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Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM24) (RING finger protein 82) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24)

 TIF1A_HUMAN             Reviewed;        1050 AA.
O15164; A4D1R7; A4D1R8; O95854;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 3.
25-OCT-2017, entry version 187.
RecName: Full=Transcription intermediary factor 1-alpha;
Short=TIF1-alpha;
EC=2.3.2.27;
AltName: Full=E3 ubiquitin-protein ligase TRIM24;
AltName: Full=RING finger protein 82;
AltName: Full=RING-type E3 ubiquitin transferase TIF1-alpha {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 24;
Name=TRIM24; Synonyms=RNF82, TIF1, TIF1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND SUBUNIT.
TISSUE=Mammary cancer;
PubMed=9115274; DOI=10.1074/jbc.272.18.12062;
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).
PubMed=10022127; DOI=10.1038/sj.onc.1202655;
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] (ISOFORM LONG).
TISSUE=Retinoblastoma;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
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.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[7]
PROTEIN SEQUENCE OF 477-510 (ISOFORM LONG).
TISSUE=Mammary cancer;
Cavailles V.;
Submitted (JAN-1999) to UniProtKB.
[8]
INTERACTION WITH NR3C2.
PubMed=10935545; DOI=10.1210/mend.14.8.0502;
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).
[9]
CHROMOSOMAL TRANSLOCATION WITH RET.
TISSUE=Thyroid;
PubMed=10439047; DOI=10.1038/sj.onc.1202824;
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-811; SER-1025 AND
SER-1028, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
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).
[11]
FUNCTION.
PubMed=16322096; DOI=10.1210/me.2005-0393;
Teyssier C., Ou C.Y., Khetchoumian K., Losson R., Stallcup M.R.;
"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.";
Mol. Endocrinol. 20:1276-1286(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-768; SER-808
AND SER-811, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
INTERACTION WITH AR.
PubMed=19909775; DOI=10.1016/j.bbamcr.2009.11.001;
Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N.,
Tanaka J., Imamura M., Hatakeyama S.;
"TRIM24 mediates ligand-dependent activation of androgen receptor and
is repressed by a bromodomain-containing protein, BRD7, in prostate
cancer cells.";
Biochim. Biophys. Acta 1793:1828-1836(2009).
[15]
FUNCTION AS E3 UBIQUITIN LIGASE, AND INTERACTION WITH TP53.
PubMed=19556538; DOI=10.1073/pnas.0813177106;
Allton K., Jain A.K., Herz H.M., Tsai W.W., Jung S.Y., Qin J.,
Bergmann A., Johnson R.L., Barton M.C.;
"Trim24 targets endogenous p53 for degradation.";
Proc. Natl. Acad. Sci. U.S.A. 106:11612-11616(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1025 AND SER-1028, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101; SER-110; SER-768
AND SER-811, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744; SER-811; THR-818;
SER-1019; SER-1028 AND SER-1042, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654; SER-744; SER-811;
SER-1025 AND SER-1028, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-711; LYS-723 AND LYS-949,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-723 AND LYS-741, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-702; LYS-723 AND LYS-1041,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-723, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-205; LYS-276;
LYS-436; LYS-458; LYS-552; LYS-641; LYS-702; LYS-711; LYS-723;
LYS-741; LYS-801; LYS-810; LYS-875 AND LYS-992, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[28]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 891-1012.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of human bromodomain protein.";
Submitted (FEB-2009) to the PDB data bank.
[29]
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,
AND INDUCTION.
PubMed=21164480; DOI=10.1038/nature09542;
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.;
"TRIM24 links a non-canonical histone signature to breast cancer.";
Nature 468:927-932(2010).
[30]
VARIANTS [LARGE SCALE ANALYSIS] THR-320; ASN-403; ASN-762 AND
SER-1009.
PubMed=17344846; DOI=10.1038/nature05610;
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).
-!- 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). {ECO:0000250,
ECO:0000269|PubMed:16322096, ECO:0000269|PubMed:19556538,
ECO:0000269|PubMed:21164480}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: 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). {ECO:0000250,
ECO:0000269|PubMed:10935545, ECO:0000269|PubMed:19556538,
ECO:0000269|PubMed:19909775, ECO:0000269|PubMed:21164480,
ECO:0000269|PubMed:9115274}.
-!- INTERACTION:
P03372:ESR1; NbExp=3; IntAct=EBI-2130378, EBI-78473;
P04637:TP53; NbExp=3; IntAct=EBI-2130378, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21164480}.
Cytoplasm {ECO:0000269|PubMed:21164480}. Note=Colocalizes with
sites of active transcription. Detected both in nucleus and
cytoplasm in some breast cancer samples. Predominantly nuclear.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=O15164-1; Sequence=Displayed;
Name=Short;
IsoId=O15164-2; Sequence=VSP_005772;
-!- INDUCTION: Up-regulated in some cases of breast cancer.
{ECO:0000269|PubMed:21164480}.
-!- PTM: Sumoylated. {ECO:0000250}.
-!- DISEASE: Note=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. {ECO:0000269|PubMed:10439047}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TRIM24ID504ch7q34.html";
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EMBL; AF009353; AAB63585.1; -; mRNA.
EMBL; AF119042; AAD17258.1; -; mRNA.
EMBL; AK075306; BAG52105.1; -; mRNA.
EMBL; AC008265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC013429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236950; EAL24046.1; -; Genomic_DNA.
EMBL; CH236950; EAL24047.1; -; Genomic_DNA.
EMBL; CH471070; EAW83884.1; -; Genomic_DNA.
EMBL; CH471070; EAW83885.1; -; Genomic_DNA.
EMBL; BC028689; AAH28689.2; -; mRNA.
CCDS; CCDS47720.1; -. [O15164-2]
CCDS; CCDS5847.1; -. [O15164-1]
RefSeq; NP_003843.3; NM_003852.3. [O15164-2]
RefSeq; NP_056989.2; NM_015905.2. [O15164-1]
UniGene; Hs.490287; -.
PDB; 2YYN; X-ray; 2.50 A; A/B/C/D=891-1012.
PDB; 3O33; X-ray; 2.00 A; A/B/C/D=824-1006.
PDB; 3O34; X-ray; 1.90 A; A=824-1006.
PDB; 3O35; X-ray; 1.76 A; A/B=824-1006.
PDB; 3O36; X-ray; 1.70 A; A/B=824-1006.
PDB; 3O37; X-ray; 2.00 A; A/B/C/D=824-1006.
PDB; 4YAB; X-ray; 1.90 A; A/B=824-1006.
PDB; 4YAD; X-ray; 1.73 A; A/B=824-1006.
PDB; 4YAT; X-ray; 2.18 A; A/B=824-1006.
PDB; 4YAX; X-ray; 2.25 A; A/B=824-1006.
PDB; 4YBM; X-ray; 1.46 A; A/B=824-1006.
PDB; 4YBS; X-ray; 1.83 A; A=824-1006.
PDB; 4YBT; X-ray; 1.82 A; A=824-1006.
PDB; 4YC9; X-ray; 1.82 A; A=824-1006.
PDB; 4ZQL; X-ray; 1.79 A; A/B=825-1006.
PDB; 5H1T; X-ray; 1.95 A; A/B/C/D=824-1006.
PDB; 5H1U; X-ray; 1.90 A; A/B/C/D=824-1006.
PDB; 5H1V; X-ray; 2.00 A; A/B=824-1006.
PDBsum; 2YYN; -.
PDBsum; 3O33; -.
PDBsum; 3O34; -.
PDBsum; 3O35; -.
PDBsum; 3O36; -.
PDBsum; 3O37; -.
PDBsum; 4YAB; -.
PDBsum; 4YAD; -.
PDBsum; 4YAT; -.
PDBsum; 4YAX; -.
PDBsum; 4YBM; -.
PDBsum; 4YBS; -.
PDBsum; 4YBT; -.
PDBsum; 4YC9; -.
PDBsum; 4ZQL; -.
PDBsum; 5H1T; -.
PDBsum; 5H1U; -.
PDBsum; 5H1V; -.
ProteinModelPortal; O15164; -.
SMR; O15164; -.
BioGrid; 114333; 93.
DIP; DIP-52713N; -.
ELM; O15164; -.
IntAct; O15164; 21.
STRING; 9606.ENSP00000340507; -.
BindingDB; O15164; -.
ChEMBL; CHEMBL3108638; -.
GuidetoPHARMACOLOGY; 2252; -.
iPTMnet; O15164; -.
PhosphoSitePlus; O15164; -.
BioMuta; TRIM24; -.
EPD; O15164; -.
MaxQB; O15164; -.
PaxDb; O15164; -.
PeptideAtlas; O15164; -.
PRIDE; O15164; -.
DNASU; 8805; -.
Ensembl; ENST00000343526; ENSP00000340507; ENSG00000122779. [O15164-1]
Ensembl; ENST00000415680; ENSP00000390829; ENSG00000122779. [O15164-2]
GeneID; 8805; -.
KEGG; hsa:8805; -.
UCSC; uc003vub.4; human. [O15164-1]
CTD; 8805; -.
DisGeNET; 8805; -.
EuPathDB; HostDB:ENSG00000122779.16; -.
GeneCards; TRIM24; -.
HGNC; HGNC:11812; TRIM24.
HPA; HPA043495; -.
HPA; HPA061717; -.
MalaCards; TRIM24; -.
MIM; 603406; gene.
neXtProt; NX_O15164; -.
OpenTargets; ENSG00000122779; -.
Orphanet; 146; Papillary or follicular thyroid carcinoma.
PharmGKB; PA36519; -.
eggNOG; ENOG410KDQG; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00890000139374; -.
HOGENOM; HOG000252971; -.
HOVERGEN; HBG054599; -.
InParanoid; O15164; -.
KO; K08881; -.
OMA; FWAQNIF; -.
OrthoDB; EOG091G01KK; -.
PhylomeDB; O15164; -.
TreeFam; TF106455; -.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
SIGNOR; O15164; -.
UniPathway; UPA00143; -.
ChiTaRS; TRIM24; human.
EvolutionaryTrace; O15164; -.
GeneWiki; TRIM24; -.
GenomeRNAi; 8805; -.
PRO; PR:O15164; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000122779; -.
CleanEx; HS_TRIM24; -.
ExpressionAtlas; O15164; baseline and differential.
Genevisible; O15164; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005719; C:nuclear euchromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005726; C:perichromatin fibrils; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0034056; F:estrogen response element binding; IDA:UniProtKB.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IEA:Ensembl.
GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005102; F:receptor binding; TAS:ProtInc.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IEA:Ensembl.
GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
CDD; cd00021; BBOX; 1.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 3.
InterPro; IPR003649; Bbox_C.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF00643; zf-B_box; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00502; BBC; 1.
SMART; SM00336; BBOX; 2.
SMART; SM00297; BROMO; 1.
SMART; SM00249; PHD; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS50119; ZF_BBOX; 2.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Bromodomain;
Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Isopeptide bond;
Metal-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Transferase; Tumor suppressor;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 1050 Transcription intermediary factor 1-
alpha.
/FTId=PRO_0000056390.
DOMAIN 932 987 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
ZN_FING 56 82 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 158 211 B box-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 218 259 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 826 873 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 754 779 Nuclear receptor binding site (NRBS).
REGION 834 840 Interaction with histone H3 that is not
methylated at 'Lys-4' (H3K4me0).
REGION 979 980 Interaction with histone H3 that is
acetylated at 'Lys-23' (H3K23ac).
COILED 289 359 {ECO:0000255}.
MOTIF 891 907 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 9 15 Poly-Ala.
COMPBIAS 344 347 Poly-Gln.
SITE 476 477 Breakpoint for translocation to form
TRIM24-RET oncogene.
SITE 827 827 Interaction with histone H3 that is not
methylated at 'Lys-4' (H3K4me0).
MOD_RES 101 101 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 469 469 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q64127}.
MOD_RES 654 654 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 660 660 Phosphoserine.
{ECO:0000250|UniProtKB:Q64127}.
MOD_RES 667 667 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 744 744 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 768 768 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 808 808 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 811 811 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 818 818 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1019 1019 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1025 1025 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 205 205 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 276 276 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 436 436 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 458 458 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 552 552 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 641 641 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 702 702 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 711 711 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 723 723 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 723 723 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 741 741 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
CROSSLNK 801 801 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 810 810 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 875 875 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 949 949 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 992 992 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1041 1041 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364}.
VAR_SEQ 477 510 Missing (in isoform Short).
{ECO:0000303|PubMed:10022127,
ECO:0000303|PubMed:9115274}.
/FTId=VSP_005772.
VARIANT 320 320 I -> T (in an ovarian serous carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042382.
VARIANT 403 403 T -> N (in a lung squamous cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042383.
VARIANT 762 762 S -> N. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_042384.
VARIANT 796 796 N -> S (in dbSNP:rs35356723).
/FTId=VAR_052148.
VARIANT 1009 1009 R -> S (in dbSNP:rs34585297).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042385.
MUTAGEN 827 827 D->A: Strongly reduced affinity for
histone H3 that is not methylated at
'Lys-4' (H3K4me0).
{ECO:0000269|PubMed:21164480}.
MUTAGEN 840 840 C->W: Abolishes interaction with histone
H3. {ECO:0000269|PubMed:21164480}.
MUTAGEN 979 980 FN->AA: Strongly reduced affinity for
histone H3 that is acetylated at 'Lys-23'
(H3K23ac). {ECO:0000269|PubMed:21164480}.
CONFLICT 14 20 AASAAAS -> RLGCAP (in Ref. 1; AAB63585).
{ECO:0000305}.
CONFLICT 24 28 SAAPS -> RGG (in Ref. 1; AAB63585).
{ECO:0000305}.
CONFLICT 109 114 GSPVSG -> ARRSA (in Ref. 1; AAB63585).
{ECO:0000305}.
CONFLICT 350 350 A -> T (in Ref. 1; AAB63585).
{ECO:0000305}.
CONFLICT 600 600 D -> N (in Ref. 1; AAB63585).
{ECO:0000305}.
CONFLICT 608 608 M -> I (in Ref. 1; AAB63585).
{ECO:0000305}.
CONFLICT 967 967 A -> R (in Ref. 1; AAB63585).
{ECO:0000305}.
STRAND 827 829 {ECO:0000244|PDB:3O33}.
TURN 830 832 {ECO:0000244|PDB:4YBM}.
STRAND 836 840 {ECO:0000244|PDB:3O37}.
STRAND 842 845 {ECO:0000244|PDB:4YBM}.
TURN 850 852 {ECO:0000244|PDB:4YBM}.
STRAND 853 855 {ECO:0000244|PDB:4YBM}.
TURN 868 870 {ECO:0000244|PDB:4YBM}.
STRAND 873 875 {ECO:0000244|PDB:4YBM}.
HELIX 881 883 {ECO:0000244|PDB:4YBM}.
TURN 889 891 {ECO:0000244|PDB:3O36}.
HELIX 902 917 {ECO:0000244|PDB:4YBM}.
HELIX 919 921 {ECO:0000244|PDB:3O37}.
HELIX 922 924 {ECO:0000244|PDB:4YBM}.
HELIX 935 938 {ECO:0000244|PDB:4YBM}.
HELIX 945 953 {ECO:0000244|PDB:4YBM}.
TURN 954 956 {ECO:0000244|PDB:4YC9}.
HELIX 962 979 {ECO:0000244|PDB:4YBM}.
HELIX 985 1004 {ECO:0000244|PDB:4YBM}.
STRAND 1005 1007 {ECO:0000244|PDB:2YYN}.
SEQUENCE 1050 AA; 116831 MW; D341E8022AACC67E CRC64;
MEVAVEKAVA AAAAASAAAS GGPSAAPSGE NEAESRQGPD SERGGEAARL NLLDTCAVCH
QNIQSRAPKL LPCLHSFCQR CLPAPQRYLM LPAPMLGSAE TPPPVPAPGS PVSGSSPFAT
QVGVIRCPVC SQECAERHII DNFFVKDTTE VPSSTVEKSN QVCTSCEDNA EANGFCVECV
EWLCKTCIRA HQRVKFTKDH TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK
LTCRDCQLLE HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKFTGNQ IQNRIIEVNQ
NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA GLSKQLEHVM
HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT NNTIQFHCDP SFWAQNIINL
GSLVIEDKES QPQMPKQNPV VEQNSQPPSG LSSNQLSKFP TQISLAQLRL QHMQQQVMAQ
RQQVQRRPAP VGLPNPRMQG PIQQPSISHQ QPPPRLINFQ NHSPKPNGPV LPPHPQQLRY
PPNQNIPRQA IKPNPLQMAF LAQQAIKQWQ ISSGQGTPST TNSTSSTPSS PTITSAAGYD
GKAFGSPMID LSSPVGGSYN LPSLPDIDCS STIMLDNIVR KDTNIDHGQP RPPSNRTVQS
PNSSVPSPGL AGPVTMTSVH PPIRSPSASS VGSRGSSGSS SKPAGADSTH KVPVVMLEPI
RIKQENSGPP ENYDFPVVIV KQESDEESRP QNANYPRSIL TSLLLNSSQS STSEETVLRS
DAPDSTGDQP GLHQDNSSNG KSEWLDPSQK SPLHVGETRK EDDPNEDWCA VCQNGGELLC
CEKCPKVFHL SCHVPTLTNF PSGEWICTFC RDLSKPEVEY DCDAPSHNSE KKKTEGLVKL
TPIDKRKCER LLLFLYCHEM SLAFQDPVPL TVPDYYKIIK NPMDLSTIKK RLQEDYSMYS
KPEDFVADFR LIFQNCAEFN EPDSEVANAG IKLENYFEEL LKNLYPEKRF PKPEFRNESE
DNKFSDDSDD DFVQPRKKRL KSIEERQLLK


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EIAAB34367 CARP-2,Caspase regulator CARP2,Caspases-8 and -10-associated RING finger protein 2,E3 ubiquitin-protein ligase rififylin,Fring,FYVE-RING finger protein Sakura,Homo sapiens,Human,RFFL,RING finger and F
EIAAB43847 E3 ubiquitin-protein ligase TRIM11,Homo sapiens,Human,Protein BIA1,RING finger protein 92,RNF92,TRIM11,Tripartite motif-containing protein 11
EIAAB43947 E3 ubiquitin-protein ligase TRIM63,Homo sapiens,Human,IRF,Iris RING finger protein,MuRF1,MURF1,MuRF-1,Muscle-specific RING finger protein 1,RING finger protein 28,RNF28,SMRZ,Striated muscle RING zinc
EIAAB43955 E3 ubiquitin-protein ligase TRIM68,GC109,Homo sapiens,Human,RING finger protein 137,RNF137,SS56,SS-56,SSA protein SS-56,TRIM68,Tripartite motif-containing protein 68
EIAAB45116 E3 ubiquitin-protein ligase UBR3,Homo sapiens,Human,KIAA2024,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,UBR3,Zinc finger protein 650,ZNF650
EIAAB45117 E3 ubiquitin-protein ligase UBR3,Kiaa2024,Mouse,Mus musculus,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,Ubr3,Zfp650,Zinc finger protein 650,Znf650
EIAAB43956 E3 ubiquitin-protein ligase TRIM68,Mouse,Mus musculus,RING finger protein 137,Rnf137,Trim68,Tripartite motif-containing protein 68
EIAAB43859 E3 ubiquitin-protein ligase TRIM17,Rat,Rattus norvegicus,Terf,Testis RING finger protein,Trim17,Tripartite motif-containing protein 17
EIAAB43934 E3 ubiquitin-protein ligase TRIM56,Homo sapiens,Human,RING finger protein 109,RNF109,TRIM56,Tripartite motif-containing protein 56
EIAAB44002 E3 ubiquitin-protein ligase TRIM9,Homo sapiens,Human,KIAA0282,RING finger protein 91,RNF91,TRIM9,Tripartite motif-containing protein 9
EIAAB44003 E3 ubiquitin-protein ligase TRIM9,Rat,Rattus norvegicus,SNAP-25-interacting RING finger protein,Spring,Trim9,Tripartite motif-containing protein 9


 

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