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O15164

- TIF1A_HUMAN

UniProt

O15164 - TIF1A_HUMAN

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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

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 kinase activity Source: Ensembl
  7. receptor binding Source: ProtInc
  8. sequence-specific DNA binding Source: Ensembl
  9. transcription coactivator activity Source: UniProtKB
  10. ubiquitin-protein transferase activity Source: UniProtKB
  11. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. calcium ion homeostasis Source: 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
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_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
Complete GO annotation...

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). 1 Publication

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

BgeeiO15164.
CleanExiHS_TRIM24.
ExpressionAtlasiO15164. baseline and differential.
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. 66 interactions.
DIPiDIP-52713N.
IntActiO15164. 8 interactions.
STRINGi9606.ENSP00000340507.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 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.
GeneTreeiENSGT00530000062982.
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

        10         20         30         40         50
MEVAVEKAVA AAAAASAAAS GGPSAAPSGE NEAESRQGPD SERGGEAARL
60 70 80 90 100
NLLDTCAVCH QNIQSRAPKL LPCLHSFCQR CLPAPQRYLM LPAPMLGSAE
110 120 130 140 150
TPPPVPAPGS PVSGSSPFAT QVGVIRCPVC SQECAERHII DNFFVKDTTE
160 170 180 190 200
VPSSTVEKSN QVCTSCEDNA EANGFCVECV EWLCKTCIRA HQRVKFTKDH
210 220 230 240 250
TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK LTCRDCQLLE
260 270 280 290 300
HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKFTGNQ IQNRIIEVNQ
310 320 330 340 350
NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA
360 370 380 390 400
GLSKQLEHVM HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT
410 420 430 440 450
NNTIQFHCDP SFWAQNIINL GSLVIEDKES QPQMPKQNPV VEQNSQPPSG
460 470 480 490 500
LSSNQLSKFP TQISLAQLRL QHMQQQVMAQ RQQVQRRPAP VGLPNPRMQG
510 520 530 540 550
PIQQPSISHQ QPPPRLINFQ NHSPKPNGPV LPPHPQQLRY PPNQNIPRQA
560 570 580 590 600
IKPNPLQMAF LAQQAIKQWQ ISSGQGTPST TNSTSSTPSS PTITSAAGYD
610 620 630 640 650
GKAFGSPMID LSSPVGGSYN LPSLPDIDCS STIMLDNIVR KDTNIDHGQP
660 670 680 690 700
RPPSNRTVQS PNSSVPSPGL AGPVTMTSVH PPIRSPSASS VGSRGSSGSS
710 720 730 740 750
SKPAGADSTH KVPVVMLEPI RIKQENSGPP ENYDFPVVIV KQESDEESRP
760 770 780 790 800
QNANYPRSIL TSLLLNSSQS STSEETVLRS DAPDSTGDQP GLHQDNSSNG
810 820 830 840 850
KSEWLDPSQK SPLHVGETRK EDDPNEDWCA VCQNGGELLC CEKCPKVFHL
860 870 880 890 900
SCHVPTLTNF PSGEWICTFC RDLSKPEVEY DCDAPSHNSE KKKTEGLVKL
910 920 930 940 950
TPIDKRKCER LLLFLYCHEM SLAFQDPVPL TVPDYYKIIK NPMDLSTIKK
960 970 980 990 1000
RLQEDYSMYS KPEDFVADFR LIFQNCAEFN EPDSEVANAG IKLENYFEEL
1010 1020 1030 1040 1050
LKNLYPEKRF PKPEFRNESE DNKFSDDSDD DFVQPRKKRL KSIEERQLLK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 218-261, 824-1006.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114333. 66 interactions.
DIPi DIP-52713N.
IntActi O15164. 8 interactions.
STRINGi 9606.ENSP00000340507.

Chemistry

ChEMBLi CHEMBL3108638.

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.
GeneTreei ENSGT00530000062982.
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

Bgeei O15164.
CleanExi HS_TRIM24.
ExpressionAtlasi O15164. baseline and differential.
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.
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Publicationsi

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  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: November 26, 2014
This is version 157 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