O15164 (TIF1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1050 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14 Ref.20
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.13 Ref.14 Ref.20
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.20
Induction	Up-regulated in some cases of breast cancer. Ref.20
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 process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Tumor suppressor
Domain	Bromodomain Coiled coil Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Ligase Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	calcium ion homeostasis Inferred from electronic annotation. Source: Compara cellular response to estrogen stimulus Inferred from direct assay Ref.20. Source: UniProtKB negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara protein autophosphorylation Inferred from electronic annotation. Source: Compara protein catabolic process Inferred from mutant phenotype Ref.14. Source: UniProtKB regulation of apoptotic process Inferred from mutant phenotype Ref.14. Source: UniProtKB regulation of protein stability Inferred from mutant phenotype Ref.14. Source: UniProtKB regulation of vitamin D receptor signaling pathway Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear euchromatin Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay Ref.20. Source: UniProtKB perichromatin fibrils Inferred from electronic annotation. Source: Compara
Molecular_function	chromatin binding Inferred from direct assay Ref.20. Source: UniProtKB estrogen response element binding Inferred from direct assay Ref.20. Source: UniProtKB histone acetyl-lysine binding Inferred from direct assay Ref.20. Source: UniProtKB protein kinase activity Inferred from electronic annotation. Source: Compara receptor binding Traceable author statement Ref.1. Source: ProtInc sequence-specific DNA binding Inferred from electronic annotation. Source: Compara transcription coactivator activity Inferred from direct assay Ref.20. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay Ref.14. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.20. 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1050

1050

Transcription intermediary factor 1-alpha

PRO_0000056390

Regions

Domain

932 – 987

56

Bromo

Zinc finger

56 – 82

27

RING-type

Zinc finger

158 – 211

54

B box-type 1

Zinc finger

218 – 259

42

B box-type 2

Zinc finger

826 – 873

48

PHD-type

Region

754 – 779

26

Nuclear receptor binding site (NRBS)

Region

834 – 840

7

Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)

Region

979 – 980

2

Interaction with histone H3 that is acetylated at 'Lys-23' (H3K23ac)

Coiled coil

289 – 359

71

Potential

Motif

891 – 907

17

Nuclear localization signal Potential

Compositional bias

9 – 15

7

Poly-Ala

Compositional bias

344 – 347

4

Poly-Gln

Sites

Site

476 – 477

2

Breakpoint for translocation to form TRIM24-RET oncogene

Site

827

1

Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)

Amino acid modifications

Modified residue

101

1

Phosphothreonine Ref.16

Modified residue

110

1

Phosphoserine Ref.16

Modified residue

667

1

Phosphoserine Ref.12

Modified residue

744

1

Phosphoserine Ref.18

Modified residue

768

1

Phosphoserine Ref.12 Ref.16

Modified residue

808

1

Phosphoserine Ref.12

Modified residue

811

1

Phosphoserine Ref.10 Ref.12 Ref.16 Ref.18

Modified residue

818

1

Phosphothreonine Ref.18

Modified residue

1019

1

Phosphoserine Ref.18

Modified residue

1025

1

Phosphoserine Ref.10 Ref.15

Modified residue

1028

1

Phosphoserine Ref.10 Ref.15 Ref.18

Modified residue

1042

1

Phosphoserine Ref.18

Cross-link

723

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Cross-link

741

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence

477 – 510

34

Missing in isoform Short.

VSP_005772

Natural variant

320

1

I → T in an ovarian serous carcinoma sample; somatic mutation. Ref.21

VAR_042382

Natural variant

403

1

T → N in a lung squamous cell carcinoma sample; somatic mutation. Ref.21

VAR_042383

Natural variant

762

1

S → N. Ref.21

VAR_042384

Natural variant

796

1

N → S.
Corresponds to variant rs35356723 [ dbSNP | Ensembl ].

VAR_052148

Natural variant

1009

1

R → S. Ref.21
Corresponds to variant rs34585297 [ dbSNP | Ensembl ].

VAR_042385

Experimental info

Mutagenesis

827

1

D → A: Strongly reduced affinity for histone H3 that is not methylated at 'Lys-4' (H3K4me0). Ref.20

Mutagenesis

840

1

C → W: Abolishes interaction with histone H3. Ref.20

Mutagenesis

979 – 980

2

FN → AA: Strongly reduced affinity for histone H3 that is acetylated at 'Lys-23' (H3K23ac).

Sequence conflict

14 – 20

7

AASAAAS → RLGCAP in AAB63585. Ref.1

Sequence conflict

24 – 28

5

SAAPS → RGG in AAB63585. Ref.1

Sequence conflict

109 – 114

6

GSPVSG → ARRSA in AAB63585. Ref.1

Sequence conflict

350

1

A → T in AAB63585. Ref.1

Sequence conflict

600

1

D → N in AAB63585. Ref.1

Sequence conflict

608

1

M → I in AAB63585. Ref.1

Sequence conflict

967

1

A → R in AAB63585. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1050

Helix Strand Turn

Details...

Beta strand

827 – 829

3

Turn

830 – 832

3

Beta strand

836 – 840

5

Beta strand

842 – 845

4

Turn

850 – 852

3

Beta strand

853 – 855

3

Turn

868 – 870

3

Beta strand

873 – 875

3

Helix

881 – 883

3

Turn

889 – 891

3

Helix

902 – 917

16

Helix

919 – 921

3

Helix

922 – 925

4

Helix

935 – 938

4

Helix

945 – 953

9

Beta strand

954 – 956

3

Helix

962 – 979

18

Helix

985 – 1004

20

Beta strand

1005 – 1007

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified January 24, 2001. Version 3. Checksum: D341E8022AACC67E	FASTA	1,050	116,831
	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
	Isoform Short [UniParc]. Checksum: 4621C94EB3A74AE2	FASTA	1,016	113,018
	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 QHMQQQQPPP 490 500 510 520 530 540 RLINFQNHSP KPNGPVLPPH PQQLRYPPNQ NIPRQAIKPN PLQMAFLAQQ AIKQWQISSG 550 560 570 580 590 600 QGTPSTTNST SSTPSSPTIT SAAGYDGKAF GSPMIDLSSP VGGSYNLPSL PDIDCSSTIM 610 620 630 640 650 660 LDNIVRKDTN IDHGQPRPPS NRTVQSPNSS VPSPGLAGPV TMTSVHPPIR SPSASSVGSR 670 680 690 700 710 720 GSSGSSSKPA GADSTHKVPV VMLEPIRIKQ ENSGPPENYD FPVVIVKQES DEESRPQNAN 730 740 750 760 770 780 YPRSILTSLL LNSSQSSTSE ETVLRSDAPD STGDQPGLHQ DNSSNGKSEW LDPSQKSPLH 790 800 810 820 830 840 VGETRKEDDP NEDWCAVCQN GGELLCCEKC PKVFHLSCHV PTLTNFPSGE WICTFCRDLS 850 860 870 880 890 900 KPEVEYDCDA PSHNSEKKKT EGLVKLTPID KRKCERLLLF LYCHEMSLAF QDPVPLTVPD 910 920 930 940 950 960 YYKIIKNPMD LSTIKKRLQE DYSMYSKPED FVADFRLIFQ NCAEFNEPDS EVANAGIKLE 970 980 990 1000 1010 NYFEELLKNL YPEKRFPKPE FRNESEDNKF SDDSDDDFVQ PRKKRLKSIE ERQLLK

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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.
[14]	"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.
[15]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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].
[18]	"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, MASS SPECTROMETRY.
[19]	"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.
[20]	"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.
[21]	"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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00005184.
IPI00184317.

RefSeq

NP_003843.3. NM_003852.3.
NP_056989.2. NM_015905.2.

UniGene

Hs.490287.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O15164.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-52713N.

IntAct

O15164. 7 interactions.

STRING

9606.ENSP00000340507.

PTM databases

PhosphoSite

O15164.

Proteomic databases

PaxDb

O15164.

PRIDE

O15164.

Protocols and materials databases

DNASU

8805.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000343526; ENSP00000340507; ENSG00000122779.
ENST00000415680; ENSP00000390829; ENSG00000122779.

GeneID

8805.

KEGG

hsa:8805.

UCSC

uc003vub.3. human.
uc003vuc.3. human.

Organism-specific databases

CTD

8805.

GeneCards

GC07P138144.

HGNC

HGNC:11812. TRIM24.

HPA

HPA043495.

MIM

188550. phenotype.
603406. gene.

neXtProt

NX_O15164.

Orphanet

146. Papillary or follicular thyroid carcinoma.

PharmGKB

PA36519.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5076.

HOGENOM

HOG000252971.

HOVERGEN

HBG054599.

InParanoid

O15164.

KO

K08881.

OMA

FWAQNIF.

OrthoDB

EOG4P8FH9.

PhylomeDB

O15164.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

O15164.

Bgee

O15164.

CleanEx

HS_TRIM24.

Genevestigator

O15164.

GermOnline

ENSG00000122779. Homo sapiens.

Family and domain databases

Gene3D

1.20.920.10. 1 hit.
3.30.40.10. 3 hits.
4.10.45.10. 1 hit.

InterPro

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]

Pfam

PF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]

SUPFAM

SSF47370. Bromodomain. 1 hit.
SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

ChiTaRS

TRIM24. human.

EvolutionaryTrace

O15164.

GenomeRNAi

8805.

NextBio

33028.

SOURCE

Search...

Entry information

Entry name

TIF1A_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 142 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.