H9LAN6 · H9LAN6_MOUSE
- ProteinHistone-lysine N-methyltransferase, H3 lysine-79 specific
- GeneDot1l
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1736 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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 = 3 H+ + N6,N6,N6-trimethyl-L-lysyl79-[histone H3] + 3 S-adenosyl-L-homocysteine
RHEA-COMP:15549 CHEBI:29969 Position: 79+ 3 CHEBI:59789 = 3 CHEBI:15378 + RHEA-COMP:15552 CHEBI:61961 Position: 79+ 3 CHEBI:57856
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 | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | protein-containing complex | |
Molecular Function | histone H3K79 methyltransferase activity | |
Molecular Function | histone H3K79 trimethyltransferase activity | |
Molecular Function | histone methyltransferase activity | |
Biological Process | DNA damage checkpoint signaling | |
Biological Process | DNA repair | |
Biological Process | gene expression | |
Biological Process | heterochromatin formation | |
Biological Process | methylation | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | positive regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameHistone-lysine N-methyltransferase, H3 lysine-79 specific
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionH9LAN6
Organism-specific databases
Subcellular Location
PTM/Processing
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-330 | DOT1 | ||||
Sequence: ESAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSNGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTEDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILENYFSSLK | ||||||
Compositional bias | 334-349 | Basic and acidic residues | ||||
Sequence: LREEQEAARRRQQREN | ||||||
Region | 334-465 | Disordered | ||||
Sequence: LREEQEAARRRQQRENKSNATTPTKVPESKAAATEAPADSGAEEEKSGVATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMSAASAERKSKKSQSTLDLLHSPPPAPPSASPQDAYRAPHSPFYQLPPST | ||||||
Compositional bias | 389-414 | Basic residues | ||||
Sequence: SPSKARKKKLNKKGRKMAGRKRGRPK | ||||||
Compositional bias | 415-430 | Basic and acidic residues | ||||
Sequence: KMSAASAERKSKKSQS | ||||||
Coiled coil | 562-634 | |||||
Sequence: LIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLSLENLRKEKQALRSQISEKQRH | ||||||
Region | 784-857 | Disordered | ||||
Sequence: SQDHTGASKAATSEPHPRPEHPKESSLPYQSPGLSNSMKLSPQDPPLASPATSPLTSEKGSEKGVKERAYSSHG | ||||||
Compositional bias | 811-826 | Polar residues | ||||
Sequence: PYQSPGLSNSMKLSPQ | ||||||
Region | 891-930 | Disordered | ||||
Sequence: RAERARSTPSPVPQPRDSSATLEKQTGASAHGAGGAGAGS | ||||||
Compositional bias | 901-916 | Polar residues | ||||
Sequence: PVPQPRDSSATLEKQT | ||||||
Region | 964-1110 | Disordered | ||||
Sequence: SAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHQLTASPRLSVTTQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSGTRGDCVQSHGQDSRKRSRRKRASAGTPSLSTGVSPKRRA | ||||||
Compositional bias | 967-1026 | Polar residues | ||||
Sequence: FDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHQLTASPRLSVTTQGSLPDTS | ||||||
Compositional bias | 1052-1078 | Polar residues | ||||
Sequence: SVGASSKQSPSTRHSPLTSGTRGDCVQ | ||||||
Compositional bias | 1143-1160 | Polar residues | ||||
Sequence: AISSPESSLKSSPTPYQD | ||||||
Region | 1143-1242 | Disordered | ||||
Sequence: AISSPESSLKSSPTPYQDHDQPPVLRKERPLGLTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLVGRKSAPSSEPINSSKW | ||||||
Region | 1284-1319 | Disordered | ||||
Sequence: AAEAKLPTHPRKSFAGSLGAAEGPSPGTNPPNGLAF | ||||||
Compositional bias | 1349-1370 | Polar residues | ||||
Sequence: SASLSFPSQRGKDSTTEANPFL | ||||||
Region | 1349-1418 | Disordered | ||||
Sequence: SASLSFPSQRGKDSTTEANPFLSRRQPEGLGGLKGEGNANKESGESLPLCGPSDKASLPHGSRASKGRDR | ||||||
Region | 1586-1631 | Disordered | ||||
Sequence: AAASVETRPPPPPPLLPPQHLGRPPAGPPVLHAPPPPNVALPPPPA | ||||||
Compositional bias | 1591-1631 | Pro residues | ||||
Sequence: ETRPPPPPPLLPPQHLGRPPAGPPVLHAPPPPNVALPPPPA |
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,736
- Mass (Da)185,300
- Last updated2012-06-13 v1
- Checksum02C56157B3D72A68
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 334-349 | Basic and acidic residues | ||||
Sequence: LREEQEAARRRQQREN | ||||||
Compositional bias | 389-414 | Basic residues | ||||
Sequence: SPSKARKKKLNKKGRKMAGRKRGRPK | ||||||
Compositional bias | 415-430 | Basic and acidic residues | ||||
Sequence: KMSAASAERKSKKSQS | ||||||
Compositional bias | 811-826 | Polar residues | ||||
Sequence: PYQSPGLSNSMKLSPQ | ||||||
Compositional bias | 901-916 | Polar residues | ||||
Sequence: PVPQPRDSSATLEKQT | ||||||
Compositional bias | 967-1026 | Polar residues | ||||
Sequence: FDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHQLTASPRLSVTTQGSLPDTS | ||||||
Compositional bias | 1052-1078 | Polar residues | ||||
Sequence: SVGASSKQSPSTRHSPLTSGTRGDCVQ | ||||||
Compositional bias | 1143-1160 | Polar residues | ||||
Sequence: AISSPESSLKSSPTPYQD | ||||||
Compositional bias | 1349-1370 | Polar residues | ||||
Sequence: SASLSFPSQRGKDSTTEANPFL | ||||||
Compositional bias | 1591-1631 | Pro residues | ||||
Sequence: ETRPPPPPPLLPPQHLGRPPAGPPVLHAPPPPNVALPPPPA |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JF508521 EMBL· GenBank· DDBJ | ADZ40239.1 EMBL· GenBank· DDBJ | mRNA |