JMJD7
entrez
100137047
canonical
uniprot
P0C870
canonical
ensembl
ENSG00000243789
resolver
ensp
ENSP00000380467
resolver
enst
ENST00000397299
resolver
genesymbol
JMJD7
resolver
hgnc
HGNC:34397
resolver
uniprot
A5D6V5
resolver
uniprot
O95712
resolver
uniprot
Q59GF9
resolver
uniprot
Q8TB10
resolver
uniprot
Q9UKV7
resolver
uniprot_entry
JMJD7_HUMAN
resolver
uniprot_sec
A5D6V5
resolver
uniprot_sec
O95712
resolver
uniprot_sec
Q59GF9
resolver
uniprot_sec
Q8TB10
resolver
uniprot_sec
Q9UKV7
resolver
amino_acid_sequence
MAEAALEAVRSELREFPAAARELCVPLAVPYLDKPPTPLHFYRDWVCPNRPCIIRNALQHWPALQKWSLPYFRATVGSTEVSVAVTPDGYADAVRGDRFMMPAERRLPLSFVLDVLEGRAQHPGVLYVQKQCSNLPSELPQLLPDLESHVPWASEALGKMPDAVNFWLGEAAAVTSLHKDHYENLYCVVSGEKHFLFHPPSDRPFIPYELYTPATYQLTEEGTFKVVDEEAMEKVPWIPLDPLAPDLARYPSYSQAQALRCTVRAGEMLYLPALWFHHVQQSQGCIAVNFWYDMEYDLKYSYFQLLDSLTKASGLD
uniprot
proteins
ec_number
1.14.11.63
uniprot
proteins
ec_number
3.4.-.-
uniprot
proteins
function
FUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase (PubMed:28847961, PubMed:29915238). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation (PubMed:28847961). Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4 (PubMed:28847961). After initial cleavage, continues to digest histones tails via its aminopeptidase activity (PubMed:28847961). Additionally, may play a role in protein biosynthesis by modifying the translation machinery (PubMed:29915238). Acts as a Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys-21' of DRG2 translation factors (TRAFAC), promoting their interaction with ribonucleic acids (RNA) (PubMed:29915238). {ECO:0000269|PubMed:28847961, ECO:0000269|PubMed:29915238}.
uniprot
proteins
mass_dalton
35932
uniprot
proteins
mutagenesis
MUTAGEN 47; /note="C->A: Impairs homodimer formation."; /evidence="ECO:0000269|PubMed:29915238"; MUTAGEN 178; /note="H->A: Loss of peptidase activity toward methylated histones and reduced anchorage-independent growth of transformed cells; when associated with A-180 and A-277. Impairs L-lysine (3S)-hydroxylase activity. Impairs the interaction with DRG1 and DRG2."; /evidence="ECO:0000269|PubMed:28847961, ECO:0000269|PubMed:29915238"; MUTAGEN 180; /note="D->A: Loss of peptidase activity toward methylated histones and reduced anchorage-independent growth of transformed cells; when associated with A-180 and A-277."; /evidence="ECO:0000269|PubMed:28847961"; MUTAGEN 277; /note="H->A: Loss of peptidase activity toward methylated histones and reduced anchorage-independent growth of transformed cells; when associated with A-180 and A-277."; /evidence="ECO:0000269|PubMed:28847961
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
23033978
uniprot
proteins
pubmed
28847961
uniprot
proteins
pubmed
29915238
uniprot
proteins
pubmed
35410347
uniprot
proteins
sequence_length
316
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29915238}. Cytoplasm {ECO:0000269|PubMed:29915238}.
uniprot
proteins