ID TRRAP_HUMAN Reviewed; 3859 AA.
AC Q9Y4A5; A4D265; O75218; Q9Y631; Q9Y6H4;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 27-MAR-2024, entry version 218.
DE RecName: Full=Transformation/transcription domain-associated protein;
DE AltName: Full=350/400 kDa PCAF-associated factor;
DE Short=PAF350/400;
DE AltName: Full=STAF40;
DE AltName: Full=Tra1 homolog;
GN Name=TRRAP; Synonyms=PAF400;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MYC AND E2F1.
RC TISSUE=Cervix carcinoma;
RX PubMed=9708738; DOI=10.1016/s0092-8674(00)81479-8;
RA McMahon S.B., Van Buskirk H.A., Dugan K.A., Copeland T.D., Cole M.D.;
RT "The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc
RT and E2F oncoproteins.";
RL Cell 94:363-374(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 41-90; 337-344;
RP 369-387; 879-892; 997-1005; 1171-1184; 1237-1247; 1545-1560; 1815-1820;
RP 1922-1934; 2211-2218; 2260-2275; 2534-2547; 2583-2594; 2706-2726;
RP 2830-2844; 3567-3573; 3583-3598; 3604-3614; 3712-3730 AND 3822-3834, AND
RP IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L; TAF5L; TAF6L;
RP TAF10; SUPT3H; TAF12 AND TAF9.
RC TISSUE=Fetal heart;
RX PubMed=9885574; DOI=10.1016/s1097-2765(00)80301-9;
RA Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L., Qin J.,
RA Nakatani Y.;
RT "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the
RT ATM superfamily.";
RL Mol. Cell 2:869-875(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H;
RP GCN5L2; KIAA0764; TAF5L; TAF6L; TADA3L; TAF10; TAF12 AND TAF9, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11564863; DOI=10.1128/mcb.21.20.6782-6795.2001;
RA Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
RA Kundu T.K., Chait B.T., Roeder R.G.;
RT "Human STAGA complex is a chromatin-acetylating transcription coactivator
RT that interacts with pre-mRNA splicing and DNA damage-binding factors in
RT vivo.";
RL Mol. Cell. Biol. 21:6782-6795(2001).
RN [7]
RP IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H;
RP TAF2; TAF4; TAF5; GCN5L2 AND TAF10.
RX PubMed=10373431; DOI=10.1074/jbc.274.26.18285;
RA Brand M., Yamamoto K., Staub A., Tora L.;
RT "Identification of TATA-binding protein-free TAFII-containing complex
RT subunits suggests a role in nucleosome acetylation and signal
RT transduction.";
RL J. Biol. Chem. 274:18285-18289(1999).
RN [8]
RP IDENTIFICATION IN THE TIP60 HAT COMPLEX WITH KAT5; RUVBL1 AND RUVBL2.
RX PubMed=10966108; DOI=10.1016/s0092-8674(00)00051-9;
RA Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M.,
RA Scully R., Qin J., Nakatani Y.;
RT "Involvement of the TIP60 histone acetylase complex in DNA repair and
RT apoptosis.";
RL Cell 102:463-473(2000).
RN [9]
RP INTERACTION WITH GCN5L2.
RX PubMed=10611234; DOI=10.1128/mcb.20.2.556-562.2000;
RA McMahon S.B., Wood M.A., Cole M.D.;
RT "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5
RT to c-Myc.";
RL Mol. Cell. Biol. 20:556-562(2000).
RN [10]
RP INTERACTION WITH E2F1 AND E2F4, AND FUNCTION.
RX PubMed=11418595; DOI=10.1074/jbc.m102067200;
RA Lang S.E., McMahon S.B., Cole M.D., Hearing P.;
RT "E2F transcriptional activation requires TRRAP and GCN5 cofactors.";
RL J. Biol. Chem. 276:32627-32634(2001).
RN [11]
RP DOMAIN.
RX PubMed=11445536; DOI=10.1101/gad.900101;
RA Park J., Kunjibettu S., McMahon S.B., Cole M.D.;
RT "The ATM-related domain of TRRAP is required for histone acetyltransferase
RT recruitment and Myc-dependent oncogenesis.";
RL Genes Dev. 15:1619-1624(2001).
RN [12]
RP FUNCTION, AND INTERACTION WITH TP53.
RX PubMed=12138177; DOI=10.1128/mcb.22.16.5650-5661.2002;
RA Ard P.G., Chatterjee C., Kunjibettu S., Adside L.R., Gralinski L.E.,
RA McMahon S.B.;
RT "Transcriptional regulation of the mdm2 oncogene by p53 requires TRRAP
RT acetyltransferase complexes.";
RL Mol. Cell. Biol. 22:5650-5661(2002).
RN [13]
RP IDENTIFICATION IN THE BAF53 COMPLEX WITH BAF53A; RUVBL1 AND SMARCA4.
RX PubMed=11839798; DOI=10.1128/mcb.22.5.1307-1316.2002;
RA Park J., Wood M.A., Cole M.D.;
RT "BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-
RT interacting nuclear cofactor for oncogenic transformation.";
RL Mol. Cell. Biol. 22:1307-1316(2002).
RN [14]
RP FUNCTION.
RX PubMed=12743606; DOI=10.1038/sj.onc.1206376;
RA Lang S.E., Hearing P.;
RT "The adenovirus E1A oncoprotein recruits the cellular TRRAP/GCN5 histone
RT acetyltransferase complex.";
RL Oncogene 22:2836-2841(2003).
RN [15]
RP FUNCTION.
RX PubMed=12660246; DOI=10.1074/jbc.m211795200;
RA Liu X., Tesfai J., Evrard Y.A., Dent S.Y.R., Martinez E.;
RT "c-Myc transformation domain recruits the human STAGA complex and requires
RT TRRAP and GCN5 acetylase activity for transcription activation.";
RL J. Biol. Chem. 278:20405-20412(2003).
RN [16]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP NUA4 COMPLEX.
RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004;
RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
RT "Structural and functional conservation of the NuA4 histone
RT acetyltransferase complex from yeast to humans.";
RL Mol. Cell. Biol. 24:1884-1896(2004).
RN [17]
RP IDENTIFICATION IN STAGA COMPLEX.
RX PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
RA Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S.,
RA Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G.,
RA Schuele R., Takeyama K., Kato S., Tora L., Devys D.;
RT "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
RT coactivates nuclear receptors, and counteracts heterochromatin silencing.";
RL Mol. Cell 29:92-101(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2051, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH NPAT.
RX PubMed=17967892; DOI=10.1128/mcb.00607-07;
RA DeRan M., Pulvino M., Greene E., Su C., Zhao J.;
RT "Transcriptional activation of histone genes requires NPAT-dependent
RT recruitment of TRRAP-Tip60 complex to histone promoters during the G1/S
RT phase transition.";
RL Mol. Cell. Biol. 28:435-447(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2051 AND SER-2077, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3078, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [22]
RP INTERACTION WITH TELO2 AND TTI1.
RX PubMed=20427287; DOI=10.1074/jbc.m110.121699;
RA Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K.,
RA Iemura S., Natsume T., Mizushima N.;
RT "Tti1 and Tel2 are critical factors in mammalian target of rapamycin
RT complex assembly.";
RL J. Biol. Chem. 285:20109-20116(2010).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP PROBABLE INVOLVEMENT IN MELANOMA, VARIANT PHE-722, AND CHARACTERIZATION OF
RP VARIANT PHE-722.
RX PubMed=21499247; DOI=10.1038/ng.810;
RA Wei X., Walia V., Lin J.C., Teer J.K., Prickett T.D., Gartner J., Davis S.,
RA Stemke-Hale K., Davies M.A., Gershenwald J.E., Robinson W., Robinson S.,
RA Rosenberg S.A., Samuels Y.;
RT "Exome sequencing identifies GRIN2A as frequently mutated in melanoma.";
RL Nat. Genet. 43:442-446(2011).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1628; SER-2051 AND SER-2077,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
RP FUNCTION, AND IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
RX PubMed=24463511; DOI=10.1038/nature12922;
RA Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M.,
RA Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C.,
RA Hamiche A.;
RT "ANP32E is a histone chaperone that removes H2A.Z from chromatin.";
RL Nature 505:648-653(2014).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2543, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [31]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-893; GLY-1070; HIS-1669; HIS-1724;
RP VAL-1925; LEU-1932; LEU-1947; GLY-2139; TRP-2302; GLY-2433; LEU-2690;
RP ASP-2750; GLU-2801 AND MET-2931.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [32]
RP INVOLVEMENT IN DEDDFA, AND VARIANT DEDDFA GLN-2004.
RX PubMed=30424743; DOI=10.1186/s12881-018-0711-9;
RA Mavros C.F., Brownstein C.A., Thyagrajan R., Genetti C.A., Tembulkar S.,
RA Graber K., Murphy Q., Cabral K., VanNoy G.E., Bainbridge M., Shi J.,
RA Agrawal P.B., Beggs A.H., D'Angelo E., Gonzalez-Heydrich J.;
RT "De novo variant of TRRAP in a patient with very early onset psychosis in
RT the context of non-verbal learning disability and obsessive-compulsive
RT disorder: a case report.";
RL BMC Med. Genet. 19:197-197(2018).
RN [33]
RP VARIANTS DEDDFA PHE-805; LEU-860; LEU-893; MET-1031; GLN-1035; ARG-1037;
RP THR-1043; GLY-1104; LYS-1106; TRP-1111; ARG-1159; CYS-1859; CYS-1866;
RP ARG-1866; ARG-1883; LEU-1932 AND GLN-3757.
RX PubMed=30827496; DOI=10.1016/j.ajhg.2019.01.010;
RG CAUSES Study;
RG Deciphering Developmental Disorders study;
RA Cogne B., Ehresmann S., Beauregard-Lacroix E., Rousseau J., Besnard T.,
RA Garcia T., Petrovski S., Avni S., McWalter K., Blackburn P.R.,
RA Sanders S.J., Uguen K., Harris J., Cohen J.S., Blyth M., Lehman A.,
RA Berg J., Li M.H., Kini U., Joss S., von der Lippe C., Gordon C.T.,
RA Humberson J.B., Robak L., Scott D.A., Sutton V.R., Skraban C.M.,
RA Johnston J.J., Poduri A., Nordenskjoeld M., Shashi V., Gerkes E.H.,
RA Bongers E.M.H.F., Gilissen C., Zarate Y.A., Kvarnung M., Lally K.P.,
RA Kulch P.A., Daniels B., Hernandez-Garcia A., Stong N., McGaughran J.,
RA Retterer K., Tveten K., Sullivan J., Geisheker M.R., Stray-Pedersen A.,
RA Tarpinian J.M., Klee E.W., Sapp J.C., Zyskind J., Holla O.L., Bedoukian E.,
RA Filippini F., Guimier A., Picard A., Busk O.L., Punetha J., Pfundt R.,
RA Lindstrand A., Nordgren A., Kalb F., Desai M., Ebanks A.H., Jhangiani S.N.,
RA Dewan T., Coban Akdemir Z.H., Telegrafi A., Zackai E.H., Begtrup A.,
RA Song X., Toutain A., Wentzensen I.M., Odent S., Bonneau D., Latypova X.,
RA Deb W., Redon S., Bilan F., Legendre M., Troyer C., Whitlock K.,
RA Caluseriu O., Murphree M.I., Pichurin P.N., Agre K., Gavrilova R.,
RA Rinne T., Park M., Shain C., Heinzen E.L., Xiao R., Amiel J., Lyonnet S.,
RA Isidor B., Biesecker L.G., Lowenstein D., Posey J.E., Denomme-Pichon A.S.,
RA Ferec C., Yang X.J., Rosenfeld J.A., Gilbert-Dussardier B.,
RA Audebert-Bellanger S., Redon R., Stessman H.A.F., Nellaker C., Yang Y.,
RA Lupski J.R., Goldstein D.B., Eichler E.E., Bolduc F., Bezieau S., Kuery S.,
RA Campeau P.M.;
RT "Missense Variants in the Histone Acetyltransferase Complex Component Gene
RT TRRAP Cause Autism and Syndromic Intellectual Disability.";
RL Am. J. Hum. Genet. 104:530-541(2019).
RN [34]
RP VARIANTS DFNA75 CYS-171 AND ASN-394, VARIANT ASP-2750, AND INVOLVEMENT IN
RP DFNA75.
RX PubMed=31231791; DOI=10.1111/cge.13590;
RA Xia W., Hu J., Ma J., Huang J., Wang X., Jiang N., Zhang J., Ma Z., Ma D.;
RT "Novel TRRAP mutation causes autosomal dominant non-syndromic hearing
RT loss.";
RL Clin. Genet. 96:300-308(2019).
CC -!- FUNCTION: Adapter protein, which is found in various multiprotein
CC chromatin complexes with histone acetyltransferase activity (HAT),
CC which gives a specific tag for epigenetic transcription activation.
CC Component of the NuA4 histone acetyltransferase complex which is
CC responsible for acetylation of nucleosomal histones H4 and H2A. Plays a
CC central role in MYC transcription activation, and also participates in
CC cell transformation by MYC. Required for p53/TP53-, E2F1- and E2F4-
CC mediated transcription activation. Also involved in transcription
CC activation mediated by the adenovirus E1A, a viral oncoprotein that
CC deregulates transcription of key genes. Probably acts by linking
CC transcription factors such as E1A, MYC or E2F1 to HAT complexes such as
CC STAGA thereby allowing transcription activation. Probably not required
CC in the steps following histone acetylation in processes of
CC transcription activation. May be required for the mitotic checkpoint
CC and normal cell cycle progression. Component of a SWR1-like complex
CC that specifically mediates the removal of histone H2A.Z/H2AZ1 from the
CC nucleosome. May play a role in the formation and maintenance of the
CC auditory system (By similarity). {ECO:0000250|UniProtKB:A0A0R4ITC5,
CC ECO:0000269|PubMed:11418595, ECO:0000269|PubMed:12138177,
CC ECO:0000269|PubMed:12660246, ECO:0000269|PubMed:12743606,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:17967892,
CC ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:9708738}.
CC -!- SUBUNIT: Interacts with MYC, E2F1 and E2F4 transcription factors.
CC Interacts directly with p53/TP53. Interacts with GCN5L2. Component of
CC various HAT complexes. Component of the PCAF complex, at least composed
CC of TADA2L/ADA2, SUPT3H, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-
CC alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. Component
CC of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L,
CC SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, GCN5L2/GCN5,
CC TAF10 and TRRAP. Component of the NuA4 histone acetyltransferase
CC complex which contains the catalytic subunit KAT5/TIP60 and the
CC subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15,
CC MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. Component of
CC the STAGA complex, at least composed of SUPT3H, GCN5L2, SUPT7L, TAF5L,
CC TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core
CC complex is associated with a subcomplex required for histone
CC deubiquitination composed of ATXN7L3, ENY2 and USP22. Component of the
CC BAF53 complex, at least composed of BAF53A, RUVBL1, SMARCA4/BRG1, and
CC TRRAP, which preferentially acetylates histone H4 (and H2A) within
CC nucleosomes. Interacts with NPAT. Interaction with TELO2 and TTI1.
CC Component of a SWR1-like complex. {ECO:0000269|PubMed:10373431,
CC ECO:0000269|PubMed:10611234, ECO:0000269|PubMed:10966108,
CC ECO:0000269|PubMed:11418595, ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:11839798, ECO:0000269|PubMed:12138177,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:17967892,
CC ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:20427287,
CC ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:9708738,
CC ECO:0000269|PubMed:9885574}.
CC -!- INTERACTION:
CC Q9Y4A5; O15265: ATXN7; NbExp=7; IntAct=EBI-399128, EBI-708350;
CC Q9Y4A5; P01106: MYC; NbExp=6; IntAct=EBI-399128, EBI-447544;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:9708738}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y4A5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4A5-2; Sequence=VSP_009102, VSP_009103;
CC -!- DOMAIN: The PI3K/PI4K domain is required for the recruitment of HAT
CC complexes, and the MYC-dependent transactivation. Although it is
CC strongly related to the PI3/PI4-kinase family, it lacks the typical
CC motifs that constitute the catalytic site of PI3/PI4-kinase proteins,
CC and lacks such activity. {ECO:0000269|PubMed:11445536}.
CC -!- DISEASE: Note=TRRAP mutation Phe-722 has been frequently found in
CC cutaneous malignant melanoma, suggesting that TRRAP may play a role in
CC the pathogenesis of melanoma. {ECO:0000269|PubMed:21499247}.
CC -!- DISEASE: Developmental delay with or without dysmorphic facies and
CC autism (DEDDFA) [MIM:618454]: An autosomal dominant neurodevelopmental
CC disorder apparent from infancy or early childhood. Some patients
CC present with intellectual disability and renal, cardiac, genitourinary
CC systems, as well as structural brain abnormalities. In some cases, the
CC phenotype is less severe, has no systemic involvement and is
CC characterized by autism spectrum disorder and/or intellectual
CC disability, sometimes associated with epilepsy. Affected individuals
CC manifest variable dysmorphic features. {ECO:0000269|PubMed:30424743,
CC ECO:0000269|PubMed:30827496}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Deafness, autosomal dominant, 75 (DFNA75) [MIM:618778]: A form
CC of non-syndromic deafness characterized by late-onset hearing loss that
CC involves mid and high frequencies, and progresses to encompass all
CC frequencies. {ECO:0000269|PubMed:31231791}. Note=The disease may be
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. TRA1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62433.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF076974; AAD09420.1; -; mRNA.
DR EMBL; AF110377; AAD04629.1; -; mRNA.
DR EMBL; AC004893; AAC62433.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004991; AAC27675.2; -; Genomic_DNA.
DR EMBL; CH471091; EAW76694.1; -; Genomic_DNA.
DR EMBL; CH236956; EAL23887.1; -; Genomic_DNA.
DR CCDS; CCDS5659.1; -. [Q9Y4A5-2]
DR CCDS; CCDS59066.1; -. [Q9Y4A5-1]
DR PIR; T02632; T02632.
DR RefSeq; NP_001231509.1; NM_001244580.1. [Q9Y4A5-1]
DR RefSeq; NP_003487.1; NM_003496.3. [Q9Y4A5-2]
DR PDB; 7KTR; EM; 2.93 A; A=369-3859.
DR PDB; 8H7G; EM; 3.70 A; C=1-3859.
DR PDBsum; 7KTR; -.
DR PDBsum; 8H7G; -.
DR EMDB; EMD-23027; -.
DR EMDB; EMD-34520; -.
DR SMR; Q9Y4A5; -.
DR BioGRID; 113900; 244.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-903; TFTC histone acetylation complex.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR ComplexPortal; CPX-989; PCAF histone acetylase complex.
DR CORUM; Q9Y4A5; -.
DR DIP; DIP-28149N; -.
DR IntAct; Q9Y4A5; 84.
DR MINT; Q9Y4A5; -.
DR STRING; 9606.ENSP00000352925; -.
DR GlyGen; Q9Y4A5; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; Q9Y4A5; -.
DR MetOSite; Q9Y4A5; -.
DR PhosphoSitePlus; Q9Y4A5; -.
DR SwissPalm; Q9Y4A5; -.
DR BioMuta; TRRAP; -.
DR DMDM; 116242829; -.
DR EPD; Q9Y4A5; -.
DR jPOST; Q9Y4A5; -.
DR MassIVE; Q9Y4A5; -.
DR MaxQB; Q9Y4A5; -.
DR PaxDb; 9606-ENSP00000352925; -.
DR PeptideAtlas; Q9Y4A5; -.
DR ProteomicsDB; 86142; -. [Q9Y4A5-1]
DR ProteomicsDB; 86143; -. [Q9Y4A5-2]
DR Pumba; Q9Y4A5; -.
DR Antibodypedia; 16027; 203 antibodies from 23 providers.
DR DNASU; 8295; -.
DR Ensembl; ENST00000355540.7; ENSP00000347733.3; ENSG00000196367.15. [Q9Y4A5-2]
DR Ensembl; ENST00000359863.8; ENSP00000352925.4; ENSG00000196367.15. [Q9Y4A5-1]
DR GeneID; 8295; -.
DR KEGG; hsa:8295; -.
DR UCSC; uc003upp.3; human. [Q9Y4A5-1]
DR AGR; HGNC:12347; -.
DR CTD; 8295; -.
DR DisGeNET; 8295; -.
DR GeneCards; TRRAP; -.
DR HGNC; HGNC:12347; TRRAP.
DR HPA; ENSG00000196367; Low tissue specificity.
DR MalaCards; TRRAP; -.
DR MIM; 603015; gene.
DR MIM; 618454; phenotype.
DR MIM; 618778; phenotype.
DR neXtProt; NX_Q9Y4A5; -.
DR OpenTargets; ENSG00000196367; -.
DR Orphanet; 90635; Rare autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR PharmGKB; PA37020; -.
DR VEuPathDB; HostDB:ENSG00000196367; -.
DR eggNOG; KOG0889; Eukaryota.
DR GeneTree; ENSGT00390000017961; -.
DR InParanoid; Q9Y4A5; -.
DR OrthoDB; 3666795at2759; -.
DR PhylomeDB; Q9Y4A5; -.
DR TreeFam; TF106414; -.
DR PathwayCommons; Q9Y4A5; -.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q9Y4A5; -.
DR SIGNOR; Q9Y4A5; -.
DR BioGRID-ORCS; 8295; 773 hits in 1197 CRISPR screens.
DR ChiTaRS; TRRAP; human.
DR GenomeRNAi; 8295; -.
DR Pharos; Q9Y4A5; Tbio.
DR PRO; PR:Q9Y4A5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y4A5; Protein.
DR Bgee; ENSG00000196367; Expressed in ventricular zone and 156 other cell types or tissues.
DR ExpressionAtlas; Q9Y4A5; baseline and differential.
DR Genevisible; Q9Y4A5; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0000812; C:Swr1 complex; IDA:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; NAS:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; NAS:ComplexPortal.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:2000779; P:regulation of double-strand break repair; NAS:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; NAS:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR CDD; cd05163; PIKK_TRRAP; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR046807; Tra1_central.
DR InterPro; IPR046805; Tra1_ring.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF1; TRANSFORMATION_TRANSCRIPTION DOMAIN-ASSOCIATED PROTEIN; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF20175; Tra1_central; 1.
DR Pfam; PF20206; Tra1_ring; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Autism spectrum disorder; Chromatin regulator; Deafness;
KW Direct protein sequencing; Disease variant; Intellectual disability;
KW Isopeptide bond; Non-syndromic deafness; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..3859
FT /note="Transformation/transcription domain-associated
FT protein"
FT /id="PRO_0000088851"
FT DOMAIN 2692..3275
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 3500..3823
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 3827..3859
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 491..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2010..2388
FT /note="Interaction with TP53"
FT /evidence="ECO:0000269|PubMed:12138177"
FT REGION 2023..2044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2543..2578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3506..3512
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3687..3695
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3707..3732
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MOTIF 2047..2062
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 491..525
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2028..2044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 1628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2051
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163"
FT MOD_RES 2077
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 3078
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 2543
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1492..1509
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9708738"
FT /id="VSP_009102"
FT VAR_SEQ 3001..3012
FT /note="GKPTWSGMHSSS -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9708738"
FT /id="VSP_009103"
FT VARIANT 171
FT /note="R -> C (in DFNA75; uncertain significance;
FT dbSNP:rs200157211)"
FT /evidence="ECO:0000269|PubMed:31231791"
FT /id="VAR_083794"
FT VARIANT 394
FT /note="D -> N (in DFNA75; uncertain significance;
FT dbSNP:rs1554407965)"
FT /evidence="ECO:0000269|PubMed:31231791"
FT /id="VAR_083795"
FT VARIANT 722
FT /note="S -> F (found in a cutaneous malignant melanoma
FT sample; somatic mutation; induces cell transformation and
FT confers resistance to apoptosis; dbSNP:rs147405090)"
FT /evidence="ECO:0000269|PubMed:21499247"
FT /id="VAR_067754"
FT VARIANT 805
FT /note="L -> F (in DEDDFA; uncertain significance;
FT dbSNP:rs1562940289)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082969"
FT VARIANT 860
FT /note="F -> L (in DEDDFA; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082970"
FT VARIANT 878
FT /note="R -> L (in dbSNP:rs17161510)"
FT /id="VAR_028359"
FT VARIANT 893
FT /note="R -> C (in an ovarian serous carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041658"
FT VARIANT 893
FT /note="R -> L (in DEDDFA; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082971"
FT VARIANT 1031
FT /note="I -> M (in DEDDFA)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082972"
FT VARIANT 1035
FT /note="R -> Q (in DEDDFA; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082973"
FT VARIANT 1037
FT /note="S -> R (in DEDDFA; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082974"
FT VARIANT 1043
FT /note="A -> T (in DEDDFA; dbSNP:rs1562945106)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082975"
FT VARIANT 1070
FT /note="S -> G (in dbSNP:rs55920979)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041659"
FT VARIANT 1104
FT /note="E -> G (in DEDDFA; dbSNP:rs1790257064)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082976"
FT VARIANT 1106
FT /note="E -> K (in DEDDFA; dbSNP:rs1584324956)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082977"
FT VARIANT 1111
FT /note="G -> W (in DEDDFA; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082978"
FT VARIANT 1159
FT /note="G -> R (in DEDDFA; dbSNP:rs1790288810)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082979"
FT VARIANT 1669
FT /note="R -> H (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs373632999)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041660"
FT VARIANT 1724
FT /note="R -> H (in a gastric adenocarcinoma sample; somatic
FT mutation; dbSNP:rs782203759)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041661"
FT VARIANT 1859
FT /note="R -> C (in DEDDFA; dbSNP:rs1791432323)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082980"
FT VARIANT 1866
FT /note="W -> C (in DEDDFA; uncertain significance;
FT dbSNP:rs1562957576)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082981"
FT VARIANT 1866
FT /note="W -> R (in DEDDFA; dbSNP:rs1562957569)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082982"
FT VARIANT 1883
FT /note="G -> R (in DEDDFA)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082983"
FT VARIANT 1925
FT /note="A -> V (in dbSNP:rs56197298)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041662"
FT VARIANT 1932
FT /note="P -> L (in DEDDFA; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:30827496"
FT /id="VAR_041663"
FT VARIANT 1947
FT /note="R -> L (in an ovarian mucinous carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041664"
FT VARIANT 2004
FT /note="R -> Q (in DEDDFA; uncertain significance;
FT dbSNP:rs1562959030)"
FT /evidence="ECO:0000269|PubMed:30424743"
FT /id="VAR_082984"
FT VARIANT 2139
FT /note="W -> G (in dbSNP:rs34185633)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041665"
FT VARIANT 2302
FT /note="R -> W (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs528967912)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041666"
FT VARIANT 2433
FT /note="S -> G (in dbSNP:rs35634065)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041667"
FT VARIANT 2690
FT /note="P -> L (in a lung large cell carcinoma sample;
FT somatic mutation; dbSNP:rs753661271)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041668"
FT VARIANT 2750
FT /note="E -> D (in dbSNP:rs55755466)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:31231791"
FT /id="VAR_041669"
FT VARIANT 2801
FT /note="K -> E (in dbSNP:rs56341061)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041670"
FT VARIANT 2931
FT /note="T -> M (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs1294404368)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041671"
FT VARIANT 3757
FT /note="R -> Q (in DEDDFA; uncertain significance;
FT dbSNP:rs987263983)"
FT /evidence="ECO:0000269|PubMed:30827496"
FT /id="VAR_082985"
FT CONFLICT 660
FT /note="E -> D (in Ref. 2; AAD04629)"
FT /evidence="ECO:0000305"
FT HELIX 371..385
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 392..406
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 413..434
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 442..469
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 535..564
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 583..599
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 600..604
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 627..639
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 644..654
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 657..664
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 669..677
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 679..681
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 682..695
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 698..702
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 704..723
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 725..732
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 733..735
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 736..747
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 754..768
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 774..779
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 780..782
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 783..795
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 800..811
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 817..820
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 821..827
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 828..835
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 839..855
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 858..865
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 866..868
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 869..879
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 885..898
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 899..903
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 923..927
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 929..931
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 934..938
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 940..951
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 957..973
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 981..988
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 992..995
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1005..1007
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1013..1029
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 1032..1034
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1035..1057
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 1058..1061
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1064..1066
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1074..1076
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 1080..1082
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1091..1101
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1107..1126
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1129..1132
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1136..1146
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1147..1150
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 1151..1153
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1154..1170
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1173..1193
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 1194..1196
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1202..1218
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 1223..1225
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1228..1248
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1254..1271
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1275..1279
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1280..1285
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 1287..1289
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1297..1299
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1302..1315
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 1317..1320
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 1327..1329
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1330..1344
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1347..1351
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1363..1375
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1380..1382
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1383..1394
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1399..1413
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1420..1431
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 1432..1434
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 1435..1437
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1442..1454
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1461..1484
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1511..1523
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1532..1546
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1555..1562
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1566..1573
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1576..1579
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1582..1592
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 1594..1596
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1598..1605
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1609..1612
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 1613..1615
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1638..1653
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1657..1659
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1661..1672
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1674..1681
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1692..1706
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1921..1925
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 1928..1931
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1939..1943
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1950..1964
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1976..1985
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 1990..2000
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2003..2016
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2021..2026
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2031..2042
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2045..2060
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2064..2073
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2077..2088
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2096..2099
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2105..2111
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2212..2219
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2226..2232
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2233..2235
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2240..2251
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2257..2273
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2278..2286
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2292..2294
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 2295..2299
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2301..2312
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2320..2331
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2340..2357
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2361..2375
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2382..2384
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2389..2406
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2411..2426
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 2429..2434
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2435..2439
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2440..2448
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2452..2464
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2470..2478
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2483..2486
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2492..2500
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 2506..2508
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 2514..2516
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2523..2527
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2530..2538
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2586..2602
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2607..2618
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2622..2639
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2642..2656
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2659..2666
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2671..2679
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2690..2699
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2703..2714
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2728..2730
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2742..2755
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2758..2768
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2772..2781
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 2782..2784
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2786..2806
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2811..2813
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2814..2830
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2834..2841
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 2844..2847
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2849..2856
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2857..2859
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2862..2872
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 2873..2875
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2878..2880
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2881..2894
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2904..2919
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2928..2930
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2931..2952
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2955..2957
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2961..2976
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 2985..3000
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3012..3020
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3028..3051
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3054..3062
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3063..3066
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3072..3089
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 3090..3092
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3095..3106
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3115..3131
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3135..3148
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3153..3170
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3173..3186
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 3192..3195
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3196..3205
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3206..3208
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3214..3222
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3228..3234
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3235..3242
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3247..3260
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3262..3283
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3295..3310
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3312..3324
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3325..3328
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3332..3354
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 3355..3358
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3365..3376
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3396..3407
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3411..3423
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 3429..3432
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3434..3452
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3457..3460
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3461..3463
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3466..3470
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 3473..3475
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 3481..3484
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3489..3491
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3495..3499
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3501..3507
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3509..3520
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3525..3531
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3536..3552
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3553..3557
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3562..3565
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3574..3578
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3581..3585
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3588..3592
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3593..3604
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3610..3625
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3631..3644
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3650..3658
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3662..3685
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3693..3695
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3696..3699
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 3700..3702
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3705..3708
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 3716..3718
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3719..3721
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 3726..3729
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3733..3739
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3741..3745
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3747..3759
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 3762..3764
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3766..3789
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3798..3800
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3804..3826
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3829..3831
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3834..3842
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3845..3848
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 3853..3855
FT /evidence="ECO:0007829|PDB:7KTR"
SQ SEQUENCE 3859 AA; 437600 MW; 391E467C0047B00B CRC64;
MAFVATQGAT VVDQTTLMKK YLQFVAALTD VNTPDETKLK MMQEVSENFE NVTSSPQYST
FLEHIIPRFL TFLQDGEVQF LQEKPAQQLR KLVLEIIHRI PTNEHLRPHT KNVLSVMFRF
LETENEENVL ICLRIIIELH KQFRPPITQE IHHFLDFVKQ IYKELPKVVN RYFENPQVIP
ENTVPPPEMV GMITTIAVKV NPEREDSETR THSIIPRGSL SLKVLAELPI IVVLMYQLYK
LNIHNVVAEF VPLIMNTIAI QVSAQARQHK LYNKELYADF IAAQIKTLSF LAYIIRIYQE
LVTKYSQQMV KGMLQLLSNC PAETAHLRKE LLIAAKHILT TELRNQFIPC MDKLFDESIL
IGSGYTARET LRPLAYSTLA DLVHHVRQHL PLSDLSLAVQ LFAKNIDDES LPSSIQTMSC
KLLLNLVDCI RSKSEQESGN GRDVLMRMLE VFVLKFHTIA RYQLSAIFKK CKPQSELGAV
EAALPGVPTA PAAPGPAPSP APVPAPPPPP PPPPPATPVT PAPVPPFEKQ GEKDKEDKQT
FQVTDCRSLV KTLVCGVKTI TWGITSCKAP GEAQFIPNKQ LQPKETQIYI KLVKYAMQAL
DIYQVQIAGN GQTYIRVANC QTVRMKEEKE VLEHFAGVFT MMNPLTFKEI FQTTVPYMVE
RISKNYALQI VANSFLANPT TSALFATILV EYLLDRLPEM GSNVELSNLY LKLFKLVFGS
VSLFAAENEQ MLKPHLHKIV NSSMELAQTA KEPYNYFLLL RALFRSIGGG SHDLLYQEFL
PLLPNLLQGL NMLQSGLHKQ HMKDLFVELC LTVPVRLSSL LPYLPMLMDP LVSALNGSQT
LVSQGLRTLE LCVDNLQPDF LYDHIQPVRA ELMQALWRTL RNPADSISHV AYRVLGKFGG
SNRKMLKESQ KLHYVVTEVQ GPSITVEFSD CKASLQLPME KAIETALDCL KSANTEPYYR
RQAWEVIKCF LVAMMSLEDN KHALYQLLAH PNFTEKTIPN VIISHRYKAQ DTPARKTFEQ
ALTGAFMSAV IKDLRPSALP FVASLIRHYT MVAVAQQCGP FLLPCYQVGS QPSTAMFHSE
ENGSKGMDPL VLIDAIAICM AYEEKELCKI GEVALAVIFD VASIILGSKE RACQLPLFSY
IVERLCACCY EQAWYAKLGG VVSIKFLMER LPLTWVLQNQ QTFLKALLFV MMDLTGEVSN
GAVAMAKTTL EQLLMRCATP LKDEERAEEI VAAQEKSFHH VTHDLVREVT SPNSTVRKQA
MHSLQVLAQV TGKSVTVIME PHKEVLQDMV PPKKHLLRHQ PANAQIGLME GNTFCTTLQP
RLFTMDLNVV EHKVFYTELL NLCEAEDSAL TKLPCYKSLP SLVPLRIAAL NALAACNYLP
QSREKIIAAL FKALNSTNSE LQEAGEACMR KFLEGATIEV DQIHTHMRPL LMMLGDYRSL
TLNVVNRLTS VTRLFPNSFN DKFCDQMMQH LRKWMEVVVI THKGGQRSDG NESISECGRC
PLSPFCQFEE MKICSAIINL FHLIPAAPQT LVKPLLEVVM KTERAMLIEA GSPFREPLIK
FLTRHPSQTV ELFMMEATLN DPQWSRMFMS FLKHKDARPL RDVLAANPNR FITLLLPGGA
QTAVRPGSPS TSTMRLDLQF QAIKIISIIV KNDDSWLASQ HSLVSQLRRV WVSENFQERH
RKENMAATNW KEPKLLAYCL LNYCKRNYGD IELLFQLLRA FTGRFLCNMT FLKEYMEEEI
PKNYSIAQKR ALFFRFVDFN DPNFGDELKA KVLQHILNPA FLYSFEKGEG EQLLGPPNPE
GDNPESITSV FITKVLDPEK QADMLDSLRI YLLQYATLLV EHAPHHIHDN NKNRNSKLRR
LMTFAWPCLL SKACVDPACK YSGHLLLAHI IAKFAIHKKI VLQVFHSLLK AHAMEARAIV
RQAMAILTPA VPARMEDGHQ MLTHWTRKII VEEGHTVPQL VHILHLIVQH FKVYYPVRHH
LVQHMVSAMQ RLGFTPSVTI EQRRLAVDLS EVVIKWELQR IKDQQPDSDM DPNSSGEGVN
SVSSSIKRGL SVDSAQEVKR FRTATGAISA VFGRSQSLPG ADSLLAKPID KQHTDTVVNF
LIRVACQVND NTNTAGSPGE VLSRRCVNLL KTALRPDMWP KSELKLQWFD KLLMTVEQPN
QVNYGNICTG LEVLSFLLTV LQSPAILSSF KPLQRGIAAC MTCGNTKVLR AVHSLLSRLM
SIFPTEPSTS SVASKYEELE CLYAAVGKVI YEGLTNYEKA TNANPSQLFG TLMILKSACS
NNPSYIDRLI SVFMRSLQKM VREHLNPQAA SGSTEATSGT SELVMLSLEL VKTRLAVMSM
EMRKNFIQAI LTSLIEKSPD AKILRAVVKI VEEWVKNNSP MAANQTPTLR EKSILLVKMM
TYIEKRFPED LELNAQFLDL VNYVYRDETL SGSELTAKLE PAFLSGLRCA QPLIRAKFFE
VFDNSMKRRV YERLLYVTCS QNWEAMGNHF WIKQCIELLL AVCEKSTPIG TSCQGAMLPS
ITNVINLADS HDRAAFAMVT HVKQEPRERE NSESKEEDVE IDIELAPGDQ TSTPKTKELS
EKDIGNQLHM LTNRHDKFLD TLREVKTGAL LSAFVQLCHI STTLAEKTWV QLFPRLWKIL
SDRQQHALAG EISPFLCSGS HQVQRDCQPS ALNCFVEAMS QCVPPIPIRP CVLKYLGKTH
NLWFRSTLML EHQAFEKGLS LQIKPKQTTE FYEQESITPP QQEILDSLAE LYSLLQEEDM
WAGLWQKRCK YSETATAIAY EQHGFFEQAQ ESYEKAMDKA KKEHERSNAS PAIFPEYQLW
EDHWIRCSKE LNQWEALTEY GQSKGHINPY LVLECAWRVS NWTAMKEALV QVEVSCPKEM
AWKVNMYRGY LAICHPEEQQ LSFIERLVEM ASSLAIREWR RLPHVVSHVH TPLLQAAQQI
IELQEAAQIN AGLQPTNLGR NNSLHDMKTV VKTWRNRLPI VSDDLSHWSS IFMWRQHHYQ
GKPTWSGMHS SSIVTAYENS SQHDPSSNNA MLGVHASASA IIQYGKIARK QGLVNVALDI
LSRIHTIPTV PIVDCFQKIR QQVKCYLQLA GVMGKNECMQ GLEVIESTNL KYFTKEMTAE
FYALKGMFLA QINKSEEANK AFSAAVQMHD VLVKAWAMWG DYLENIFVKE RQLHLGVSAI
TCYLHACRHQ NESKSRKYLA KVLWLLSFDD DKNTLADAVD KYCIGVPPIQ WLAWIPQLLT
CLVGSEGKLL LNLISQVGRV YPQAVYFPIR TLYLTLKIEQ RERYKSDPGP IRATAPMWRC
SRIMHMQREL HPTLLSSLEG IVDQMVWFRE NWHEEVLRQL QQGLAKCYSV AFEKSGAVSD
AKITPHTLNF VKKLVSTFGV GLENVSNVST MFSSAASESL ARRAQATAQD PVFQKLKGQF
TTDFDFSVPG SMKLHNLISK LKKWIKILEA KTKQLPKFFL IEEKCRFLSN FSAQTAEVEI
PGEFLMPKPT HYYIKIARFM PRVEIVQKHN TAARRLYIRG HNGKIYPYLV MNDACLTESR
REERVLQLLR LLNPCLEKRK ETTKRHLFFT VPRVVAVSPQ MRLVEDNPSS LSLVEIYKQR
CAKKGIEHDN PISRYYDRLA TVQARGTQAS HQVLRDILKE VQSNMVPRSM LKEWALHTFP
NATDYWTFRK MFTIQLALIG FAEFVLHLNR LNPEMLQIAQ DTGKLNVAYF RFDINDATGD
LDANRPVPFR LTPNISEFLT TIGVSGPLTA SMIAVARCFA QPNFKVDGIL KTVLRDEIIA
WHKKTQEDTS SPLSAAGQPE NMDSQQLVSL VQKAVTAIMT RLHNLAQFEG GESKVNTLVA
AANSLDNLCR MDPAWHPWL
//
