Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2YDW7 (SETD8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. 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

Names and origin

Protein namesRecommended name:
N-lysine methyltransferase SETD8

EC=2.1.1.-
Alternative name(s):
H4-K20-HMTase SETD8
Histone-lysine N-methyltransferase SETD8
EC=2.1.1.43
PR/SET domain-containing protein 07
Short name=PR-Set7
Short name=PR/SET07
SET domain-containing protein 8
Gene names
Name:Setd8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration By similarity.

Catalytic activity

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

Subunit structure

Interacts with L3MBTL1 By similarity.

Subcellular location

Nucleus By similarity. Chromosome By similarity. Note: Specifically localizes to mitotic chromosomes. Associates with silent chromatin on euchromatic arms. Not associated with constitutive heterochromatin By similarity.

Domain

Although the SET domain contains the active site of enzymatic activity, both sequences upstream and downstream of the SET domain are required for methyltransferase activity By similarity.

Post-translational modification

Ubiquitinated and degraded by the DCX(DTL) complex Probable.

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. PR/SET subfamily.

Contains 1 SET domain.

Sequence caution

The sequence BAC27178.1 differs from that shown. Reason: Frameshift at position 20.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Repressor
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone lysine methylation

Inferred from sequence or structural similarity. Source: GOC

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-lysine monomethylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhistone-lysine N-methyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

p53 binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein-lysine N-methyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349N-lysine methyltransferase SETD8
PRO_0000228689

Regions

Domain213 – 334122SET
Region223 – 2253S-adenosyl-L-methionine binding By similarity
Region295 – 2962S-adenosyl-L-methionine binding By similarity
Compositional bias12 – 2413Ala-rich

Sites

Binding site2681S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue571Phosphoserine By similarity

Experimental info

Sequence conflict2041N → ID in BAC27178. Ref.1
Sequence conflict2601V → A in BAC27178. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q2YDW7 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: C89BAE59660DA5AF

FASTA34938,845
        10         20         30         40         50         60 
MARGRKMCKP RAVEAAAAAV AATAPGPEMV EQRGPGRPRS DGENVFAGQS KIYAYMSPNK 

        70         80         90        100        110        120 
CSAMRSPLQE ENSVAHHEVK CPGKPLAGIY RKREEKRNTG NVIRSAVKSD EQKSKDTRRG 

       130        140        150        160        170        180 
PLAPFPNQKS EAAEPPKTPP PSCDSTNVAV AKQALKKSLK GKQAPRKKSQ GKTQQNRKLT 

       190        200        210        220        230        240 
DFYPVRRSSR KSKAELQSEE RKKNELIESG KEEGMKIDLI DGKGRGVIAT KQFSRGDFVV 

       250        260        270        280        290        300 
EYHGDLIEIT DAKKREALYV QDPSTGCYMY YFQYLSKTYC VDATQETNRL GRLINHSKCG 

       310        320        330        340 
NCQTKLHDID GVPHLILIAS RDIAAGEELL YDYGDRSKAS IEAYPWLKH 

« Hide

References

[1]"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: C57BL/6J.
Tissue: Thymus.
[2]"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: NMRI.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK030904 mRNA. Translation: BAC27178.1. Frameshift.
BC108333 mRNA. Translation: AAI08334.1.
RefSeqNP_084517.2. NM_030241.2.
UniGeneMm.137966.

3D structure databases

ProteinModelPortalQ2YDW7.
SMRQ2YDW7. Positions 190-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212564. 1 interaction.
IntActQ2YDW7. 2 interactions.
MINTMINT-4113899.

PTM databases

PhosphoSiteQ2YDW7.

Proteomic databases

PaxDbQ2YDW7.
PRIDEQ2YDW7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID67956.
KEGGmmu:67956.

Organism-specific databases

CTD387893.
MGIMGI:1915206. Setd8.

Phylogenomic databases

eggNOGCOG2940.
HOGENOMHOG000020818.
HOVERGENHBG067546.
KOK11428.

Gene expression databases

GenevestigatorQ2YDW7.

Family and domain databases

InterProIPR016858. Hist_H4-K20_MeTrfase.
IPR001214. SET_dom.
[Graphical view]
PfamPF00856. SET. 1 hit.
[Graphical view]
PIRSFPIRSF027717. Histone_H4-K20_mtfrase. 1 hit.
SMARTSM00317. SET. 1 hit.
[Graphical view]
PROSITEPS51571. SAM_MT43_PR_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSETD8. mouse.
NextBio326066.
PROQ2YDW7.
SOURCESearch...

Entry information

Entry nameSETD8_MOUSE
AccessionPrimary (citable) accession number: Q2YDW7
Secondary accession number(s): Q8C0J9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: December 20, 2005
Last modified: April 16, 2014
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

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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