaxDbQ3U8K7.
PRIDEQ3U8K7.

Protocols and materials databases

DNASU225888.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005518; ENSMUSP00000005518; ENSMUSG00000045098. [Q3U8K7-4]
ENSMUST00000052699; ENSMUSP00000060162; ENSMUSG00000045098. [Q3U8K7-2]
ENSMUST00000113967; ENSMUSP00000109600; ENSMUSG00000045098. [Q3U8K7-4]
ENSMUST00000113968; ENSMUSP00000109601; ENSMUSG00000045098. [Q3U8K7-4]
ENSMUST00000113970; ENSMUSP00000109603; ENSMUSG00000045098. [Q3U8K7-2]
ENSMUST00000113972; ENSMUSP00000109605; ENSMUSG00000045098. [Q3U8K7-1]
ENSMUST00000113973; ENSMUSP00000109606; ENSMUSG00000045098. [Q3U8K7-1]
ENSMUST00000113974; ENSMUSP00000109607; ENSMUSG00000045098. [Q3U8K7-3]
ENSMUST00000113977; ENSMUSP00000109610; ENSMUSG00000045098. [Q3U8K7-3]
ENSMUST00000176262; ENSMUSP00000135563; ENSMUSG00000045098. [Q3U8K7-3]
GeneID225888.
KEGGmmu:225888.
UCSCuc008fww.2. mouse. [Q3U8K7-4]
uc008fwz.2. mouse. [Q3U8K7-2]
uc008fxa.2. mouse. [Q3U8K7-1]
uc008fxc.2. mouse. [Q3U8K7-3]

Organism-specific databases

CTD51111.
MGIMGI:2444557. Suv420h1.

Phylogenomic databases

eggNOGNOG240704.
GeneTreeENSGT00520000055640.
HOVERGENHBG105761.
InParanoidQ3U8K7.
KOK11429.
OMAKLEMGNL.
OrthoDBEOG7MKW6P.
PhylomeDBQ3U8K7.
TreeFamTF106433.

Gene expression databases

ArrayExpressQ3U8K7.
BgeeQ3U8K7.
GenevestigatorQ3U8K7.

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]
PROSITEPS51570. SAM_MT43_SUVAR420_2. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSUV420H1. mouse.
NextBio377853.
PROQ3U8K7.
SOURCESearch...

Entry information

Entry nameSV421_MOUSE
AccessionPrimary (citable) accession number: Q3U8K7
Secondary accession number(s): Q3UTP6 expand/collapse secondary AC list , Q6DI74, Q6Q784, Q8BU67, Q8BUN0, Q8BUT7, Q8BW73, Q8BZ24, Q91X81
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: April 16, 2014
This is version 75 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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