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Q8TDD1 (DDX54_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent RNA helicase DDX54

EC=3.6.4.13
Alternative name(s):
ATP-dependent RNA helicase DP97
DEAD box RNA helicase 97 kDa
DEAD box protein 54
Gene names
Name:DDX54
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length881 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has RNA-dependent ATPase activity. Represses the transcriptional activity of nuclear receptors. Ref.3

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Interacts in a hormone-dependent manner with nuclear receptors.

Subcellular location

Nucleusnucleolus Ref.5.

Sequence similarities

Belongs to the DEAD box helicase family. DDX54/DBP10 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence AAN59978.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.3. Source: GOC

RNA metabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

RNA processing

Inferred from direct assay Ref.3. Source: UniProtKB

intracellular estrogen receptor signaling pathway

Traceable author statement Ref.3. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from direct assay Ref.3. Source: UniProtKB

nucleus

Inferred from direct assay Ref.3. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent RNA helicase activity

Inferred from direct assay Ref.3. Source: UniProtKB

estrogen receptor binding

Inferred from direct assay Ref.3. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

receptor binding

Inferred from direct assay Ref.3. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TDD1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8TDD1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     804-804: Q → QA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 881881ATP-dependent RNA helicase DDX54
PRO_0000055056

Regions

Domain127 – 299173Helicase ATP-binding
Domain326 – 473148Helicase C-terminal
Nucleotide binding140 – 1478ATP By similarity
Region605 – 64743Interaction with nuclear receptors
Motif96 – 12429Q motif
Motif247 – 2504DEAD box

Amino acid modifications

Modified residue341Phosphoserine Ref.7 Ref.9
Modified residue391Phosphoserine Ref.9 Ref.12
Modified residue411Phosphoserine Ref.9 Ref.12
Modified residue751Phosphoserine Ref.7
Modified residue6441Phosphoserine Ref.7
Modified residue6961Phosphoserine Ref.10
Modified residue6981Phosphoserine Ref.10
Modified residue7821Phosphoserine Ref.6 Ref.7 Ref.9 Ref.10 Ref.12
Modified residue7881Phosphoserine Ref.7

Natural variations

Alternative sequence8041Q → QA in isoform 2.
VSP_040135
Natural variant5701R → H.
Corresponds to variant rs35519289 [ dbSNP | Ensembl ].
VAR_052171
Natural variant6931R → Q.
Corresponds to variant rs11564 [ dbSNP | Ensembl ].
VAR_052172
Natural variant7121V → A.
Corresponds to variant rs10354 [ dbSNP | Ensembl ].
VAR_052173
Natural variant8211P → L.
Corresponds to variant rs1048889 [ dbSNP | Ensembl ].
VAR_033860

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 26, 2004. Version 2.
Checksum: 9823C75156D998C4

FASTA88198,595
        10         20         30         40         50         60 
MAADKGPAAG PRSRAAMAQW RKKKGLRKRR GAASQARGSD SEDGEFEIQA EDDARARKLG 

        70         80         90        100        110        120 
PGRPLPTFPT SECTSDVEPD TREMVRAQNK KKKKSGGFQS MGLSYPVFKG IMKKGYKVPT 

       130        140        150        160        170        180 
PIQRKTIPVI LDGKDVVAMA RTGSGKTACF LLPMFERLKT HSAQTGARAL ILSPTRELAL 

       190        200        210        220        230        240 
QTLKFTKELG KFTGLKTALI LGGDRMEDQF AALHENPDII IATPGRLVHV AVEMSLKLQS 

       250        260        270        280        290        300 
VEYVVFDEAD RLFEMGFAEQ LQEIIARLPG GHQTVLFSAT LPKLLVEFAR AGLTEPVLIR 

       310        320        330        340        350        360 
LDVDTKLNEQ LKTSFFLVRE DTKAAVLLHL LHNVVRPQDQ TVVFVATKHH AEYLTELLTT 

       370        380        390        400        410        420 
QRVSCAHIYS ALDPTARKIN LAKFTLGKCS TLIVTDLAAR GLDIPLLDNV INYSFPAKGK 

       430        440        450        460        470        480 
LFLHRVGRVA RAGRSGTAYS LVAPDEIPYL LDLHLFLGRS LTLARPLKEP SGVAGVDGML 

       490        500        510        520        530        540 
GRVPQSVVDE EDSGLQSTLE ASLELRGLAR VADNAQQQYV RSRPAPSPES IKRAKEMDLV 

       550        560        570        580        590        600 
GLGLHPLFSS RFEEEELQRL RLVDSIKNYR SRATIFEINA SSRDLCSQVM RAKRQKDRKA 

       610        620        630        640        650        660 
IARFQQGQQG RQEQQEGPVG PAPSRPALQE KQPEKEEEEE AGESVEDIFS EVVGRKRQRS 

       670        680        690        700        710        720 
GPNRGAKRRR EEARQRDQEF YIPYRPKDFD SERGLSISGE GGAFEQQAAG AVLDLMGDEA 

       730        740        750        760        770        780 
QNLTRGRQQL KWDRKKKRFV GQSGQEDKKK IKTESGRYIS SSYKRDLYQK WKQKQKIDDR 

       790        800        810        820        830        840 
DSDEEGASDR RGPERRGGKR DRGQGASRPH APGTPAGRVR PELKTKQQIL KQRRRAQKLH 

       850        860        870        880 
FLQRGGLKQL SARNRRRVQE LQQGAFGRGA RSKKGKMRKR M 

« Hide

Isoform 2 [UniParc].

Checksum: 947F50470F865F96
Show »

FASTA88298,666

References

« Hide 'large scale' references
[1]"Positional cloning of the Flv gene."
Perelygin A.A.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Placenta.
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Regulation of nuclear receptor transcriptional activity by a novel DEAD box RNA helicase (DP97)."
Rajendran R.R., Nye A.C., Frasor J., Balsara R.D., Martini P.G., Katzenellenbogen B.S.
J. Biol. Chem. 278:4628-4638(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-881 (ISOFORM 1), FUNCTION.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-881 (ISOFORM 1).
Tissue: Kidney.
[5]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-75; SER-644; SER-782 AND SER-788, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-39; SER-41 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-698 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-41 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF478457 mRNA. Translation: AAL85336.1.
AC089999 Genomic DNA. No translation available.
AY148094 mRNA. Translation: AAN59978.1. Sequence problems.
BC005848 mRNA. Translation: AAH05848.2.
CCDSCCDS31907.1. [Q8TDD1-1]
CCDS44984.1. [Q8TDD1-2]
RefSeqNP_001104792.1. NM_001111322.1. [Q8TDD1-2]
NP_076977.3. NM_024072.3. [Q8TDD1-1]
UniGeneHs.506861.

3D structure databases

ProteinModelPortalQ8TDD1.
SMRQ8TDD1. Positions 98-470.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122503. 19 interactions.
IntActQ8TDD1. 6 interactions.
MINTMINT-3045390.
STRING9606.ENSP00000323858.

PTM databases

PhosphoSiteQ8TDD1.

Polymorphism databases

DMDM46576615.

2D gel databases

SWISS-2DPAGEQ8TDD1.

Proteomic databases

MaxQBQ8TDD1.
PaxDbQ8TDD1.
PRIDEQ8TDD1.

Protocols and materials databases

DNASU79039.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306014; ENSP00000304072; ENSG00000123064. [Q8TDD1-1]
ENST00000314045; ENSP00000323858; ENSG00000123064. [Q8TDD1-2]
GeneID79039.
KEGGhsa:79039.
UCSCuc001tup.3. human. [Q8TDD1-1]
uc001tuq.4. human. [Q8TDD1-2]

Organism-specific databases

CTD79039.
GeneCardsGC12M113598.
HGNCHGNC:20084. DDX54.
HPAHPA028244.
MIM611665. gene.
neXtProtNX_Q8TDD1.
PharmGKBPA134992026.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000246455.
HOVERGENHBG051333.
InParanoidQ8TDD1.
KOK14808.
OMAENVVNYD.
OrthoDBEOG786H2W.
PhylomeDBQ8TDD1.
TreeFamTF105707.

Gene expression databases

ArrayExpressQ8TDD1.
BgeeQ8TDD1.
CleanExHS_DDX54.
GenevestigatorQ8TDD1.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR012541. DBP10CT.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF08147. DBP10CT. 1 hit.
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
ProDomPD024971. DBP10CT. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDDX54. human.
GenomeRNAi79039.
NextBio67773.
PROQ8TDD1.
SOURCESearch...

Entry information

Entry nameDDX54_HUMAN
AccessionPrimary (citable) accession number: Q8TDD1
Secondary accession number(s): Q86YT8, Q9BRZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM