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O15164 (TIF1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription intermediary factor 1-alpha

Short name=TIF1-alpha
EC=6.3.2.-
Alternative name(s):
E3 ubiquitin-protein ligase TRIM24
RING finger protein 82
Tripartite motif-containing protein 24
Gene names
Name:TRIM24
Synonyms:RNF82, TIF1, TIF1A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1050 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. 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. Ref.11 Ref.15 Ref.22

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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). Ref.1 Ref.8 Ref.14 Ref.15 Ref.22

Subcellular location

Nucleus. Cytoplasm. Note: Colocalizes with sites of active transcription. Detected both in nucleus and cytoplasm in some breast cancer samples. Predominantly nuclear. Ref.22

Induction

Up-regulated in some cases of breast cancer. Ref.22

Post-translational modification

Sumoylated By similarity.

Involvement in disease

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.

Sequence similarities

Contains 2 B box-type zinc fingers.

Contains 1 bromo domain.

Contains 1 PHD-type zinc finger.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseTumor suppressor
   DomainBromodomain
Coiled coil
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionLigase
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to estrogen stimulus

Inferred from direct assay Ref.22. Source: UniProtKB

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein catabolic process

Inferred from mutant phenotype Ref.15. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.15. Source: UniProtKB

regulation of apoptotic process

Inferred from mutant phenotype Ref.15. Source: UniProtKB

regulation of protein stability

Inferred from mutant phenotype Ref.15. Source: UniProtKB

regulation of signal transduction by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

regulation of vitamin D receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nuclear euchromatin

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.22. Source: UniProtKB

perichromatin fibrils

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionchromatin binding

Inferred from direct assay Ref.22. Source: UniProtKB

estrogen response element binding

Inferred from direct assay Ref.22. Source: UniProtKB

lysine-acetylated histone binding

Inferred from direct assay Ref.22. Source: UniProtKB

p53 binding

Inferred from physical interaction Ref.15. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.14. Source: UniProtKB

protein kinase activity

Inferred from electronic annotation. Source: Ensembl

receptor binding

Traceable author statement Ref.1. Source: ProtInc

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

transcription coactivator activity

Inferred from direct assay Ref.22. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.15. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.22. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: O15164-1)

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.
Isoform Short (identifier: O15164-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10501050Transcription intermediary factor 1-alpha
PRO_0000056390

Regions

Domain932 – 98756Bromo
Zinc finger56 – 8227RING-type
Zinc finger158 – 21154B box-type 1
Zinc finger218 – 25942B box-type 2
Zinc finger826 – 87348PHD-type
Region754 – 77926Nuclear receptor binding site (NRBS)
Region834 – 8407Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)
Region979 – 9802Interaction with histone H3 that is acetylated at 'Lys-23' (H3K23ac)
Coiled coil289 – 35971 Potential
Motif891 – 90717Nuclear localization signal Potential
Compositional bias9 – 157Poly-Ala
Compositional bias344 – 3474Poly-Gln

Sites

Site476 – 4772Breakpoint for translocation to form TRIM24-RET oncogene
Site8271Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)

Amino acid modifications

Modified residue1011Phosphothreonine Ref.17
Modified residue1101Phosphoserine Ref.17
Modified residue6671Phosphoserine Ref.12
Modified residue7441Phosphoserine Ref.19
Modified residue7681Phosphoserine Ref.12 Ref.17
Modified residue8081Phosphoserine Ref.12
Modified residue8111Phosphoserine Ref.10 Ref.12 Ref.17 Ref.19
Modified residue8181Phosphothreonine Ref.19
Modified residue10191Phosphoserine Ref.19
Modified residue10251Phosphoserine Ref.10 Ref.16
Modified residue10281Phosphoserine Ref.10 Ref.16 Ref.19
Modified residue10421Phosphoserine Ref.19
Cross-link723Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link741Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence477 – 51034Missing in isoform Short.
VSP_005772
Natural variant3201I → T in an ovarian serous carcinoma sample; somatic mutation. Ref.23
VAR_042382
Natural variant4031T → N in a lung squamous cell carcinoma sample; somatic mutation. Ref.23
VAR_042383
Natural variant7621S → N. Ref.23
VAR_042384
Natural variant7961N → S.
Corresponds to variant rs35356723 [ dbSNP | Ensembl ].
VAR_052148
Natural variant10091R → S. Ref.23
Corresponds to variant rs34585297 [ dbSNP | Ensembl ].
VAR_042385

Experimental info

Mutagenesis8271D → A: Strongly reduced affinity for histone H3 that is not methylated at 'Lys-4' (H3K4me0). Ref.22
Mutagenesis8401C → W: Abolishes interaction with histone H3. Ref.22
Mutagenesis979 – 9802FN → AA: Strongly reduced affinity for histone H3 that is acetylated at 'Lys-23' (H3K23ac).
Sequence conflict14 – 207AASAAAS → RLGCAP in AAB63585. Ref.1
Sequence conflict24 – 285SAAPS → RGG in AAB63585. Ref.1
Sequence conflict109 – 1146GSPVSG → ARRSA in AAB63585. Ref.1
Sequence conflict3501A → T in AAB63585. Ref.1
Sequence conflict6001D → N in AAB63585. Ref.1
Sequence conflict6081M → I in AAB63585. Ref.1
Sequence conflict9671A → R in AAB63585. Ref.1

Secondary structure

.................................. 1050
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified January 24, 2001. Version 3.
Checksum: D341E8022AACC67E

FASTA1,050116,831
        10         20         30         40         50         60 
MEVAVEKAVA AAAAASAAAS GGPSAAPSGE NEAESRQGPD SERGGEAARL NLLDTCAVCH 

        70         80         90        100        110        120 
QNIQSRAPKL LPCLHSFCQR CLPAPQRYLM LPAPMLGSAE TPPPVPAPGS PVSGSSPFAT 

       130        140        150        160        170        180 
QVGVIRCPVC SQECAERHII DNFFVKDTTE VPSSTVEKSN QVCTSCEDNA EANGFCVECV 

       190        200        210        220        230        240 
EWLCKTCIRA HQRVKFTKDH TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK 

       250        260        270        280        290        300 
LTCRDCQLLE HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKFTGNQ IQNRIIEVNQ 

       310        320        330        340        350        360 
NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA GLSKQLEHVM 

       370        380        390        400        410        420 
HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT NNTIQFHCDP SFWAQNIINL 

       430        440        450        460        470        480 
GSLVIEDKES QPQMPKQNPV VEQNSQPPSG LSSNQLSKFP TQISLAQLRL QHMQQQVMAQ 

       490        500        510        520        530        540 
RQQVQRRPAP VGLPNPRMQG PIQQPSISHQ QPPPRLINFQ NHSPKPNGPV LPPHPQQLRY 

       550        560        570        580        590        600 
PPNQNIPRQA IKPNPLQMAF LAQQAIKQWQ ISSGQGTPST TNSTSSTPSS PTITSAAGYD 

       610        620        630        640        650        660 
GKAFGSPMID LSSPVGGSYN LPSLPDIDCS STIMLDNIVR KDTNIDHGQP RPPSNRTVQS 

       670        680        690        700        710        720 
PNSSVPSPGL AGPVTMTSVH PPIRSPSASS VGSRGSSGSS SKPAGADSTH KVPVVMLEPI 

       730        740        750        760        770        780 
RIKQENSGPP ENYDFPVVIV KQESDEESRP QNANYPRSIL TSLLLNSSQS STSEETVLRS 

       790        800        810        820        830        840 
DAPDSTGDQP GLHQDNSSNG KSEWLDPSQK SPLHVGETRK EDDPNEDWCA VCQNGGELLC 

       850        860        870        880        890        900 
CEKCPKVFHL SCHVPTLTNF PSGEWICTFC RDLSKPEVEY DCDAPSHNSE KKKTEGLVKL 

       910        920        930        940        950        960 
TPIDKRKCER LLLFLYCHEM SLAFQDPVPL TVPDYYKIIK NPMDLSTIKK RLQEDYSMYS 

       970        980        990       1000       1010       1020 
KPEDFVADFR LIFQNCAEFN EPDSEVANAG IKLENYFEEL LKNLYPEKRF PKPEFRNESE 

      1030       1040       1050 
DNKFSDDSDD DFVQPRKKRL KSIEERQLLK 

« Hide

Isoform Short [UniParc].

Checksum: 4621C94EB3A74AE2
Show »

FASTA1,016113,018

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Trim24 targets endogenous p53 for degradation."
Allton K., Jain A.K., Herz H.M., Tsai W.W., Jung S.Y., Qin J., Bergmann A., Johnson R.L., Barton M.C.
Proc. Natl. Acad. Sci. U.S.A. 106:11612-11616(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"TRIM24 links a non-canonical histone signature to breast cancer."
Tsai W.W., Wang Z., Yiu T.T., Akdemir K.C., Xia W., Winter S., Tsai C.Y., Shi X., Schwarzer D., Plunkett W., Aronow B., Gozani O., Fischle W., Hung M.C., Patel D.J., Barton M.C.
Nature 468:927-932(2010) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS47720.1. [O15164-2]
CCDS5847.1. [O15164-1]
RefSeqNP_003843.3. NM_003852.3. [O15164-2]
NP_056989.2. NM_015905.2. [O15164-1]
UniGeneHs.490287.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalO15164.
SMRO15164. Positions 50-87, 218-261, 824-1006.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114333. 61 interactions.
DIPDIP-52713N.
IntActO15164. 7 interactions.
STRING9606.ENSP00000340507.

PTM databases

PhosphoSiteO15164.

Proteomic databases

MaxQBO15164.
PaxDbO15164.
PRIDEO15164.

Protocols and materials databases

DNASU8805.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343526; ENSP00000340507; ENSG00000122779. [O15164-1]
ENST00000415680; ENSP00000390829; ENSG00000122779. [O15164-2]
GeneID8805.
KEGGhsa:8805.
UCSCuc003vub.3. human. [O15164-2]
uc003vuc.3. human. [O15164-1]

Organism-specific databases

CTD8805.
GeneCardsGC07P138144.
HGNCHGNC:11812. TRIM24.
HPAHPA043495.
MIM188550. phenotype.
603406. gene.
neXtProtNX_O15164.
Orphanet146. Papillary or follicular thyroid carcinoma.
PharmGKBPA36519.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000252971.
HOVERGENHBG054599.
InParanoidO15164.
KOK08881.
OMAPGLHQEN.
OrthoDBEOG790FZZ.
PhylomeDBO15164.
TreeFamTF106455.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressO15164.
BgeeO15164.
CleanExHS_TRIM24.
GenevestigatorO15164.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 3 hits.
4.10.45.10. 1 hit.
InterProIPR003649. 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]
PfamPF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS00633. 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]
ProtoNetSearch...

Other

ChiTaRSTRIM24. human.
EvolutionaryTraceO15164.
GeneWikiTRIM24.
GenomeRNAi8805.
NextBio33028.
PROO15164.
SOURCESearch...

Entry information

Entry nameTIF1A_HUMAN
AccessionPrimary (citable) accession number: O15164
Secondary accession number(s): A4D1R7, A4D1R8, O95854
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 24, 2001
Last modified: July 9, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM