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ATP-dependent RNA helicase DDX1

 
Known also as: DEAD box protein 1, DEAD box protein retinoblastoma

Known abbreviations: DDX1, DBP-RB

 

FUNCTION:
 
Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation. Acts as a positive transcriptional regulator of cyclin CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates with chromatin at the NF-kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Required for HIV-1 Rev function as well as for HIV-1 replication. Binds to the RRE sequence of HIV-1 mRNAs. 
 
CATALYTIC ACTIVITY:
 
ATP + H2O = ADP + phosphate.
 
SUBUNIT STRUCTURE:
 
Interacts with PHF5A (via C-terminus) By similarity. Interacts with MBNL1. Interacts with CSTF2. Interacts with HNRNPK. Interacts with ATM. Interacts with RELA (via C-terminus). Interacts (via C-terminus) with the replicase polyprotein 1ab Nsp14 of the avian infectious bronchitis virus (IBV). Interacts with Rev of HIV-1. Interacts with severe acute respiratory syndrome coronavirus (SARS-CoV) (via N-terminus). Component of the tRNA-splicing ligase complex.
 
CELLULAR LOCALIZATION:
 
Nucleus. Cytoplasm. Cytoplasmic granule. Note: Localized with MBNL1, TIAL1 and YBX1 in stress granules upon stress. Localized with CSTF2 in cleavage bodies. Forms large aggregates called DDX1 bodies. Relocalized into multiple foci (IR-induced foci or IRIF) after IR treatment, a process that depends on the presence of chromosomal DNA and/or RNA-DNA duplexes. Relocalized at sites of DNA double-strand breaks (DSBs) in an ATM-dependent manner after IR treatment. Colocalized with RELA in the nucleus upon TNF-alpha induction. Relocalized to the cytoplasm with a perinuclear staining pattern in avian infectious bronchitis virus (IBV)-infected cells. Required for proper localization of HIV-1 Rev. 
 
TISSUE SPECIFICITY:
 
Highest levels of transcription in 2 retinoblastoma cell lines and in tissues of neuroectodermal origin including the retina, brain, and spinal cord. 
 
DOMAIN:
 
The helicase domain is involved in the stimulation of RELA transcriptional activity.
 
POST-TRANSLATIONAL MODIFICATION:
 
Phosphorylated. Phosphorylated by ATM kinase; phosphorylation is increased in response to ionizing radiation (IR).



This protein can be a part of a given complexes: Activities in which ATP-dependent RNA helicase DDX1 is involved: Pathways in which ATP-dependent RNA helicase DDX1 is involved:

NCBI GI number(s): 4826686
379317168

Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q92499 Q92499
BRENDA - -
KEGG hsa:1653 hsa:1653
PFAM: PF00270
PF00271
PF00622
PF00270
PF00271
PF00622
InterPro: IPR001870
IPR008985
IPR011545
IPR014001
IPR001650
IPR014014
IPR018355
IPR003877
IPR001870
IPR008985
IPR011545
IPR014001
IPR001650
IPR014014
IPR018355
IPR003877
CATH: - -
SCOP: - -


Protein sequence:
MAAFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGS
GKTGAFSIPVIQIVYETLKDQQEGKKGKTTIKTGASVLNKWQMNPYDRGS
AFAIGSDGLCCQSREVKEWHGCRATKGLMKGKHYYEVSCHDQGLCRVGWS
TMQASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDK
GHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEEEFKFP
PKDGFVALSKAPDGYIVKSQHSGNAQVTQTKFLPNAPKALIVEPSRELAE
QTLNNIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRL
DDLVSTGKLNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPQVTSDGKR
LQVIVCSATLHSFDVKKLSEKIMHFPTWVDLKGEDSVPDTVHHVVVPVNP
KTDRLWERLGKSHIRTDDVHAKDNTRPGANSPEMWSEAIKILKGEYAVRA
IKEHKMDQAIIFCRTKIDCDNLEQYFIQQGGGPDKKGHQFSCVCLHGDRK
PHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYV
HRIGRVGRAERMGLAISLVATEKEKVWYHVCSSRGKGCYNTRLKEDGGCT
IWYNEMQLLSEIEEHLNCTISQVEPDIKVPVDEFDGKVTYGQKRAAGGGS
YKGHVDILAPTVQELAALEKEAQTSFLHLGYLPNQLFRTF

ATP-dependent RNA helicase DDX1 (Homo sapiens) is product of expression of DDX1 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, K Genome Res 2004-10-01 (14) 15489334
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M Science 2009-08-14 (325) 19608861
Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A Proc Natl Acad Sci U S A 2007-01-13 (104) 17287340
Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ Cell 2007-12-14 (131) 18083107
HSPC117 is the essential subunit of a human tRNA splicing ligase complex. Popow J, Englert M, Weitzer S, Schleiffer A, Mierzwa B, Mechtler K, Trowitzsch S, Will CL, Luhrmann R, Soll D, Martinez J Science 2011-01-11 (331) 21311021
Amplification of a DEAD box protein gene in retinoblastoma cell lines. Godbout R, Squire J Proc Natl Acad Sci U S A 1993-08-15 (90) 7689221
Association of human DEAD box protein DDX1 with a cleavage stimulation factor involved in 3'-end processing of pre-MRNA. Bleoo S, Sun X, Hendzel MJ, Rowe JM, Packer M, Godbout R Mol Biol Cell 2001-10-01 (12) 11598190
An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous nuclear ribonucleoprotein K. Chen HC, Lin WC, Tsay YG, Lee SC, Chang CJ J Biol Chem 2002-10-25 (277) 12183465
A DEAD box protein facilitates HIV-1 replication as a cellular co-factor of Rev. Fang J, Kubota S, Yang B, Zhou N, Zhang H, Godbout R, Pomerantz RJ Virology 2004-12-20 (330) 15567440
MBNL1 associates with YB-1 in cytoplasmic stress granules. Onishi H, Kino Y, Morita T, Futai E, Sasagawa N, Ishiura S J Neurosci Res 2008-07-01 (86) 18335541
A role for DEAD box 1 at DNA double-strand breaks. Li L, Monckton EA, Godbout R Mol Cell Biol 2008-10-01 (28) 18710941
The DEAD-box RNA helicase DDX1 interacts with RelA and enhances nuclear factor kappaB-mediated transcription. Ishaq M, Ma L, Wu X, Mu Y, Pan J, Hu J, Hu T, Fu Q, Guo D J Cell Biochem 2009-01-01 (106) 19058135
The cellular RNA helicase DDX1 interacts with coronavirus nonstructural protein 14 and enhances viral replication. Xu L, Khadijah S, Fang S, Wang L, Tay FP, Liu DX J Virol 2010-09-01 (84) 20573827



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Last modification of this entry: Sept. 25, 2012.

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