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Q64127

- TIF1A_MOUSE

UniProt

Q64127 - TIF1A_MOUSE

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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

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 kinase activity Source: MGI
  8. sequence-specific DNA binding Source: MGI
  9. transcription coactivator activity Source: UniProtKB
  10. ubiquitin-protein transferase activity Source: UniProtKB
  11. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ64127.
CleanExiMM_TRIM24.
ExpressionAtlasiQ64127. baseline and differential.
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 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

        10         20         30         40         50
MEVAVEKAAA AAAPAGGPAA AAPSGENEAE SRQGPDSESG GEASRLNLLD
60 70 80 90 100
TCAVCHQNIQ SRVPKLLPCL HSFCQRCLPA PQRYLMLTAP ALGSAETPPP
110 120 130 140 150
APAPAPAPGS PAGGPSPFAT QVGVIRCPVC SQECAERHII DNFFVKDTTE
160 170 180 190 200
VPSSTVEKSN QVCTSCEDNA EANGFCVECV EWLCKTCIRA HQRVKFTKDH
210 220 230 240 250
TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK LTCRDCQLLE
260 270 280 290 300
HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKYTGNQ IQNRIIEINQ
310 320 330 340 350
NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA
360 370 380 390 400
GLSKQLEHVM HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT
410 420 430 440 450
NTTIQFHCDP SFWAQNIINL GSLVIEDKES QPQMPKQNPV VEQSSQPPGG
460 470 480 490 500
LPSNQLSKFP TQISLAQLRL QHIQQQVMAQ RQQVQRRPAP VGLPNPRMQG
510 520 530 540 550
PIQQPSISHQ HPPPRLINFQ NHSPKPNGPV LPPYPQQLRY SPSQNVPRQT
560 570 580 590 600
TIKPNPLQMA FLAQQAIKQW QISSVQAPPT TASSSSSTPS SPTITSAAGY
610 620 630 640 650
DGKAFSSPMI DLSAPVGGSY NLPSLPDIDC SSTIMLDNIA RKDTGVDHAQ
660 670 680 690 700
PRPPSNRTVQ SPNSSVPSPG LAGPVTMTSV HPPIRSPSAS SVGSRGSSGS
710 720 730 740 750
SSKPAGADST HKVPVVMLEP IRIKQENSGP PENYDFPVVI VKQESDEESR
760 770 780 790 800
PQNTNYPRSI LTSLLLNSSQ SSASEETVLR SDAPDSTGDQ PGLHQENSSN
810 820 830 840 850
GKSEWSDASQ KSPVHVGETR KEDDPNEDWC AVCQNGGELL CCEKCPKVFH
860 870 880 890 900
LTCHVPTLTN FPSGEWICTF CRDLSKPEVD YDCDVPSHHS EKRKSEGLTK
910 920 930 940 950
LTPIDKRKCE RLLLFLYCHE MSLAFQDPVP LTVPDYYKII KNPMDLSTIK
960 970 980 990 1000
KRLQEDYCMY TKPEDFVADF RLIFQNCAEF NEPDSEVANA GIKLESYFEE
1010 1020 1030 1040 1050
LLKNLYPEKR FPKVEFRHEA EDCKFSDDSD DDFVQPRKKR LKSTEDRQLL

K
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 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

Bgeei Q64127.
CleanExi MM_TRIM24.
ExpressionAtlasi Q64127. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 145 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