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Protein

Histone-lysine N-methyltransferase, H3 lysine-79 specific

Gene

DOT1L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones (PubMed:12123582). Binds to DNA (PubMed:12628190).2 Publications

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 activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N6-methyl-L-lysine-[histone].PROSITE-ProRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei186S-adenosyl-L-methionine1

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • histone-lysine N-methyltransferase activity Source: UniProtKB
  • histone methyltransferase activity Source: MGI
  • histone methyltransferase activity (H3-K79 specific) Source: GO_Central
  • transcription factor binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, DNA-binding, Methyltransferase, Transferase
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-HSA-3214841 PKMTs methylate histone lysines
SIGNORiQ8TEK3

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase, H3 lysine-79 specificCurated (EC:2.1.1.431 Publication)
Alternative name(s):
DOT1-like protein
Histone H3-K79 methyltransferase
Short name:
H3-K79-HMTase
Lysine N-methyltransferase 4
Gene namesi
Name:DOT1LImported
Synonyms:KIAA1814, KMT4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000104885.17
HGNCiHGNC:24948 DOT1L
MIMi607375 gene
neXtProtiNX_Q8TEK3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi163 – 165GSG → RCR: Abolishes methyltransferase activity. 1 Publication3
Mutagenesisi241N → A or D: Loss of activity. 1 Publication1
Mutagenesisi312Y → A: Loss of activity. 1 Publication1
Mutagenesisi312Y → F: No effect. 1 Publication1

Organism-specific databases

DisGeNETi84444
OpenTargetsiENSG00000104885
PharmGKBiPA134993717

Chemistry databases

ChEMBLiCHEMBL1795117
GuidetoPHARMACOLOGYi2650

Polymorphism and mutation databases

BioMutaiDOT1L
DMDMi25090171

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001860891 – 1537Histone-lysine N-methyltransferase, H3 lysine-79 specificAdd BLAST1537

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei297PhosphoserineCombined sources1
Modified residuei374PhosphoserineCombined sources1
Modified residuei448PhosphoserineCombined sources1
Modified residuei471PhosphoserineCombined sources1
Modified residuei480PhosphothreonineCombined sources1
Modified residuei775PhosphoserineCombined sources1
Modified residuei786PhosphoserineCombined sources1
Modified residuei826PhosphoserineCombined sources1
Modified residuei834PhosphoserineCombined sources1
Modified residuei900PhosphothreonineCombined sources1
Modified residuei902PhosphoserineCombined sources1
Modified residuei984PhosphothreonineCombined sources1
Modified residuei997PhosphoserineCombined sources1
Modified residuei1001PhosphoserineCombined sources1
Modified residuei1009PhosphoserineCombined sources1
Modified residuei1035PhosphoserineCombined sources1
Modified residuei1093PhosphoserineCombined sources1
Modified residuei1104PhosphoserineCombined sources1
Modified residuei1213PhosphoserineCombined sources1
Modified residuei1246PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8TEK3
MaxQBiQ8TEK3
PaxDbiQ8TEK3
PeptideAtlasiQ8TEK3
PRIDEiQ8TEK3
ProteomicsDBi74468
74469 [Q8TEK3-2]

PTM databases

iPTMnetiQ8TEK3
PhosphoSitePlusiQ8TEK3

Expressioni

Gene expression databases

BgeeiENSG00000104885 Expressed in 144 organ(s), highest expression level in testis
CleanExiHS_DOT1L
ExpressionAtlasiQ8TEK3 baseline and differential
GenevisibleiQ8TEK3 HS

Organism-specific databases

HPAiHPA011875
HPA071217

Interactioni

Subunit structurei

Interacts with MLLT10.2 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi124082, 45 interactors
DIPiDIP-56410N
IntActiQ8TEK3, 28 interactors
MINTiQ8TEK3
STRINGi9606.ENSP00000381657

Chemistry databases

BindingDBiQ8TEK3

Structurei

Secondary structure

11537
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ8TEK3
SMRiQ8TEK3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TEK3

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 330DOT1PROSITE-ProRule annotationAdd