Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Thyroid hormone receptor-associated protein 3 (BCLAF1 and THRAP3 family member 2) (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150)

 TR150_HUMAN             Reviewed;         955 AA.
Q9Y2W1; D3DPS5; Q5VTK6;
28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 2.
12-SEP-2018, entry version 177.
RecName: Full=Thyroid hormone receptor-associated protein 3;
AltName: Full=BCLAF1 and THRAP3 family member 2 {ECO:0000312|HGNC:HGNC:22964};
AltName: Full=Thyroid hormone receptor-associated protein complex 150 kDa component;
Short=Trap150;
Name=THRAP3 {ECO:0000312|HGNC:HGNC:22964};
Synonyms=BCLAF2 {ECO:0000312|HGNC:HGNC:22964}, TRAP150;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 490-500, TISSUE
SPECIFICITY, IDENTIFICATION IN TRAP COMPLEX, AND VARIANT VAL-201.
TISSUE=Cervix carcinoma;
PubMed=10198638; DOI=10.1016/S1097-2765(00)80463-3;
Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S.,
Fu Z.-Y., Zhang X., Qin J., Roeder R.G.;
"Identity between TRAP and SMCC complexes indicates novel pathways for
the function of nuclear receptors and diverse mammalian activators.";
Mol. Cell 3:361-370(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-201.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-201.
TISSUE=Brain;
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).
[5]
PROTEIN SEQUENCE OF 186-202; 216-245; 253-261; 314-333; 376-387;
443-451; 468-481; 486-498; 573-591; 609-653; 678-687; 710-718;
792-802; 864-876; 879-893 AND 927-944, METHYLATION AT ARG-17,
PHOSPHORYLATION AT SER-243; SER-320 AND SER-682, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Lilla S.,
von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-243; SER-248;
SER-253; SER-315; SER-320; SER-575; SER-672 AND SER-928, 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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[10]
SUBUNIT.
PubMed=17095540; DOI=10.1261/rna.336807;
Merz C., Urlaub H., Will C.L., Luhrmann R.;
"Protein composition of human mRNPs spliced in vitro and differential
requirements for mRNP protein recruitment.";
RNA 13:116-128(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
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).
[12]
IDENTIFICATION IN THE SNARP COMPLEX.
PubMed=18794151; DOI=10.1158/0008-5472.CAN-08-1217;
Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M.,
Perkins N.D.;
"Regulation of cyclin D1 RNA stability by SNIP1.";
Cancer Res. 68:7621-7628(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-248 AND
SER-253, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-237; SER-240;
SER-243; SER-248; SER-253; SER-379; SER-406; SER-408; SER-575;
SER-682; THR-874; SER-928 AND SER-939, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-928, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[18]
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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-874; SER-928 AND
SER-939, 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).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221; LYS-455; LYS-519 AND
LYS-811, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
FUNCTION, AND INTERACTION WITH SFPQ.
PubMed=20932480; DOI=10.1016/j.molcel.2010.09.013;
Heyd F., Lynch K.W.;
"Phosphorylation-dependent regulation of PSF by GSK3 controls CD45
alternative splicing.";
Mol. Cell 40:126-137(2010).
[22]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NXF1.
PubMed=20123736; DOI=10.1093/nar/gkq017;
Lee K.M., Hsu I.W., Tarn W.Y.;
"TRAP150 activates pre-mRNA splicing and promotes nuclear mRNA
degradation.";
Nucleic Acids Res. 38:3340-3350(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-243; SER-248;
SER-253; SER-257; SER-315; SER-320; SER-379; SER-408; SER-575;
SER-622; SER-682; SER-698; SER-928 AND SER-939, 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).
[24]
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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-253; SER-315;
SER-320; SER-339; SER-379; SER-406; SER-408; SER-535; SER-575;
SER-622; SER-682; SER-698; SER-928 AND SER-939, 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).
[26]
FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-406 AND SER-408.
PubMed=22424773; DOI=10.1016/j.molcel.2012.01.026;
Beli P., Lukashchuk N., Wagner S.A., Weinert B.T., Olsen J.V.,
Baskcomb L., Mann M., Jackson S.P., Choudhary C.;
"Proteomic investigations reveal a role for RNA processing factor
THRAP3 in the DNA damage response.";
Mol. Cell 46:212-225(2012).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[28]
IDENTIFICATION IN A MACOM-LIKE COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=24100041; DOI=10.1074/jbc.M113.500397;
Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T.,
Hamakubo T.;
"Identification of Wilms' tumor 1-associating protein complex and its
role in alternative splicing and the cell cycle.";
J. Biol. Chem. 288:33292-33302(2013).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-232; SER-237;
SER-240; SER-243; SER-248; SER-253; SER-257; SER-315; SER-320;
SER-323; SER-326; SER-377; SER-379; THR-397; SER-406; SER-408;
SER-444; SER-468; SER-560; SER-562; SER-575; SER-619; SER-682;
SER-698; THR-874; SER-928 AND SER-939, 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).
[30]
ADP-RIBOSYLATION.
PubMed=24055347; DOI=10.1016/j.molcel.2013.08.026;
Jungmichel S., Rosenthal F., Altmeyer M., Lukas J., Hottiger M.O.,
Nielsen M.L.;
"Proteome-wide identification of poly(ADP-Ribosyl)ation targets in
different genotoxic stress responses.";
Mol. Cell 52:272-285(2013).
[31]
FUNCTION, INTERACTION WITH HELZ2 AND PPARG, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=23525231; DOI=10.1210/me.2012-1332;
Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T.,
Ishii S., Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H.,
Hashimoto K., Okada S., Yamada M., Mori M.;
"THRAP3 interacts with HELZ2 and plays a novel role in adipocyte
differentiation.";
Mol. Endocrinol. 27:769-780(2013).
[32]
FUNCTION.
PubMed=24043798; DOI=10.1073/pnas.1305980110;
Lande-Diner L., Boyault C., Kim J.Y., Weitz C.J.;
"A positive feedback loop links circadian clock factor CLOCK-BMAL1 to
the basic transcriptional machinery.";
Proc. Natl. Acad. Sci. U.S.A. 110:16021-16026(2013).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-253; SER-257;
SER-320; SER-377; SER-560; SER-575; SER-682 AND SER-684, AND
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).
[34]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-66; ARG-101; ARG-108 AND
LYS-252, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-451; LYS-467; LYS-470;
LYS-486; LYS-705; LYS-711; LYS-756 AND LYS-759, 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).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-202; LYS-387 AND LYS-451,
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).
[37]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-486, 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).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-396; LYS-427; LYS-451;
LYS-470; LYS-486; LYS-527; LYS-697; LYS-705 AND LYS-711, 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).
[39]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-202; LYS-215; LYS-221;
LYS-252; LYS-333; LYS-346; LYS-353; LYS-375; LYS-387; LYS-389;
LYS-396; LYS-401; LYS-421; LYS-427; LYS-451; LYS-455; LYS-461;
LYS-467; LYS-470; LYS-481; LYS-486; LYS-527; LYS-551; LYS-558;
LYS-602; LYS-697; LYS-705; LYS-709; LYS-711; LYS-876 AND LYS-879, 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).
-!- FUNCTION: Involved in pre-mRNA splicing. Remains associated with
spliced mRNA after splicing which probably involves interactions
with the exon junction complex (EJC). Can trigger mRNA decay which
seems to be independent of nonsense-mediated decay involving
premature stop codons (PTC) recognition. May be involved in
nuclear mRNA decay. Involved in regulation of signal-induced
alternative splicing. During splicing of PTPRC/CD45 is proposed to
sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting
T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by
acting as component of the SNARP complex which associates with
both the 3'end of the CCND1 gene and its mRNA. Involved in
response to DNA damage. Is excluced from DNA damage sites in a
manner that parallels transcription inhibition; the function may
involve the SNARP complex. Initially thought to play a role in
transcriptional coactivation through its association with the TRAP
complex; however, it is not regarded as a stable Mediator complex
subunit. Cooperatively with HELZ2, enhances the transcriptional
activation mediated by PPARG, maybe through the stabilization of
the PPARG binding to DNA in presence of ligand. May play a role in
the terminal stage of adipocyte differentiation. Plays a role in
the positive regulation of the circadian clock. Acts as a
coactivator of the CLOCK-ARNTL/BMAL1 heterodimer and promotes its
transcriptional activator activity and binding to circadian target
genes (PubMed:24043798). {ECO:0000269|PubMed:20123736,
ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:22424773,
ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:24043798}.
-!- SUBUNIT: Associated with the large multiprotein complex TRAP
(Mediator complex-like). Interacts with SFPQ; the interaction is
dependent on SFPQ phosphorylation at 'Thr-687' and inhibits
binding of SFPQ to an ESS1 exonic splicing silencer element-
containing RNA. Interacts with NXF1. Component of the SNARP
complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and
PNN. Associated with spliced mRNP complexes. Interacts with HELZ2
and PPARG. Interacts with CLOCK and ARNTL/BMAL1 (By similarity).
Component of a MACOM-like complex, named WTAP complex, composed of
WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3.
{ECO:0000250|UniProtKB:Q569Z6, ECO:0000269|PubMed:10198638,
ECO:0000269|PubMed:17095540, ECO:0000269|PubMed:18794151,
ECO:0000269|PubMed:20123736, ECO:0000269|PubMed:20932480,
ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:24100041}.
-!- INTERACTION:
P38919:EIF4A3; NbExp=2; IntAct=EBI-352039, EBI-299104;
Q9UBU9:NXF1; NbExp=4; IntAct=EBI-352039, EBI-398874;
P23246:SFPQ; NbExp=6; IntAct=EBI-352039, EBI-355453;
Q13573:SNW1; NbExp=4; IntAct=EBI-352039, EBI-632715;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20123736,
ECO:0000269|PubMed:23525231}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:24100041}. Nucleus speckle
{ECO:0000269|PubMed:24100041}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10198638}.
-!- PTM: ADP-ribosylation during genotoxic stress promotes
accumulation in nuclear speckles.
-!- SIMILARITY: Belongs to the BCLAF1/THRAP3 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH37554.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/THRAP3ID42960ch1p34.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF117756; AAD22034.1; -; mRNA.
EMBL; AL591845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07379.1; -; Genomic_DNA.
EMBL; CH471059; EAX07380.1; -; Genomic_DNA.
EMBL; BC037554; AAH37554.1; ALT_SEQ; mRNA.
EMBL; BC112330; AAI12331.1; -; mRNA.
EMBL; BC112350; AAI12351.1; -; mRNA.
CCDS; CCDS405.1; -.
RefSeq; NP_001308400.1; NM_001321471.1.
RefSeq; NP_001308402.1; NM_001321473.1.
RefSeq; NP_005110.2; NM_005119.3.
UniGene; Hs.744057; -.
ProteinModelPortal; Q9Y2W1; -.
BioGrid; 115292; 163.
CORUM; Q9Y2W1; -.
IntAct; Q9Y2W1; 58.
MINT; Q9Y2W1; -.
STRING; 9606.ENSP00000346634; -.
iPTMnet; Q9Y2W1; -.
PhosphoSitePlus; Q9Y2W1; -.
SwissPalm; Q9Y2W1; -.
BioMuta; THRAP3; -.
DMDM; 97537467; -.
EPD; Q9Y2W1; -.
MaxQB; Q9Y2W1; -.
PaxDb; Q9Y2W1; -.
PeptideAtlas; Q9Y2W1; -.
PRIDE; Q9Y2W1; -.
ProteomicsDB; 85914; -.
TopDownProteomics; Q9Y2W1; -.
DNASU; 9967; -.
Ensembl; ENST00000354618; ENSP00000346634; ENSG00000054118.
Ensembl; ENST00000469141; ENSP00000433825; ENSG00000054118.
GeneID; 9967; -.
KEGG; hsa:9967; -.
UCSC; uc001cae.5; human.
CTD; 9967; -.
DisGeNET; 9967; -.
EuPathDB; HostDB:ENSG00000054118.13; -.
GeneCards; THRAP3; -.
HGNC; HGNC:22964; THRAP3.
HPA; CAB017472; -.
HPA; HPA012041; -.
HPA; HPA063765; -.
MIM; 603809; gene.
neXtProt; NX_Q9Y2W1; -.
OpenTargets; ENSG00000054118; -.
PharmGKB; PA134893249; -.
eggNOG; ENOG410IE11; Eukaryota.
eggNOG; ENOG410ZR5P; LUCA.
GeneTree; ENSGT00530000063211; -.
HOGENOM; HOG000231570; -.
HOVERGEN; HBG054554; -.
InParanoid; Q9Y2W1; -.
KO; K13112; -.
OMA; MKEKGSF; -.
OrthoDB; EOG091G03HU; -.
PhylomeDB; Q9Y2W1; -.
TreeFam; TF335939; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
SignaLink; Q9Y2W1; -.
SIGNOR; Q9Y2W1; -.
ChiTaRS; THRAP3; human.
GeneWiki; THRAP3; -.
GenomeRNAi; 9967; -.
PRO; PR:Q9Y2W1; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000054118; Expressed in 205 organ(s), highest expression level in lung.
CleanEx; HS_THRAP3; -.
ExpressionAtlas; Q9Y2W1; baseline and differential.
Genevisible; Q9Y2W1; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0030374; F:nuclear receptor transcription coactivator activity; NAS:UniProtKB.
GO; GO:0051219; F:phosphoprotein binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
GO; GO:0042809; F:vitamin D receptor binding; NAS:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0048255; P:mRNA stabilization; IMP:UniProtKB.
GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IDA:UniProtKB.
GO; GO:0042753; P:positive regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
InterPro; IPR026667; THRAP3.
InterPro; IPR029199; THRAP3_BCLAF1.
PANTHER; PTHR15268; PTHR15268; 1.
PANTHER; PTHR15268:SF16; PTHR15268:SF16; 1.
Pfam; PF15440; THRAP3_BCLAF1; 1.
1: Evidence at protein level;
Acetylation; Activator; ADP-ribosylation; ATP-binding;
Biological rhythms; Complete proteome; Direct protein sequencing;
Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 955 Thyroid hormone receptor-associated
protein 3.
/FTId=PRO_0000065583.
NP_BIND 552 559 ATP. {ECO:0000255}.
REGION 2 190 Required for mRNA splicing activation.
REGION 359 955 Required for mRNA decay activity.
COMPBIAS 7 339 Ser-rich.
COMPBIAS 12 161 Arg-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 17 17 Dimethylated arginine.
{ECO:0000269|Ref.5}.
MOD_RES 66 66 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 101 101 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 108 108 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 221 221 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.5}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 252 252 N6-methyllysine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|Ref.5}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 324 324 Phosphothreonine.
{ECO:0000250|UniProtKB:Q569Z6}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 328 328 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q569Z6}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 346 346 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q569Z6}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 379 379 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 397 397 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 444 444 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 455 455 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 470 470 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q569Z6}.
MOD_RES 481 481 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q569Z6}.
MOD_RES 519 519 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 527 527 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q569Z6}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 558 558 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q569Z6}.
MOD_RES 560 560 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 562 562 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 575 575 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 619 619 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 622 622 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 672 672 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 682 682 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|Ref.5}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 698 698 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 811 811 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 845 845 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q569Z6}.
MOD_RES 874 874 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 928 928 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 939 939 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 202 202 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 202 202 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 215 215 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 221 221 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 252 252 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 333 333 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 346 346 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 353 353 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 375 375 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 387 387 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 387 387 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 389 389 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 396 396 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 401 401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 421 421 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 427 427 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 451 451 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 451 451 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 455 455 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 461 461 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 467 467 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 470 470 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 481 481 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 486 486 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 527 527 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 551 551 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 558 558 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 602 602 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 697 697 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 705 705 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 709 709 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{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:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 756 756 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 759 759 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 876 876 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 879 879 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 201 201 A -> V (in dbSNP:rs6425977).
{ECO:0000269|PubMed:10198638,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_024552.
MUTAGEN 406 406 S->A: Reduces phosphorylation upon DNA
damage; when associated with A-408.
{ECO:0000269|PubMed:22424773}.
MUTAGEN 408 408 S->A: Reduces phosphorylation upon DNA
damage; when associated with A-406.
{ECO:0000269|PubMed:22424773}.
SEQUENCE 955 AA; 108666 MW; 01131D2479B8C0F4 CRC64;
MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSLSRS RKRRLSSRSR SRSYSPAHNR
ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN RGGYGNYRSN WQNYRQAYSP
RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS SDRSRRSSSS RSSSNHSRVE SSKRKSAKEK
KSSSKDSRPS QAAGDNQGDE AKEQTFSGGT SQDTKASESS KPWPDATYGT GSASRASAVS
ELSPRERSPA LKSPLQSVVV RRRSPRPSPV PKPSPPLSST SQMGSTLPSG AGYQSGTHQG
QFDHGSGSLS PSKKSPVGKS PPSTGSTYGS SQKEESAASG GAAYTKRYLE EQKTENGKDK
EQKQTNTDKE KIKEKGSFSD TGLGDGKMKS DSFAPKTDSE KPFRGSQSPK RYKLRDDFEK
KMADFHKEEM DDQDKDKAKG RKESEFDDEP KFMSKVIGAN KNQEEEKSGK WEGLVYAPPG
KEKQRKTEEL EEESFPERSK KEDRGKRSEG GHRGFVPEKN FRVTAYKAVQ EKSSSPPPRK
TSESRDKLGA KGDFPTGKSS FSITREAQVN VRMDSFDEDL ARPSGLLAQE RKLCRDLVHS
NKKEQEFRSI FQHIQSAQSQ RSPSELFAQH IVTIVHHVKE HHFGSSGMTL HERFTKYLKR
GTEQEAAKNK KSPEIHRRID ISPSTFRKHG LAHDEMKSPR EPGYKAEGKY KDDPVDLRLD
IERRKKHKER DLKRGKSRES VDSRDSSHSR ERSAEKTEKT HKGSKKQKKH RRARDRSRSS
SSSSQSSHSY KAEEYTEETE EREESTTGFD KSRLGTKDFV GPSERGGGRA RGTFQFRARG
RGWGRGNYSG NNNNNSNNDF QKRNREEEWD PEYTPKSKKY YLHDDREGEG SDKWVSRGRG
RGAFPRGRGR FMFRKSSTSP KWAHDKFSGE EGEIEDDESG TENREEKDNI QPTTE


Related products :

Catalog number Product name Quantity
EIAAB43730 Homo sapiens,Human,THRAP3,Thyroid hormone receptor-associated protein 3,Thyroid hormone receptor-associated protein complex 150 kDa component,Trap150,TRAP150
EIAAB43729 Mouse,Mus musculus,Thrap3,Thyroid hormone receptor-associated protein 3,Thyroid hormone receptor-associated protein complex 150 kDa component,Trap150,Trap150
EIAAB43728 Rat,Rattus norvegicus,Thrap3,Thyroid hormone receptor-associated protein 3,Thyroid hormone receptor-associated protein complex 150 kDa component,Trap150,Trap150
18-003-42176 Thyroid hormone receptor-associated protein complex 95 kDa component - Trap95; Thyroid hormone receptor-associated protein 5; Vitamin D3 receptor-interacting protein complex component DRIP92 Polyclona 0.1 mg Protein A
GWB-95AD1D Thyroid Hormone Receptor-associated Protein 150 KDa Subunit (TRAP150) (THRAP3) Rabbit anti-Human Polyclonal (aa930-955) Antibod
THRAP3 THRAP3 Gene thyroid hormone receptor associated protein 3
H6065 Thyroid hormone receptor-associated protein 3 (THRAP3), Rat, ELISA Kit 96T
CSB-EL023511RA Rat Thyroid hormone receptor-associated protein 3(THRAP3) ELISA kit 96T
ARP32301_T200 Anti-Thyroid hormone receptor-associated protein complex 95 kDa component(THRAP5) Species_Reactivity: Human
H6064 Thyroid hormone receptor-associated protein 3 (THRAP3), Mouse, ELISA Kit 96T
CSB-EL023511RA Rat Thyroid hormone receptor-associated protein 3(THRAP3) ELISA kit SpeciesRat 96T
H6063 Thyroid hormone receptor-associated protein 3 (THRAP3), Human, ELISA Kit 96T
CSB-EL023511MO Mouse Thyroid hormone receptor-associated protein 3(THRAP3) ELISA kit 96T
CSB-EL023511HU Human Thyroid hormone receptor-associated protein 3(THRAP3) ELISA kit 96T
CSB-EL023511MO Mouse Thyroid hormone receptor-associated protein 3(THRAP3) ELISA kit SpeciesMouse 96T
CSB-EL023511HU Human Thyroid hormone receptor-associated protein 3(THRAP3) ELISA kit SpeciesHuman 96T
TR150_RAT ELISA Kit FOR Thyroid hormone receptor-associated protein 3; organism: Rat; gene name: Thrap3 96T
TR150_MOUSE ELISA Kit FOR Thyroid hormone receptor-associated protein 3; organism: Mouse; gene name: Thrap3 96T
CSB-EL023511RA Rat thyroid hormone receptor associated protein 3 (THRAP3) ELISA kit, Species Rat, Sample Type serum, plasma 96T
28-321 THRB is a nuclear hormone receptor for triiodothyronine. It is one of the several receptors for thyroid hormone, and has been shown to mediate the biological activities of thyroid hormone. Knockout st 0.05 mg
28-322 THRB is a nuclear hormone receptor for triiodothyronine. It is one of the several receptors for thyroid hormone, and has been shown to mediate the biological activities of thyroid hormone. Knockout st 0.05 mg
18-003-43213 Thyroid receptor-interacting protein 13 - Thyroid hormone receptor interactor 13; Trip-13; Human papillomavirus type 16 E1 protein-binding protein; HPV16 E1 protein-binding protein; 16E1-BP Polyclonal 0.1 mg Protein A
18-003-42687 Thyroid receptor-interacting protein 13 - Thyroid hormone receptor interactor 13; Trip-13; Human papillomavirus type 16 E1 protein-binding protein; HPV16 E1 protein-binding protein; 16E1-BP Polyclonal 0.1 mg Protein A
20-372-60288 thyroid hormone receptor interactor 13 (TRIP13) - Mouse monoclonal anti-human TRIP13 antibody; TRIP-13; Thyroid hormone receptor interactor 13; Human papillomavirus type 16 E1 protein-binding protein; 0.1 mg
10-288-22014F Thyroid receptor-interacting protein 13 - Thyroid hormone receptor interactor 13; Trip-13; Human papillomavirus type 16 E1 protein-binding protein; HPV16 E1 protein-binding protein; 16E1-BP 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur