ATAD2_PONAB
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 03-AUG-2022, entry version 86.
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}.
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DR EMBL; CR857768; CAH90033.1; -; mRNA.
DR RefSeq; NP_001127227.1; NM_001133755.1.
DR AlphaFoldDB; Q5RDX4; -.
DR SMR; Q5RDX4; -.
DR PRIDE; Q5RDX4; -.
DR GeneID; 100174282; -.
DR KEGG; pon:100174282; -.
DR CTD; 29028; -.
DR eggNOG; KOG0732; Eukaryota.
DR InParanoid; Q5RDX4; -.
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 GO; GO:0006325; P:chromatin organization; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR031252; ANCCA.
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; PTHR23069; 2.
DR PANTHER; PTHR23069:SF4; PTHR23069:SF4; 2.
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; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 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
