Q8TEK3 · DOT1L_HUMAN
- ProteinHistone-lysine N-methyltransferase, H3 lysine-79 specific
- GeneDOT1L
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1537 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds to DNA (PubMed:12628190).
Miscellaneous
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
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone-lysine N-methyltransferase, H3 lysine-79 specific
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TEK3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_088679 | 45 | found in a patient with developmental delay and intellectual disability; uncertain significance | |||
Sequence: C → G | ||||||
Natural variant | VAR_088680 | 100 | found in a patient with developmental delay and intellectual disability; likely pathogenic; dbSNP:rs781606489 | |||
Sequence: T → M | ||||||
Natural variant | VAR_088681 | 123 | found in patients with developmental delay and intellectual disability; likely pathogenic; causes an almost 4-fold increase in H3K79 methylation in vitro; dbSNP:rs2022775856 | |||
Sequence: E → K | ||||||
Natural variant | VAR_088682 | 129 | found in a patient with developmental delay and intellectual disability; likely pathogenic; dbSNP:rs2144742354 | |||
Sequence: E → K | ||||||
Mutagenesis | 163-165 | Abolishes methyltransferase activity. | ||||
Sequence: GSG → RCR | ||||||
Mutagenesis | 241 | Loss of activity. | ||||
Sequence: N → A or D | ||||||
Natural variant | VAR_088683 | 292 | in dbSNP:rs2144814855 | |||
Sequence: R → C | ||||||
Mutagenesis | 312 | Loss of activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 312 | No effect. | ||||
Sequence: Y → F | ||||||
Natural variant | VAR_088684 | 451 | in dbSNP:rs377185393 | |||
Sequence: D → G | ||||||
Natural variant | VAR_088685 | 626 | found in a patient with developmental delay and intellectual disability; likely pathogenic | |||
Sequence: L → V | ||||||
Natural variant | VAR_014287 | 726 | in dbSNP:rs880525 | |||
Sequence: L → M | ||||||
Natural variant | VAR_088686 | 853 | found in a patient with developmental delay and intellectual disability; likely pathogenic; slightly increases H3K79 methylation in vitro; dbSNP:rs1599605821 | |||
Sequence: R → C | ||||||
Natural variant | VAR_088687 | 1025 | found in a patient with developmental delay and intellectual disability; uncertain significance; dbSNP:rs753193665 | |||
Sequence: K → M | ||||||
Natural variant | VAR_014288 | 1386 | in dbSNP:rs3815308 | |||
Sequence: G → S | ||||||
Natural variant | VAR_014289 | 1418 | in dbSNP:rs2302061 | |||
Sequence: V → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,580 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000186089 | 1-1537 | UniProt | Histone-lysine N-methyltransferase, H3 lysine-79 specific | |||
Sequence: MGEKLELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSTGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILENYFSSLKNPKLREEQEAARRRQQRESKSNAATPTKGPEGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMNTANPERKPKKNQTALDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSVQRHSPNPLLVAPTPPALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKARCEELQLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKSCVPPDDALSLHLRGKGALGRELEPDASRLHLELDCTKFSLPHLSSMSPELSMNGQAAGYELCGVLSRPSSKQNTPQYLASPLDQEVVPCTPSHVGRPRLEKLSGLAAPDYTRLSPAKIVLRRHLSQDHTVPGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQLAGEKSSEKGLRERAYGSSGELITSLPISIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVLQPRDPSSTLEKQIGANAHGAGSRSLALAPAGFSYAGSVAISGALAGSPASLTPGAEPATLDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAHQLSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAKRRIVFTITTGAGSAKQSPSSKHSPLTASARGDCVPSHGQDSRRRGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSPLNLNSMVSNINQPLEITAISSPETSLKSSPVPYQDHDQPPVLKKERPLSQTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLAGRKPAPAGEPVNSSKWKSTFSPISDIGLAKSADSPLQASSALSQNSLFTFRPALEEPSADAKLAAHPRKGFPGSLSGADGLSPGTNPANGCTFGGGLAADLSLHSFSDGASLPHKGPEAAGLSSPLSFPSQRGKEGSDANPFLSKRQLDGLAGLKGEGSRGKEAGEGGLPLCGPTDKTPLLSGKAAKARDREVDLKNGHNLFISAAAVPPGSLLSGPGLAPAASSAGGAASSAQTHRSFLGPFPPGPQFALGPMSLQANLGSVAGSSVLQSLFSSVPAAAGLVHVSSAATRLTNSHAMGSFSGVAGGTVGGN | |||||||
Modified residue | 297 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 297 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 374 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 374 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 390 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 392 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 447 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 448 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 448 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 458 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 471 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 471 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 480 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 480 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 764 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 772 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 775 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 775 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 786 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 786 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 816 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 826 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 826 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 834 | UniProt | Phosphoserine; by MAPK11 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 834 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 899 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 900 | UniProt | Phosphothreonine; by MAPK11 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 900 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 902 | UniProt | Phosphoserine; by MAPK11 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 902 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 984 | UniProt | Phosphothreonine; by MAPK11 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 984 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 997 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 997 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1001 | UniProt | Phosphoserine; by MAPK11 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1001 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1007 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1008 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1009 | UniProt | Phosphoserine; by MAPK11 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1009 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1030 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1032 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1035 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1035 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1039 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1059 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1061 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1065 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1083 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1093 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1093 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1096 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1100 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1104 | UniProt | Phosphoserine; by MAPK11 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1104 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1152 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1153 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1211 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1213 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1213 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1246 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1246 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1259 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1348 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1349 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TEK3 | MLLT1 Q03111 | 6 | EBI-2619253, EBI-1384215 | |
BINARY | Q8TEK3 | MLLT3 P42568 | 6 | EBI-2619253, EBI-716132 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-330 | DOT1 | ||||
Sequence: EPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSTGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILENYFSSLK | ||||||
Compositional bias | 334-349 | Basic and acidic residues | ||||
Sequence: LREEQEAARRRQQRES | ||||||
Region | 334-467 | Disordered | ||||
Sequence: LREEQEAARRRQQRESKSNAATPTKGPEGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMNTANPERKPKKNQTALDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSV | ||||||
Compositional bias | 390-415 | Basic residues | ||||
Sequence: SPSKARKKKLNKKGRKMAGRKRGRPK | ||||||
Region | 391-416 | Required for interaction with nucleosomes and DNA | ||||
Sequence: PSKARKKKLNKKGRKMAGRKRGRPKK | ||||||
Compositional bias | 416-431 | Basic and acidic residues | ||||
Sequence: KMNTANPERKPKKNQT | ||||||
Compositional bias | 433-467 | Polar residues | ||||
Sequence: LDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSV | ||||||
Region | 785-853 | Disordered | ||||
Sequence: LSQDHTVPGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQLAGEKSSEKGLRER | ||||||
Compositional bias | 809-823 | Polar residues | ||||
Sequence: ENGLPYQSPSVPGSM | ||||||
Region | 893-912 | Disordered | ||||
Sequence: RAERARSTPSPVLQPRDPSS | ||||||
Region | 957-1128 | Disordered | ||||
Sequence: TPGAEPATLDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAHQLSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAKRRIVFTITTGAGSAKQSPSSKHSPLTASARGDCVPSHGQDSRRRGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSPLNLN | ||||||
Compositional bias | 962-991 | Polar residues | ||||
Sequence: PATLDESSSSGSLFATVGSRSSTPQHPLLL | ||||||
Compositional bias | 998-1012 | Polar residues | ||||
Sequence: LPASPAHQLSSSPRL | ||||||
Compositional bias | 1051-1068 | Polar residues | ||||
Sequence: TGAGSAKQSPSSKHSPLT | ||||||
Region | 1145-1243 | Disordered | ||||
Sequence: SPETSLKSSPVPYQDHDQPPVLKKERPLSQTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLAGRKPAPAGEPVNSSKWKS | ||||||
Region | 1334-1410 | Disordered | ||||
Sequence: GASLPHKGPEAAGLSSPLSFPSQRGKEGSDANPFLSKRQLDGLAGLKGEGSRGKEAGEGGLPLCGPTDKTPLLSGKA |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8TEK3-2
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.
- Name1
- Length1,537
- Mass (Da)164,856
- Last updated2018-09-12 v3
- Checksum9CEA12850DC4ACB1
Q8TEK3-1
- Name2
- Differences from canonical
- 1537-1537: N → VVFNHAVPSASAHPFGARVGRGAACGSATLGPSPLQAAASASASSFQAPASVETRPPPPPPPPPPPLPPPAHLGRSPAGPPVLHAPPPPNAALPPPPTLLASNPEPALLQSLASLPPNQAFLPPTSAASLPPANASLSIKLTSLPHKGARPSFTVHHQPLPRLALAQAAPGIPQASATGPSAVWVSLGMPPPYAAHLSGVKPR
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5QL06 | A0A8I5QL06_HUMAN | DOT1L | 1738 | ||
C9JH95 | C9JH95_HUMAN | DOT1L | 208 | ||
V9GY76 | V9GY76_HUMAN | DOT1L | 142 | ||
H7C2S2 | H7C2S2_HUMAN | DOT1L | 653 | ||
A0A087X1A7 | A0A087X1A7_HUMAN | DOT1L | 69 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 210 | in Ref. 4; BAB84946 | ||||
Sequence: G → E | ||||||
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 | 433-467 | Polar residues | ||||
Sequence: LDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSV | ||||||
Sequence conflict | 454-467 | in Ref. 3 | ||||
Sequence: RSPHSPFYQLPPSV → TLRTPSGSPRRTKL | ||||||
Sequence conflict | 464 | in Ref. 4; BAB84946 | ||||
Sequence: P → L | ||||||
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 | ||||||
Alternative sequence | VSP_059795 | 1537 | in isoform 2 | |||
Sequence: N → VVFNHAVPSASAHPFGARVGRGAACGSATLGPSPLQAAASASASSFQAPASVETRPPPPPPPPPPPLPPPAHLGRSPAGPPVLHAPPPPNAALPPPPTLLASNPEPALLQSLASLPPNQAFLPPTSAASLPPANASLSIKLTSLPHKGARPSFTVHHQPLPRLALAQAAPGIPQASATGPSAVWVSLGMPPPYAAHLSGVKPR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF509504 EMBL· GenBank· DDBJ | AAM88322.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004490 EMBL· GenBank· DDBJ | AAC08316.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AB058717 EMBL· GenBank· DDBJ | BAB47443.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074120 EMBL· GenBank· DDBJ | BAB84946.1 EMBL· GenBank· DDBJ | mRNA |