ID ATAD2_PONAB Reviewed; 1091 AA. AC Q5RDX4; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 24-JAN-2024, entry version 91. DE RecName: Full=ATPase family AAA domain-containing protein 2; DE EC=3.6.1.-; GN Name=ATAD2; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May be a transcriptional coactivator of the nuclear receptor CC ESR1 required to induce the expression of a subset of estradiol target CC genes, such as CCND1, MYC and E2F1. May play a role in the recruitment CC or occupancy of CREBBP at some ESR1 target gene promoters. May be CC required for histone hyperacetylation (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC -!- SUBUNIT: Interaction with ESR1 and NCOA3 is enhanced by estradiol. CC Interacts with acetylated lysine residues on histone H1.4, H2A, H2B and CC H3 (in vitro) (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. {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; CR857768; CAH90033.1; -; mRNA. DR RefSeq; NP_001127227.1; NM_001133755.1. DR AlphaFoldDB; Q5RDX4; -. DR SMR; Q5RDX4; -. DR STRING; 9601.ENSPPYP00000021158; -. DR GeneID; 100174282; -. DR KEGG; pon:100174282; -. DR CTD; 29028; -. DR eggNOG; KOG0732; Eukaryota. DR InParanoid; Q5RDX4; -. DR OrthoDB; 2783776at2759; -. DR Proteomes; UP000001595; Unplaced. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR CDD; cd05528; Bromo_AAA; 1. DR CDD; cd19517; RecA-like_Yta7-like; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR045199; ATAD2-like. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23069; AAA DOMAIN-CONTAINING; 1. DR PANTHER; PTHR23069:SF4; ATPASE FAMILY AAA DOMAIN-CONTAINING PROTEIN 2; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF17862; AAA_lid_3; 1. DR Pfam; PF00439; Bromodomain; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00382; AAA; 1. DR SMART; SM00297; BROMO; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00674; AAA; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. PE 2: Evidence at transcript level; KW Activator; ATP-binding; Bromodomain; Coiled coil; Hydrolase; KW Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..1091 FT /note="ATPase family AAA domain-containing protein 2" FT /id="PRO_0000084798" FT DOMAIN 832..902 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT REGION 32..211 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 961..985 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 801..825 FT /evidence="ECO:0000255" FT COILED 917..943 FT /evidence="ECO:0000255" FT COMPBIAS 67..119 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 298..305 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 158 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT MOD_RES 168 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT MOD_RES 173 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT MOD_RES 241 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT MOD_RES 577 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT MOD_RES 582 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT MOD_RES 970 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT MOD_RES 980 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT MOD_RES 983 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT MOD_RES 1003 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT MOD_RES 1024 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT CROSSLNK 148 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT CROSSLNK 959 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" FT CROSSLNK 979 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q6PL18" SQ SEQUENCE 1091 AA; 124963 MW; 897E5BB49007AD6F CRC64; MLFDKLITNT AEAVLQKMDD MKKMRRQRMR ELEDLGVFNE TEESNLNMYT RGKQKDIQRT DEETTDNQEG SVESSEEGED QEHEDDGEDE DDEDEDDDDD DDDDDDDDED DEDEEDGEED NQKRYYLRQR KATVYYQAPL EKPRHQRKPN IFYSGPASPA RPRYRLSSAG PRSPYCKRMN RRRHAIHSSD STSSSSSEDE QHFERRRKRS RNRAINRYLP LNFRKDELKG IYKDRMKIGA SLADVDPMQL DSSVRFDSVG GLSNHIAALK EMVVFPLLYP EVFEKFKIQP PRGCLFYGPP GTGKTLVARA LANECSQGDK RVAFFMRKGA DCLSKWVGES ERQLRLLFDQ AYQMRPSIIF FDEIDGLAPV RSSRQDQIHS SIVSTLLALM DGLDSRGEIV VIGATNRLDA IDPALRRPGR FDREFLFSLP DKEARKEILK IHTRDWNPKP LDTFLEELAE NCVGYRGADI KSICAEAALC ALRRRYPQIY TTSEKLQLDL SSINISAKDF EVAMQKMIPA SQRAVTSPGQ ALSTVVKPLL QNTVDKILEA LQRVFPHAEF RTNKTLDSDI SCPLLESDLA YSDDDVPSVY ENGLSQKSSH KAKDNFNFLH LNRNACYQPM SFRPRILIVG EPGFGQGSHL APAVIHALEK FTVYTLDIPV LFGVSATSPE ETCAQVIREA KRTAPSIVYV PHIHVWWEIV GPTLKATFTT LLQNIPSFAP VLLLATSDKS HSALPEEVQE LFIRDYGEIF NVQLPGKEER TKFFEDLILK QAAKPPISKK KAVLQALEVL PVAPPPEPRS LTAEEVKRLE EQEEDTFREL RIFLRNVTHR LAIDKRFRVF TKPVDPDEVP DYVTVIKQPM DLSSVISKID LHKYLTVKDY LRDIDLICSN ALEYNPDRDP GDRLIRHRAC ALRDTAYAII KEELDEDFEQ LCEEIQESRK KRGCSSSKYA PSYYHVMPKQ NSTLVGDKRS DPEQNEKLKT PSTPVACSTP EMCVLRMTRA RRSQVEQQQL ISVEKALAIL SQPTPSLVVD HERLKNLLKT VVKKSRNYNI FQLENLYAVI SQCIYQHRKD YDKTSLIQKM EQEVENFSCS R //