DDX5
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Official Full Name
DEAD (Asp-Glu-Ala-Asp) box helicase 5 -
Overview
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, and cellular growth and division. This gene encodes a DEAD box protein, which is a 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. [provided by RefSeq, Jul 2008] -
Synonyms
DDX5;DEAD (Asp-Glu-Ala-Asp) box helicase 5;p68;HLR1;G17P1;HUMP68;probable ATP-dependent RNA helicase DDX5;DEAD box-5;RNA helicase p68;DEAD box protein 5;ATP-dependent RNA helicase DDX5;DEAD (Asp-Glu-Ala-Asp) box polypeptide 5;DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 5 (RNA helicase, 68kD)
Recombinant Proteins
- Zebrafish
- Rhesus macaque
- Human
- Cynomolgus
- Chicken
- Mouse
- Mammalian Cells
- Wheat Germ
- HEK293
- HeLa
- In Vitro Cell Free System
- E.coli
- His
- GST
- DDK
- Myc
- Non
- Avi
- Fc
- Flag
Involved Pathway
DDX5 involved in several pathways and played different roles in them. We selected most pathways DDX5 participated on our site, such as Direct p53 effectors,Proteoglycans in cancer,Spliceosome, which may be useful for your reference. Also, other proteins which involved in the same pathway with DDX5 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Spliceosome | TRA2A,PRPF40A,SNRNP27,HNRNPA1L2,SRSF9,SMX5,SF3B14,LSM3,TCERG1A,DDX23 |
| Transcriptional misregulation in cancer | MET,MMP3,SFPI1,HIST1H3E,SPI1,IGFBP3,SP1,GOLPH3,TRP53,ZBTB17 |
| Proteoglycans in cancer | WNT2B,FLNA,ERBB3,PRKCG,ITGA2,CAMK2B,MAPK12,PRKCB,TGFB1,RRAS |
| Direct p53 effectors | FDXR,HIC1,DDB2,DUSP5,FOXA1,CCNK,PCBP4,CD82,S100A2,DUSP1 |
Protein Function
DDX5 has several biochemical functions, for example, ATP binding,ATP-dependent RNA helicase activity,RNA helicase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by DDX5 itself. We selected most functions DDX5 had, and list some proteins which have the same functions with DDX5. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| transcription coactivator activity | NR2F1,BRCA1,PIAS2,MTDH,SRA1,RB1,MKL1,GTF2F1,MNT,PIAS1 |
| enzyme binding | UGT1A3,RPS2,CCND1,APBA3,SRC,MAP2K7,PPARG,RFC5,SLPI,HIST1H2AK |
| protein binding | TESC,TRMT2B,TMEM132D,THRA,CRHBP,KLHL22,VHLL,SOX15,KLRG1,IL12B |
| androgen receptor binding | FHL2,NRIP1,NCOA3,PRKCBB,RNF4,KDM4C,KAT5,CCNE1,PKN1,RB1 |
| calcium-dependent protein binding | S100A6,SYT8,CHP1,ANXA1,CALM2,PLSCR3,MBL2,VAMP2,SYT1,TSG101 |
| RNA helicase activity | CCDC111,PRIM2,DDX6,CTU1,RAD54B,DHX16,CHST13,SKIV2L2,DDX10,DDX17 |
| estrogen receptor binding | LEF1,TMEM38A,WIPI1,DDX54,MED1,NCOA1,PPARGC1A,NKX3,XBP1,NRIP1 |
| pre-mRNA binding | SRSF2,RBM22,TARBP2,PTBP1 |
| calmodulin binding | MYO6,ITPKB,MYH7,CTH,CAMK2D1,OBSCN,CAMKV,RYR3,RIT2,EWSR1 |
Interacting Protein
DDX5 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with DDX5 here. Most of them are supplied by our site. Hope this information will be useful for your research of DDX5.
ESR1;p27958-pro_0000037577
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References
- Geissler, V; Altmeyer, S; et al. The RNA helicase Ddx5/p68 binds to hUpf3 and enhances NMD of Ddx17/p72 and Smg5 mRNA. NUCLEIC ACIDS RESEARCH 41:7875-7888(2013).
- Nishida, Y; Aida, K; et al. Antibody-Validated Proteins in Inflamed Islets of Fulminant Type 1 Diabetes Profiled by Laser-Capture Microdissection Followed by Mass Spectrometry. PLOS ONE 9:-(2014).
