EP400_HUMAN
ID EP400_HUMAN Reviewed; 3159 AA.
AC Q96L91; O15411; Q6P2F5; Q8N8Q7; Q8NE05; Q96JK7; Q9P230;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=E1A-binding protein p400;
DE EC=3.6.4.-;
DE AltName: Full=CAG repeat protein 32;
DE AltName: Full=Domino homolog;
DE Short=hDomino;
DE AltName: Full=Trinucleotide repeat-containing gene 12 protein;
DE AltName: Full=p400 kDa SWI2/SNF2-related protein;
GN Name=EP400; Synonyms=CAGH32, KIAA1498, KIAA1818, TNRC12;
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), IDENTIFICATION BY MASS
RP SPECTROMETRY, ROLE OF EP400-CONTAINING COMPLEXES IN CELLULAR TRANSFORMATION
RP BY ADENOVIRUS E1A PROTEIN, TISSUE SPECIFICITY, AND INTERACTION WITH TRRAP;
RP RUVBL1 AND RUVBL2.
RX PubMed=11509179; DOI=10.1016/s0092-8674(01)00450-0;
RA Fuchs M., Gerber J., Drapkin R., Sif S., Ikura T., Ogryzko V., Lane W.S.,
RA Nakatani Y., Livingston D.M.;
RT "The p400 complex is an essential E1A transformation target.";
RL Cell 106:297-307(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1847 (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-897 (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-978 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-895 (ISOFORM 3).
RC TISSUE=Lymph, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2004-3159.
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2463-3159.
RC TISSUE=Brain;
RX PubMed=9225980; DOI=10.1007/s004390050476;
RA Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S.,
RA Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.;
RT "cDNAs with long CAG trinucleotide repeats from human brain.";
RL Hum. Genet. 100:114-122(1997).
RN [8]
RP IDENTIFICATION IN NUA4 COMPLEX.
RX PubMed=12963728; DOI=10.1074/jbc.c300389200;
RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
RA Conaway R.C., Conaway J.W.;
RT "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-
RT containing histone acetyltransferase complex.";
RL J. Biol. Chem. 278:42733-42736(2003).
RN [9]
RP REVIEW ON NUA4 COMPLEX.
RX PubMed=15196461; DOI=10.1016/j.gde.2004.02.009;
RA Doyon Y., Cote J.;
RT "The highly conserved and multifunctional NuA4 HAT complex.";
RL Curr. Opin. Genet. Dev. 14:147-154(2004).
RN [10]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4
RP COMPLEX, AND IDENTIFICATION IN SRCAP-CONTAINING 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941; THR-945; SER-1728 AND
RP SER-1732, AND 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 [13]
RP INTERACTION WITH HADV5 E1A.
RX PubMed=18413597; DOI=10.1073/pnas.0802095105;
RA Tworkowski K.A., Chakraborty A.A., Samuelson A.V., Seger Y.R., Narita M.,
RA Hannon G.J., Lowe S.W., Tansey W.P.;
RT "Adenovirus E1A targets p400 to induce the cellular oncoprotein Myc.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6103-6108(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1472; LYS-2349 AND LYS-2356, AND
RP IDENTIFICATION BY MASS 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736 AND THR-2813, AND
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 [18]
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 [19]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS UL27.
RX PubMed=21320693; DOI=10.1016/j.chom.2011.01.006;
RA Reitsma J.M., Savaryn J.P., Faust K., Sato H., Halligan B.D., Terhune S.S.;
RT "Antiviral inhibition targeting the HCMV kinase pUL97 requires pUL27-
RT dependent proteasomal degradation of Tip60 acetyltransferase and cell-cycle
RT arrest.";
RL Cell Host Microbe 9:103-114(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736; SER-1547; SER-2686 AND
RP THR-2813, 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736, AND IDENTIFICATION BY
RP 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 [23]
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).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of select genes principally
CC by acetylation of nucleosomal histones H4 and H2A. This modification
CC may both alter nucleosome - DNA interactions and promote interaction of
CC the modified histones with other proteins which positively regulate
CC transcription. May be required for transcriptional activation of E2F1
CC and MYC target genes during cellular proliferation. The NuA4 complex
CC ATPase and helicase activities seem to be, at least in part,
CC contributed by the association of RUVBL1 and RUVBL2 with EP400. May
CC regulate ZNF42 transcription activity. Component of a SWR1-like complex
CC that specifically mediates the removal of histone H2A.Z/H2AZ1 from the
CC nucleosome. {ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:24463511}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC YEATS4/GAS41, VPS72/YL1 and MEAF6. May also participate in the
CC formation of NuA4 related complexes which lack the KAT5/TIP60 catalytic
CC subunit, but which include the SWI/SNF related protein SRCAP. The NuA4
CC complex interacts with MYC and the adenovirus E1A protein. EP400
CC interacts with TRRAP, RUVBL1 and RUVBL2. Component of a SWR1-like
CC complex. Interacts with ZNF42. Interacts with PHF5A. Interacts with
CC human cytomegalovirus UL27. Interacts with human adenovirus 5 E1A
CC protein; this interaction stabilizes MYC (PubMed:18413597).
CC {ECO:0000250, ECO:0000269|PubMed:18413597,
CC ECO:0000269|PubMed:21320693}.
CC -!- INTERACTION:
CC Q96L91; P13196: ALAS1; NbExp=4; IntAct=EBI-399163, EBI-3905054;
CC Q96L91; P01106: MYC; NbExp=6; IntAct=EBI-399163, EBI-447544;
CC Q96L91; Q9Y230: RUVBL2; NbExp=2; IntAct=EBI-399163, EBI-352939;
CC Q96L91; Q93009: USP7; NbExp=2; IntAct=EBI-399163, EBI-302474;
CC Q96L91-2; P01106: MYC; NbExp=2; IntAct=EBI-15698003, EBI-447544;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96L91-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96L91-2; Sequence=VSP_011992;
CC Name=3;
CC IsoId=Q96L91-3; Sequence=VSP_011992, VSP_011993, VSP_011994;
CC Name=4;
CC IsoId=Q96L91-4; Sequence=VSP_011992, VSP_011995;
CC Name=5;
CC IsoId=Q96L91-5; Sequence=VSP_011992, VSP_011993;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11509179}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB91441.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH37208.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAH64554.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA96022.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EP400ID40457ch12q24.html";
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DR EMBL; AY044869; AAK97789.1; -; mRNA.
DR EMBL; AC137590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB040931; BAA96022.1; ALT_INIT; mRNA.
DR EMBL; AK096311; BAC04759.1; -; mRNA.
DR EMBL; BC037208; AAH37208.1; ALT_SEQ; mRNA.
DR EMBL; BC064554; AAH64554.1; ALT_SEQ; mRNA.
DR EMBL; AB058721; BAB47447.1; -; mRNA.
DR EMBL; U80743; AAB91441.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31929.2; -. [Q96L91-2]
DR RefSeq; NP_056224.3; NM_015409.4. [Q96L91-2]
DR SMR; Q96L91; -.
DR BioGRID; 121676; 156.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR CORUM; Q96L91; -.
DR DIP; DIP-29915N; -.
DR IntAct; Q96L91; 78.
DR MINT; Q96L91; -.
DR STRING; 9606.ENSP00000374213; -.
DR GlyGen; Q96L91; 30 sites, 2 O-linked glycans (30 sites).
DR iPTMnet; Q96L91; -.
DR PhosphoSitePlus; Q96L91; -.
DR BioMuta; EP400; -.
DR DMDM; 317373565; -.
DR EPD; Q96L91; -.
DR jPOST; Q96L91; -.
DR MassIVE; Q96L91; -.
DR MaxQB; Q96L91; -.
DR PaxDb; Q96L91; -.
DR PeptideAtlas; Q96L91; -.
DR PRIDE; Q96L91; -.
DR ProteomicsDB; 77156; -. [Q96L91-1]
DR ProteomicsDB; 77157; -. [Q96L91-2]
DR ProteomicsDB; 77158; -. [Q96L91-3]
DR ProteomicsDB; 77159; -. [Q96L91-4]
DR ProteomicsDB; 77160; -. [Q96L91-5]
DR Antibodypedia; 19445; 103 antibodies from 19 providers.
DR DNASU; 57634; -.
DR Ensembl; ENST00000389561.7; ENSP00000374212.2; ENSG00000183495.14. [Q96L91-2]
DR GeneID; 57634; -.
DR KEGG; hsa:57634; -.
DR MANE-Select; ENST00000389561.7; ENSP00000374212.2; NM_015409.5; NP_056224.3. [Q96L91-2]
DR UCSC; uc001ujn.3; human. [Q96L91-1]
DR CTD; 57634; -.
DR DisGeNET; 57634; -.
DR GeneCards; EP400; -.
DR HGNC; HGNC:11958; EP400.
DR HPA; ENSG00000183495; Low tissue specificity.
DR MIM; 606265; gene.
DR neXtProt; NX_Q96L91; -.
DR OpenTargets; ENSG00000183495; -.
DR PharmGKB; PA27808; -.
DR VEuPathDB; HostDB:ENSG00000183495; -.
DR eggNOG; KOG0391; Eukaryota.
DR GeneTree; ENSGT00940000154764; -.
DR HOGENOM; CLU_000397_0_0_1; -.
DR InParanoid; Q96L91; -.
DR OMA; YGEDCRG; -.
DR OrthoDB; 188211at2759; -.
DR PhylomeDB; Q96L91; -.
DR TreeFam; TF106424; -.
DR PathwayCommons; Q96L91; -.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q96L91; -.
DR BioGRID-ORCS; 57634; 484 hits in 1048 CRISPR screens.
DR ChiTaRS; EP400; human.
DR GeneWiki; EP400; -.
DR GenomeRNAi; 57634; -.
DR Pharos; Q96L91; Tbio.
DR PRO; PR:Q96L91; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96L91; protein.
DR Bgee; ENSG00000183495; Expressed in tendon of biceps brachii and 197 other tissues.
DR ExpressionAtlas; Q96L91; baseline and differential.
DR Genevisible; Q96L91; HS.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0000812; C:Swr1 complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:1990405; F:protein antigen binding; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031575; EP400_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF15790; EP400_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Chromatin regulator;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..3159
FT /note="E1A-binding protein p400"
FT /id="PRO_0000074312"
FT DOMAIN 799..871
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 1103..1268
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1899..2056
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2360..2429
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1365
FT /note="Interactions with RUVBL1 and RUVBL2"
FT REGION 997..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1787..1807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2119..2144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2287..2311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2524..2789
FT /note="Interaction with ZNF42"
FT /evidence="ECO:0000250"
FT REGION 2524..2602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2665..2688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2821..2869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3115..3159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1219..1222
FT /note="DEAH box-like"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..961
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2287..2310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2539..2591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2826..2840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2841..2869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3115..3141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1116..1123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHI8"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHI8"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHI8"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHI8"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHI8"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHI8"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 945
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHI8"
FT MOD_RES 1472
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2349
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2356
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2813
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 446..481
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:10819331,
FT ECO:0000303|PubMed:11509179, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011992"
FT VAR_SEQ 482
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011993"
FT VAR_SEQ 515..550
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011994"
FT VAR_SEQ 1519..1600
FT /note="AAAAPFQTSQASASAPRHQPASASSTAASPAHPAKLRAQTTAQASTPGQPPP
FT QPQAPSHAAGQSALPQRLVLPSQAQARLPS -> G (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_011995"
FT VARIANT 1308
FT /note="T -> I (in dbSNP:rs13377636)"
FT /id="VAR_046957"
FT CONFLICT 537
FT /note="D -> G (in Ref. 5; AAH37208)"
FT /evidence="ECO:0000305"
FT CONFLICT 810
FT /note="S -> P (in Ref. 5; AAH37208)"
FT /evidence="ECO:0000305"
FT CONFLICT 1563
FT /note="S -> F (in Ref. 1; AAK97789)"
FT /evidence="ECO:0000305"
FT CONFLICT 1642
FT /note="L -> F (in Ref. 1; AAK97789)"
FT /evidence="ECO:0000305"
FT CONFLICT 1645
FT /note="L -> F (in Ref. 1; AAK97789)"
FT /evidence="ECO:0000305"
FT CONFLICT 2756
FT /note="Q -> QQ (in Ref. 1; AAK97789, 6; BAB47447 and 7;
FT AAB91441)"
FT /evidence="ECO:0000305"
FT CONFLICT 2844
FT /note="T -> A (in Ref. 1; AAK97789 and 7; AAB91441)"
FT /evidence="ECO:0000305"
FT CONFLICT 2897
FT /note="A -> S (in Ref. 1; AAK97789 and 7; AAB91441)"
FT /evidence="ECO:0000305"
FT CONFLICT 2912..2914
FT /note="ALA -> PLP (in Ref. 1; AAK97789 and 7; AAB91441)"
FT /evidence="ECO:0000305"
FT CONFLICT 2990
FT /note="A -> T (in Ref. 1; AAK97789)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3159 AA; 343489 MW; 0E502CE1BE9CFAC1 CRC64;
MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA PQSPSYQIQQ
LMNRSPATGQ NVNITLQSVG PVVGGNQQIT LAPLPLPSPT SPGFQFSAQP RRFEHGSPSY
IQVTSPLSQQ VQTQSPTQPS PGPGQALQNV RAGAPGPGLG LCSSSPTGGF VDASVLVRQI
SLSPSSGGHF VFQDGSGLTQ IAQGAQVQLQ HPGTPITVRE RRPSQPHTQS GGTIHHLGPQ
SPAAAGGAGL QPLASPSHIT TANLPPQISS IIQGQLVQQQ QVLQGPPLPR PLGFERTPGV
LLPGAGGAAG FGMTSPPPPT SPSRTAVPPG LSSLPLTSVG NTGMKKVPKK LEEIPPASPE
MAQMRKQCLD YHYQEMQALK EVFKEYLIEL FFLQHFQGNM MDFLAFKKKH YAPLQAYLRQ
NDLDIEEEEE EEEEEEEKSE VINDEVKVVT GKDGQTGTPV AIATQLPPKV SAAFSSQQQP
FQQALAGSLV AGAGSTVETD LFKRQQAMPS TGMAEQSKRP RLEVGHQGVV FQHPGADAGV
PLQQLMPTAQ GGMPPTPQAA QLAGQRQSQQ QYDPSTGPPV QNAASLHTPL PQLPGRLPPA
GVPTAALSSA LQFAQQPQVV EAQTQLQIPV KTQQPNVPIP APPSSQLPIP PSQPAQLALH
VPTPGKVQVQ ASQLSSLPQM VASTRLPVDP APPCPRPLPT SSTSSLAPVS GSGPGPSPAR
SSPVNRPSSA TNKALSPVTS RTPGVVASAP TKPQSPAQNA TSSQDSSQDT LTEQITLENQ
VHQRIAELRK AGLWSQRRLP KLQEAPRPKS HWDYLLEEMQ WMATDFAQER RWKVAAAKKL
VRTVVRHHEE KQLREERGKK EEQSRLRRIA ASTAREIECF WSNIEQVVEI KLRVELEEKR
KKALNLQKVS RRGKELRPKG FDALQESSLD SGMSGRKRKA SISLTDDEVD DEEETIEEEE
ANEGVVDHQT ELSNLAKEAE LPLLDLMKLY EGAFLPSSQW PRPKPDGEDT SGEEDADDCP
GDRESRKDLV LIDSLFIMDQ FKAAERMNIG KPNAKDIADV TAVAEAILPK GSARVTTSVK
FNAPSLLYGA LRDYQKIGLD WLAKLYRKNL NGILADEAGL GKTVQIIAFF AHLACNEGNW
GPHLVVVRSC NILKWELELK RWCPGLKILS YIGSHRELKA KRQEWAEPNS FHVCITSYTQ
FFRGLTAFTR VRWKCLVIDE MQRVKGMTER HWEAVFTLQS QQRLLLIDSP LHNTFLELWT
MVHFLVPGIS RPYLSSPLRA PSEESQDYYH KVVIRLHRVT QPFILRRTKR DVEKQLTKKY
EHVLKCRLSN RQKALYEDVI LQPGTQEALK SGHFVNVLSI LVRLQRICNH PGLVEPRHPG
SSYVAGPLEY PSASLILKAL ERDFWKEADL SMFDLIGLEN KITRHEAELL SKKKIPRKLM
EEISTSAAPA ARPAAAKLKA SRLFQPVQYG QKPEGRTVAF PSTHPPRTAA PTTASAAPQG
PLRGRPPIAT FSANPEAKAA AAPFQTSQAS ASAPRHQPAS ASSTAASPAH PAKLRAQTTA
QASTPGQPPP QPQAPSHAAG QSALPQRLVL PSQAQARLPS GEVVKIAQLA SITGPQSRVA
QPETPVTLQF QGSKFTLSHS QLRQLTAGQP LQLQGSVLQI VSAPGQPYLR APGPVVMQTV
SQAGAVHGAL GSKPPAGGPS PAPLTPQVGV PGRVAVNALA VGEPGTASKP ASPIGGPTQE
EKTRLLKERL DQIYLVNERR CSQAPVYGRD LLRICALPSH GRVQWRGSLD GRRGKEAGPA
HSYTSSSESP SELMLTLCRC GESLQDVIDR VAFVIPPVVA APPSLRVPRP PPLYSHRMRI
LRQGLREHAA PYFQQLRQTT APRLLQFPEL RLVQFDSGKL EALAILLQKL KSEGRRVLIL
SQMILMLDIL EMFLNFHYLT YVRIDENASS EQRQELMRSF NRDRRIFCAI LSTHSRTTGI
NLVEADTVVF YDNDLNPVMD AKAQEWCDRI GRCKDIHIYR LVSGNSIEEK LLKNGTKDLI
REVAAQGNDY SMAFLTQRTI QELFEVYSPM DDAGFPVKAE EFVVLSQEPS VTETIAPKIA
RPFIEALKSI EYLEEDAQKS AQEGVLGPHT DALSSDSENM PCDEEPSQLE ELADFMEQLT
PIEKYALNYL ELFHTSIEQE KERNSEDAVM TAVRAWEFWN LKTLQEREAR LRLEQEEAEL
LTYTREDAYS MEYVYEDVDG QTEVMPLWTP PTPPQDDSDI YLDSVMCLMY EATPIPEAKL
PPVYVRKERK RHKTDPSAAG RKKKQRHGEA VVPPRSLFDR ATPGLLKIRR EGKEQKKNIL
LKQQVPFAKP LPTFAKPTAE PGQDNPEWLI SEDWALLQAV KQLLELPLNL TIVSPAHTPN
WDLVSDVVNS CSRIYRSSKQ CRNRYENVII PREEGKSKNN RPLRTSQIYA QDENATHTQL
YTSHFDLMKM TAGKRSPPIK PLLGMNPFQK NPKHASVLAE SGINYDKPLP PIQVASLRAE
RIAKEKKALA DQQKAQQPAV AQPPPPQPQP PPPPQQPPPP LPQPQAAGSQ PPAGPPAVQP
QPQPQPQTQP QPVQAPAKAQ PAITTGGSAA VLAGTIKTSV TGTSMPTGAV SGNVIVNTIA
GVPAATFQSI NKRLASPVAP GALTTPGGSA PAQVVHTQPP PRAVGSPATA TPDLVSMATT
QGVRAVTSVT ASAVVTTNLT PVQTPARSLV PQVSQATGVQ LPGKTITPAH FQLLRQQQQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQTTTTSQ VQVPQIQGQA QSPAQIKAVG KLTPEHLIKM
QKQKLQMPPQ PPPPQAQSAP PQPTAQVQVQ TSQPPQQQSP QLTTVTAPRP GALLTGTTVA
NLQVARLTRV PTSQLQAQGQ MQTQAPQPAQ VALAKPPVVS VPAAVVSSPG VTTLPMNVAG
ISVAIGQPQK AAGQTVVAQP VHMQQLLKLK QQAVQQQKAI QPQAAQGPAA VQQKITAQQI
TTPGAQQKVA YAAQPALKTQ FLTTPISQAQ KLAGAQQVQT QIQVAKLPQV VQQQTPVASI
QQVASASQQA SPQTVALTQA TAAGQQVQMI PAVTATAQVV QQKLIQQQVV TTASAPLQTP
GAPNPAQVPA SSDSPSQQPK LQMRVPAVRL KTPTKPPCQ
