DDX55_HUMAN
ID DDX55_HUMAN Reviewed; 600 AA.
AC Q8NHQ9; Q658L6; Q8IYH0; Q9HCH7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=ATP-dependent RNA helicase DDX55;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 55;
GN Name=DDX55; Synonyms=KIAA1595;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-532 (ISOFORM 1), AND VARIANT
RP SER-264.
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-600 (ISOFORM 1).
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-594, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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 -!- INTERACTION:
CC Q8NHQ9; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-5459844, EBI-741181;
CC Q8NHQ9; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-5459844, EBI-10171774;
CC Q8NHQ9; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5459844, EBI-79165;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NHQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NHQ9-2; Sequence=VSP_056155;
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC subfamily. {ECO:0000305}.
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DR EMBL; AC055713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030020; AAH30020.1; -; mRNA.
DR EMBL; BC035911; AAH35911.1; -; mRNA.
DR EMBL; AL833756; CAH56233.1; -; mRNA.
DR EMBL; AB046815; BAB13421.1; -; mRNA.
DR CCDS; CCDS9251.1; -. [Q8NHQ9-1]
DR RefSeq; NP_065987.1; NM_020936.2. [Q8NHQ9-1]
DR AlphaFoldDB; Q8NHQ9; -.
DR SMR; Q8NHQ9; -.
DR BioGRID; 121721; 178.
DR IntAct; Q8NHQ9; 17.
DR MINT; Q8NHQ9; -.
DR STRING; 9606.ENSP00000238146; -.
DR GlyGen; Q8NHQ9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NHQ9; -.
DR PhosphoSitePlus; Q8NHQ9; -.
DR BioMuta; DDX55; -.
DR DMDM; 296439376; -.
DR EPD; Q8NHQ9; -.
DR jPOST; Q8NHQ9; -.
DR MassIVE; Q8NHQ9; -.
DR MaxQB; Q8NHQ9; -.
DR PaxDb; Q8NHQ9; -.
DR PeptideAtlas; Q8NHQ9; -.
DR PRIDE; Q8NHQ9; -.
DR ProteomicsDB; 71173; -.
DR ProteomicsDB; 73741; -. [Q8NHQ9-1]
DR Antibodypedia; 19284; 169 antibodies from 25 providers.
DR DNASU; 57696; -.
DR Ensembl; ENST00000238146.9; ENSP00000238146.3; ENSG00000111364.16. [Q8NHQ9-1]
DR Ensembl; ENST00000421670.3; ENSP00000442332.1; ENSG00000111364.16. [Q8NHQ9-2]
DR GeneID; 57696; -.
DR KEGG; hsa:57696; -.
DR MANE-Select; ENST00000238146.9; ENSP00000238146.3; NM_020936.3; NP_065987.1.
DR UCSC; uc001ufi.4; human. [Q8NHQ9-1]
DR CTD; 57696; -.
DR GeneCards; DDX55; -.
DR HGNC; HGNC:20085; DDX55.
DR HPA; ENSG00000111364; Low tissue specificity.
DR neXtProt; NX_Q8NHQ9; -.
DR OpenTargets; ENSG00000111364; -.
DR PharmGKB; PA134984021; -.
DR VEuPathDB; HostDB:ENSG00000111364; -.
DR eggNOG; KOG0331; Eukaryota.
DR eggNOG; KOG0345; Eukaryota.
DR GeneTree; ENSGT00550000074969; -.
DR HOGENOM; CLU_003041_26_4_1; -.
DR InParanoid; Q8NHQ9; -.
DR OMA; DRAIHDK; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q8NHQ9; -.
DR TreeFam; TF314573; -.
DR PathwayCommons; Q8NHQ9; -.
DR SignaLink; Q8NHQ9; -.
DR BioGRID-ORCS; 57696; 546 hits in 1075 CRISPR screens.
DR ChiTaRS; DDX55; human.
DR GenomeRNAi; 57696; -.
DR Pharos; Q8NHQ9; Tdark.
DR PRO; PR:Q8NHQ9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8NHQ9; protein.
DR Bgee; ENSG00000111364; Expressed in sural nerve and 166 other tissues.
DR ExpressionAtlas; Q8NHQ9; baseline and differential.
DR Genevisible; Q8NHQ9; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 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 Alternative splicing; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..600
FT /note="ATP-dependent RNA helicase DDX55"
FT /id="PRO_0000252210"
FT DOMAIN 40..223
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 254..402
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 500..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..37
FT /note="Q motif"
FT MOTIF 171..174
FT /note="DEAD box"
FT COMPBIAS 500..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..534
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..393
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056155"
FT VARIANT 101
FT /note="V -> L (in dbSNP:rs17881657)"
FT /id="VAR_027789"
FT VARIANT 154
FT /note="E -> G (in dbSNP:rs17886035)"
FT /id="VAR_027790"
FT VARIANT 264
FT /note="N -> S (in dbSNP:rs11057306)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_027791"
FT VARIANT 556
FT /note="N -> S (in dbSNP:rs10773019)"
FT /id="VAR_027792"
FT CONFLICT 130..134
FT /note="FKQQG -> LSFQS (in Ref. 4; BAB13421)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="M -> L (in Ref. 2; AAH30020)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> T (in Ref. 2; AAH30020)"
FT /evidence="ECO:0000305"
FT CONFLICT 445..450
FT /note="DLDFAS -> G (in Ref. 3; CAH56233)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="D -> G (in Ref. 2; AAH30020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 68547 MW; D696ABBED51B370B CRC64;
MEHVTEGSWE SLPVPLHPQV LGALRELGFP YMTPVQSATI PLFMRNKDVA AEAVTGSGKT
LAFVIPILEI LLRREEKLKK SQVGAIIITP TRELAIQIDE VLSHFTKHFP EFSQILWIGG
RNPGEDVERF KQQGGNIIVA TPGRLEDMFR RKAEGLDLAS CVRSLDVLVL DEADRLLDMG
FEASINTILE FLPKQRRTGL FSATQTQEVE NLVRAGLRNP VRVSVKEKGV AASSAQKTPS
RLENYYMVCK ADEKFNQLVH FLRNHKQEKH LVFFSTCACV EYYGKALEVL VKGVKIMCIH
GKMKYKRNKI FMEFRKLQSG ILVCTDVMAR GIDIPEVNWV LQYDPPSNAS AFVHRCGRTA
RIGHGGSALV FLLPMEESYI NFLAINQKCP LQEMKPQRNT ADLLPKLKSM ALADRAVFEK
GMKAFVSYVQ AYAKHECNLI FRLKDLDFAS LARGFALLRM PKMPELRGKQ FPDFVPVDVN
TDTIPFKDKI REKQRQKLLE QQRREKTENE GRRKFIKNKA WSKQKAKKEK KKKMNEKRKR
EEGSDIEDED MEELLNDTRL LKKLKKGKIT EEEFEKGLLT TGKRTIKTVD LGISDLEDDC
