ID DHX9_HUMAN Reviewed; 1270 AA. AC Q08211; B2RNV4; Q5VY62; Q6PD69; Q99556; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 4. DT 30-NOV-2010, entry version 120. DE RecName: Full=ATP-dependent RNA helicase A; DE EC=3.6.4.13; DE AltName: Full=DEAH box protein 9; DE AltName: Full=Nuclear DNA helicase II; DE Short=NDH II; GN Name=DHX9; Synonyms=DDX9, LKP, NDH2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT RP VAL-894. RX MEDLINE=93346440; PubMed=8344961; RA Lee C.-G., Hurwitz J.; RT "Human RNA helicase A is homologous to the maleless protein of RT Drosophila."; RL J. Biol. Chem. 268:16822-16830(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=97269062; PubMed=9111062; DOI=10.1074/jbc.272.17.11487; RA Zhang S., Grosse F.; RT "Domain structure of human nuclear DNA helicase II (RNA helicase A)."; RL J. Biol. Chem. 272:11487-11494(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Uterus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PARTIAL PROTEIN SEQUENCE, INTERACTION WITH SMN1, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX MEDLINE=21067068; PubMed=11149922; DOI=10.1083/jcb.152.1.75; RA Pellizzoni L., Charroux B., Rappsilber J., Mann M., Dreyfuss G.; RT "A functional interaction between the survival motor neuron complex RT and RNA polymerase II."; RL J. Cell Biol. 152:75-85(2001). RN [7] RP INTERACTION WITH CREBBP AND RNA POLYMERASE II, AND MUTAGENESIS OF RP LYS-417. RX MEDLINE=97462911; PubMed=9323138; DOI=10.1016/S0092-8674(00)80376-1; RA Nakajima T., Uchida C., Anderson S.F., Lee C.-G., Hurwitz J., RA Parvin J.D., Montminy M.; RT "RNA helicase A mediates association of CBP with RNA polymerase II."; RL Cell 90:1107-1112(1997). RN [8] RP INTERACTION WITH BRCA1. RX PubMed=9662397; DOI=10.1038/930; RA Anderson S.F., Schlegel B.P., Nakajima T., Wolpin E.S., Parvin J.D.; RT "BRCA1 protein is linked to the RNA polymerase II holoenzyme complex RT via RNA helicase A."; RL Nat. Genet. 19:254-256(1998). RN [9] RP DOMAIN NTD, AND MUTAGENESIS OF LYS-1163 AND ARG-1166. RX PubMed=10207077; RA Tang H., McDonald D., Middlesworth T., Hope T.J., Wong-Staal F.; RT "The carboxyl terminus of RNA helicase A contains a bidirectional RT nuclear transport domain."; RL Mol. Cell. Biol. 19:3540-3550(1999). RN [10] RP DOMAIN MTAD, AND MUTAGENESIS OF TRP-332; TRP-339 AND TRP-342. RX PubMed=11416126; DOI=10.1128/MCB.21.14.4460-4469.2001; RA Aratani S., Fujii R., Oishi T., Fujita H., Amano T., Ohshima T., RA Hagiwara M., Fukamizu A., Nakajima T.; RT "Dual roles of RNA helicase A in CREB-dependent transcription."; RL Mol. Cell. Biol. 21:4460-4469(2001). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE RP SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX MEDLINE=22317277; PubMed=12429849; DOI=10.1091/mbc.E02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [12] RP INTERACTION WITH MBD2. RX PubMed=12665568; DOI=10.1128/MCB.23.8.2645-2657.2003; RA Fujita H., Fujii R., Aratani S., Amano T., Fukamizu A., Nakajima T.; RT "Antithetic effects of MBD2a on gene regulation."; RL Mol. Cell. Biol. 23:2645-2657(2003). RN [13] RP INTERACTION WITH TOP2A. RX MEDLINE=22598199; PubMed=12711669; DOI=10.1093/nar/gkg328; RA Zhou K., Choe K.-T., Zaidi Z., Wang Q., Mathews M.B., Lee C.-G.; RT "RNA helicase A interacts with dsDNA and topoisomerase IIalpha."; RL Nucleic Acids Res. 31:2253-2260(2003). RN [14] RP INTERACTION WITH RELA, AND MUTAGENESIS OF LYS-417. RX PubMed=15355351; DOI=10.1111/j.1432-1033.2004.04314.x; RA Tetsuka T., Uranishi H., Sanda T., Asamitsu K., Yang J.-P., RA Wong-Staal F., Okamoto T.; RT "RNA helicase A interacts with nuclear factor kappaB p65 and functions RT as a transcriptional coactivator."; RL Eur. J. Biochem. 271:3741-3751(2004). RN [15] RP INTERACTION WITH XRCC5, AND PHOSPHORYLATION BY PRKDC. RX PubMed=14704337; DOI=10.1093/nar/gkg933; RA Zhang S., Schlott B., Goerlach M., Grosse F.; RT "DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA RT helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent RT manner."; RL Nucleic Acids Res. 32:1-10(2004). RN [16] RP METHYLATION. RX PubMed=15084609; DOI=10.1074/jbc.C300512200; RA Smith W.A., Schurter B.T., Wong-Staal F., David M.; RT "Arginine methylation of RNA helicase a determines its subcellular RT localization."; RL J. Biol. Chem. 279:22795-22798(2004). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [18] RP INTERACTION WITH H2AFX. RX PubMed=15613478; DOI=10.1074/jbc.M411444200; RA Mischo H.E., Hemmerich P., Grosse F., Zhang S.; RT "Actinomycin D induces histone gamma-H2AX foci and complex formation RT of gamma-H2AX with Ku70 and nuclear DNA helicase II."; RL J. Biol. Chem. 280:9586-9594(2005). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1234 AND TYR-1241, AND RP MASS SPECTROMETRY. 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [20] RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, RP AND SUBCELLULAR LOCATION. RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200; RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., RA Johnsen A.H., Christiansen J., Nielsen F.C.; RT "Molecular composition of IMP1 ribonucleoprotein granules."; RL Mol. Cell. Proteomics 6:798-811(2007). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-321, AND MASS RP SPECTROMETRY. 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 [23] RP FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=19029303; DOI=10.1261/rna.1175909; RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., RA Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.; RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RT RNPs."; RL RNA 15:104-115(2009). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [25] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191; LYS-199 AND LYS-1024, RP AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., 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). CC -!- FUNCTION: Unwinds double-stranded DNA and RNA in a 3' to 5' CC direction. Alteration of secondary structure may subsequently CC influence interactions with proteins or other nucleic acids. CC Functions as a transcriptional activator. Component of the CRD- CC mediated complex that promotes MYC mRNA stability. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBUNIT: Component of the coding region determinant (CRD)-mediated CC complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. CC Identified in a mRNP complex, at least composed of DHX9, DDX3X, CC ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, CC SYNCRIP and YBX1. Identified in a mRNP granule complex, at least CC composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, CC HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, CC NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, CC RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. CC Interacts with IGF2BP1. Binds MBD2, HRMT1L2/PRMT1, and RELA. May CC act to directly link BRCA1, CREBBP or SMN1 and the RNA polymerase CC II complex. Can also interact with XRCC5 and with TOP2A in an RNA CC dependent manner; these interactions may be indirect. Interaction CC with TOP2A is promoted by UBC9. Interacts with histone H2AFX and CC this requires phosphorylation of H2AFX on 'Ser-139'. CC -!- INTERACTION: CC P52565:ARHGDIA; NbExp=1; IntAct=EBI-352022, EBI-712693; CC P62633:CNBP; NbExp=1; IntAct=EBI-352022, EBI-1047529; CC Q9NX58:LYAR; NbExp=1; IntAct=EBI-352022, EBI-713507; CC Q9UBU9:NXF1; NbExp=4; IntAct=EBI-352022, EBI-398874; CC Q99873:PRMT1; NbExp=1; IntAct=EBI-352022, EBI-78738; CC Q04206:RELA; NbExp=3; IntAct=EBI-352022, EBI-73886; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. CC Note=Localized in cytoplasmic mRNP granules containing CC untranslated mRNAs. Can shuttle between nucleus and cytoplasm. CC -!- DOMAIN: The MTAD domain mediates interaction with the RNA CC polymerase II holoenzyme. The NTD domain is necessary and CC sufficient for nucleo-cytoplasmic shuttling and interaction with CC HRMT1L2 and SMN1. CC -!- PTM: Methylated. HRMT1L2 mediated methylation of undefined Arg CC residues in the NTD is required for nuclear localization. CC -!- PTM: May be phosphorylated by PRKDC/XRCC7. Phosphorylated upon DNA CC damage, probably by ATM or ATR. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH CC subfamily. CC -!- SIMILARITY: Contains 2 DRBM (double-stranded RNA-binding) domains. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. 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; L13848; AAB48855.1; -; mRNA. DR EMBL; Y10658; CAA71668.1; -; mRNA. DR EMBL; AL355999; CAH71701.1; -; Genomic_DNA. DR EMBL; AL662837; CAH71701.1; JOINED; Genomic_DNA. DR EMBL; AL662837; CAI19277.1; -; Genomic_DNA. DR EMBL; AL355999; CAI19277.1; JOINED; Genomic_DNA. DR EMBL; CH471067; EAW91138.1; -; Genomic_DNA. DR EMBL; BC058896; AAH58896.1; -; mRNA. DR EMBL; BC137136; AAI37137.1; -; mRNA. DR IPI; IPI00844578; -. DR RefSeq; NP_001348.2; NM_001357.4. DR UniGene; Hs.191518; -. DR PDB; 3LLM; X-ray; 2.80 A; A/B=329-563. DR PDBsum; 3LLM; -. DR ProteinModelPortal; Q08211; -. DR SMR; Q08211; 4-89, 166-260, 329-1114. DR DIP; DIP-31504N; -. DR IntAct; Q08211; 47. DR MINT; MINT-5000572; -. DR STRING; Q08211; -. DR PhosphoSite; Q08211; -. DR SWISS-2DPAGE; Q08211; -. DR PRIDE; Q08211; -. DR Ensembl; ENST00000367549; ENSP00000356520; ENSG00000135829. DR GeneID; 1660; -. DR KEGG; hsa:1660; -. DR UCSC; uc001gpr.1; human. DR CTD; 1660; -. DR GeneCards; GC01P182808; -. DR H-InvDB; HIX0001404; -. DR HGNC; HGNC:2750; DHX9. DR HPA; CAB011819; -. DR HPA; HPA028050; -. DR MIM; 603115; gene. DR PharmGKB; PA27232; -. DR HOGENOM; HBG444787; -. DR HOVERGEN; HBG039429; -. DR InParanoid; Q08211; -. DR OMA; GLRGVSH; -. DR OrthoDB; EOG9Z0DRN; -. DR Reactome; REACT_1675; mRNA Processing. DR Reactome; REACT_71; Gene Expression. DR NextBio; 6832; -. DR PMAP-CutDB; Q08211; -. DR ArrayExpress; Q08211; -. DR Bgee; Q08211; -. DR CleanEx; HS_DHX9; -. DR Genevestigator; Q08211; -. DR GermOnline; ENSG00000135829; Homo sapiens. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IMP:UniProtKB. DR GO; GO:0008380; P:RNA splicing; EXP:Reactome. DR InterPro; IPR014001; DEAD-like_N. DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N. DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS. DR InterPro; IPR001159; Ds-RNA-bd. DR InterPro; IPR014720; dsRNA-bd-like. DR InterPro; IPR011709; DUF1605. DR InterPro; IPR007502; Helicase-assoc_dom. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd. DR Gene3D; G3DSA:3.30.160.20; dsRNA-bd-like; 2. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00035; dsrm; 2. DR Pfam; PF07717; DUF1605; 1. DR Pfam; PF04408; HA2; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00358; DSRM; 2. DR SMART; SM00847; HA2; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1. DR PROSITE; PS50137; DS_RBD; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; ATP-binding; Complete proteome; KW Cytoplasm; Direct protein sequencing; DNA-binding; Helicase; KW Hydrolase; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; KW Polymorphism; Repeat; RNA-binding. FT CHAIN 1 1270 ATP-dependent RNA helicase A. FT /FTId=PRO_0000055157. FT DOMAIN 3 71 DRBM 1. FT DOMAIN 180 252 DRBM 2. FT DOMAIN 398 564 Helicase ATP-binding. FT DOMAIN 636 809 Helicase C-terminal. FT NP_BIND 411 418 ATP (By similarity). FT REGION 1 250 Interaction with CREBBP. FT REGION 230 325 Interaction with BRCA1. FT REGION 331 380 MTAD. FT REGION 1151 1260 NTD. FT MOTIF 511 514 DEIH box. FT MOTIF 586 595 Nuclear localization signal (Potential). FT MOD_RES 87 87 Phosphoserine. FT MOD_RES 191 191 N6-acetyllysine. FT MOD_RES 199 199 N6-acetyllysine. FT MOD_RES 321 321 Phosphoserine. FT MOD_RES 1024 1024 N6-acetyllysine. FT MOD_RES 1234 1234 Phosphotyrosine. FT MOD_RES 1241 1241 Phosphotyrosine. FT VARIANT 894 894 I -> V (in dbSNP:rs1049264). FT /FTId=VAR_052179. FT MUTAGEN 332 332 W->A: Abrogates transcriptional FT activation by the MTAD domain. FT MUTAGEN 339 339 W->A: Abrogates transcriptional FT activation and RNA polymerase II binding FT by the MTAD domain. FT MUTAGEN 342 342 W->A: Abrogates transcriptional FT activation by the MTAD domain. FT MUTAGEN 417 417 K->R: Abrogates transcriptional FT activation. FT MUTAGEN 1163 1163 Missing: Abolishes nuclear localization. FT MUTAGEN 1166 1166 R->L: Abolishes nuclear localization. FT MUTAGEN 1166 1166 Missing: Abolishes nuclear localization. FT CONFLICT 20 20 S -> T (in Ref. 1; AAB48855). FT CONFLICT 108 109 TM -> HH (in Ref. 1; AAB48855). FT CONFLICT 114 116 PPH -> LHI (in Ref. 1; AAB48855). FT CONFLICT 186 186 N -> I (in Ref. 1; AAB48855). FT CONFLICT 260 260 S -> T (in Ref. 1; AAB48855). FT CONFLICT 478 478 I -> V (in Ref. 1; AAB48855). FT CONFLICT 521 521 D -> S (in Ref. 1; AAB48855). FT CONFLICT 541 541 L -> F (in Ref. 1; AAB48855). FT CONFLICT 560 565 IIEVYG -> SLKLW (in Ref. 1; AAB48855). FT CONFLICT 749 749 A -> S (in Ref. 1; AAB48855 and 2; FT CAA71668). FT CONFLICT 768 770 VRP -> STA (in Ref. 1; AAB48855 and 2; FT CAA71668). FT CONFLICT 899 899 R -> Q (in Ref. 1; AAB48855). FT CONFLICT 1037 1037 K -> N (in Ref. 1; AAB48855). FT CONFLICT 1063 1063 T -> P (in Ref. 1; AAB48855 and 2; FT CAA71668). FT CONFLICT 1140 1140 R -> E (in Ref. 1; AAB48855). FT CONFLICT 1204 1211 NSFRAGYG -> TPSGRIC (in Ref. 1; FT AAB48855). FT CONFLICT 1261 1270 FGQGRGGGGY -> LDIEEEVAAIKLGYVSSVCRQ (in FT Ref. 1; AAB48855). FT TURN 341 344 FT HELIX 358 374 FT HELIX 376 386 FT HELIX 389 393 FT HELIX 394 403 FT STRAND 405 410 FT TURN 418 420 FT HELIX 421 431 FT HELIX 435 437 FT STRAND 439 446 FT HELIX 447 459 FT STRAND 482 490 FT HELIX 494 499 FT STRAND 507 510 FT HELIX 518 533 FT STRAND 537 542 FT HELIX 549 554 FT TURN 555 557 SQ SEQUENCE 1270 AA; 140958 MW; A607DA8F4C4B217A CRC64; MGDVKNFLYA WCGKRKMTPS YEIRAVGNKN RQKFMCEVQV EGYNYTGMGN STNKKDAQSN AARDFVNYLV RINEIKSEEV PAFGVASPPP LTDTPDTTAN AEGDLPTTMG GPLPPHLALK AENNSEVGAS GYGVPGPTWD RGANLKDYYS RKEEQEVQAT LESEEVDLNA GLHGNWTLEN AKARLNQYFQ KEKIQGEYKY TQVGPDHNRS FIAEMTIYIK QLGRRIFARE HGSNKKLAAQ SCALSLVRQL YHLGVVEAYS GLTKKKEGET VEPYKVNLSQ DLEHQLQNII QELNLEILPP PEDPSVPVAL NIGKLAQFEP SQRQNQVGVV PWSPPQSNWN PWTSSNIDEG PLAFATPEQI SMDLKNELMY QLEQDHDLQA ILQERELLPV KKFESEILEA ISQNSVVIIR GATGCGKTTQ VPQFILDDFI QNDRAAECNI VVTQPRRISA VSVAERVAFE RGEEPGKSCG YSVRFESILP RPHASIMFCT VGVLLRKLEA GIRGISHVIV DEIHERDINT DFLLVVLRDV VQAYPEVRIV LMSATIDTSM FCEYFFNCPI IEVYGRTYPV QEYFLEDCIQ MTHFVPPPKD KKKKDKDDDG GEDDDANCNL ICGDEYGPET RLSMSQLNEK ETPFELIEAL LKYIETLNVP GAVLVFLPGW NLIYTMQKHL EMNPHFGSHR YQILPLHSQI PREEQRKVFD PVPVGVTKVI LSTNIAETSI TINDVVYVID SCKQKVKLFT AHNNMTNYAT VWASKTNLEQ RKGRAGRVRP GFCFHLCSRA RFERLETHMT PEMFRTPLHE IALSIKLLRL GGIGQFLAKA IEPPPLDAVI EAEHTLRELD ALDANDELTP LGRILAKLPI EPRFGKMMIM GCIFYVGDAI CTIAAATCFP EPFINEGKRL GYIHRNFAGN RFSDHVALLS VFQAWDDARM GGEEAEIRFC EHKRLNMATL RMTWEAKVQL KEILINSGFP EDCLLTQVFT NTGPDNNLDV VISLLAFGVY PNVCYHKEKR KILTTEGRNA LIHKSSVNCP FSSQDMKYPS PFFVFGEKIR TRAISAKGMT LVTPLQLLLF ASKKVQSDGQ IVLVDDWIKL QISHEAAACI TGLRAAMEAL VVEVTKQPAI ISQLDPVNER MLNMIRQISR PSAAGINLMI GSTRYGDGPR PPKMARYDNG SGYRRGGSSY SGGGYGGGYS SGGYGSGGYG GSANSFRAGY GAGVGGGYRG VSRGGFRGNS GGDYRGPSGG YRGSGGFQRG GGRGAYGTGY FGQGRGGGGY //