TRIM24
entrez
8805
canonical
uniprot
O15164
canonical
ensembl
ENSG00000122779
resolver
ensp
ENSP00000340507
resolver
ensp
ENSP00000390829
resolver
ensp
ENSP00000591932
resolver
genesymbol
TRIM24
resolver
genesymbol_syn
RNF82
resolver
genesymbol_syn
TIF1
resolver
genesymbol_syn
TIF1A
resolver
hgnc
HGNC:11812
resolver
uniprot
A4D1R7
resolver
uniprot
A4D1R8
resolver
uniprot
O95854
resolver
uniprot_entry
TIF1A_HUMAN
resolver
uniprot_sec
A4D1R7
resolver
uniprot_sec
A4D1R8
resolver
uniprot_sec
O95854
resolver
amino_acid_sequence
MEVAVEKAVAAAAAASAAASGGPSAAPSGENEAESRQGPDSERGGEAARLNLLDTCAVCHQNIQSRAPKLLPCLHSFCQRCLPAPQRYLMLPAPMLGSAETPPPVPAPGSPVSGSSPFATQVGVIRCPVCSQECAERHIIDNFFVKDTTEVPSSTVEKSNQVCTSCEDNAEANGFCVECVEWLCKTCIRAHQRVKFTKDHTVRQKEEVSPEAVGVTSQRPVFCPFHKKEQLKLYCETCDKLTCRDCQLLEHKEHRYQFIEEAFQNQKVIIDTLITKLMEKTKYIKFTGNQIQNRIIEVNQNQKQVEQDIKVAIFTLMVEINKKGKALLHQLESLAKDHRMKLMQQQQEVAGLSKQLEHVMHFSKWAVSSGSSTALLYSKRLITYRLRHLLRARCDASPVTNNTIQFHCDPSFWAQNIINLGSLVIEDKESQPQMPKQNPVVEQNSQPPSGLSSNQLSKFPTQISLAQLRLQHMQQQVMAQRQQVQRRPAPVGLPNPRMQGPIQQPSISHQQPPPRLINFQNHSPKPNGPVLPPHPQQLRYPPNQNIPRQAIKPNPLQMAFLAQQAIKQWQISSGQGTPSTTNSTSSTPSSPTITSAAGYDGKAFGSPMIDLSSPVGGSYNLPSLPDIDCSSTIMLDNIVRKDTNIDHGQPRPPSNRTVQSPNSSVPSPGLAGPVTMTSVHPPIRSPSASSVGSRGSSGSSSKPAGADSTHKVPVVMLEPIRIKQENSGPPENYDFPVVIVKQESDEESRPQNANYPRSILTSLLLNSSQSSTSEETVLRSDAPDSTGDQPGLHQDNSSNGKSEWLDPSQKSPLHVGETRKEDDPNEDWCAVCQNGGELLCCEKCPKVFHLSCHVPTLTNFPSGEWICTFCRDLSKPEVEYDCDAPSHNSEKKKTEGLVKLTPIDKRKCERLLLFLYCHEMSLAFQDPVPLTVPDYYKIIKNPMDLSTIKKRLQEDYSMYSKPEDFVADFRLIFQNCAEFNEPDSEVANAGIKLENYFEELLKNLYPEKRFPKPEFRNESEDNKFSDDSDDDFVQPRKKRLKSIEERQLLK
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving TRIM24/TIF1 is found in papillary thyroid carcinomas (PTCs). Translocation t(7;10)(q32;q11) with RET. The translocation generates the TRIM24/RET (PTC6) oncogene. {ECO:0000269|PubMed:10439047}.
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. During the DNA damage response, participates in an autoregulatory feedback loop with TP53. Early in response to DNA damage, ATM kinase phosphorylates TRIM24 leading to its ubiquitination and degradation. After sufficient DNA repair has occurred, TP53 activates TRIM24 transcription, ultimately leading to TRIM24-mediated TP53 ubiquitination and degradation (PubMed:24820418). Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity). Also participates in innate immunity by mediating the specific 'Lys-63'-linked ubiquitination of TRAF3 leading to activation of downstream signal transduction of the type I IFN pathway (PubMed:32324863). Additionally, negatively regulates NLRP3/CASP1/IL-1beta-mediated pyroptosis and cell migration probably by ubiquitinating NLRP3 (PubMed:33724611). {ECO:0000250, ECO:0000269|PubMed:16322096, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:21164480, ECO:0000269|PubMed:24820418, ECO:0000269|PubMed:32324863, ECO:0000269|PubMed:33724611}.
uniprot
proteins
mass_dalton
116831
uniprot
proteins
mutagenesis
MUTAGEN 768; /note="S->A: Ubiquitination is significantly lower than wild-type."; /evidence="ECO:0000269|PubMed:24820418"; MUTAGEN 827; /note="D->A: Strongly reduced affinity for histone H3 that is not methylated at 'Lys-4' (H3K4me0)."; /evidence="ECO:0000269|PubMed:21164480"; MUTAGEN 840; /note="C->W: Abolishes interaction with histone H3."; /evidence="ECO:0000269|PubMed:21164480"; MUTAGEN 979..980; /note="FN->AA: Strongly reduced affinity for histone H3 that is acetylated at 'Lys-23' (H3K23ac)."; /evidence="ECO:0000269|PubMed:21164480
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-768 by ATM kinase induces ubiquitination and degradation during DNA damage. {ECO:0000269|PubMed:24820418}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:Q64127}.; PTM: Undergoes ubiquitination-mediated degradation in response to DNA damage. {ECO:0000269|PubMed:24820418}.
uniprot
proteins
pubmed
10022127
uniprot
proteins
pubmed
10439047
uniprot
proteins
pubmed
10935545
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16322096
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19556538
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19909775
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21164480
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22629402
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24820418
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25593309
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
32324863
uniprot
proteins
pubmed
33724611
uniprot
proteins
pubmed
9115274
uniprot
proteins
sequence_length
1050
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21164480, ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:32324863}. Cytoplasm {ECO:0000269|PubMed:21164480}. Mitochondrion {ECO:0000269|PubMed:32324863}. Note=Colocalizes with sites of active transcription. Predominantly nuclear. Translocated from nucleus to mitochondria to mediate antiviral immunity (PubMed:32324863). Localizes to sites of DNA damage (PubMed:25593309). {ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:32324863}.
uniprot
proteins