A0A1C9J735 · A0A1C9J735_HUMAN
- ProteinHistone-lysine N-methyltransferase, H3 lysine-79 specific
- GeneDOT1L
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1537 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
Histone methyltransferase. Methylates 'Lys-79' of histone H3.
Miscellaneous
In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Catalytic activity
- L-lysyl79-[histone H3] + 3 S-adenosyl-L-methionine = N6,N6,N6-trimethyl-L-lysyl79-[histone H3] + 3 S-adenosyl-L-homocysteine + 3 H+
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 136-139 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: YGET | ||||||
Binding site | 159-168 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: FVDLGSGVGQ | ||||||
Binding site | 186 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 222-223 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DF |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | histone H3K79 trimethyltransferase activity | |
Biological Process | DNA damage checkpoint signaling | |
Biological Process | DNA repair | |
Biological Process | heterochromatin formation | |
Biological Process | methylation |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameHistone-lysine N-methyltransferase, H3 lysine-79 specific
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A1C9J735
Subcellular Location
PTM/Processing
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-330 | DOT1 | ||||
Sequence: EPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSTGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILENYFSSLK | ||||||
Compositional bias | 334-349 | Basic and acidic residues | ||||
Sequence: LREEQEAARRRQQRES | ||||||
Region | 334-480 | Disordered | ||||
Sequence: LREEQEAARRRQQRESKSNAATPTKGPEGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMNTANPERKPKKNQTALDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSVQRHSPNPLLVAPT | ||||||
Compositional bias | 390-415 | Basic residues | ||||
Sequence: SPSKARKKKLNKKGRKMAGRKRGRPK | ||||||
Compositional bias | 416-431 | Basic and acidic residues | ||||
Sequence: KMNTANPERKPKKNQT | ||||||
Compositional bias | 433-469 | Polar residues | ||||
Sequence: LDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSVQR | ||||||
Coiled coil | 529-636 | |||||
Sequence: AQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKARCEELQLDWATLSLEKLLKEKQALKSQISEKQRH | ||||||
Region | 785-853 | Disordered | ||||
Sequence: LSQDHTVPGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQLAGEKSSEKGLRER | ||||||
Compositional bias | 809-823 | Polar residues | ||||
Sequence: ENGLPYQSPSVPGSM | ||||||
Region | 950-1269 | Disordered | ||||
Sequence: AGSPASLTPGAEPATLDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAHQLSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAKRRIVFTITTGAGSAKQSPSSKHSPLTASARGDCVPSHGQDSRRRGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSPLNLNSMVSNINQPLEITAISSPETSLKSSPVPYQDHDQPPVLKKERPLSQTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLAGRKPAPAGEPVNSSKWKSTFSPISDIGLAKSADSPLQASSALSQ | ||||||
Compositional bias | 962-991 | Polar residues | ||||
Sequence: PATLDESSSSGSLFATVGSRSSTPQHPLLL | ||||||
Compositional bias | 998-1012 | Polar residues | ||||
Sequence: LPASPAHQLSSSPRL | ||||||
Compositional bias | 1051-1068 | Polar residues | ||||
Sequence: TGAGSAKQSPSSKHSPLT | ||||||
Compositional bias | 1116-1156 | Polar residues | ||||
Sequence: LFTQPSGSPLNLNSMVSNINQPLEITAISSPETSLKSSPVP | ||||||
Region | 1284-1319 | Disordered | ||||
Sequence: ADAKLAAHPRKGFPGSLSGADGLSPGTNPANGCTFG | ||||||
Region | 1331-1406 | Disordered | ||||
Sequence: FSDGASLPHKGPEAAGLSSPLSFPSQRGKEGSDANPFLSKRQLDGLAGLKGEGSRXKEAGEGGLPLCGPTDKTPLL |
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,537
- Mass (Da)164,910
- Last updated2016-11-30 v1
- Checksum5520736A0DDA5D56
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 334-349 | Basic and acidic residues | ||||
Sequence: LREEQEAARRRQQRES | ||||||
Compositional bias | 390-415 | Basic residues | ||||
Sequence: SPSKARKKKLNKKGRKMAGRKRGRPK | ||||||
Compositional bias | 416-431 | Basic and acidic residues | ||||
Sequence: KMNTANPERKPKKNQT | ||||||
Compositional bias | 433-469 | Polar residues | ||||
Sequence: LDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSVQR | ||||||
Compositional bias | 809-823 | Polar residues | ||||
Sequence: ENGLPYQSPSVPGSM | ||||||
Compositional bias | 962-991 | Polar residues | ||||
Sequence: PATLDESSSSGSLFATVGSRSSTPQHPLLL | ||||||
Compositional bias | 998-1012 | Polar residues | ||||
Sequence: LPASPAHQLSSSPRL | ||||||
Compositional bias | 1051-1068 | Polar residues | ||||
Sequence: TGAGSAKQSPSSKHSPLT | ||||||
Compositional bias | 1116-1156 | Polar residues | ||||
Sequence: LFTQPSGSPLNLNSMVSNINQPLEITAISSPETSLKSSPVP |