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O15164

- TIF1A_HUMAN

UniProt

O15164 - TIF1A_HUMAN

Protein

Transcription intermediary factor 1-alpha

Gene

TRIM24

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (24 Jan 2001)
      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). 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, 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.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei476 – 4772Breakpoint for translocation to form TRIM24-RET oncogene
    Sitei827 – 8271Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri56 – 8227RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri158 – 21154B box-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri218 – 25942B box-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri826 – 87348PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. estrogen response element binding Source: UniProtKB
    3. ligase activity Source: UniProtKB-KW
    4. lysine-acetylated histone binding Source: UniProtKB
    5. p53 binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein kinase activity Source: Ensembl
    8. receptor binding Source: ProtInc
    9. sequence-specific DNA binding Source: Ensembl
    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: Ensembl
    2. cellular response to estrogen stimulus Source: UniProtKB
    3. negative regulation of cell proliferation Source: Ensembl
    4. negative regulation of transcription, DNA-templated Source: Ensembl
    5. positive regulation of transcription, DNA-templated Source: Ensembl
    6. protein autophosphorylation Source: Ensembl
    7. protein catabolic process Source: UniProtKB
    8. protein ubiquitination Source: UniProtKB
    9. regulation of apoptotic process Source: UniProtKB
    10. regulation of protein stability Source: UniProtKB
    11. regulation of signal transduction by p53 class mediator Source: Ensembl
    12. regulation of vitamin D receptor signaling pathway Source: Ensembl
    13. response to peptide hormone Source: Ensembl
    14. transcription from RNA polymerase II promoter Source: ProtInc

    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_121141. 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
    RING finger protein 82
    Tripartite motif-containing protein 24
    Gene namesi
    Name:TRIM24
    Synonyms:RNF82, TIF1, TIF1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:11812. TRIM24.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Colocalizes with sites of active transcription. Detected both in nucleus and cytoplasm in some breast cancer samples. Predominantly nuclear.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nuclear euchromatin Source: Ensembl
    3. nucleus Source: UniProtKB
    4. perichromatin fibrils Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Thyroid papillary carcinoma (TPC) [MIM:188550]: A common tumor of the thyroid that typically arises as an irregular, solid or cystic mass from otherwise normal thyroid tissue. Papillary carcinomas are malignant neoplasm characterized by the formation of numerous, irregular, finger-like projections of fibrous stroma that is covered with a surface layer of neoplastic epithelial cells.
    Note: The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving TRIM24/TIF1 is found in thyroid papillary carcinomas. Translocation t(7;10)(q32;q11) with RET. The translocation generates the TRIM24/RET (PTC6) oncogene.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi827 – 8271D → A: Strongly reduced affinity for histone H3 that is not methylated at 'Lys-4' (H3K4me0). 1 Publication
    Mutagenesisi840 – 8401C → W: Abolishes interaction with histone H3. 1 Publication
    Mutagenesisi979 – 9802FN → AA: Strongly reduced affinity for histone H3 that is acetylated at 'Lys-23' (H3K23ac).

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    MIMi188550. phenotype.
    Orphaneti146. Papillary or follicular thyroid carcinoma.
    PharmGKBiPA36519.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10501050Transcription intermediary factor 1-alphaPRO_0000056390Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei101 – 1011Phosphothreonine1 Publication
    Modified residuei110 – 1101Phosphoserine1 Publication
    Modified residuei667 – 6671Phosphoserine1 Publication
    Cross-linki723 – 723Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki741 – 741Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei744 – 7441Phosphoserine1 Publication
    Modified residuei768 – 7681Phosphoserine2 Publications
    Modified residuei808 – 8081Phosphoserine1 Publication
    Modified residuei811 – 8111Phosphoserine4 Publications
    Modified residuei818 – 8181Phosphothreonine1 Publication
    Modified residuei1019 – 10191Phosphoserine1 Publication
    Modified residuei1025 – 10251Phosphoserine2 Publications
    Modified residuei1028 – 10281Phosphoserine3 Publications
    Modified residuei1042 – 10421Phosphoserine1 Publication

    Post-translational modificationi

    Sumoylated.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO15164.
    PaxDbiO15164.
    PRIDEiO15164.

    PTM databases

    PhosphoSiteiO15164.

    Expressioni

    Inductioni

    Up-regulated in some cases of breast cancer.1 Publication

    Gene expression databases

    ArrayExpressiO15164.
    BgeeiO15164.
    CleanExiHS_TRIM24.
    GenevestigatoriO15164.

    Organism-specific databases

    HPAiHPA043495.

    Interactioni

    Subunit structurei

    Interacts with CARM1, NCOA2/GRIP1, PML, KAT5/TIP60, BRD7, CBX1, CBX3 and CBX5. Part of a coactivator complex containing TRIM24, NCOA2 and CARM1 By similarity. Interacts with NR3C2/MCR. Interacts with the ligand-binding domain of estrogen receptors (in vitro). Interaction with DNA-bound estrogen receptors requires the presence of estradiol. Interacts with AR and p53/TP53. 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).By similarity5 Publications

    Protein-protein interaction databases

    BioGridi114333. 62 interactions.
    DIPiDIP-52713N.
    IntActiO15164. 7 interactions.
    STRINGi9606.ENSP00000340507.

    Structurei

    Secondary structure

    1
    1050
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi827 – 8293
    Turni830 – 8323
    Beta strandi836 – 8405
    Beta strandi842 – 8454
    Turni850 – 8523
    Beta strandi853 – 8553
    Turni868 – 8703
    Beta strandi873 – 8753
    Helixi881 – 8833
    Turni889 – 8913
    Helixi902 – 91716
    Helixi919 – 9213
    Helixi922 – 9254
    Helixi935 – 9384
    Helixi945 – 9539
    Beta strandi954 – 9563
    Helixi962 – 97918
    Helixi985 – 100420
    Beta strandi1005 – 10073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YYNX-ray2.50A/B/C/D891-1012[»]
    3O33X-ray2.00A/B/C/D824-1006[»]
    3O34X-ray1.90A824-1006[»]
    3O35X-ray1.76A/B824-1006[»]
    3O36X-ray1.70A/B824-1006[»]
    3O37X-ray2.00A/B/C/D824-1006[»]
    ProteinModelPortaliO15164.
    SMRiO15164. Positions 50-87, 218-261, 824-1006.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15164.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini932 – 98756BromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni754 – 77926Nuclear receptor binding site (NRBS)Add
    BLAST
    Regioni834 – 8407Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)
    Regioni979 – 9802Interaction with histone H3 that is acetylated at 'Lys-23' (H3K23ac)

    Coiled coil

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

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi891 – 90717Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 157Poly-Ala
    Compositional biasi344 – 3474Poly-Gln

    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 fingeri56 – 8227RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri158 – 21154B box-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri218 – 25942B box-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri826 – 87348PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5076.
    HOGENOMiHOG000252971.
    HOVERGENiHBG054599.
    InParanoidiO15164.
    KOiK08881.
    OMAiPGLHQEN.
    OrthoDBiEOG790FZZ.
    PhylomeDBiO15164.
    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: O15164-1) [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

    MEVAVEKAVA AAAAASAAAS GGPSAAPSGE NEAESRQGPD SERGGEAARL     50
    NLLDTCAVCH QNIQSRAPKL LPCLHSFCQR CLPAPQRYLM LPAPMLGSAE 100
    TPPPVPAPGS PVSGSSPFAT QVGVIRCPVC SQECAERHII DNFFVKDTTE 150
    VPSSTVEKSN QVCTSCEDNA EANGFCVECV EWLCKTCIRA HQRVKFTKDH 200
    TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK LTCRDCQLLE 250
    HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKFTGNQ IQNRIIEVNQ 300
    NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA 350
    GLSKQLEHVM HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT 400
    NNTIQFHCDP SFWAQNIINL GSLVIEDKES QPQMPKQNPV VEQNSQPPSG 450
    LSSNQLSKFP TQISLAQLRL QHMQQQVMAQ RQQVQRRPAP VGLPNPRMQG 500
    PIQQPSISHQ QPPPRLINFQ NHSPKPNGPV LPPHPQQLRY PPNQNIPRQA 550
    IKPNPLQMAF LAQQAIKQWQ ISSGQGTPST TNSTSSTPSS PTITSAAGYD 600
    GKAFGSPMID LSSPVGGSYN LPSLPDIDCS STIMLDNIVR KDTNIDHGQP 650
    RPPSNRTVQS PNSSVPSPGL AGPVTMTSVH PPIRSPSASS VGSRGSSGSS 700
    SKPAGADSTH KVPVVMLEPI RIKQENSGPP ENYDFPVVIV KQESDEESRP 750
    QNANYPRSIL TSLLLNSSQS STSEETVLRS DAPDSTGDQP GLHQDNSSNG 800
    KSEWLDPSQK SPLHVGETRK EDDPNEDWCA VCQNGGELLC CEKCPKVFHL 850
    SCHVPTLTNF PSGEWICTFC RDLSKPEVEY DCDAPSHNSE KKKTEGLVKL 900
    TPIDKRKCER LLLFLYCHEM SLAFQDPVPL TVPDYYKIIK NPMDLSTIKK 950
    RLQEDYSMYS KPEDFVADFR LIFQNCAEFN EPDSEVANAG IKLENYFEEL 1000
    LKNLYPEKRF PKPEFRNESE DNKFSDDSDD DFVQPRKKRL KSIEERQLLK 1050
    Length:1,050
    Mass (Da):116,831
    Last modified:January 24, 2001 - v3
    Checksum:iD341E8022AACC67E
    GO
    Isoform Short (identifier: O15164-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,016
    Mass (Da):113,018
    Checksum:i4621C94EB3A74AE2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 207AASAAAS → RLGCAP in AAB63585. (PubMed:9115274)Curated
    Sequence conflicti24 – 285SAAPS → RGG in AAB63585. (PubMed:9115274)Curated
    Sequence conflicti109 – 1146GSPVSG → ARRSA in AAB63585. (PubMed:9115274)Curated
    Sequence conflicti350 – 3501A → T in AAB63585. (PubMed:9115274)Curated
    Sequence conflicti600 – 6001D → N in AAB63585. (PubMed:9115274)Curated
    Sequence conflicti608 – 6081M → I in AAB63585. (PubMed:9115274)Curated
    Sequence conflicti967 – 9671A → R in AAB63585. (PubMed:9115274)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti320 – 3201I → T in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
    VAR_042382
    Natural varianti403 – 4031T → N in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
    VAR_042383
    Natural varianti762 – 7621S → N.1 Publication
    VAR_042384
    Natural varianti796 – 7961N → S.
    Corresponds to variant rs35356723 [ dbSNP | Ensembl ].
    VAR_052148
    Natural varianti1009 – 10091R → S.1 Publication
    Corresponds to variant rs34585297 [ dbSNP | Ensembl ].
    VAR_042385

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei477 – 51034Missing in isoform Short. 2 PublicationsVSP_005772Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF009353 mRNA. Translation: AAB63585.1.
    AF119042 mRNA. Translation: AAD17258.1.
    AK075306 mRNA. Translation: BAG52105.1.
    AC008265 Genomic DNA. No translation available.
    AC013429 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24046.1.
    CH236950 Genomic DNA. Translation: EAL24047.1.
    CH471070 Genomic DNA. Translation: EAW83884.1.
    CH471070 Genomic DNA. Translation: EAW83885.1.
    BC028689 mRNA. Translation: AAH28689.2.
    CCDSiCCDS47720.1. [O15164-2]
    CCDS5847.1. [O15164-1]
    RefSeqiNP_003843.3. NM_003852.3. [O15164-2]
    NP_056989.2. NM_015905.2. [O15164-1]
    UniGeneiHs.490287.

    Genome annotation databases

    EnsembliENST00000343526; ENSP00000340507; ENSG00000122779. [O15164-1]
    ENST00000415680; ENSP00000390829; ENSG00000122779. [O15164-2]
    GeneIDi8805.
    KEGGihsa:8805.
    UCSCiuc003vub.3. human. [O15164-2]
    uc003vuc.3. human. [O15164-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF009353 mRNA. Translation: AAB63585.1 .
    AF119042 mRNA. Translation: AAD17258.1 .
    AK075306 mRNA. Translation: BAG52105.1 .
    AC008265 Genomic DNA. No translation available.
    AC013429 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24046.1 .
    CH236950 Genomic DNA. Translation: EAL24047.1 .
    CH471070 Genomic DNA. Translation: EAW83884.1 .
    CH471070 Genomic DNA. Translation: EAW83885.1 .
    BC028689 mRNA. Translation: AAH28689.2 .
    CCDSi CCDS47720.1. [O15164-2 ]
    CCDS5847.1. [O15164-1 ]
    RefSeqi NP_003843.3. NM_003852.3. [O15164-2 ]
    NP_056989.2. NM_015905.2. [O15164-1 ]
    UniGenei Hs.490287.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YYN X-ray 2.50 A/B/C/D 891-1012 [» ]
    3O33 X-ray 2.00 A/B/C/D 824-1006 [» ]
    3O34 X-ray 1.90 A 824-1006 [» ]
    3O35 X-ray 1.76 A/B 824-1006 [» ]
    3O36 X-ray 1.70 A/B 824-1006 [» ]
    3O37 X-ray 2.00 A/B/C/D 824-1006 [» ]
    ProteinModelPortali O15164.
    SMRi O15164. Positions 50-87, 218-261, 824-1006.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114333. 62 interactions.
    DIPi DIP-52713N.
    IntActi O15164. 7 interactions.
    STRINGi 9606.ENSP00000340507.

    PTM databases

    PhosphoSitei O15164.

    Proteomic databases

    MaxQBi O15164.
    PaxDbi O15164.
    PRIDEi O15164.

    Protocols and materials databases

    DNASUi 8805.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343526 ; ENSP00000340507 ; ENSG00000122779 . [O15164-1 ]
    ENST00000415680 ; ENSP00000390829 ; ENSG00000122779 . [O15164-2 ]
    GeneIDi 8805.
    KEGGi hsa:8805.
    UCSCi uc003vub.3. human. [O15164-2 ]
    uc003vuc.3. human. [O15164-1 ]

    Organism-specific databases

    CTDi 8805.
    GeneCardsi GC07P138144.
    HGNCi HGNC:11812. TRIM24.
    HPAi HPA043495.
    MIMi 188550. phenotype.
    603406. gene.
    neXtProti NX_O15164.
    Orphaneti 146. Papillary or follicular thyroid carcinoma.
    PharmGKBi PA36519.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOGENOMi HOG000252971.
    HOVERGENi HBG054599.
    InParanoidi O15164.
    KOi K08881.
    OMAi PGLHQEN.
    OrthoDBi EOG790FZZ.
    PhylomeDBi O15164.
    TreeFami TF106455.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_121141. Signaling by FGFR1 fusion mutants.

    Miscellaneous databases

    ChiTaRSi TRIM24. human.
    EvolutionaryTracei O15164.
    GeneWikii TRIM24.
    GenomeRNAii 8805.
    NextBioi 33028.
    PROi O15164.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15164.
    Bgeei O15164.
    CleanExi HS_TRIM24.
    Genevestigatori O15164.

    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. "Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1."
      Thenot S., Henriquet C., Rochefort H., Cavailles V.
      J. Biol. Chem. 272:12062-12068(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), SUBUNIT.
      Tissue: Mammary cancer.
    2. "TIF1gamma, a novel member of the transcriptional intermediary factor 1 family."
      Venturini L., You J., Stadler M., Galien R., Lallemand V., Koken M.H.M., Mattei M.-G., Ganser A., Chambon P., Losson R., De The H.
      Oncogene 18:1209-1217(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Retinoblastoma.
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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).
      Tissue: Testis.
    7. Cavailles V.
      Submitted (JAN-1999) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 477-510 (ISOFORM LONG).
      Tissue: Mammary cancer.
    8. "Crucial role of the H11-H12 loop in stabilizing the active conformation of the human mineralocorticoid receptor."
      Hellal-Levy C., Fagart J., Souque A., Wurtz J.-M., Moras D., Rafestin-Oblin M.-E.
      Mol. Endocrinol. 14:1210-1221(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR3C2.
    9. "The transcription coactivator HTIF1 and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas."
      Klugbauer S., Rabes H.M.
      Oncogene 18:4388-4393(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH RET.
      Tissue: Thyroid.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-811; SER-1025 AND SER-1028, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-768; SER-808 AND SER-811, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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: INTERACTION WITH AR.
    15. Cited for: FUNCTION AS E3 UBIQUITIN LIGASE, INTERACTION WITH TP53.
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1025 AND SER-1028, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101; SER-110; SER-768 AND SER-811, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744; SER-811; THR-818; SER-1019; SER-1028 AND SER-1042, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Crystal structure of human bromodomain protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 891-1012.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 824-1006 IN COMPLEXES WITH METHYLATED HISTONE PEPTIDES AND ZINC IONS, FUNCTION, MUTAGENESIS OF ASP-827; CYS-840 AND 979-PHE-ASN-980, SUBCELLULAR LOCATION, SUBUNIT, INDUCTION.
    23. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-320; ASN-403; ASN-762 AND SER-1009.

    Entry informationi

    Entry nameiTIF1A_HUMAN
    AccessioniPrimary (citable) accession number: O15164
    Secondary accession number(s): A4D1R7, A4D1R8, O95854
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 24, 2001
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3