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 27-MAR-2024, entry version 204. 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 Q96L91-2; 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="https://atlasgeneticsoncology.org/gene/40457/EP400"; 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; 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; 182. 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.ENSP00000374212; -. DR GlyCosmos; Q96L91; 30 sites, 2 glycans. DR GlyGen; Q96L91; 53 sites, 3 O-linked glycans (53 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; 9606-ENSP00000374213; -. DR PeptideAtlas; 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 Pumba; Q96L91; -. DR Antibodypedia; 19445; 123 antibodies from 19 providers. DR DNASU; 57634; -. DR Ensembl; ENST00000389561.7; ENSP00000374212.2; ENSG00000183495.15. [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 AGR; HGNC:11958; -. 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; 5475375at2759; -. 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 SIGNOR; Q96L91; -. DR BioGRID-ORCS; 57634; 497 hits in 1112 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 199 other cell types or tissues. DR ExpressionAtlas; Q96L91; baseline and differential. 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: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:2000779; P:regulation of double-strand break repair; NAS:ComplexPortal. DR CDD; cd18793; SF2_C_SNF; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 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; IPR049730; SNF2/RAD54-like_C. DR InterPro; IPR000330; SNF2_N. DR PANTHER; PTHR46459:SF1; E1A-BINDING PROTEIN P400; 1. DR PANTHER; PTHR46459; E1A-BINDING PROTEIN P400-RELATED; 1. 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; P-loop containing nucleoside triphosphate hydrolases; 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. DR Genevisible; Q96L91; HS. 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 //