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Q64127

- TIF1A_MOUSE

UniProt

Q64127 - TIF1A_MOUSE

Protein

Transcription intermediary factor 1-alpha

Gene

Trim24

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    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) By similarity. Has E3 protein-ubiquitin ligase activity. Promotes ubiquitination and proteasomal degradation of p53/TP53. Plays a role in the regulation of cell proliferation and apoptosis 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, such as RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes. Required for normal transition from proliferating neonatal hepatocytes to quiescent adult hepatocytes.By similarity7 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei332 – 3332Breakpoint for translocation to form TRIM24-BRAF oncogene
    Sitei828 – 8281Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri52 – 7726RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri158 – 21154B box-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri218 – 25942B box-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri827 – 87448PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. estrogen response element binding Source: UniProtKB
    3. ligand-dependent nuclear receptor binding Source: MGI
    4. ligase activity Source: UniProtKB-KW
    5. lysine-acetylated histone binding Source: UniProtKB
    6. p53 binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein kinase activity Source: MGI
    9. sequence-specific DNA binding Source: MGI
    10. transcription coactivator activity Source: UniProtKB
    11. ubiquitin-protein transferase activity Source: UniProtKB
    12. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. calcium ion homeostasis Source: MGI
    2. cellular response to estrogen stimulus Source: UniProtKB
    3. negative regulation of cell proliferation Source: MGI
    4. negative regulation of transcription, DNA-templated Source: MGI
    5. positive regulation of gene expression Source: MGI
    6. positive regulation of transcription, DNA-templated Source: MGI
    7. protein autophosphorylation Source: MGI
    8. protein catabolic process Source: UniProtKB
    9. protein phosphorylation Source: MGI
    10. protein ubiquitination Source: UniProtKB
    11. regulation of apoptotic process Source: Ensembl
    12. regulation of protein stability Source: UniProtKB
    13. regulation of signal transduction by p53 class mediator Source: MGI
    14. regulation of vitamin D receptor signaling pathway Source: MGI
    15. response to peptide hormone Source: Ensembl
    16. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_196460. Signaling by FGFR1 fusion mutants.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription intermediary factor 1-alpha (EC:6.3.2.-)
    Short name:
    TIF1-alpha
    Alternative name(s):
    E3 ubiquitin-protein ligase Trim24
    Tripartite motif-containing protein 24
    Gene namesi
    Name:Trim24
    Synonyms:Tif1, Tif1a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:109275. Trim24.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Detected in the cytoplasm of the zygote. Translocates into the pronucleus at the time of genome activation. Colocalizes with sites of active transcription.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nuclear euchromatin Source: MGI
    3. nucleus Source: UniProtKB
    4. perichromatin fibrils Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving TRIM24 produces a TRIM24-BRAF (T18) oncogene originally isolated from a furfural-induced hepatoma.

    Disruption phenotypei

    No visible phenotype during the first few months. Impaired transition from proliferating neonatal hepatocytes to quiescent adult hepatocytes. Hepatocytes continue to proliferate throughout adulthood. High incidence hypertrophic hepatocytes with enlarged nuclei after three months. After nine months, about half of the mice have hepatocellular adenomas. Very high incidence of hepatocarcinoma in 13 to 29 month old mice, increasing from 40% to 80%. When one copy of Rara is disrupted, mice do not develop liver tumors or liver dysplasia.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi724 – 7241K → R: Loss of sumoylation; when associated with R-742. 1 Publication
    Mutagenesisi742 – 7421K → R: Loss of sumoylation; when associated with R-724. 1 Publication

    Keywords - Diseasei

    Proto-oncogene, Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10511051Transcription intermediary factor 1-alphaPRO_0000056391Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei97 – 971PhosphothreonineBy similarity
    Modified residuei110 – 1101PhosphoserineBy similarity
    Modified residuei668 – 6681PhosphoserineBy similarity
    Cross-linki724 – 724Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Cross-linki742 – 742Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Modified residuei745 – 7451PhosphoserineBy similarity
    Modified residuei769 – 7691PhosphoserineBy similarity
    Modified residuei809 – 8091PhosphoserineBy similarity
    Modified residuei812 – 8121PhosphoserineBy similarity
    Modified residuei819 – 8191PhosphothreonineBy similarity
    Modified residuei1026 – 10261Phosphoserine1 Publication
    Modified residuei1029 – 10291Phosphoserine1 Publication
    Modified residuei1043 – 10431PhosphoserineBy similarity

    Post-translational modificationi

    Sumoylated.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ64127.
    PaxDbiQ64127.
    PRIDEiQ64127.

    PTM databases

    PhosphoSiteiQ64127.

    Expressioni

    Tissue specificityi

    Detected in embryonic and adult liver. Detected in zygote and throughout embryogenesis (at protein level). Detected in all adult tissues, with the highest expression level in testis.2 Publications

    Inductioni

    Before puberty, highly expressed in liver from males and females. After puberty, expression is considerably higher in liver from females compared to males. Up-regulated in males by continuous exposure to growth hormone.1 Publication

    Gene expression databases

    ArrayExpressiQ64127.
    BgeeiQ64127.
    CleanExiMM_TRIM24.
    GenevestigatoriQ64127.

    Interactioni

    Subunit structurei

    Interacts (via bromo domain) with histone H3 (via N-terminus), provided that it is not methylated at 'Lys-4' (H3K4me0). Does not interact with histone H3 that is methylated at 'Lys-4' (H3K4me1, H3K4me2 or H3K4me3). Interacts (via bromo domain) with histone H3 (via N-terminus) that is acetylated at 'Lys-23' (H3K23ac). Has the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has very low affinity for histone H3 that is methylated at 'Lys-9' (H3K9me), or acetylated at both 'Lys-9' (H3K9ac) and 'Lys-14' (H3K14ac), or acetylated at 'Lys-27' (H3K27ac) (in vitro). Interacts with NR3C2/MCR By similarity. Interacts with the ligand-binding domain of estrogen receptors (in vitro). Interaction with DNA-bound estrogen receptors requires the presence of estradiol By similarity. Interacts with AR, CARM1, KAT5/TIP60, NCOA2/GRIP1, BRD7, CBX1, CBX3 and CBX5. Part of a coactivator complex containing TRIM24, NCOA2/GRIP1 and CARM1. Interacts with p53/TP53 and PML.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Cbx1P839174EBI-307947,EBI-78119
    Cbx5Q616864EBI-307947,EBI-307973

    Protein-protein interaction databases

    BioGridi204196. 11 interactions.
    DIPiDIP-31476N.
    IntActiQ64127. 10 interactions.
    MINTiMINT-4137892.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64127.
    SMRiQ64127. Positions 50-83, 218-261, 825-1013.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini933 – 98856BromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni755 – 78026Nuclear receptor binding site (NRBS)Add
    BLAST
    Regioni835 – 8417Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)By similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili289 – 35971Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi892 – 90817Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi8 – 158Poly-Ala
    Compositional biasi19 – 224Poly-Ala
    Compositional biasi344 – 3474Poly-Gln
    Compositional biasi583 – 5875Poly-Ser

    Sequence similaritiesi

    Contains 2 B box-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri52 – 7726RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri158 – 21154B box-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri218 – 25942B box-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri827 – 87448PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5076.
    GeneTreeiENSGT00530000062982.
    HOGENOMiHOG000252971.
    HOVERGENiHBG054599.
    InParanoidiQ64127.
    KOiK08881.
    OMAiPGLHQEN.
    OrthoDBiEOG790FZZ.
    PhylomeDBiQ64127.
    TreeFamiTF106455.

    Family and domain databases

    Gene3Di1.20.920.10. 1 hit.
    3.30.40.10. 3 hits.
    4.10.45.10. 1 hit.
    InterProiIPR003649. Bbox_C.
    IPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR000315. Znf_B-box.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00439. Bromodomain. 1 hit.
    PF00628. PHD. 1 hit.
    PF00643. zf-B_box. 2 hits.
    [Graphical view]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00502. BBC. 1 hit.
    SM00336. BBOX. 2 hits.
    SM00297. BROMO. 1 hit.
    SM00249. PHD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
    PS50014. BROMODOMAIN_2. 1 hit.
    PS50119. ZF_BBOX. 2 hits.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q64127-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEVAVEKAAA AAAPAGGPAA AAPSGENEAE SRQGPDSESG GEASRLNLLD     50
    TCAVCHQNIQ SRVPKLLPCL HSFCQRCLPA PQRYLMLTAP ALGSAETPPP 100
    APAPAPAPGS PAGGPSPFAT QVGVIRCPVC SQECAERHII DNFFVKDTTE 150
    VPSSTVEKSN QVCTSCEDNA EANGFCVECV EWLCKTCIRA HQRVKFTKDH 200
    TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK LTCRDCQLLE 250
    HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKYTGNQ IQNRIIEINQ 300
    NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA 350
    GLSKQLEHVM HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT 400
    NTTIQFHCDP SFWAQNIINL GSLVIEDKES QPQMPKQNPV VEQSSQPPGG 450
    LPSNQLSKFP TQISLAQLRL QHIQQQVMAQ RQQVQRRPAP VGLPNPRMQG 500
    PIQQPSISHQ HPPPRLINFQ NHSPKPNGPV LPPYPQQLRY SPSQNVPRQT 550
    TIKPNPLQMA FLAQQAIKQW QISSVQAPPT TASSSSSTPS SPTITSAAGY 600
    DGKAFSSPMI DLSAPVGGSY NLPSLPDIDC SSTIMLDNIA RKDTGVDHAQ 650
    PRPPSNRTVQ SPNSSVPSPG LAGPVTMTSV HPPIRSPSAS SVGSRGSSGS 700
    SSKPAGADST HKVPVVMLEP IRIKQENSGP PENYDFPVVI VKQESDEESR 750
    PQNTNYPRSI LTSLLLNSSQ SSASEETVLR SDAPDSTGDQ PGLHQENSSN 800
    GKSEWSDASQ KSPVHVGETR KEDDPNEDWC AVCQNGGELL CCEKCPKVFH 850
    LTCHVPTLTN FPSGEWICTF CRDLSKPEVD YDCDVPSHHS EKRKSEGLTK 900
    LTPIDKRKCE RLLLFLYCHE MSLAFQDPVP LTVPDYYKII KNPMDLSTIK 950
    KRLQEDYCMY TKPEDFVADF RLIFQNCAEF NEPDSEVANA GIKLESYFEE 1000
    LLKNLYPEKR FPKVEFRHEA EDCKFSDDSD DDFVQPRKKR LKSTEDRQLL 1050
    K 1051
    Length:1,051
    Mass (Da):116,657
    Last modified:November 1, 1996 - v1
    Checksum:i610584C1C6885972
    GO
    Isoform Short (identifier: Q64127-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         477-510: Missing.

    Show »
    Length:1,017
    Mass (Da):112,844
    Checksum:i0EDAF4BC938F56B6
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei477 – 51034Missing in isoform Short. CuratedVSP_005773Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S78221 mRNA. Translation: AAB34290.1.
    S78219 mRNA. Translation: AAB34289.1.
    BC056959 mRNA. Translation: AAH56959.1.
    CCDSiCCDS20008.1. [Q64127-1]
    CCDS71751.1. [Q64127-2]
    PIRiS55259.
    RefSeqiNP_001258993.1. NM_001272064.1. [Q64127-2]
    NP_001259005.1. NM_001272076.1.
    NP_659542.3. NM_145076.4. [Q64127-1]
    UniGeneiMm.41063.

    Genome annotation databases

    EnsembliENSMUST00000031859; ENSMUSP00000031859; ENSMUSG00000029833. [Q64127-1]
    ENSMUST00000120428; ENSMUSP00000113063; ENSMUSG00000029833. [Q64127-2]
    GeneIDi21848.
    KEGGimmu:21848.
    UCSCiuc009bjk.1. mouse. [Q64127-1]
    uc009bjl.1. mouse. [Q64127-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S78221 mRNA. Translation: AAB34290.1 .
    S78219 mRNA. Translation: AAB34289.1 .
    BC056959 mRNA. Translation: AAH56959.1 .
    CCDSi CCDS20008.1. [Q64127-1 ]
    CCDS71751.1. [Q64127-2 ]
    PIRi S55259.
    RefSeqi NP_001258993.1. NM_001272064.1. [Q64127-2 ]
    NP_001259005.1. NM_001272076.1.
    NP_659542.3. NM_145076.4. [Q64127-1 ]
    UniGenei Mm.41063.

    3D structure databases

    ProteinModelPortali Q64127.
    SMRi Q64127. Positions 50-83, 218-261, 825-1013.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204196. 11 interactions.
    DIPi DIP-31476N.
    IntActi Q64127. 10 interactions.
    MINTi MINT-4137892.

    PTM databases

    PhosphoSitei Q64127.

    Proteomic databases

    MaxQBi Q64127.
    PaxDbi Q64127.
    PRIDEi Q64127.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031859 ; ENSMUSP00000031859 ; ENSMUSG00000029833 . [Q64127-1 ]
    ENSMUST00000120428 ; ENSMUSP00000113063 ; ENSMUSG00000029833 . [Q64127-2 ]
    GeneIDi 21848.
    KEGGi mmu:21848.
    UCSCi uc009bjk.1. mouse. [Q64127-1 ]
    uc009bjl.1. mouse. [Q64127-2 ]

    Organism-specific databases

    CTDi 8805.
    MGIi MGI:109275. Trim24.

    Phylogenomic databases

    eggNOGi COG5076.
    GeneTreei ENSGT00530000062982.
    HOGENOMi HOG000252971.
    HOVERGENi HBG054599.
    InParanoidi Q64127.
    KOi K08881.
    OMAi PGLHQEN.
    OrthoDBi EOG790FZZ.
    PhylomeDBi Q64127.
    TreeFami TF106455.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_196460. Signaling by FGFR1 fusion mutants.

    Miscellaneous databases

    ChiTaRSi TRIM24. mouse.
    NextBioi 301326.
    PROi Q64127.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q64127.
    Bgeei Q64127.
    CleanExi MM_TRIM24.
    Genevestigatori Q64127.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 3 hits.
    4.10.45.10. 1 hit.
    InterProi IPR003649. Bbox_C.
    IPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR000315. Znf_B-box.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00439. Bromodomain. 1 hit.
    PF00628. PHD. 1 hit.
    PF00643. zf-B_box. 2 hits.
    [Graphical view ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00502. BBC. 1 hit.
    SM00336. BBOX. 2 hits.
    SM00297. BROMO. 1 hit.
    SM00249. PHD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
    PS50014. BROMODOMAIN_2. 1 hit.
    PS50119. ZF_BBOX. 2 hits.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18."
      le Douarin B., Zechel C., Garnier J.-M., Lutz Y., Tora L., Pierrat B., Heery D., Gronemeyer H., Chambon P., Losson R.
      EMBO J. 14:2020-2033(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESTROGEN RECEPTOR, SUBCELLULAR LOCATION.
      Tissue: Carcinoma.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Strain: C57BL/6.
      Tissue: Brain.
    3. "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors."
      le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F., Losson R., Chambon P.
      EMBO J. 15:6701-6715(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBX1 AND CBX3.
    4. "A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins."
      Zhong S., Delva L., Rachez C., Cenciarelli C., Gandini D., Zhang H., Kalantry S., Freedman L.P., Pandolfi P.P.
      Nat. Genet. 23:287-295(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML.
    5. "Common properties of nuclear protein SP100 and TIF1alpha chromatin factor: role of SUMO modification."
      Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T., Chambon P., Dejean A.
      Mol. Cell. Biol. 21:3314-3324(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH CBX5, MUTAGENESIS OF LYS-724 AND LYS-742.
    6. "Role of TIF1alpha as a modulator of embryonic transcription in the mouse zygote."
      Torres-Padilla M.E., Zernicka-Goetz M.
      J. Cell Biol. 174:329-338(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    7. "Transcriptional intermediary factor 1alpha mediates physical interaction and functional synergy between the coactivator-associated arginine methyltransferase 1 and glucocorticoid receptor-interacting protein 1 nuclear receptor coactivators."
      Teyssier C., Ou C.Y., Khetchoumian K., Losson R., Stallcup M.R.
      Mol. Endocrinol. 20:1276-1286(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CARM1, IDENTIFICATION IN A COACTIVATOR COMPLEX WITH CARM1 AND NCOA2/GRIP1.
    8. "Characterization of three growth hormone-responsive transcription factors preferentially expressed in adult female liver."
      Laz E.V., Holloway M.G., Chen C.S., Waxman D.J.
      Endocrinology 148:3327-3337(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, TISSUE SPECIFICITY.
    9. "Loss of Trim24 (Tif1alpha) gene function confers oncogenic activity to retinoic acid receptor alpha."
      Khetchoumian K., Teletin M., Tisserand J., Mark M., Herquel B., Ignat M., Zucman-Rossi J., Cammas F., Lerouge T., Thibault C., Metzger D., Chambon P., Losson R.
      Nat. Genet. 39:1500-1506(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1026 AND SER-1029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "Arterial calcifications and increased expression of vitamin D receptor targets in mice lacking TIF1alpha."
      Ignat M., Teletin M., Tisserand J., Khetchoumian K., Dennefeld C., Chambon P., Losson R., Mark M.
      Proc. Natl. Acad. Sci. U.S.A. 105:2598-2603(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    12. "TRIM24 mediates ligand-dependent activation of androgen receptor and is repressed by a bromodomain-containing protein, BRD7, in prostate cancer cells."
      Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J., Imamura M., Hatakeyama S.
      Biochim. Biophys. Acta 1793:1828-1836(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AR; KAT5/TIP60 AND BRD7.
    13. Cited for: FUNCTION, INTERACTION WITH TP53, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiTIF1A_MOUSE
    AccessioniPrimary (citable) accession number: Q64127
    Secondary accession number(s): Q64126
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3