UniProt Accession

 DDX1_MOUSE; Q91VR5; Q3TU41 

Genbank Protein ID

 AK028341; AK153335; AK160982; BC010624 

Genbank Nucleotide ID

 BAC25893.1; BAE31914.1; BAE36130.1; AAH10624.1 

Protein Name

 ATP-dependent RNA helicase DDX1 

Protein Synonyms/Alias

 DEAD box protein 1 

Gene Name

 Ddx1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
117	CCQSREVKEWHGCRG	acetylation	[1]
132	TRGLLKGKHYYEVSC	acetylation	[2]
172	FGFGGTGKKSHNKQF	ubiquitination	[3]
268	APDNYIVKSQHTGNA	acetylation	[2]
268	APDNYIVKSQHTGNA	ubiquitination	[3]
281	NAQVSQTKFLPNAPK	acetylation	[2, 4, 5]
281	NAQVSQTKFLPNAPK	ubiquitination	[3]
288	KFLPNAPKALIVEPS	ubiquitination	[3]
358	DDLVSTGKLNLSQVR	ubiquitination	[3]

Reference

 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 2 428 Helicase ATP-binding.
 DOMAIN 70 247 B30.2/SPRY.
 DOMAIN 493 681 Helicase C-terminal.
 NP_BIND 46 53 ATP (By similarity).
 REGION 1 525 Necessary for interaction with RELA (By
 REGION 1 295 Necessary for interaction with HNRNPK (By
 REGION 525 740 Necessary for interaction with HNRNPK (By
 MOTIF 370 373 DEAD box.
 MOD_RES 239 239 N6-acetyllysine (By similarity).
 MOD_RES 268 268 N6-acetyllysine (By similarity).
 MOD_RES 281 281 N6-acetyllysine (By similarity).
 MOD_RES 481 481 Phosphoserine (By similarity).  

Keyword

 Acetylation; Activator; ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Exonuclease; Helicase; Hydrolase; mRNA processing; Nuclease; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 740 AA 

Protein Sequence

Gene Ontology

 GO:0071920; C:cleavage body; ISS:UniProtKB.
 GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
 GO:0072669; C:tRNA-splicing ligase complex; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008026; F:ATP-dependent helicase activity; ISS:UniProtKB.
 GO:0003682; F:chromatin binding; ISS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0033677; F:DNA/RNA helicase activity; ISS:UniProtKB.
 GO:0003725; F:double-stranded RNA binding; IDA:MGI.
 GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
 GO:0004518; F:nuclease activity; ISS:UniProtKB.
 GO:0008143; F:poly(A) RNA binding; ISS:UniProtKB.
 GO:0003712; F:transcription cofactor activity; ISS:UniProtKB.
 GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
 GO:0006302; P:double-strand break repair; ISS:UniProtKB.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0007275; P:multicellular organismal development; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
 GO:0009615; P:response to virus; IMP:MGI.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR001870; B30.2/SPRY.
 IPR008985; ConA-like_lec_gl_sf.
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR014014; RNA_helicase_DEAD_Q_motif.
 IPR018355; SPla/RYanodine_receptor_subgr.
 IPR003877; SPRY_rcpt. 

Pfam

 PF00270; DEAD
 PF00271; Helicase_C
 PF00622; SPRY 

SMART

 SM00487; DEXDc
 SM00490; HELICc
 SM00449; SPRY 

PROSITE

 PS50188; B302_SPRY
 PS00039; DEAD_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS51195; Q_MOTIF 

PRINTS