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UniProtKB/Swiss-Prot entry O15164


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TIF1A_HUMAN
Primary accession number O15164
Secondary accession number O95854
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on January 24, 2001 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 100)
Name and origin of the protein
Protein name Transcription intermediary factor 1-alpha
Synonyms TIF1-alpha
Tripartite motif-containing protein 24
RING finger protein 82
Gene name
Name: TRIM24
Synonyms: RNF82, TIF1, TIF1A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
TISSUE=Mammary cancer;
DOI=10.1074/jbc.272.18.12062; PubMed=9115274 [NCBI, ExPASy, EBI, Israel, Japan]
Thenot S., Henriquet C., Rochefort H., Cavailles V.;
"Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1.";
J. Biol. Chem. 272:12062-12068(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
DOI=10.1038/sj.onc.1202655; PubMed=10022127 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"TIF1gamma, a novel member of the transcriptional intermediary factor 1 family.";
Oncogene 18:1209-1217(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 477-510 (ISOFORM LONG).
TISSUE=Mammary cancer;
Cavailles V.;
Submitted (JAN-1999) to UniProtKB.
[5]
INTERACTION WITH NR3C2.
DOI=10.1210/me.14.8.1210; PubMed=10935545 [NCBI, ExPASy, EBI, Israel, Japan]
Hellal-Levy C., Fagart J., Souque A., Wurtz J.-M., Moras D., Rafestin-Oblin M.-E.;
"Crucial role of the H11-H12 loop in stabilizing the active conformation of the human mineralocorticoid receptor.";
Mol. Endocrinol. 14:1210-1221(2000).
[6]
CHROMOSOMAL TRANSLOCATION WITH RET.
TISSUE=Thyroid;
DOI=10.1038/sj.onc.1202824; PubMed=10439047 [NCBI, ExPASy, EBI, Israel, Japan]
Klugbauer S., Rabes H.M.;
"The transcription coactivator HTIF1 and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas.";
Oncogene 18:4388-4393(1999).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-811, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-768, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660; SER-667; SER-768; SER-808; SER-811; SER-1019; SER-1025 AND SER-1028, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[11]
VARIANTS [LARGE SCALE ANALYSIS] THR-320; ASN-403; ASN-762 AND SER-1009.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF009353; AAB63585.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF119042; AAD17258.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC028689; AAH28689.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00005184; -.
IPI00184317; -.
RefSeq NP_056989.2; -.
UniGene Hs.490287
3D structure databases
PDB
2YYN; X-ray; 2.50 A; A/B/C/D=891-1012.[ExPASy / RCSB / EBI]
PDBsum 2YYN; -.
ModBase O15164.
PTM databases
PhosphoSite O15164; -.
Organism-specific databases
GeneCards GC07P137795; -.
H-InvDB HIX0007122; -.
HGNC HGNC:11812; TRIM24.
GenAtlas TRIM24.
MIM 188550; phenotype. [NCBI / EBI]
603406; gene. [NCBI / EBI]
Orphanet 146; Thyroid carcinoma, papillary or follicular.
PharmGKB PA36519; -.
Gene expression databases
ArrayExpress O15164; -.
Bgee O15164; -.
CleanEx HS_TRIM24; -.
GermOnline ENSG00000122779; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (traceable author statement from ProtInc).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005102; Molecular function: receptor binding (traceable author statement from ProtInc).
GO:0032183; Molecular function: SUMO binding (inferred from physical interaction from UniProtKB).
GO:0003713; Molecular function: transcription coactivator activity (traceable author statement from ProtInc).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006366; Biological process: transcription from RNA polymerase II promoter (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR003649; Bbox_C.
IPR001487; Bromodomain.
IPR018359; Bromodomain_CS.
IPR019786; Zinc_finger_PHD-type_CS.
IPR000315; Znf_B-box.
IPR018957; Znf_C3HC4_RING-type.
IPR001965; Znf_PHD.
IPR019787; Znf_PHD-finger.
IPR001841; Znf_RING.
IPR017907; Znf_RING_CS.
Graphical view of domain structure.
Gene3D G3DSA:1.20.920.10; Bromodomain; 1.
Pfam PF00439; Bromodomain; 1.
PF00628; PHD; 1.
PF00643; zf-B_box; 2.
PF00097; zf-C3HC4; 1.
Pfam graphical view of domain structure.
PRINTS PR00503; BROMODOMAIN.
SMART SM00502; BBC; 1.
SM00336; BBOX; 2.
SM00297; BROMO; 1.
SM00249; PHD; 1.
SM00184; RING; 1.
SMART graphical view of domain structure.
PROSITE PS00633; BROMODOMAIN_1; 1.
PS50014; BROMODOMAIN_2; 1.
PS50119; ZF_BBOX; 2.
PS01359; ZF_PHD_1; 1.
PS50016; ZF_PHD_2; 1.
PS00518; ZF_RING_1; 1.
PS50089; ZF_RING_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O15164; -.
Genome annotation databases
Ensembl ENSG00000122779; Homo sapiens. [Contig view]
GeneID 8805; -.
Phylogenomic databases
HOGENOM O15164; -.
HOVERGEN O15164; -.
OMA O15164; GPYNLPS.
Other
NextBio 33028; -.
SOURCE TRIM24; Homo sapiens.
ProtoNet O15164.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Bromodomain; Chromosomal rearrangement; Coiled coil; Direct protein sequencing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Repeat; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1050  1050     Transcription intermediary factor 1-alpha. PRO_0000056390
DOMAIN   932    987  56     Bromo. 
ZN_FING   56     82  27     RING-type. 
ZN_FING   158    211  54     B box-type 1. 
ZN_FING   218    259  42     B box-type 2. 
ZN_FING   826    873  48     PHD-type. 
REGION   754    779  26     Nuclear receptor binding site (NRBS). 
COILED   289    359  71     Potential. 
MOTIF   891    907  17     Nuclear localization signal (Potential). 
COMPBIAS   9     15  7     Poly-Ala. 
COMPBIAS   344    347  4     Poly-Gln. 
SITE   476    477  2     Breakpoint for translocation to form TIF1-RET oncogene. 
MOD_RES   660    660        Phosphoserine. 
MOD_RES   667    667        Phosphoserine. 
MOD_RES   768    768        Phosphoserine. 
MOD_RES   808    808        Phosphoserine. 
MOD_RES   811    811        Phosphoserine. 
MOD_RES   1019   1019        Phosphoserine. 
MOD_RES   1025   1025        Phosphoserine. 
MOD_RES   1028   1028        Phosphoserine. 
VAR_SEQ   477    510        Missing (in isoform Short). VSP_005772
VARIANT   320    320  1     I -> T (in an ovarian serous carcinoma sample; somatic mutation). VAR_042382 
VARIANT   403    403  1     T -> N (in a lung squamous cell carcinoma sample; somatic mutation). VAR_042383 
VARIANT   762    762  1     S -> N. VAR_042384 
VARIANT   796    796  1     N -> S (in dbSNP:rs35356723 [NCBI]). VAR_052148 
VARIANT   1009   1009  1     R -> S. VAR_042385 [3D]
CONFLICT   14     20        AASAAAS -> RLGCAP (in Ref. 1; AAB63585). 
CONFLICT   24     28        SAAPS -> RGG (in Ref. 1; AAB63585). 
CONFLICT   109    114        GSPVSG -> ARRSA (in Ref. 1; AAB63585). 
CONFLICT   350    350        A -> T (in Ref. 1; AAB63585). 
CONFLICT   600    600        D -> N (in Ref. 1; AAB63585). 
CONFLICT   608    608        M -> I (in Ref. 1; AAB63585). 
CONFLICT   967    967        A -> R (in Ref. 1; AAB63585). 
HELIX   902    916  15      
HELIX   919    924  6      
HELIX   935    938  4      
HELIX   945    953  9      
STRAND   954    956  3      
HELIX   962    979  18      
HELIX   985   1004  20      
STRAND   1005   1007  3      
Sequence information
Length: 1050 AA [This is the length of the unprocessed precursor] Molecular weight: 116831 Da [This is the MW of the unprocessed precursor] CRC64: D341E8022AACC67E [This is a checksum on the sequence]
        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 

O15164 in FASTA format

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