DDX53_HUMAN
ID DDX53_HUMAN Reviewed; 631 AA.
AC Q86TM3; Q0D2N2; Q6NVV4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX53;
DE EC=3.6.4.13;
DE AltName: Full=Cancer-associated gene protein;
DE AltName: Full=Cancer/testis antigen 26;
DE Short=CT26;
DE AltName: Full=DEAD box protein 53;
DE AltName: Full=DEAD box protein CAGE;
GN Name=DDX53; Synonyms=CAGE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11922625; DOI=10.1006/bbrc.2002.6701;
RA Cho B., Lim Y., Lee D.Y., Park S.Y., Lee H., Kim W.H., Yang H., Bang Y.J.,
RA Jeoung D.I.;
RT "Identification and characterization of a novel cancer/testis antigen gene
RT CAGE.";
RL Biochem. Biophys. Res. Commun. 292:715-726(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 204-430 IN COMPLEX WITH AMP.
RX PubMed=20941364; DOI=10.1371/journal.pone.0012791;
RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M.,
RA Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M.,
RA Thorsell A.G., Schuler H.;
RT "Comparative structural analysis of human DEAD-box RNA helicases.";
RL PLoS ONE 5:E12791-E12791(2010).
RN [4]
RP VARIANT THR-141.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11922625}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. Wide expression in various
CC cancer tissues and cancer cell lines. {ECO:0000269|PubMed:11922625}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR EMBL; AY039237; AAK72102.1; -; mRNA.
DR EMBL; BC051703; AAH51703.1; -; mRNA.
DR EMBL; BC067878; AAH67878.1; -; mRNA.
DR CCDS; CCDS35214.1; -.
DR PIR; JC7831; JC7831.
DR RefSeq; NP_874358.2; NM_182699.3.
DR PDB; 3IUY; X-ray; 2.40 A; A/B=204-430.
DR PDBsum; 3IUY; -.
DR AlphaFoldDB; Q86TM3; -.
DR SMR; Q86TM3; -.
DR BioGRID; 127960; 5.
DR IntAct; Q86TM3; 1.
DR STRING; 9606.ENSP00000368667; -.
DR iPTMnet; Q86TM3; -.
DR PhosphoSitePlus; Q86TM3; -.
DR BioMuta; DDX53; -.
DR DMDM; 143811384; -.
DR EPD; Q86TM3; -.
DR MassIVE; Q86TM3; -.
DR PaxDb; Q86TM3; -.
DR PeptideAtlas; Q86TM3; -.
DR PRIDE; Q86TM3; -.
DR ProteomicsDB; 69712; -.
DR Antibodypedia; 563; 158 antibodies from 24 providers.
DR DNASU; 168400; -.
DR Ensembl; ENST00000327968.7; ENSP00000368667.2; ENSG00000184735.7.
DR GeneID; 168400; -.
DR KEGG; hsa:168400; -.
DR MANE-Select; ENST00000327968.7; ENSP00000368667.2; NM_182699.4; NP_874358.2.
DR UCSC; uc004daj.4; human.
DR CTD; 168400; -.
DR DisGeNET; 168400; -.
DR GeneCards; DDX53; -.
DR HGNC; HGNC:20083; DDX53.
DR HPA; ENSG00000184735; Group enriched (brain, testis).
DR MIM; 301079; gene.
DR neXtProt; NX_Q86TM3; -.
DR OpenTargets; ENSG00000184735; -.
DR PharmGKB; PA134863598; -.
DR VEuPathDB; HostDB:ENSG00000184735; -.
DR eggNOG; KOG0336; Eukaryota.
DR GeneTree; ENSGT00940000167221; -.
DR HOGENOM; CLU_003041_16_8_1; -.
DR InParanoid; Q86TM3; -.
DR OMA; MAEQYKL; -.
DR OrthoDB; 471730at2759; -.
DR PhylomeDB; Q86TM3; -.
DR TreeFam; TF312949; -.
DR PathwayCommons; Q86TM3; -.
DR SignaLink; Q86TM3; -.
DR BioGRID-ORCS; 168400; 14 hits in 697 CRISPR screens.
DR EvolutionaryTrace; Q86TM3; -.
DR GenomeRNAi; 168400; -.
DR Pharos; Q86TM3; Tbio.
DR PRO; PR:Q86TM3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q86TM3; protein.
DR Bgee; ENSG00000184735; Expressed in sperm and 12 other tissues.
DR Genevisible; Q86TM3; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR Gene3D; 3.30.1370.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00013; KH_1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..631
FT /note="Probable ATP-dependent RNA helicase DDX53"
FT /id="PRO_0000054973"
FT DOMAIN 48..109
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 253..428
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 440..601
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 222..250
FT /note="Q motif"
FT MOTIF 376..379
FT /note="DEAD box"
FT BINDING 244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 268..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT VARIANT 62
FT /note="V -> A (in dbSNP:rs4412516)"
FT /id="VAR_052168"
FT VARIANT 141
FT /note="N -> T (found in a renal cell carcinoma case;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064707"
FT VARIANT 381
FT /note="M -> I (in dbSNP:rs5925720)"
FT /id="VAR_052169"
FT VARIANT 391
FT /note="R -> M (in dbSNP:rs5926203)"
FT /id="VAR_052170"
FT CONFLICT 243
FT /note="V -> L (in Ref. 2; AAH67878)"
FT /evidence="ECO:0000305"
FT CONFLICT 557..569
FT /note="YIGRTGKTGTSVT -> SLDGQERLHISS (in Ref. 1; AAK72102)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="K -> E (in Ref. 2; AAH67878)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="Q -> R (in Ref. 2; AAH51703)"
FT /evidence="ECO:0000305"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3IUY"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3IUY"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:3IUY"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:3IUY"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:3IUY"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:3IUY"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:3IUY"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:3IUY"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:3IUY"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:3IUY"
FT HELIX 339..343
FT /evidence="ECO:0007829|PDB:3IUY"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:3IUY"
FT HELIX 353..361
FT /evidence="ECO:0007829|PDB:3IUY"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:3IUY"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:3IUY"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:3IUY"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:3IUY"
FT HELIX 412..419
FT /evidence="ECO:0007829|PDB:3IUY"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:3IUY"
SQ SEQUENCE 631 AA; 71154 MW; 27E72027AADAA193 CRC64;
MSHWAPEWKR AEANPRDLGA SWDVRGSRGS GWSGPFGHQG PRAAGSREPP LCFKIKNNMV
GVVIGYSGSK IKDLQHSTNT KIQIINGESE AKVRIFGNRE MKAKAKAAIE TLIRKQESYN
SESSVDNAAS QTPIGRNLGR NDIVGEAEPL SNWDRIRAAV VECEKRKWAD LPPVKKNFYI
ESKATSCMSE MQVINWRKEN FNITCDDLKS GEKRLIPKPT CRFKDAFQQY PDLLKSIIRV
GIVKPTPIQS QAWPIILQGI DLIVVAQTGT GKTLSYLMPG FIHLDSQPIS REQRNGPGML
VLTPTRELAL HVEAECSKYS YKGLKSICIY GGRNRNGQIE DISKGVDIII ATPGRLNDLQ
MNNSVNLRSI TYLVIDEADK MLDMEFEPQI RKILLDVRPD RQTVMTSATW PDTVRQLALS
YLKDPMIVYV GNLNLVAVNT VKQNIIVTTE KEKRALTQEF VENMSPNDKV IMFVSQKHIA
DDLSSDFNIQ GISAESLHGN SEQSDQERAV EDFKSGNIKI LITTDIVSRG LDLNDVTHVY
NYDFPRNIDV YVHRVGYIGR TGKTGTSVTL ITQRDSKMAG ELIKILDRAN QSVPEDLVVM
AEQYKLNQQK RHRETRSRKP GQRRKEFYFL S
