ATAD2_MOUSE
ID ATAD2_MOUSE Reviewed; 1040 AA.
AC Q8CDM1; Q3UYW6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=ATPase family AAA domain-containing protein 2;
DE EC=3.6.1.-;
GN Name=Atad2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-801 AND SER-883, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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: Interacts with ESR1 and NCOA3 and these interactions are
CC enhanced by estradiol. Interacts with acetylated lysine residues on
CC histone H1.4, H2A, H2B and H3 (in vitro) (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q8CDM1; P62806: H4c1; NbExp=2; IntAct=EBI-2944582, EBI-299632;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CDM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CDM1-2; Sequence=VSP_035804, VSP_035805, VSP_035806,
CC VSP_035807;
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AK029867; BAC26651.1; -; mRNA.
DR EMBL; AK134319; BAE22095.1; -; mRNA.
DR RefSeq; NP_081711.2; NM_027435.2.
DR AlphaFoldDB; Q8CDM1; -.
DR SMR; Q8CDM1; -.
DR BioGRID; 214078; 2.
DR IntAct; Q8CDM1; 2.
DR MINT; Q8CDM1; -.
DR STRING; 10090.ENSMUSP00000043691; -.
DR iPTMnet; Q8CDM1; -.
DR PhosphoSitePlus; Q8CDM1; -.
DR EPD; Q8CDM1; -.
DR jPOST; Q8CDM1; -.
DR MaxQB; Q8CDM1; -.
DR PaxDb; Q8CDM1; -.
DR PeptideAtlas; Q8CDM1; -.
DR PRIDE; Q8CDM1; -.
DR ProteomicsDB; 265137; -. [Q8CDM1-1]
DR ProteomicsDB; 265138; -. [Q8CDM1-2]
DR DNASU; 70472; -.
DR Ensembl; ENSMUST00000228783; ENSMUSP00000153936; ENSMUSG00000022360. [Q8CDM1-1]
DR GeneID; 70472; -.
DR KEGG; mmu:70472; -.
DR UCSC; uc007vtg.1; mouse. [Q8CDM1-2]
DR CTD; 29028; -.
DR MGI; MGI:1917722; Atad2.
DR VEuPathDB; HostDB:ENSMUSG00000022360; -.
DR eggNOG; KOG0732; Eukaryota.
DR GeneTree; ENSGT00940000165417; -.
DR InParanoid; Q8CDM1; -.
DR OrthoDB; 443983at2759; -.
DR PhylomeDB; Q8CDM1; -.
DR Reactome; R-MMU-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR BioGRID-ORCS; 70472; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Atad2; mouse.
DR PRO; PR:Q8CDM1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CDM1; protein.
DR Bgee; ENSMUSG00000022360; Expressed in embryonic post-anal tail and 68 other tissues.
DR ExpressionAtlas; Q8CDM1; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
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; 1.
DR PANTHER; PTHR23069:SF4; PTHR23069:SF4; 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; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ATP-binding; Bromodomain; Coiled coil;
KW Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1040
FT /note="ATPase family AAA domain-containing protein 2"
FT /id="PRO_0000084797"
FT DOMAIN 650..720
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 619..643
FT /evidence="ECO:0000255"
FT COILED 735..761
FT /evidence="ECO:0000255"
FT COMPBIAS 811..829
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..920
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PL18"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PL18"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PL18"
FT MOD_RES 801
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 825
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PL18"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PL18"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PL18"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PL18"
FT MOD_RES 972
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PL18"
FT CROSSLNK 777
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PL18"
FT CROSSLNK 797
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PL18"
FT VAR_SEQ 1..201
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035804"
FT VAR_SEQ 202..203
FT /note="IH -> MF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035805"
FT VAR_SEQ 601
FT /note="V -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035806"
FT VAR_SEQ 602..1040
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035807"
SQ SEQUENCE 1040 AA; 117943 MW; 50DF23CA677ABC38 CRC64;
MSLLKMRRHA IHSSDSTSSS SSEDDCFERR TKRNRNRAIN RCLPLNFRKD EIRGIYKDRM
KIGASLADVD PMQLDTSVRF DSVGGLSSHI AALKEMVVFP LLYPEVFEKF KIQPPRGCLF
YGPPGTGKTL VARALANECS RGDKRVAFFM RKGADCLSKW VGESERQLRL LFDQAYQMRP
AIIFFDEIDG LAPVRSSRQD QIHSSIVSTL LALMDGLDSR GEIVVIGATN RLDSIDPALR
RPGRFDREFL FSLPDKNARK EILKIHTRDW NPKPVDMFLE ELAEHCVGYC GADIKSICAE
AALCALRRRY PQIYTTSEKL QLDLSSITIS AKDFEAALQK IRPASQRAVT SPGQALSAIV
KPLLQNTVHR ILDALQKVFP HVEVGTNKSL NSDVSCPFLE SDLAYSDDDT PSVYENGLSQ
KENLNFLHLN RNACYQPMSF RPRLLIVGEP GFGQSSHLAP AVIHALEKFT VYTLDIPVLF
GISTTSPEEA CSQMIREAKR TAPSIVYVPH IHLWWEIVGP TLKATFTTLL QTIPSFAPVL
LLATSEKPYS ALPEEVQELF THDYGEIFNV QLPDKEERTK FFEDLILKQA SKPPVSQKKA
VLQALEVLPV APPPEPRPLT AEEVKRLEEQ EEDTFRELRI FLRNVTHRLA IDKRFRVFTK
PVDPDEVPDY VTVIKQPMDL SSVISKIDLH KYLTVKDYLK DIDLICSNAL EYNPDRDPGD
RLIRHRACAL RDTAYAIIKE ELDEDFEQLC EEIQESRKKR GCSSSKYAPS YYHVMPKQNS
PPVGDKKPDQ EQNEKLKVPC TPVACSTPAQ LKRKFHKKSK WHVGTKIKRR KISQAKDNSL
NAMNSSSRSD TEDSQHTHAE HTEPGNTDES SVEESDKQNR LESNIDLKNN SSSSNIENEL
EEPKETTEGT ELRKDRIVCR GDASASQVTD IPEDSESKEM DFLRMTLARG SQVEQQELIS
MEQALAILSQ PTPSLVLDHK QLTNILKTVV KKSQKYNIFQ LENLYAVISQ CIYEHRRDYD
KTALVQKMEQ AVENFNCSRS
