DHX57_MOUSE
ID DHX57_MOUSE Reviewed; 1388 AA.
AC Q6P5D3; Q3TS93; Q6NZK4; Q6P1B4; Q8BI63; Q8BIA2; Q8R360;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Putative ATP-dependent RNA helicase DHX57;
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 57;
GN Name=Dhx57;
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 3; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Eye, and Urinary bladder;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Spleen;
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: Probable ATP-binding RNA helicase.
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=3.6.4.13;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6P5D3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P5D3-2; Sequence=VSP_018063;
CC Name=3;
CC IsoId=Q6P5D3-3; Sequence=VSP_018065, VSP_018066;
CC Name=4;
CC IsoId=Q6P5D3-4; Sequence=VSP_018062, VSP_018064;
CC Name=5;
CC IsoId=Q6P5D3-5; Sequence=VSP_018061;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {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; AK035344; BAC29042.1; -; mRNA.
DR EMBL; AK053628; BAC35451.1; -; mRNA.
DR EMBL; AK162192; BAE36782.1; -; mRNA.
DR EMBL; BC026474; AAH26474.1; -; mRNA.
DR EMBL; BC062952; AAH62952.1; -; mRNA.
DR EMBL; BC065169; AAH65169.1; -; mRNA.
DR EMBL; BC066091; AAH66091.1; -; mRNA.
DR CCDS; CCDS28990.1; -. [Q6P5D3-2]
DR CCDS; CCDS50188.1; -. [Q6P5D3-1]
DR RefSeq; NP_001157231.1; NM_001163759.1. [Q6P5D3-1]
DR RefSeq; NP_945180.2; NM_198942.2. [Q6P5D3-2]
DR RefSeq; XP_006523510.1; XM_006523447.1. [Q6P5D3-1]
DR RefSeq; XP_006523511.1; XM_006523448.1. [Q6P5D3-2]
DR RefSeq; XP_017172691.1; XM_017317202.1.
DR AlphaFoldDB; Q6P5D3; -.
DR SMR; Q6P5D3; -.
DR BioGRID; 223127; 5.
DR IntAct; Q6P5D3; 1.
DR MINT; Q6P5D3; -.
DR STRING; 10090.ENSMUSP00000083742; -.
DR iPTMnet; Q6P5D3; -.
DR PhosphoSitePlus; Q6P5D3; -.
DR EPD; Q6P5D3; -.
DR MaxQB; Q6P5D3; -.
DR PaxDb; Q6P5D3; -.
DR PeptideAtlas; Q6P5D3; -.
DR PRIDE; Q6P5D3; -.
DR ProteomicsDB; 279767; -. [Q6P5D3-1]
DR ProteomicsDB; 279768; -. [Q6P5D3-2]
DR ProteomicsDB; 279769; -. [Q6P5D3-3]
DR ProteomicsDB; 279770; -. [Q6P5D3-4]
DR ProteomicsDB; 279771; -. [Q6P5D3-5]
DR Antibodypedia; 29537; 60 antibodies from 16 providers.
DR DNASU; 106794; -.
DR Ensembl; ENSMUST00000038166; ENSMUSP00000041069; ENSMUSG00000035051. [Q6P5D3-2]
DR Ensembl; ENSMUST00000086555; ENSMUSP00000083742; ENSMUSG00000035051. [Q6P5D3-1]
DR GeneID; 106794; -.
DR KEGG; mmu:106794; -.
DR UCSC; uc008dqx.2; mouse. [Q6P5D3-5]
DR UCSC; uc008dqy.2; mouse. [Q6P5D3-4]
DR UCSC; uc008dqz.2; mouse. [Q6P5D3-2]
DR UCSC; uc008dra.2; mouse. [Q6P5D3-1]
DR UCSC; uc008drb.1; mouse. [Q6P5D3-3]
DR CTD; 90957; -.
DR MGI; MGI:2147067; Dhx57.
DR VEuPathDB; HostDB:ENSMUSG00000035051; -.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000156883; -.
DR HOGENOM; CLU_001832_4_1_1; -.
DR InParanoid; Q6P5D3; -.
DR OMA; PKCRFAH; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; Q6P5D3; -.
DR TreeFam; TF324744; -.
DR BioGRID-ORCS; 106794; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Dhx57; mouse.
DR PRO; PR:Q6P5D3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6P5D3; protein.
DR Bgee; ENSMUSG00000035051; Expressed in saccule of membranous labyrinth and 243 other tissues.
DR Genevisible; Q6P5D3; MM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd14317; UBA_DHX57; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR042615; DHX57_UBA.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..1388
FT /note="Putative ATP-dependent RNA helicase DHX57"
FT /id="PRO_0000233152"
FT DOMAIN 175..220
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 555..722
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 832..1012
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 299..326
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 669..672
FT /note="DEVH box"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 568..575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P158"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P158"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P158"
FT VAR_SEQ 1..1160
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018061"
FT VAR_SEQ 1..1000
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018062"
FT VAR_SEQ 77..129
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018063"
FT VAR_SEQ 1001..1006
FT /note="LEQLCL -> MILFFF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018064"
FT VAR_SEQ 1008..1025
FT /note="IKILEMFSTHNLQSVFSR -> LCPSGPPSACLGPAPPPI (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018065"
FT VAR_SEQ 1026..1388
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018066"
FT CONFLICT 488
FT /note="A -> T (in Ref. 2; AAH66091)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="S -> P (in Ref. 2; AAH62952)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="A -> T (in Ref. 2; AAH66091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1137
FT /note="T -> A (in Ref. 1; BAC29042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1388 AA; 155762 MW; D3E57C648E53A805 CRC64;
MSSSVRRKGK PGKGDGKGSS RGGRGGKGHM NKSHGGGGGG GGSCGGGGGG SRKASNRIWD
DGDDFCVFTE PKRPSRPCDS NKSKGETRPK WKPKAKVPLQ TLHMTSENQE KVKALLRDLQ
EQGADAGSER GTSGEEEDSE PQCGEEQGWP AGQEPIFLPD CSPWEYIGPE EVEPPVPECA
VSPLAVQKLS RYGFHTEHCQ LALRICDGDL GAALEHLLRQ CFSETFGERM ALSEAAVYVS
LNECVEQRQE ETLALKSICG EKFIERIQNR VWTIGLELDY LTNKFCKSKQ KESSKNVRDT
SPETCKFYLK GNCKFGSKCK FKHEVPPHQM IGRAERNVND PHLDADDDTT FMYELQIRFS
KDHKYPYQAP LVAFYSTNEN LPLACRLHIS EFLYGKALEF AKTSEPVVYS LITLLEEESE
IVKLLTHTQH KYSVPPVNVP PVPSETRISK PAYRKPVVPS NTFLSNQMLE GERLSELEED
ADEDEGPASI IVENESYVNL KKRSYKRYDR PAKSLFAENS KICRQFQMKQ ASRQFHAILQ
ERQLLPAWEE RETILKLLSK HQVVVISGMT GCGKTTQIPQ FILDNSLNGP PERVANIICT
QPRRISAISV AERVAKERAE RVGLTVGYQI RLESVKSSAT RLLYCTTGVL LRRLEGDATL
QGVTHIIVDE VHERTEESDF LLLVLKDIVM QRATLQVILM SATLDAGLFS KYFSYCPVIT
IPGRAFPVDQ FFLEDALAVT RYVLQDGSPY MRSMKQIAKE KLKARHNRTA QEEVEEDLRL
SLHLQDEEES VKDTIPDQQL DFKQLLIRYK GVSKSVIKTM SVMDFEKVNL ELIEALLEWI
VDGKHAYPPG AVLVFLPGLA EIKMLYEQLQ SNSLFNNRRS HRCVIHPLHS SLSSEEQQAV
FVKPPMGVTK IIISTNIAET SITIDDVVYV IDSGKMKEKR YDAGKGMESL EDTFVSQANA
LQRKGRAGRV ASGVCFHLFT SHHYNHQLLK QQLPEIQRVP LEQLCLRIKI LEMFSTHNLQ
SVFSRLIEPP HIDSLRASKV RLRDLGALTP DEKLTPLGYH LASLPVDVRI GKLMLLGSIF
RCLDPALTIA ASLAFKSPFV SPWDKKEEAN QKKLEFAFAN SDYLALLCAY KGWQLSTKES
ARASYNYCRQ NFLSGRTLQE MASLKRQFTE LLSDIGFVKE GLRAKEIEKR AQGGDGVLDA
TGEEANTNAE NPKLISAVLC AALYPNVVQV KTPEGKFQKT SSGVVRLQPK SAELKFVTKN
DGYVHIHPSS VNYQVRHFDS PYLLYHEKIK TSRVFIRDCS MVSVYPLVLF GGGQVNVQLQ
RGAFVVSLDD GWIRFVAASH QVAELVKELR CELDQLLQDK IKNPSMDLCS CPRGSRIISM
IVKLITTQ
