KDM4A
entrez
9682
canonical
uniprot
O75164
canonical
ensembl
ENSG00000066135
resolver
ensp
ENSP00000361473
resolver
genesymbol
KDM4A
resolver
genesymbol_syn
JHDM3A
resolver
genesymbol_syn
JMJD2
resolver
genesymbol_syn
JMJD2A
resolver
genesymbol_syn
KIAA0677
resolver
hgnc
HGNC:22978
resolver
uniprot
Q5VVB1
resolver
uniprot_entry
KDM4A_HUMAN
resolver
uniprot_sec
Q5VVB1
resolver
activity_regulation
ACTIVITY REGULATION: Several specific inhibitors are being developed and tested. {ECO:0000269|PubMed:26741168}.
uniprot
proteins
amino_acid_sequence
MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESELPPRAGNEEECPEEDMEGVEDGEEGDLKTSLAKHRIGTKRHRVCLEIPQEVSQSELFPKEDLSSEQYEMTECPAALAPVRPTHSSVRQVEDGLTFPDYSDSTEVKFEELKNVKLEEEDEEEEQAAAALDLSVNPASVGGRLVFSGSKKKSSSSLGSGSSRDSISSDSETSEPLSCRAQGQTGVLTVHSYAKGDGRVTVGEPCTRKKGSAARSFSERELAEVADEYMFSLEENKKSKGRRQPLSKLPRHHPLVLQECVSDDETSEQLTPEEEAEETEAWAKPLSQLWQNRPPNFEAEKEFNETMAQQAPHCAVCMIFQTYHQVEFGGFNQNCGNASDLAPQKQRTKPLIPEMCFTSTGCSTDINLSTPYLEEDGTSILVSCKKCSVRVHASCYGVPPAKASEDWMCSRCSANALEEDCCLCSLRGGALQRANDDRWVHVSCAVAILEARFVNIAERSPVDVSKIPLPRFKLKCIFCKKRRKRTAGCCVQCSHGRCPTAFHVSCAQAAGVMMQPDDWPFVVFITCFRHKIPNLERAKGALQSITAGQKVISKHKNGRFYQCEVVRLTTETFYEVNFDDGSFSDNLYPEDIVSQDCLQFGPPAEGEVVQVRWTDGQVYGAKFVASHPIQMYQVEFEDGSQLVVKRDDVYTLDEELPKRVKSRLSVASDMRFNEIFTEKEVKQEKKRQRVINSRYREDYIEPALYRAIME
uniprot
proteins
ec_number
1.14.11.66
uniprot
proteins
ec_number
1.14.11.69
uniprot
proteins
function
FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code (PubMed:16603238, PubMed:26741168, PubMed:21768309). Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20' (PubMed:16603238, PubMed:26741168, PubMed:21768309). Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues (PubMed:16603238, PubMed:26741168, PubMed:21768309). Demethylation of Lys residue generates formaldehyde and succinate (PubMed:16603238). Also able to demethylate histone H1-4 methylated at 'Lys-26' (H1.4K26me1, H1.4K26me2 and H1.4K26me3) (PubMed:19144645, PubMed:30156264). Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively (PubMed:16024779). {ECO:0000269|PubMed:16024779, ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:19144645, ECO:0000269|PubMed:21768309, ECO:0000269|PubMed:26741168, ECO:0000269|PubMed:30156264}.; FUNCTION: [Isoform 2]: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain. {ECO:0000269|PubMed:21694756}.
uniprot
proteins
mass_dalton
120662
uniprot
proteins
mutagenesis
MUTAGEN 133; /note="G->A: Abolishes histone demethylase activity; when associated with A-138."; /evidence="ECO:0000269|PubMed:16677698"; MUTAGEN 138; /note="G->A: Abolishes histone demethylase activity; when associated with A-138."; /evidence="ECO:0000269|PubMed:16677698"; MUTAGEN 165; /note="G->A: Abolishes histone demethylase activity; when associated with A-165."; /evidence="ECO:0000269|PubMed:16677698"; MUTAGEN 170; /note="G->A: Abolishes histone demethylase activity; when associated with A-165."; /evidence="ECO:0000269|PubMed:16677698"; MUTAGEN 188; /note="H->A: Abolishes histone demethylase activity without affecting ability to bind H4K20me2."; /evidence="ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:22373579"; MUTAGEN 288..289; /note="ST->AI: Displays histone demethylase activity for both dimethylated and H3-K9Me3."; MUTAGEN 288..289; /note="ST->TV,NV,GG: Abolishes histone demethylase activity."; MUTAGEN 471; /note="K->R: Complete loss of SUMO modification by human herpes virus 8 protein K-bZIP/K8."; /evidence="ECO:0000269|PubMed:28212444"; MUTAGEN 939; /note="D->R: Impairs binding to H4K20me2, promoting partial recruitment of TP53BP1."; /evidence="ECO:0000269|PubMed:22373579"; MUTAGEN 945; /note="D->A: Impairs binding to H3K4me3."; /evidence="ECO:0000269|PubMed:16601153"; MUTAGEN 945; /note="D->R: Abolishes binding to H3K4me3."; /evidence="ECO:0000269|PubMed:16601153"; MUTAGEN 967; /note="W->H: Abolishes binding to H3K4me3."; /evidence="ECO:0000269|PubMed:16601153"; MUTAGEN 973; /note="Y->A: Abolishes binding to H3K4me3."; /evidence="ECO:0000269|PubMed:16601153, ECO:0000269|PubMed:16677698
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) SUMOylated by human herpesvirus 8 E3 SUMO-protein ligase K-bZIP/K8 at Lys-471; thereby modulating the chromatin binding and histone demethylase activity of KDM4A. {ECO:0000269|PubMed:28212444}.; PTM: Ubiquitinated by RNF8 and RNF168 following DNA damage, leading to its degradation. Degradation promotes accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited. Also ubiquitinated by the SCF(FBXO22) complex; leading to proteasomal degradation (PubMed:21768309). {ECO:0000269|PubMed:21768309, ECO:0000269|PubMed:22373579}.
uniprot
proteins
protein_family
JHDM3 histone demethylase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15927959
uniprot
proteins
pubmed
16024779
uniprot
proteins
pubmed
16415788
uniprot
proteins
pubmed
16601153
uniprot
proteins
pubmed
16603238
uniprot
proteins
pubmed
16677698
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19144645
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21694756
uniprot
proteins
pubmed
21768309
uniprot
proteins
pubmed
22373579
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
26741168
uniprot
proteins
pubmed
27214403
uniprot
proteins
pubmed
28212444
uniprot
proteins
pubmed
30156264
uniprot
proteins
pubmed
37179361
uniprot
proteins
pubmed
9734811
uniprot
proteins
sequence_length
1064
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:16024779}.
uniprot
proteins