Q5U3H2 · KMT5B_DANRE
- ProteinHistone-lysine N-methyltransferase KMT5B
- Genekmt5b
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids808 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Histone methyltransferase that specifically methylates monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription and maintenance of genome integrity. In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes (By similarity).
H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity).
Plays a role in myogenesis by regulating the expression of target genes, such as EID3. Facilitates TP53BP1 foci formation upon DNA damage and proficient non-homologous end-joining (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity).
May play a role in class switch reconbination by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity).
H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity).
Plays a role in myogenesis by regulating the expression of target genes, such as EID3. Facilitates TP53BP1 foci formation upon DNA damage and proficient non-homologous end-joining (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity).
May play a role in class switch reconbination by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity).
Catalytic activity
- N6-methyl-L-lysyl20-[histone H4] + S-adenosyl-L-methionine = H+ + N6,N6-dimethyl-L-lysyl20-[histone H4] + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
RHEA-COMP:15555 CHEBI:61929 Position: 20+ CHEBI:59789 = CHEBI:15378 + RHEA-COMP:15556 CHEBI:61976 Position: 20+ CHEBI:57856 - N6,N6-dimethyl-L-lysyl20-[histone H4] + S-adenosyl-L-methionine = H+ + N6,N6,N6-trimethyl-L-lysyl20-[histone H4] + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 96 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 178-181 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: YSSE | ||||||
Binding site | 185 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 232 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 247-248 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: NH | ||||||
Binding site | 250 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 294 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 295 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 296 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 299 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Molecular Function | histone H4K20 methyltransferase activity | |
Molecular Function | histone H4K20 monomethyltransferase activity | |
Molecular Function | histone H4K20me methyltransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | S-adenosyl-L-methionine binding | |
Biological Process | DNA repair | |
Biological Process | methylation | |
Biological Process | muscle organ development | |
Biological Process | positive regulation of double-strand break repair via nonhomologous end joining | |
Biological Process | positive regulation of isotype switching | |
Biological Process | regulation of multicellular organism growth |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone-lysine N-methyltransferase KMT5B
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionQ5U3H2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with pericentric heterochromatin.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000281790 | 1-808 | Histone-lysine N-methyltransferase KMT5B | |||
Sequence: MGESKNMVLNGRRHGRKFSSNQPVSKSRLQNTQRSHLRQNKGSPSVRRCSRRCGGAPPEAERRHVPSSGMTAKELCEYDDLSTSLILDPYLGFQTHKMNTRFRPIKGRQRELREIIELFKKHDNLEKAFQALTSGDWTRHHFLNKTKSQEKLFKAHVFVYLRMFASDSGFEILSCNRYSSEQNGAKIVATKDWKRNDKIEHLVGCIAELSPSEERMLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKVLRDIEPGEEISCYYGDGFFGENNEFCECYTCERRGTGAFKSKPGLPVEAPVINSKYGLRETDKRLNRLKKLGESCRNSDSQSVSSNAEADSQEPTTVQTSLRKRTSQSCVKKHGEAKAVTRQTLSSTPSSTSSSKRSQANISSLPKRLKSKPTQTLSKGRRRCRGLWTKGSSRVSASGNLKESSRRDTDRRRSASKGSVARSSENNRSSSKGASPCKDSTLCPYRTRRSTRTSLGAQGAEGTEASNHPASPSIVLKSEPGEFIPVTLGHQMSTPSLDSSCPKKGTCPRRRRTVKQEDSYGESFVQEGVPDLRHAVRAADVADCGKVVLGLPDRHQHYNGSSKSSKALRRGKGKKKRQITRYDAQLILQNNSGIPKITLRRRRDSSSSKNEPRETSSSSSSKISIKFSKEHEKDRSSSYVAKLNNGFSHGPHSSSTKLKIQLKREEDPASLHRTYPEDVTLGIVQRDAADVLDHKAAAQVGQDMEVESMSSEDDDDDYFDNEDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA |
Proteomic databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-68 | Disordered | ||||
Sequence: MGESKNMVLNGRRHGRKFSSNQPVSKSRLQNTQRSHLRQNKGSPSVRRCSRRCGGAPPEAERRHVPSS | ||||||
Compositional bias | 15-46 | Polar residues | ||||
Sequence: GRKFSSNQPVSKSRLQNTQRSHLRQNKGSPSV | ||||||
Domain | 168-283 | SET | ||||
Sequence: SGFEILSCNRYSSEQNGAKIVATKDWKRNDKIEHLVGCIAELSPSEERMLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKVLRDIEPGEEISCYYG | ||||||
Region | 339-569 | Disordered | ||||
Sequence: LGESCRNSDSQSVSSNAEADSQEPTTVQTSLRKRTSQSCVKKHGEAKAVTRQTLSSTPSSTSSSKRSQANISSLPKRLKSKPTQTLSKGRRRCRGLWTKGSSRVSASGNLKESSRRDTDRRRSASKGSVARSSENNRSSSKGASPCKDSTLCPYRTRRSTRTSLGAQGAEGTEASNHPASPSIVLKSEPGEFIPVTLGHQMSTPSLDSSCPKKGTCPRRRRTVKQEDSYGE | ||||||
Compositional bias | 343-373 | Polar residues | ||||
Sequence: CRNSDSQSVSSNAEADSQEPTTVQTSLRKRT | ||||||
Compositional bias | 387-420 | Polar residues | ||||
Sequence: VTRQTLSSTPSSTSSSKRSQANISSLPKRLKSKP | ||||||
Compositional bias | 421-435 | Basic residues | ||||
Sequence: TQTLSKGRRRCRGLW | ||||||
Compositional bias | 448-465 | Basic and acidic residues | ||||
Sequence: LKESSRRDTDRRRSASKG | ||||||
Compositional bias | 466-484 | Polar residues | ||||
Sequence: SVARSSENNRSSSKGASPC | ||||||
Compositional bias | 491-520 | Polar residues | ||||
Sequence: PYRTRRSTRTSLGAQGAEGTEASNHPASPS | ||||||
Region | 599-684 | Disordered | ||||
Sequence: PDRHQHYNGSSKSSKALRRGKGKKKRQITRYDAQLILQNNSGIPKITLRRRRDSSSSKNEPRETSSSSSSKISIKFSKEHEKDRSS |
Sequence similarities
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar4-20 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length808
- Mass (Da)90,438
- Last updated2007-04-03 v2
- Checksum11510B288E3195B0
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 15-46 | Polar residues | ||||
Sequence: GRKFSSNQPVSKSRLQNTQRSHLRQNKGSPSV | ||||||
Compositional bias | 343-373 | Polar residues | ||||
Sequence: CRNSDSQSVSSNAEADSQEPTTVQTSLRKRT | ||||||
Compositional bias | 387-420 | Polar residues | ||||
Sequence: VTRQTLSSTPSSTSSSKRSQANISSLPKRLKSKP | ||||||
Compositional bias | 421-435 | Basic residues | ||||
Sequence: TQTLSKGRRRCRGLW | ||||||
Compositional bias | 448-465 | Basic and acidic residues | ||||
Sequence: LKESSRRDTDRRRSASKG | ||||||
Compositional bias | 466-484 | Polar residues | ||||
Sequence: SVARSSENNRSSSKGASPC | ||||||
Compositional bias | 491-520 | Polar residues | ||||
Sequence: PYRTRRSTRTSLGAQGAEGTEASNHPASPS | ||||||
Sequence conflict | 535 | in Ref. 2; AAH85544 | ||||
Sequence: L → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX571884 EMBL· GenBank· DDBJ | CAK05146.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC085544 EMBL· GenBank· DDBJ | AAH85544.1 EMBL· GenBank· DDBJ | mRNA |