GenomeNet

Database: UniProt
Entry: Q8NHQ9
LinkDB: Q8NHQ9
Original site: Q8NHQ9 
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   13-NOV-2019, entry version 147.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   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.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   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.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., 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
RT   project: 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
RP   VARIANT 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.
RT   XVIII. The complete sequences of 100 new cDNA clones from brain which
RT   code for large proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION
RP   BY 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.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient 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
RP   BY 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
RP   BY 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation 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.,
RA   Buerckstuemmer T., 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
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome 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
RP   BY 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       Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-5459844, EBI-741181;
CC       P60410:KRTAP10-8; NbExp=3; IntAct=EBI-5459844, EBI-10171774;
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         Note=No experimental confirmation available.;
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC       subfamily. {ECO:0000305}.
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   SMR; Q8NHQ9; -.
DR   BioGrid; 121721; 40.
DR   IntAct; Q8NHQ9; 15.
DR   MINT; Q8NHQ9; -.
DR   STRING; 9606.ENSP00000238146; -.
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   Ensembl; ENST00000238146; ENSP00000238146; ENSG00000111364. [Q8NHQ9-1]
DR   Ensembl; ENST00000421670; ENSP00000442332; ENSG00000111364. [Q8NHQ9-2]
DR   GeneID; 57696; -.
DR   KEGG; hsa:57696; -.
DR   UCSC; uc001ufi.4; human. [Q8NHQ9-1]
DR   CTD; 57696; -.
DR   GeneCards; DDX55; -.
DR   HGNC; HGNC:20085; DDX55.
DR   HPA; HPA039962; -.
DR   HPA; HPA044101; -.
DR   neXtProt; NX_Q8NHQ9; -.
DR   OpenTargets; ENSG00000111364; -.
DR   PharmGKB; PA134984021; -.
DR   eggNOG; KOG0345; Eukaryota.
DR   eggNOG; ENOG410XNT7; LUCA.
DR   GeneTree; ENSGT00550000074969; -.
DR   HOGENOM; HOG000268803; -.
DR   InParanoid; Q8NHQ9; -.
DR   KO; K14809; -.
DR   OMA; RRHKETP; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q8NHQ9; -.
DR   TreeFam; TF314573; -.
DR   ChiTaRS; DDX55; human.
DR   GenomeRNAi; 57696; -.
DR   Pharos; Q8NHQ9; -.
DR   PRO; PR:Q8NHQ9; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000111364; Expressed in 185 organ(s), highest expression level in cerebellar hemisphere.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; Complete proteome; Helicase;
KW   Hydrolase; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW   Reference proteome; RNA-binding.
FT   CHAIN         1    600       ATP-dependent RNA helicase DDX55.
FT                                /FTId=PRO_0000252210.
FT   DOMAIN       40    223       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      254    402       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      53     60       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF         9     37       Q motif.
FT   MOTIF       171    174       DEAD box.
FT   COMPBIAS    487    568       Lys-rich.
FT   MOD_RES     544    544       Phosphoserine.
FT                                {ECO:0000244|PubMed:18220336,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     594    594       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   VAR_SEQ       1    393       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_056155.
FT   VARIANT     101    101       V -> L (in dbSNP:rs17881657).
FT                                /FTId=VAR_027789.
FT   VARIANT     154    154       E -> G (in dbSNP:rs17886035).
FT                                /FTId=VAR_027790.
FT   VARIANT     264    264       N -> S (in dbSNP:rs11057306).
FT                                {ECO:0000269|PubMed:17974005}.
FT                                /FTId=VAR_027791.
FT   VARIANT     556    556       N -> S (in dbSNP:rs10773019).
FT                                /FTId=VAR_027792.
FT   CONFLICT    130    134       FKQQG -> LSFQS (in Ref. 4; BAB13421).
FT                                {ECO:0000305}.
FT   CONFLICT    148    148       M -> L (in Ref. 2; AAH30020).
FT                                {ECO:0000305}.
FT   CONFLICT    286    286       A -> T (in Ref. 2; AAH30020).
FT                                {ECO:0000305}.
FT   CONFLICT    445    450       DLDFAS -> G (in Ref. 3; CAH56233).
FT                                {ECO:0000305}.
FT   CONFLICT    599    599       D -> G (in Ref. 2; AAH30020).
FT                                {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
//
DBGET integrated database retrieval system