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Database: UniProt
Entry: Q99NG0
LinkDB: Q99NG0
Original site: Q99NG0 
ID   ARIP4_MOUSE             Reviewed;        1466 AA.
AC   Q99NG0; Q3UPJ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   18-SEP-2019, entry version 123.
DE   RecName: Full=Helicase ARIP4;
DE            EC=3.6.4.12;
DE   AltName: Full=Androgen receptor-interacting protein 4;
DE   AltName: Full=RAD54-like protein 2;
DE   AltName: Full=Steroid receptor-interacting SNF2 domain-containing protein-like;
GN   Name=Rad54l2; Synonyms=Arip4, Srisnf2l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP   DNA-BINDING, INTERACTION WITH AR, AND MUTAGENESIS OF LYS-310 AND
RP   462-ASP-GLU-463.
RC   STRAIN=Swiss Webster; TISSUE=Embryo;
RX   PubMed=12058073; DOI=10.1091/mbc.01-10-0484.;
RA   Rouleau N., Domans'kyi A., Reeben M., Moilanen A.-M., Havas K.,
RA   Kang Z., Owen-Hughes T., Palvimo J.J., Jaenne O.A.;
RT   "Novel ATPase of SNF2-like protein family interacts with androgen
RT   receptor and modulates androgen-dependent transcription.";
RL   Mol. Biol. Cell 13:2106-2119(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-1466.
RC   STRAIN=C57BL/6J;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH DYRK1A.
RX   PubMed=15199138; DOI=10.1128/mcb.24.13.5821-5834.2004;
RA   Sitz J.H., Tigges M., Baumgaertel K., Khaspekov L.G., Lutz B.;
RT   "Dyrk1A potentiates steroid hormone-induced transcription via the
RT   chromatin remodeling factor Arip4.";
RL   Mol. Cell. Biol. 24:5821-5834(2004).
RN   [5]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP   INTERACTION WITH AR, SUMOYLATION, AND MUTAGENESIS OF LYS-361; LYS-573;
RP   LYS-664; LYS-935; LYS-961 AND LYS-1013.
RX   PubMed=16212558; DOI=10.1042/bj20050823;
RA   Domanskyi A., Virtanen K.T., Palvimo J.J., Jaenne O.A.;
RT   "Biochemical characterization of androgen receptor-interacting protein
RT   4.";
RL   Biochem. J. 393:789-795(2006).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17003240; DOI=10.1152/ajpendo.00287.2006;
RA   Domanskyi A., Zhang F.-P., Nurmio M., Palvimo J.J., Toppari J.,
RA   Jaenne O.A.;
RT   "Expression and localization of androgen receptor-interacting protein-
RT   4 in the testis.";
RL   Am. J. Physiol. 292:E513-E522(2007).
RN   [7]
RP   DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=17374848; DOI=10.1210/me.2007-0052;
RA   Zhang F.-P., Domanskyi A., Palvimo J.J., Sariola H., Partanen J.,
RA   Jaenne O.A.;
RT   "An adenosine triphosphatase of the sucrose nonfermenting 2 family,
RT   androgen receptor-interacting protein 4, is essential for mouse
RT   embryonic development and cell proliferation.";
RL   Mol. Endocrinol. 21:1430-1442(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1168 AND SER-1171, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: DNA helicase that modulates androgen receptor (AR)-
CC       dependent transactivation in a promoter-dependent manner. Not able
CC       to remodel mononucleosomes in vitro. Acts as an AR-coregulator in
CC       Sertoli cells. {ECO:0000269|PubMed:12058073,
CC       ECO:0000269|PubMed:16212558}.
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; EC=3.6.4.12;
CC   -!- ACTIVITY REGULATION: Enzyme activity is enhanced by dsDNA (double-
CC       stranded DNA) and ssDNA (single-stranded DNA).
CC       {ECO:0000269|PubMed:16212558}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=40 nM for DNA {ECO:0000269|PubMed:16212558};
CC         KM=25 uM for ATP {ECO:0000269|PubMed:16212558};
CC   -!- SUBUNIT: Interacts with AR via its N-terminus. Interacts with
CC       DYRK1A. Binds DNA and mononucleosomes, but does not seem to form
CC       large multiprotein complexes. {ECO:0000269|PubMed:12058073,
CC       ECO:0000269|PubMed:15199138, ECO:0000269|PubMed:16212558}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12058073,
CC       ECO:0000269|PubMed:15199138}. Note=Localizes in speckle-like
CC       nuclear compartments.
CC   -!- TISSUE SPECIFICITY: Expressed at relatively low level, with
CC       highest expression in testis, liver and kidney. In brain, it is
CC       expressed in hippocampal and cerebellar neurons. In testis, it is
CC       present at high level in Sertoli cell nuclei. Also present in
CC       Leydig cell (at protein level). {ECO:0000269|PubMed:15199138,
CC       ECO:0000269|PubMed:17003240}.
CC   -!- DEVELOPMENTAL STAGE: Mainly expressed in the neural tube and limb
CC       buds during early embryonic development. Also present in testis:
CC       at the onset of spermatogenesis, it is expressed in spermatogonia,
CC       pachytene, and diplotene spermatocytes. In Sertoli cells it is
CC       expressed in a stage-dependent manner, with high expression levels
CC       at stages II-VI and VII-VIII. {ECO:0000269|PubMed:17003240,
CC       ECO:0000269|PubMed:17374848}.
CC   -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to be
CC       important for the association with nuclear receptors.
CC       {ECO:0000250}.
CC   -!- PTM: Sumoylated. {ECO:0000269|PubMed:16212558}.
CC   -!- DISRUPTION PHENOTYPE: Death by 11.5 dpc. At 9.5 dpc and 10.5 dpc,
CC       almost all major tissues are proportionally smaller, and the
CC       neural tube is shrunk in some embryos. Dramatically reduced cell
CC       proliferation and increased apoptosis are observed in 9.5 dpc and
CC       10.5 dpc embryos. Embryonic fibroblasts stop to grow after 2 or 3
CC       passages and exhibit increased apoptosis and decreased DNA
CC       synthesis compared with wild-type. {ECO:0000269|PubMed:17374848}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
DR   EMBL; AJ132389; CAC24703.1; -; mRNA.
DR   EMBL; BC133714; AAI33715.1; -; mRNA.
DR   EMBL; AK143506; BAE25404.1; -; mRNA.
DR   RefSeq; NP_109655.2; NM_030730.2.
DR   BioGrid; 219861; 1.
DR   IntAct; Q99NG0; 1.
DR   STRING; 10090.ENSMUSP00000045454; -.
DR   iPTMnet; Q99NG0; -.
DR   PhosphoSitePlus; Q99NG0; -.
DR   EPD; Q99NG0; -.
DR   MaxQB; Q99NG0; -.
DR   PaxDb; Q99NG0; -.
DR   PRIDE; Q99NG0; -.
DR   GeneID; 81000; -.
DR   KEGG; mmu:81000; -.
DR   CTD; 23132; -.
DR   MGI; MGI:1933196; Rad54l2.
DR   eggNOG; KOG1015; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   HOGENOM; HOG000168429; -.
DR   InParanoid; Q99NG0; -.
DR   KO; K10876; -.
DR   OrthoDB; 815681at2759; -.
DR   PhylomeDB; Q99NG0; -.
DR   ChiTaRS; Rad54l2; mouse.
DR   PRO; PR:Q99NG0; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IDA:MGI.
DR   GO; GO:0016887; F:ATPase activity; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019901; F:protein kinase binding; IPI:MGI.
DR   GO; GO:0003712; F:transcription coregulator activity; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; DNA-binding; Helicase; Hydrolase;
KW   Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN         1   1466       Helicase ARIP4.
FT                                /FTId=PRO_0000315782.
FT   DOMAIN      291    511       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      727    895       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     304    311       ATP. {ECO:0000305}.
FT   MOTIF       462    465       DEAH box.
FT   MOTIF       550    554       LXXLL motif 1.
FT   MOTIF      1328   1332       LXXLL motif 2.
FT   COMPBIAS     18     42       Glu-rich.
FT   COMPBIAS    222    228       Poly-Glu.
FT   MOD_RES    1168   1168       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1171   1171       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1259   1259       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9Y4B4}.
FT   CROSSLNK    114    114       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4B4}.
FT   CROSSLNK    126    126       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4B4}.
FT   CROSSLNK    271    271       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4B4}.
FT   CROSSLNK    664    664       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4B4}.
FT   CROSSLNK    681    681       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4B4}.
FT   CROSSLNK    758    758       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4B4}.
FT   CROSSLNK    900    900       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4B4}.
FT   CROSSLNK   1013   1013       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4B4}.
FT   CROSSLNK   1017   1017       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9Y4B4}.
FT   MUTAGEN     310    310       K->A: Abolishes ATP-binding.
FT                                {ECO:0000269|PubMed:12058073}.
FT   MUTAGEN     361    361       K->E: Decreased sumoylation; when
FT                                associated with E-573; E-664; E-935; E-
FT                                961 and E-1013.
FT                                {ECO:0000269|PubMed:16212558}.
FT   MUTAGEN     462    463       DE->AA: Abolishes ATPase activity.
FT                                {ECO:0000269|PubMed:12058073}.
FT   MUTAGEN     573    573       K->E: Decreased sumoylation; when
FT                                associated with E-361; E-664; E-935; E-
FT                                961 and E-1013.
FT                                {ECO:0000269|PubMed:16212558}.
FT   MUTAGEN     664    664       K->E: Decreased sumoylation; when
FT                                associated with E-361; E-573; E-935; E-
FT                                961 and E-1013.
FT                                {ECO:0000269|PubMed:16212558}.
FT   MUTAGEN     935    935       K->E: Decreased sumoylation; when
FT                                associated with E-361; E-573; E-664; E-
FT                                961 and E-1013.
FT                                {ECO:0000269|PubMed:16212558}.
FT   MUTAGEN     961    961       K->E: Decreased sumoylation; when
FT                                associated with E-361; E-573; E-664; E-
FT                                935 and E-1013.
FT                                {ECO:0000269|PubMed:16212558}.
FT   MUTAGEN    1013   1013       K->E: Decreased sumoylation; when
FT                                associated with E-361; E-573; E-664; E-
FT                                935 and E-961.
FT                                {ECO:0000269|PubMed:16212558}.
FT   CONFLICT   1197   1197       I -> V (in Ref. 3; BAE25404).
FT                                {ECO:0000305}.
FT   CONFLICT   1267   1267       I -> V (in Ref. 3; BAE25404).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1466 AA;  162540 MW;  D5945AD802B03D12 CRC64;
     MSDESASGSD PDLDPDVELE DEEEEEEEEE VAVEEHDRDD EEGLLDDTSL EGMCGTEHAQ
     LGEDGQRPPR CTSTTSSQSE PSEQLRHQGK ILASEDPKKK RAQKPSHMRR NIRKLLREDQ
     LEPVTKAAQQ EELERRKRLE QQRKEYAAPI PTVPLEFLPE EIVLRASDGP QLPPRVLAQE
     VICLDSSSGS EDEKSSRDEV IELSSGEEDT LHIVDSSESV SEEDEEEEKG GTHVNDALNQ
     HDALGRVLVN LNHPPEEENV FLAPQLARAV KPHQIGGIRF LYDNLVESLE RFKTSSGFGC
     ILAHSMGLGK TLQVISFIDV LFRHTPAKTV LAIVPVNTLQ NWLAEFNMWL PAPEALPADS
     KPEEVQPRFF KVHILNDEHK TVASRAKVTA DWVSEGGVLL MGYEMYRLLT LKKSLATSRP
     KKTKKRSHPV IIDLDEEDRQ QEFRREFEKA LCRPGPDVVI CDEGHRIKNC QASTSQALKN
     IRSRRRVVLT GYPLQNNLIE YWCMVDFVRP DFLGTRQEFS NMFERPILNG QCIDSTPQDV
     RLMRYRSHVL HSLLEGFVQR RGHTVLKIHL PAKEENVILV RLSQIQRDLY TQFMDRFRDC
     GTSGWLGLNP LKAFCVCCKI WNHPDVLYEA LQKENLANEQ DLDVEELGSA GTSARCPPHG
     TKVKGEDSAL PSSMGEATNS KFLQGVGFNP FQERGNNIVT YEWAKELLTN YQTGVLENSP
     KMVLLFHLIE ESVKLGDKIL VFSQSLSTLA LIEEFLGKRD MPCLPGAEGQ GTQKWVRNVS
     YFRLDGSTPA FERERLINQF NDPSNLTTWL FLLSTRAGCL GVNLIGANRV VVFDASWNPC
     HDAQAVCRVY RYGQKKPCHI YRLVADYTLE KKIYDRQISK QGMSDRVVDD LNPMLNFTRK
     EVENLLHFVE KEPAPQTSLD IKGIKESVLQ LACLKYPHLI TKEPFEHESL LLNRKDHKLT
     KAEKKAAKKS YEEDKRTSVP YTRPSYAQYY PASDQSLTSI PAFSQRNWQP TLKGDEKPVA
     SVRPVQSTPI PMMPRHVPLS GGVSSASSTN TSMNFPINYL QRAGVLVQKV VTTTDIVIPG
     LNSSTDVQAR INAGESIHII RGTKGTYIRT SDGRIFAVRA TGKPKAPEDG RMAASGSQGP
     SLASTSNGRH SASSPKAPDP EGLARPVSPD SPEIISELQQ YADVAAARES RQSSPSISAA
     LPGPPGQLMD NSTIPGTALG TEPCLGGHCL NSSLLVTGQP SGGRHPVLDL RGHKRKLATP
     SVTQESIRRR SRKGHLPAPV QPYEHGYPVS GGFAMPPVSL NHNLTTPFTS QAGENSLFMG
     SNPSYYQLSN LLADARLVFP VTTDPLVPAG PVSSSSTATS VTASNPSFML NPSVPGMLPS
     YSLPFSQPLL SEPRMFAPFP SPGLPSNLSR GVSVYPGYMS PHAGYPAGGL LRSQVPPFDS
     HEVAEVGFSS NDDEDKDDDV IEVTGK
//
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