DDX5

DDX5
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3FE2, 4A4D
Identifiers
Aliases	DDX5, G17P1, HLR1, HUMP68, p68, DEAD-box helicase 5
External IDs	OMIM: 180630; MGI: 105037; HomoloGene: 1655; GeneCards: DDX5; OMA:DDX5 - orthologs
Gene location (Human)
Chr.	Chromosome 17 (human)
End	64,508,199 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	106,680,011 bp
RNA expression pattern
	Top expressed in
	Achilles tendon; ; bone marrow cell; ; granulocyte; ; anterior pituitary; ; right adrenal cortex; ; smooth muscle tissue; ; epithelium of colon; ; gonad; ; monocyte; ; right lobe of thyroid gland;
	Top expressed in
	lobe of cerebellum; ; cerebellar vermis; ; neural layer of retina; ; olfactory tubercle; ; granulocyte; ; habenula; ; median eminence; ; pineal gland; ; arcuate nucleus; ; lateral septal nucleus;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; helicase activity; calcium-dependent protein binding; calmodulin binding; protein binding; androgen receptor binding; nucleic acid binding; enzyme binding; pre-mRNA binding; hydrolase activity; ATP binding; RNA helicase activity; RNA binding; mRNA 3'-UTR binding; ribonucleoprotein complex binding; promoter-specific chromatin binding; MH2 domain binding; SMAD binding; R-SMAD binding; primary miRNA binding; transcription coregulator activity;
Cellular component	catalytic step 2 spliceosome; membrane; nucleolus; spliceosomal complex; extracellular exosome; nucleus; extracellular matrix; nucleoplasm; SMAD protein complex; cytoplasm; ribonucleoprotein complex;
Biological process	regulation of skeletal muscle cell differentiation; regulation of transcription, DNA-templated; rhythmic process; regulation of viral genome replication; mRNA processing; mRNA transcription; negative regulation of transcription by RNA polymerase II; transcription, DNA-templated; cell growth; regulation of osteoblast differentiation; RNA secondary structure unwinding; intrinsic apoptotic signaling pathway by p53 class mediator; RNA splicing; regulation of androgen receptor signaling pathway; positive regulation of DNA damage response, signal transduction by p53 class mediator; mRNA splicing, via spliceosome; regulation of alternative mRNA splicing, via spliceosome; nuclear-transcribed mRNA catabolic process; alternative mRNA splicing, via spliceosome; regulation of transcription by RNA polymerase II; intracellular estrogen receptor signaling pathway; androgen receptor signaling pathway; epithelial to mesenchymal transition; myoblast differentiation; pri-miRNA transcription by RNA polymerase II; BMP signaling pathway; regulation of pri-miRNA transcription by RNA polymerase II; positive regulation of production of miRNAs involved in gene silencing by miRNA;
	Sources:Amigo / QuickGO
Orthologs
	1655
	13207
	ENSG00000108654
	ENSMUSG00000020719
	P17844
	Q61656
	NM_004396; NM_001320595; NM_001320596; NM_001320597
	NM_007840; NM_001355676; NM_001355677
	NP_001307524; NP_001307525; NP_001307526; NP_004387
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

Probable ATP-dependent RNA helicase DDX5 also known as DEAD box protein 5 or RNA helicase p68 is an enzyme that in humans is encoded by the DDX5 gene.^[5]

Function

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure, such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis,^[6] and cellular growth and division. This gene encodes a DEAD box protein, which is an RNA-dependent ATPase, and also a proliferation-associated nuclear antigen, specifically reacting with the simian virus 40 tumor antigen. This gene consists of 13 exons, and alternatively spliced transcripts containing several intron sequences have been detected, but no isoforms encoded by these transcripts have been identified.^[5]

Interactions

DDX5 has been shown to interact with:

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000108654 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020719 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "Entrez Gene: DDX5 DEAD (Asp-Glu-Ala-Asp) box polypeptide 5".
↑ Legrand JM, Chan AL, La HM, Rossello FJ, Änkö ML, Fuller-Pace FV, et al. (May 2019). "DDX5 plays essential transcriptional and post-transcriptional roles in the maintenance and function of spermatogonia". Nature Communications. 10 (1) 2278. Bibcode:2019NatCo..10.2278L. doi:10.1038/s41467-019-09972-7. PMC 6533336. PMID 31123254.
↑ Akileswaran L, Taraska JW, Sayer JA, Gettemy JM, Coghlan VM (May 2001). "A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix and associates with p68 RNA helicase". The Journal of Biological Chemistry. 276 (20): 17448–17454. doi:10.1074/jbc.M101171200. PMID 11279182.
↑ Ogilvie VC, Wilson BJ, Nicol SM, Morrice NA, Saunders LR, Barber GN, et al. (March 2003). "The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells". Nucleic Acids Research. 31 (5): 1470–1480. doi:10.1093/nar/gkg236. PMC 149829. PMID 12595555.
↑ Wilson BJ, Giguère V (2007). "Identification of novel pathway partners of p68 and p72 RNA helicases through Oncomine meta-analysis". BMC Genomics. 8: 419. doi:10.1186/1471-2164-8-419. PMC 3225811. PMID 18005418.
↑ Rossow KL, Janknecht R (January 2003). "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300". Oncogene. 22 (1): 151–156. doi:10.1038/sj.onc.1206067. PMID 12527917.
↑ Nicol SM, Causevic M, Prescott AR, Fuller-Pace FV (June 2000). "The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase". Experimental Cell Research. 257 (2): 272–280. doi:10.1006/excr.2000.4886. PMID 10837141.
↑ Wilson BJ, Bates GJ, Nicol SM, Gregory DJ, Perkins ND, Fuller-Pace FV (August 2004). "The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner". BMC Molecular Biology. 5 11. doi:10.1186/1471-2199-5-11. PMC 514542. PMID 15298701.
↑ Bates GJ, Nicol SM, Wilson BJ, Jacobs AM, Bourdon JC, Wardrop J, et al. (February 2005). "The DEAD box protein p68: a novel transcriptional coactivator of the p53 tumour suppressor". The EMBO Journal. 24 (3): 543–553. doi:10.1038/sj.emboj.7600550. PMC 548656. PMID 15660129.
↑ Yao H, Brick K, Evrard Y, Xiao T, Camerini-Otero RD, Felsenfeld G (2010). "Mediation of CTCF transcriptional insulation by DEAD-box RNA-binding protein p68 and steroid receptor RNA activator SRA". Genes & Development. 24 (22): 2543–2555. doi:10.1101/gad.1967810. PMC 2975930. PMID 20966046.

Iggo RD, Jamieson DJ, MacNeill SA, Southgate J, McPheat J, Lane DP (March 1991). "p68 RNA helicase: identification of a nucleolar form and cloning of related genes containing a conserved intron in yeasts". Molecular and Cellular Biology. 11 (3): 1326–1333. doi:10.1128/MCB.11.3.1326. PMC 369403. PMID 1996094.
Hloch P, Schiedner G, Stahl H (1990). "Complete cDNA sequence of the human p68 protein". Nucleic Acids Research. 18 (10): 3045. doi:10.1093/nar/18.10.3045. PMC 330836. PMID 2349099.
Ford MJ, Anton IA, Lane DP (1988). "Nuclear protein with sequence homology to translation initiation factor eIF-4A". Nature. 332 (6166): 736–738. Bibcode:1988Natur.332..736F. doi:10.1038/332736a0. PMID 2451786. S2CID 4351448.
Iggo R, Gough A, Xu W, Lane DP, Spurr NK (August 1989). "Chromosome mapping of the human gene encoding the 68-kDa nuclear antigen (p68) by using the polymerase chain reaction". Proceedings of the National Academy of Sciences of the United States of America. 86 (16): 6211–6214. Bibcode:1989PNAS...86.6211I. doi:10.1073/pnas.86.16.6211. PMC 297807. PMID 2762324.
Buelt MK, Glidden BJ, Storm DR (1994). "Regulation of p68 RNA helicase by calmodulin and protein kinase C". The Journal of Biological Chemistry. 269 (47): 29367–29370. doi:10.1016/S0021-9258(18)43885-9. PMID 7525583.
Brody LC, Abel KJ, Castilla LH, Couch FJ, McKinley DR, Yin G, et al. (January 1995). "Construction of a transcription map surrounding the BRCA1 locus of human chromosome 17". Genomics. 25 (1): 238–247. doi:10.1016/0888-7543(95)80131-5. PMID 7774924.
Rössler OG, Hloch P, Schütz N, Weitzenegger T, Stahl H (February 2000). "Structure and expression of the human p68 RNA helicase gene". Nucleic Acids Research. 28 (4): 932–939. doi:10.1093/nar/28.4.932. PMC 102575. PMID 10648785.
Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, et al. (January 2002). "Directed proteomic analysis of the human nucleolus". Current Biology. 12 (1): 1–11. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ (April 2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA. 8 (4) S1355838202021088. New York, N.Y. doi:10.1017/S1355838202021088. PMC 1370266. PMID 11991638.
Liu ZR (August 2002). "p68 RNA helicase is an essential human splicing factor that acts at the U1 snRNA-5' splice site duplex". Molecular and Cellular Biology. 22 (15): 5443–5450. doi:10.1128/MCB.22.15.5443-5450.2002. PMC 133941. PMID 12101238.
Guil S, Gattoni R, Carrascal M, Abián J, Stévenin J, Bach-Elias M (April 2003). "Roles of hnRNP A1, SR proteins, and p68 helicase in c-H-ras alternative splicing regulation". Molecular and Cellular Biology. 23 (8): 2927–2941. doi:10.1128/MCB.23.8.2927-2941.2003. PMC 152554. PMID 12665590.
Fujita T, Kobayashi Y, Wada O, Tateishi Y, Kitada L, Yamamoto Y, et al. (July 2003). "Full activation of estrogen receptor alpha activation function-1 induces proliferation of breast cancer cells". The Journal of Biological Chemistry. 278 (29): 26704–26714. doi:10.1074/jbc.M301031200. PMID 12738788.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000108654 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020719 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] 1 2 "Entrez Gene: DDX5 DEAD (Asp-Glu-Ala-Asp) box polypeptide 5".

[6] Legrand JM, Chan AL, La HM, Rossello FJ, Änkö ML, Fuller-Pace FV, et al. (May 2019). "DDX5 plays essential transcriptional and post-transcriptional roles in the maintenance and function of spermatogonia". Nature Communications. 10 (1) 2278. Bibcode:2019NatCo..10.2278L. doi:10.1038/s41467-019-09972-7. PMC 6533336. PMID 31123254.

[pmid11279182-7] Akileswaran L, Taraska JW, Sayer JA, Gettemy JM, Coghlan VM (May 2001). "A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix and associates with p68 RNA helicase". The Journal of Biological Chemistry. 276 (20): 17448–17454. doi:10.1074/jbc.M101171200. PMID 11279182.

[pmid12595555-8] Ogilvie VC, Wilson BJ, Nicol SM, Morrice NA, Saunders LR, Barber GN, et al. (March 2003). "The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells". Nucleic Acids Research. 31 (5): 1470–1480. doi:10.1093/nar/gkg236. PMC 149829. PMID 12595555.

[pmid18005418-9] Wilson BJ, Giguère V (2007). "Identification of novel pathway partners of p68 and p72 RNA helicases through Oncomine meta-analysis". BMC Genomics. 8: 419. doi:10.1186/1471-2164-8-419. PMC 3225811. PMID 18005418.

[pmid12527917-10] Rossow KL, Janknecht R (January 2003). "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300". Oncogene. 22 (1): 151–156. doi:10.1038/sj.onc.1206067. PMID 12527917.

[pmid10837141-11] Nicol SM, Causevic M, Prescott AR, Fuller-Pace FV (June 2000). "The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase". Experimental Cell Research. 257 (2): 272–280. doi:10.1006/excr.2000.4886. PMID 10837141.

[pmid15298701-12] Wilson BJ, Bates GJ, Nicol SM, Gregory DJ, Perkins ND, Fuller-Pace FV (August 2004). "The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner". BMC Molecular Biology. 5 11. doi:10.1186/1471-2199-5-11. PMC 514542. PMID 15298701.

[pmid15660129-13] Bates GJ, Nicol SM, Wilson BJ, Jacobs AM, Bourdon JC, Wardrop J, et al. (February 2005). "The DEAD box protein p68: a novel transcriptional coactivator of the p53 tumour suppressor". The EMBO Journal. 24 (3): 543–553. doi:10.1038/sj.emboj.7600550. PMC 548656. PMID 15660129.

[pmid20966046-14] Yao H, Brick K, Evrard Y, Xiao T, Camerini-Otero RD, Felsenfeld G (2010). "Mediation of CTCF transcriptional insulation by DEAD-box RNA-binding protein p68 and steroid receptor RNA activator SRA". Genes & Development. 24 (22): 2543–2555. doi:10.1101/gad.1967810. PMC 2975930. PMID 20966046.

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Function

Interactions

References

Further reading