TIF1A_MOUSE
ID TIF1A_MOUSE Reviewed; 1051 AA.
AC Q64127; Q64126;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Transcription intermediary factor 1-alpha;
DE Short=TIF1-alpha;
DE EC=2.3.2.27;
DE AltName: Full=E3 ubiquitin-protein ligase Trim24;
DE AltName: Full=RING-type E3 ubiquitin transferase TIF1-alpha {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 24;
GN Name=Trim24; Synonyms=Tif1, Tif1a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESTROGEN RECEPTOR,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Carcinoma;
RX PubMed=7744009;
RA le Douarin B., Zechel C., Garnier J.-M., Lutz Y., Tora L., Pierrat B.,
RA Heery D., Gronemeyer H., Chambon P., Losson R.;
RT "The N-terminal part of TIF1, a putative mediator of the ligand-dependent
RT activation function (AF-2) of nuclear receptors, is fused to B-raf in the
RT oncogenic protein T18.";
RL EMBO J. 14:2020-2033(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH CBX1 AND CBX3.
RX PubMed=8978696;
RA le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F.,
RA Losson R., Chambon P.;
RT "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT control of transcription by nuclear receptors.";
RL EMBO J. 15:6701-6715(1996).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML.
RX PubMed=10610177; DOI=10.1038/15463;
RA Zhong S., Delva L., Rachez C., Cenciarelli C., Gandini D., Zhang H.,
RA Kalantry S., Freedman L.P., Pandolfi P.P.;
RT "A RA-dependent, tumour-growth suppressive transcription complex is the
RT target of the PML-RARalpha and T18 oncoproteins.";
RL Nat. Genet. 23:287-295(1999).
RN [5]
RP SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH CBX5, AND MUTAGENESIS
RP OF LYS-724 AND LYS-742.
RX PubMed=11313457; DOI=10.1128/mcb.21.10.3314-3324.2001;
RA Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T., Chambon P.,
RA Dejean A.;
RT "Common properties of nuclear protein SP100 and TIF1alpha chromatin factor:
RT role of SUMO modification.";
RL Mol. Cell. Biol. 21:3314-3324(2001).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16880268; DOI=10.1083/jcb.200603146;
RA Torres-Padilla M.E., Zernicka-Goetz M.;
RT "Role of TIF1alpha as a modulator of embryonic transcription in the mouse
RT zygote.";
RL J. Cell Biol. 174:329-338(2006).
RN [7]
RP FUNCTION, INTERACTION WITH CARM1, AND IDENTIFICATION IN A COACTIVATOR
RP COMPLEX WITH CARM1 AND NCOA2/GRIP1.
RX PubMed=16322096; DOI=10.1210/me.2005-0393;
RA Teyssier C., Ou C.Y., Khetchoumian K., Losson R., Stallcup M.R.;
RT "Transcriptional intermediary factor 1alpha mediates physical interaction
RT and functional synergy between the coactivator-associated arginine
RT methyltransferase 1 and glucocorticoid receptor-interacting protein 1
RT nuclear receptor coactivators.";
RL Mol. Endocrinol. 20:1276-1286(2006).
RN [8]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=17412818; DOI=10.1210/en.2006-1192;
RA Laz E.V., Holloway M.G., Chen C.S., Waxman D.J.;
RT "Characterization of three growth hormone-responsive transcription factors
RT preferentially expressed in adult female liver.";
RL Endocrinology 148:3327-3337(2007).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18026104; DOI=10.1038/ng.2007.15;
RA Khetchoumian K., Teletin M., Tisserand J., Mark M., Herquel B., Ignat M.,
RA Zucman-Rossi J., Cammas F., Lerouge T., Thibault C., Metzger D.,
RA Chambon P., Losson R.;
RT "Loss of Trim24 (Tif1alpha) gene function confers oncogenic activity to
RT retinoic acid receptor alpha.";
RL Nat. Genet. 39:1500-1506(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1026, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=18287084; DOI=10.1073/pnas.0712030105;
RA Ignat M., Teletin M., Tisserand J., Khetchoumian K., Dennefeld C.,
RA Chambon P., Losson R., Mark M.;
RT "Arterial calcifications and increased expression of vitamin D receptor
RT targets in mice lacking TIF1alpha.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2598-2603(2008).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AR; KAT5/TIP60 AND
RP BRD7.
RX PubMed=19909775; DOI=10.1016/j.bbamcr.2009.11.001;
RA Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J.,
RA Imamura M., Hatakeyama S.;
RT "TRIM24 mediates ligand-dependent activation of androgen receptor and is
RT repressed by a bromodomain-containing protein, BRD7, in prostate cancer
RT cells.";
RL Biochim. Biophys. Acta 1793:1828-1836(2009).
RN [13]
RP FUNCTION, INTERACTION WITH TP53, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19556538; DOI=10.1073/pnas.0813177106;
RA Allton K., Jain A.K., Herz H.M., Tsai W.W., Jung S.Y., Qin J., Bergmann A.,
RA Johnson R.L., Barton M.C.;
RT "Trim24 targets endogenous p53 for degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:11612-11616(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661; SER-668; SER-812 AND
RP SER-1026, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-469, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Transcriptional coactivator that interacts with numerous
CC nuclear receptors and coactivators and modulates the transcription of
CC target genes. Interacts with chromatin depending on histone H3
CC modifications, having the highest affinity for histone H3 that is both
CC unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac)
CC (By similarity). Has E3 protein-ubiquitin ligase activity. Promotes
CC ubiquitination and proteasomal degradation of p53/TP53. Plays a role in
CC the regulation of cell proliferation and apoptosis via its effects on
CC p53/TP53 levels. Up-regulates ligand-dependent transcription activation
CC by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates
CC transcription activation by retinoic acid (RA) receptors, such as RARA.
CC Plays a role in regulating retinoic acid-dependent proliferation of
CC hepatocytes. Required for normal transition from proliferating neonatal
CC hepatocytes to quiescent adult hepatocytes. {ECO:0000250,
CC ECO:0000269|PubMed:10610177, ECO:0000269|PubMed:16322096,
CC ECO:0000269|PubMed:16880268, ECO:0000269|PubMed:18026104,
CC ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:19909775,
CC ECO:0000269|PubMed:7744009}.
CC -!- FUNCTION: Transcriptional coactivator that interacts with numerous
CC nuclear receptors and coactivators and modulates the transcription of
CC target genes. Interacts with chromatin depending on histone H3
CC modifications, having the highest affinity for histone H3 that is both
CC unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac).
CC Has E3 protein-ubiquitin ligase activity. During the DNA damage
CC response, participates in an autoregulatory feedback loop with TP53.
CC Early in response to DNA damage, ATM kinase phosphorylates TRIM24
CC leading to its ubiquitination and degradation. After sufficient DNA
CC repair has occurred, TP53 activates TRIM24 transcription, ultimately
CC leading to TRIM24-mediated TP53 ubiquitination and degradation (By
CC similarity). Plays a role in the regulation of cell proliferation and
CC apoptosis, at least in part via its effects on p53/TP53 levels. Up-
CC regulates ligand-dependent transcription activation by AR, GCR/NR3C1,
CC thyroid hormone receptor (TR) and ESR1. Modulates transcription
CC activation by retinoic acid (RA) receptors, including RARA. Plays a
CC role in regulating retinoic acid-dependent proliferation of hepatocytes
CC (By similarity). Participates also in innate immunity by mediating the
CC specific 'Lys-63'-linked ubiquitination of TRAF3 leading to activation
CC of downstream signal transduction of the type I IFN pathway.
CC Additionally, negatively regulates NLRP3/CASP1/IL-1beta-mediated
CC pyroptosis and cell migration probably by ubiquitinating NLRP3 (By
CC similarity). {ECO:0000250|UniProtKB:O15164,
CC ECO:0000269|PubMed:10610177, ECO:0000269|PubMed:16322096,
CC ECO:0000269|PubMed:16880268, ECO:0000269|PubMed:18026104,
CC ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:19909775,
CC ECO:0000269|PubMed:7744009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via bromo domain) with histone H3 (via N-terminus),
CC provided that it is not methylated at 'Lys-4' (H3K4me0). Does not
CC interact with histone H3 that is methylated at 'Lys-4' (H3K4me1,
CC H3K4me2 or H3K4me3). Interacts (via bromo domain) with histone H3 (via
CC N-terminus) that is acetylated at 'Lys-23' (H3K23ac). Has the highest
CC affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0)
CC and acetylated at 'Lys-23' (H3K23ac). Has very low affinity for histone
CC H3 that is methylated at 'Lys-9' (H3K9me), or acetylated at both 'Lys-
CC 9' (H3K9ac) and 'Lys-14' (H3K14ac), or acetylated at 'Lys-27' (H3K27ac)
CC (in vitro). Interacts with TRIM16. Interacts with NR3C2/MCR (By
CC similarity). Interacts with the ligand-binding domain of estrogen
CC receptors (in vitro). Interaction with DNA-bound estrogen receptors
CC requires the presence of estradiol (By similarity). Interacts with AR,
CC CARM1, KAT5/TIP60, NCOA2/GRIP1, BRD7, CBX1, CBX3 and CBX5. Part of a
CC coactivator complex containing TRIM24, NCOA2/GRIP1 and CARM1. Interacts
CC with p53/TP53 and PML. {ECO:0000250, ECO:0000269|PubMed:10610177,
CC ECO:0000269|PubMed:11313457, ECO:0000269|PubMed:16322096,
CC ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:19909775,
CC ECO:0000269|PubMed:7744009, ECO:0000269|PubMed:8978696}.
CC -!- INTERACTION:
CC Q64127; P83917: Cbx1; NbExp=4; IntAct=EBI-307947, EBI-78119;
CC Q64127; Q61686: Cbx5; NbExp=4; IntAct=EBI-307947, EBI-307973;
CC Q64127; P02340: Tp53; NbExp=2; IntAct=EBI-307947, EBI-474016;
CC Q64127; Q99PP7: Trim33; NbExp=2; IntAct=EBI-307947, EBI-3043980;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Detected in the
CC cytoplasm of the zygote. Translocates into the pronucleus at the time
CC of genome activation. Colocalizes with sites of active transcription.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q64127-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q64127-2; Sequence=VSP_005773;
CC -!- TISSUE SPECIFICITY: Detected in embryonic and adult liver. Detected in
CC zygote and throughout embryogenesis (at protein level). Detected in all
CC adult tissues, with the highest expression level in testis.
CC {ECO:0000269|PubMed:17412818, ECO:0000269|PubMed:18026104}.
CC -!- INDUCTION: Before puberty, highly expressed in liver from males and
CC females. After puberty, expression is considerably higher in liver from
CC females compared to males. Up-regulated in males by continuous exposure
CC to growth hormone. {ECO:0000269|PubMed:17412818}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:11313457}.
CC -!- PTM: Phosphorylated at Ser-768 by ATM kinase induces ubiquitination and
CC degradation during DNA damage. {ECO:0000250|UniProtKB:O15164}.
CC -!- PTM: Undergoes ubiquitination-mediated degradation in response to DNA
CC damage. {ECO:0000250|UniProtKB:O15164}.
CC -!- DISEASE: Note=A chromosomal aberration involving TRIM24 produces a
CC TRIM24-BRAF (T18) oncogene originally isolated from a furfural-induced
CC hepatoma.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype during the first few months.
CC Impaired transition from proliferating neonatal hepatocytes to
CC quiescent adult hepatocytes. Hepatocytes continue to proliferate
CC throughout adulthood. High incidence hypertrophic hepatocytes with
CC enlarged nuclei after three months. After nine months, about half of
CC the mice have hepatocellular adenomas. Very high incidence of
CC hepatocarcinoma in 13 to 29 month old mice, increasing from 40% to 80%.
CC When one copy of Rara is disrupted, mice do not develop liver tumors or
CC liver dysplasia. {ECO:0000269|PubMed:18026104,
CC ECO:0000269|PubMed:18287084}.
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DR EMBL; S78221; AAB34290.1; -; mRNA.
DR EMBL; S78219; AAB34289.1; -; mRNA.
DR EMBL; BC056959; AAH56959.1; -; mRNA.
DR CCDS; CCDS20008.1; -. [Q64127-1]
DR CCDS; CCDS71751.1; -. [Q64127-2]
DR PIR; S55259; S55259.
DR RefSeq; NP_001258993.1; NM_001272064.1. [Q64127-2]
DR RefSeq; NP_001259005.1; NM_001272076.1.
DR RefSeq; NP_659542.3; NM_145076.4. [Q64127-1]
DR AlphaFoldDB; Q64127; -.
DR SMR; Q64127; -.
DR BioGRID; 204196; 17.
DR DIP; DIP-31476N; -.
DR IntAct; Q64127; 12.
DR STRING; 10090.ENSMUSP00000031859; -.
DR iPTMnet; Q64127; -.
DR PhosphoSitePlus; Q64127; -.
DR EPD; Q64127; -.
DR jPOST; Q64127; -.
DR MaxQB; Q64127; -.
DR PaxDb; Q64127; -.
DR PeptideAtlas; Q64127; -.
DR PRIDE; Q64127; -.
DR ProteomicsDB; 262780; -. [Q64127-1]
DR ProteomicsDB; 262781; -. [Q64127-2]
DR Antibodypedia; 32326; 563 antibodies from 39 providers.
DR DNASU; 21848; -.
DR Ensembl; ENSMUST00000031859; ENSMUSP00000031859; ENSMUSG00000029833. [Q64127-1]
DR Ensembl; ENSMUST00000120428; ENSMUSP00000113063; ENSMUSG00000029833. [Q64127-2]
DR GeneID; 21848; -.
DR KEGG; mmu:21848; -.
DR UCSC; uc009bjk.2; mouse. [Q64127-1]
DR UCSC; uc009bjl.2; mouse. [Q64127-2]
DR CTD; 8805; -.
DR MGI; MGI:109275; Trim24.
DR VEuPathDB; HostDB:ENSMUSG00000029833; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159863; -.
DR HOGENOM; CLU_005817_0_1_1; -.
DR InParanoid; Q64127; -.
DR OMA; WIGPSHT; -.
DR OrthoDB; 756911at2759; -.
DR PhylomeDB; Q64127; -.
DR TreeFam; TF106455; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 21848; 13 hits in 80 CRISPR screens.
DR ChiTaRS; Trim24; mouse.
DR PRO; PR:Q64127; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q64127; protein.
DR Bgee; ENSMUSG00000029833; Expressed in animal zygote and 271 other tissues.
DR ExpressionAtlas; Q64127; baseline and differential.
DR Genevisible; Q64127; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0000791; C:euchromatin; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005726; C:perichromatin fibrils; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0034056; F:estrogen response element binding; ISS:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IDA:MGI.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:MGI.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; ISS:UniProtKB.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IGI:MGI.
DR GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IMP:MGI.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Bromodomain; Chromosomal rearrangement; Coiled coil;
KW Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Transferase;
KW Tumor suppressor; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1051
FT /note="Transcription intermediary factor 1-alpha"
FT /id="PRO_0000056391"
FT DOMAIN 933..988
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 52..77
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 158..211
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 218..259
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 827..874
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..780
FT /note="Nuclear receptor binding site (NRBS)"
FT REGION 771..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..841
FT /note="Interaction with histone H3 that is not methylated
FT at 'Lys-4' (H3K4me0)"
FT /evidence="ECO:0000250"
FT REGION 1024..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..359
FT /evidence="ECO:0000255"
FT MOTIF 892..908
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 95..113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT SITE 332..333
FT /note="Breakpoint for translocation to form TRIM24-BRAF
FT oncogene"
FT SITE 828
FT /note="Interaction with histone H3 that is not methylated
FT at 'Lys-4' (H3K4me0)"
FT /evidence="ECO:0000250"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT MOD_RES 469
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 819
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT MOD_RES 1043
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 436
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 642
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 703
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 712
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 724
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000305"
FT CROSSLNK 724
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 724
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 742
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000305"
FT CROSSLNK 742
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 802
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 811
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 876
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 950
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 993
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT CROSSLNK 1042
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15164"
FT VAR_SEQ 477..510
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_005773"
FT MUTAGEN 724
FT /note="K->R: Loss of sumoylation; when associated with R-
FT 742."
FT /evidence="ECO:0000269|PubMed:11313457"
FT MUTAGEN 742
FT /note="K->R: Loss of sumoylation; when associated with R-
FT 724."
FT /evidence="ECO:0000269|PubMed:11313457"
SQ SEQUENCE 1051 AA; 116657 MW; 610584C1C6885972 CRC64;
MEVAVEKAAA AAAPAGGPAA AAPSGENEAE SRQGPDSESG GEASRLNLLD TCAVCHQNIQ
SRVPKLLPCL HSFCQRCLPA PQRYLMLTAP ALGSAETPPP APAPAPAPGS PAGGPSPFAT
QVGVIRCPVC SQECAERHII DNFFVKDTTE VPSSTVEKSN QVCTSCEDNA EANGFCVECV
EWLCKTCIRA HQRVKFTKDH TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK
LTCRDCQLLE HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKYTGNQ IQNRIIEINQ
NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA GLSKQLEHVM
HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT NTTIQFHCDP SFWAQNIINL
GSLVIEDKES QPQMPKQNPV VEQSSQPPGG LPSNQLSKFP TQISLAQLRL QHIQQQVMAQ
RQQVQRRPAP VGLPNPRMQG PIQQPSISHQ HPPPRLINFQ NHSPKPNGPV LPPYPQQLRY
SPSQNVPRQT TIKPNPLQMA FLAQQAIKQW QISSVQAPPT TASSSSSTPS SPTITSAAGY
DGKAFSSPMI DLSAPVGGSY NLPSLPDIDC SSTIMLDNIA RKDTGVDHAQ PRPPSNRTVQ
SPNSSVPSPG LAGPVTMTSV HPPIRSPSAS SVGSRGSSGS SSKPAGADST HKVPVVMLEP
IRIKQENSGP PENYDFPVVI VKQESDEESR PQNTNYPRSI LTSLLLNSSQ SSASEETVLR
SDAPDSTGDQ PGLHQENSSN GKSEWSDASQ KSPVHVGETR KEDDPNEDWC AVCQNGGELL
CCEKCPKVFH LTCHVPTLTN FPSGEWICTF CRDLSKPEVD YDCDVPSHHS EKRKSEGLTK
LTPIDKRKCE RLLLFLYCHE MSLAFQDPVP LTVPDYYKII KNPMDLSTIK KRLQEDYCMY
TKPEDFVADF RLIFQNCAEF NEPDSEVANA GIKLESYFEE LLKNLYPEKR FPKVEFRHEA
EDCKFSDDSD DDFVQPRKKR LKSTEDRQLL K
