DDX52_HUMAN
ID DDX52_HUMAN Reviewed; 599 AA.
AC Q9Y2R4; Q86YG1; Q8N213; Q9NVE0; Q9Y482;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX52;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase ROK1-like;
DE AltName: Full=DEAD box protein 52;
GN Name=DDX52; Synonyms=ROK1; ORFNames=HUSSY-19;
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].
RA Mao M., Liu T., Zhang J., Zhang Q., Fu G., Zhou J., Wu J., Shen Y., Yu M.,
RA Ye M., Chen S., Chen Z.;
RT "Human putative ATP-dependent RNA helicase rok1 mRNA.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 180-599.
RC TISSUE=Liver, and Spleen;
RX PubMed=11124703;
RX DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h;
RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N.,
RA Zimbello R., Lanfranchi G., Valle G.;
RT "Characterization of 16 novel human genes showing high similarity to yeast
RT sequences.";
RL Yeast 18:69-80(2001).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-15, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 139-381 IN COMPLEX WITH ADP.
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).
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, nucleolus {ECO:0000269|PubMed:12429849}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX52/ROK1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27766.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AK093661; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAA91812.1; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305};
CC Sequence=CAA09374.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF077033; AAD27766.1; ALT_FRAME; mRNA.
DR EMBL; AK001652; BAA91812.1; ALT_SEQ; mRNA.
DR EMBL; AK093661; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC091199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041785; AAH41785.1; -; mRNA.
DR EMBL; AJ010840; CAA09374.1; ALT_FRAME; mRNA.
DR CCDS; CCDS11323.1; -.
DR RefSeq; NP_001278405.1; NM_001291476.1.
DR RefSeq; NP_008941.3; NM_007010.4.
DR PDB; 3DKP; X-ray; 2.10 A; A=139-381.
DR PDBsum; 3DKP; -.
DR AlphaFoldDB; Q9Y2R4; -.
DR BioGRID; 116241; 188.
DR IntAct; Q9Y2R4; 50.
DR MINT; Q9Y2R4; -.
DR STRING; 9606.ENSP00000479504; -.
DR iPTMnet; Q9Y2R4; -.
DR PhosphoSitePlus; Q9Y2R4; -.
DR SwissPalm; Q9Y2R4; -.
DR BioMuta; DDX52; -.
DR DMDM; 296439375; -.
DR SWISS-2DPAGE; Q9Y2R4; -.
DR EPD; Q9Y2R4; -.
DR jPOST; Q9Y2R4; -.
DR MassIVE; Q9Y2R4; -.
DR MaxQB; Q9Y2R4; -.
DR PaxDb; Q9Y2R4; -.
DR PeptideAtlas; Q9Y2R4; -.
DR PRIDE; Q9Y2R4; -.
DR ProteomicsDB; 85879; -.
DR Antibodypedia; 74465; 117 antibodies from 23 providers.
DR DNASU; 11056; -.
DR Ensembl; ENST00000615769.2; ENSP00000480030.1; ENSG00000277594.2.
DR Ensembl; ENST00000617633.5; ENSP00000479504.1; ENSG00000278053.5.
DR GeneID; 11056; -.
DR KEGG; hsa:11056; -.
DR MANE-Select; ENST00000617633.5; ENSP00000479504.1; NM_007010.5; NP_008941.3.
DR UCSC; uc002hoi.3; human.
DR CTD; 11056; -.
DR DisGeNET; 11056; -.
DR GeneCards; DDX52; -.
DR HGNC; HGNC:20038; DDX52.
DR HPA; ENSG00000278053; Low tissue specificity.
DR MIM; 612500; gene.
DR neXtProt; NX_Q9Y2R4; -.
DR OpenTargets; ENSG00000278053; -.
DR PharmGKB; PA134904836; -.
DR VEuPathDB; HostDB:ENSG00000278053; -.
DR eggNOG; KOG0344; Eukaryota.
DR GeneTree; ENSGT00550000074863; -.
DR HOGENOM; CLU_003041_1_4_1; -.
DR InParanoid; Q9Y2R4; -.
DR OrthoDB; 400908at2759; -.
DR PhylomeDB; Q9Y2R4; -.
DR TreeFam; TF314448; -.
DR PathwayCommons; Q9Y2R4; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9Y2R4; -.
DR BioGRID-ORCS; 11056; 499 hits in 1044 CRISPR screens.
DR ChiTaRS; DDX52; human.
DR EvolutionaryTrace; Q9Y2R4; -.
DR GeneWiki; DDX52; -.
DR GenomeRNAi; 11056; -.
DR Pharos; Q9Y2R4; Tbio.
DR PRO; PR:Q9Y2R4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y2R4; protein.
DR Bgee; ENSG00000278053; Expressed in sural nerve and 106 other tissues.
DR ExpressionAtlas; Q9Y2R4; baseline and differential.
DR Genevisible; Q9Y2R4; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR CDD; cd17957; DEADc_DDX52; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044764; DDX52/Rok1_DEADc.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..599
FT /note="Probable ATP-dependent RNA helicase DDX52"
FT /id="PRO_0000055060"
FT DOMAIN 196..374
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 385..546
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 59..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 165..193
FT /note="Q motif"
FT MOTIF 318..321
FT /note="DEAD box"
FT COMPBIAS 68..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 209..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 403
FT /note="V -> M (in dbSNP:rs7216445)"
FT /id="VAR_060235"
FT CONFLICT 299
FT /note="L -> S (in Ref. 2; AK093661)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="K -> R (in Ref. 2; BAA91812)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="V -> F (in Ref. 4; CAA09374)"
FT /evidence="ECO:0000305"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:3DKP"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:3DKP"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:3DKP"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:3DKP"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:3DKP"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3DKP"
FT HELIX 215..227
FT /evidence="ECO:0007829|PDB:3DKP"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:3DKP"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:3DKP"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:3DKP"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3DKP"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:3DKP"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3DKP"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:3DKP"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:3DKP"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:3DKP"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:3DKP"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:3DKP"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:3DKP"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:3DKP"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:3DKP"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3DKP"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:3DKP"
SQ SEQUENCE 599 AA; 67466 MW; 0EA504577A8BB7DB CRC64;
MDVHDLFRRL GAGAKFDTRR FSADAARFQI GKRKYDFDSS EVLQGLDFFG NKKSVPGVCG
ASQTHQKPQN GEKKEESLTE RKREQSKKKR KTMTSEIASQ EEGATIQWMS SVEAKIEDKK
VQRESKLTSG KLENLRKEKI NFLRNKHKIH VQGTDLPDPI ATFQQLDQEY KINSRLLQNI
LDAGFQMPTP IQMQAIPVML HGRELLASAP TGSGKTLAFS IPILMQLKQP ANKGFRALII
SPTRELASQI HRELIKISEG TGFRIHMIHK AAVAAKKFGP KSSKKFDILV TTPNRLIYLL
KQDPPGIDLA SVEWLVVDES DKLFEDGKTG FRDQLASIFL ACTSHKVRRA MFSATFAYDV
EQWCKLNLDN VISVSIGARN SAVETVEQEL LFVGSETGKL LAVRELVKKG FNPPVLVFVQ
SIERAKELFH ELIYEGINVD VIHAERTQQQ RDNTVHSFRA GKIWVLICTA LLARGIDFKG
VNLVINYDFP TSSVEYIHRI GRTGRAGNKG KAITFFTEDD KPLLRSVANV IQQAGCPVPE
YIKGFQKLLS KQKKKMIKKP LERESISTTP KCFLEKAKDK QKKVTGQNSK KKVALEDKS
