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Protein

Transcription intermediary factor 1-alpha

Gene

TRIM24

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 similarity3 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri56 – 82RING-typePROSITE-ProRule annotationAdd BLAST27
Zinc fingeri158 – 211B box-type 1PROSITE-ProRule annotationAdd BLAST54
Zinc fingeri218 – 259B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri826 – 873PHD-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • estrogen response element binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • lysine-acetylated histone binding Source: UniProtKB
  • p53 binding Source: UniProtKB
  • protein tyrosine kinase activity Source: Reactome
  • receptor binding Source: ProtInc
  • sequence-specific DNA binding Source: Ensembl
  • transcription coactivator activity Source: UniProtKB
  • ubiquitin protein ligase activity Source: Ensembl
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • calcium ion homeostasis Source: Ensembl
  • cellular response to estrogen stimulus Source: UniProtKB
  • negative regulation of cell proliferation Source: Ensembl
  • negative regulation of transcription, DNA-templated Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: Ensembl
  • protein autophosphorylation Source: Ensembl
  • protein catabolic process Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
  • regulation of protein stability Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Ensembl
  • regulation of vitamin D receptor signaling pathway Source: Ensembl
  • response to peptide hormone Source: Ensembl
  • 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

BioCyciZFISH:ENSG00000122779-MONOMER.
ReactomeiR-HSA-1839117. Signaling by cytosolic FGFR1 fusion mutants.
R-HSA-5655302. Signaling by FGFR1 in disease.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
SIGNORiO15164.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:11812. TRIM24.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • nuclear euchromatin Source: Ensembl
  • nucleus Source: UniProtKB
  • perichromatin fibrils Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving TRIM24/TIF1 is found in papillary thyroid carcinomas (PTCs). Translocation t(7;10)(q32;q11) with RET. The translocation generates the TRIM24/RET (PTC6) oncogene.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi827D → A: Strongly reduced affinity for histone H3 that is not methylated at 'Lys-4' (H3K4me0). 1 Publication1
Mutagenesisi840C → W: Abolishes interaction with histone H3. 1 Publication1
Mutagenesisi979 – 980FN → AA: Strongly reduced affinity for histone H3 that is acetylated at 'Lys-23' (H3K23ac). 1 Publication2

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei476 – 477Breakpoint for translocation to form TRIM24-RET oncogene2

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi8805.
MalaCardsiTRIM24.
OpenTargetsiENSG00000122779.
Orphaneti146. Papillary or follicular thyroid carcinoma.
PharmGKBiPA36519.

Chemistry databases

ChEMBLiCHEMBL3108638.
GuidetoPHARMACOLOGYi2252.

Polymorphism and mutation databases

BioMutaiTRIM24.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000563901 – 1050Transcription intermediary factor 1-alphaAdd BLAST1050

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei101PhosphothreonineCombined sources1
Modified residuei110PhosphoserineCombined sources1
Modified residuei469Omega-N-methylarginineBy similarity1
Modified residuei654PhosphoserineCombined sources1
Modified residuei660PhosphoserineBy similarity1
Modified residuei667PhosphoserineCombined sources1
Cross-linki702Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki711Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki723Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki723Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki741Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei744PhosphoserineCombined sources1
Modified residuei768PhosphoserineCombined sources1
Modified residuei808PhosphoserineCombined sources1
Modified residuei811PhosphoserineCombined sources1
Modified residuei818PhosphothreonineCombined sources1
Cross-linki949Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1019PhosphoserineCombined sources1
Modified residuei1025PhosphoserineCombined sources1
Modified residuei1028PhosphoserineCombined sources1
Cross-linki1041Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1042PhosphoserineCombined sources1

Post-translational modificationi

Sumoylated.By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO15164.
MaxQBiO15164.
PaxDbiO15164.
PeptideAtlasiO15164.
PRIDEiO15164.

PTM databases

iPTMnetiO15164.
PhosphoSitePlusiO15164.

Expressioni

Inductioni

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

Gene expression databases

BgeeiENSG00000122779.
CleanExiHS_TRIM24.
ExpressionAtlasiO15164. baseline and differential.
GenevisibleiO15164. HS.

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei827Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)1

GO - Molecular functioni

  • lysine-acetylated histone binding Source: UniProtKB
  • p53 binding Source: UniProtKB
  • receptor binding Source: ProtInc

Protein-protein interaction databases

BioGridi114333. 85 interactors.
DIPiDIP-52713N.
IntActiO15164. 12 interactors.
STRINGi9606.ENSP00000340507.

Chemistry databases

BindingDBiO15164.

Structurei

Secondary structure

11050
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi827 – 829Combined sources3
Turni830 – 832Combined sources3
Beta strandi836 – 840Combined sources5
Beta strandi842 – 845Combined sources4
Turni850 – 852Combined sources3
Beta strandi853 – 855Combined sources3
Turni868 – 870Combined sources3
Beta strandi873 – 875Combined sources3
Helixi881 – 883Combined sources3
Turni889 – 891Combined sources3
Helixi902 – 917Combined sources16
Helixi919 – 921Combined sources3
Helixi922 – 924Combined sources3
Helixi935 – 938Combined sources4
Helixi945 – 953Combined sources9
Turni954 – 956Combined sources3
Helixi962 – 979Combined sources18
Helixi985 – 1004Combined sources20
Beta strandi1005 – 1007Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4YABX-ray1.90A/B824-1006[»]
4YADX-ray1.73A/B824-1006[»]
4YATX-ray2.18A/B824-1006[»]
4YAXX-ray2.25A/B824-1006[»]
4YBMX-ray1.46A/B824-1006[»]
4YBSX-ray1.83A824-1006[»]
4YBTX-ray1.82A824-1006[»]
4YC9X-ray1.82A824-1006[»]
4ZQLX-ray1.79A/B825-1006[»]
ProteinModelPortaliO15164.
SMRiO15164.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15164.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini932 – 987BromoPROSITE-ProRule annotationAdd BLAST56

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni754 – 779Nuclear receptor binding site (NRBS)Add BLAST26
Regioni834 – 840Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)7
Regioni979 – 980Interaction with histone H3 that is acetylated at 'Lys-23' (H3K23ac)2

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili289 – 359Sequence analysisAdd BLAST71

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi891 – 907Nuclear localization signalSequence analysisAdd BLAST17

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi9 – 15Poly-Ala7
Compositional biasi344 – 347Poly-Gln4

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)DescriptionActionsGraphical viewLength
Zinc fingeri56 – 82RING-typePROSITE-ProRule annotationAdd BLAST27
Zinc fingeri158 – 211B box-type 1PROSITE-ProRule annotationAdd BLAST54
Zinc fingeri218 – 259B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri826 – 873PHD-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410KDQG. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00530000062982.
HOGENOMiHOG000252971.
HOVERGENiHBG054599.
InParanoidiO15164.
KOiK08881.
OMAiSNPCDSA.
OrthoDBiEOG091G01KK.
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. 1 hit.
[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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti14 – 20AASAAAS → RLGCAP in AAB63585 (PubMed:9115274).Curated7
Sequence conflicti24 – 28SAAPS → RGG in AAB63585 (PubMed:9115274).Curated5
Sequence conflicti109 – 114GSPVSG → ARRSA in AAB63585 (PubMed:9115274).Curated6
Sequence conflicti350A → T in AAB63585 (PubMed:9115274).Curated1
Sequence conflicti600D → N in AAB63585 (PubMed:9115274).Curated1
Sequence conflicti608M → I in AAB63585 (PubMed:9115274).Curated1
Sequence conflicti967A → R in AAB63585 (PubMed:9115274).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042382320I → T in an ovarian serous carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042383403T → N in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042384762S → N.1 Publication1
Natural variantiVAR_052148796N → S.Corresponds to variant rs35356723dbSNPEnsembl.1
Natural variantiVAR_0423851009R → S.1 PublicationCorresponds to variant rs34585297dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005772477 – 510Missing in isoform Short. 2 PublicationsAdd BLAST34

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.4. 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.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4YABX-ray1.90A/B824-1006[»]
4YADX-ray1.73A/B824-1006[»]
4YATX-ray2.18A/B824-1006[»]
4YAXX-ray2.25A/B824-1006[»]
4YBMX-ray1.46A/B824-1006[»]
4YBSX-ray1.83A824-1006[»]
4YBTX-ray1.82A824-1006[»]
4YC9X-ray1.82A824-1006[»]
4ZQLX-ray1.79A/B825-1006[»]
ProteinModelPortaliO15164.
SMRiO15164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114333. 85 interactors.
DIPiDIP-52713N.
IntActiO15164. 12 interactors.
STRINGi9606.ENSP00000340507.

Chemistry databases

BindingDBiO15164.
ChEMBLiCHEMBL3108638.
GuidetoPHARMACOLOGYi2252.

PTM databases

iPTMnetiO15164.
PhosphoSitePlusiO15164.

Polymorphism and mutation databases

BioMutaiTRIM24.

Proteomic databases

EPDiO15164.
MaxQBiO15164.
PaxDbiO15164.
PeptideAtlasiO15164.
PRIDEiO15164.

Protocols and materials databases

DNASUi8805.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343526; ENSP00000340507; ENSG00000122779. [O15164-1]
ENST00000415680; ENSP00000390829; ENSG00000122779. [O15164-2]
GeneIDi8805.
KEGGihsa:8805.
UCSCiuc003vub.4. human. [O15164-1]

Organism-specific databases

CTDi8805.
DisGeNETi8805.
GeneCardsiTRIM24.
HGNCiHGNC:11812. TRIM24.
HPAiHPA043495.
MalaCardsiTRIM24.
MIMi603406. gene.
neXtProtiNX_O15164.
OpenTargetsiENSG00000122779.
Orphaneti146. Papillary or follicular thyroid carcinoma.
PharmGKBiPA36519.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410KDQG. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00530000062982.
HOGENOMiHOG000252971.
HOVERGENiHBG054599.
InParanoidiO15164.
KOiK08881.
OMAiSNPCDSA.
OrthoDBiEOG091G01KK.
PhylomeDBiO15164.
TreeFamiTF106455.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000122779-MONOMER.
ReactomeiR-HSA-1839117. Signaling by cytosolic FGFR1 fusion mutants.
R-HSA-5655302. Signaling by FGFR1 in disease.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
SIGNORiO15164.

Miscellaneous databases

ChiTaRSiTRIM24. human.
EvolutionaryTraceiO15164.
GeneWikiiTRIM24.
GenomeRNAii8805.
PROiO15164.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000122779.
CleanExiHS_TRIM24.
ExpressionAtlasiO15164. baseline and differential.
GenevisibleiO15164. HS.

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. 1 hit.
[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]
ProtoNetiSearch...

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 30, 2016
This is version 178 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.