Overview
| Uniprot ID | H0V5X7 |
|---|
| Protein Name | ATP-dependent RNA helicase DDX42 |
|---|
| Gene Name | DDX42 |
|---|
| Organism | Cavia porcellus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 649 |
FKGGKGKKLNIGGGG |
Function
ATP-dependent RNA helicase that binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Also mediates RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Required for assembly of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs: DDX42 associates transiently with the SF3B subcomplex of the 17S U2 SnRNP complex and is released after fulfilling its role in the assembly of 17S U2 SnRNP. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm
Protein Sequence
10
MNWNKGGPGT
20
KRGFGFGGFA
30
ISAGKKEETK
40
LPQQSHSAFG
50
ATSSSSGFGK
60
SAPPQLPSFY
70
KIGSKRANFD
80
EENAYFEDEE
90
EDSSNVDLPY
100
IPAENSPTRQ
110
QFHSKPADSD
120
SDDDPLEAFM
130
AEVEDQAARD
140
MKRLEEKDKE
150
RKNVKGIRDD
160
IEEEDDQEAY
170
FRYMAENPTA
180
GVVQEEEEDN
190
LEYDSDGNPI
200
APSKKIIDPL
210
PPIDHSEIDY
220
PPFEKNFYNE
230
HEEITNLTPQ
240
QLIDLRHKLN
250
LRVSGAAPPR
260
PGSSFAHFGF
270
DEQLMHQIRK
280
SEYTQPTPIQ
290
CQGVPVALSG
300
RDMIGIAKTG
310
SGKTAAFIWP
320
MLIHIMDQKE
330
LEPGDGPIAV
340
IVCPTRLCQQ
350
IHAECKRFGK
360
AYNLRSVAVY
370
GGGSMWEQAK
380
ALQEGAEIVV
390
CTPGRLIDHV
400
KKKATNLQRV
410
SYLVFDEADR
420
MFDMGFEYQV
430
RSIASHVRPD
440
RQTLLFSATF
450
RKKIEKLARD
460
ILIDPIRVVQ
470
GDIGEANEDV
480
TQIVEILHSG
490
PSKWNWLTRR
500
LVEFTSSGSV
510
LLFVTKKANA
520
EELANNLKQE
530
GHNLGLLHGD
540
MDQSERNKVI
550
SDFKKKDIPV
560
LVATDVAARG
570
LDIPSIKTVI
580
NYDVARDIDT
590
HTHRIGRTGR
600
AGEKGVAYTL
610
LTPKDSNFAG
620
DLVRNLEGAN
630
QHVSKELLDL
640
AMQNAWFRKS
650
RFKGGKGKKL
660
NIGGGGLGYR
670
ERPGLGSENT
680
DRGNNNNVMS
690
NYEAYKPSTG
700
AMGDRLTAMK
710
AAFQSQYKSH
720
FVAASLSNQK
730
AGSSAAGPSG
740
WTSAGSLNSV
750
PTNSAQQGHS
760
SPDSPIASSA
770
KSIPGFGSAG
780
NISNAPVTYP
790
SLGTQGANNT
800
ASGNNSREGI
810
GGGNGKRERY
820
TDNRGGSRHS
830
HGESGIRHGD
840
GGRHGDGYRY
850
PESSSSSRHT
860
DGHRHGENRH
870
GGSTGRHGES
880
RGTNDGRNGE
890
SRKESCNRES
900
KMDPKVDSKM
910
DSKTDKTADG
920
FAVPEPPKRK
KSRWDS
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Biological Process |
GO:0042981 |
regulation of apoptotic process |
| Biological Process |
GO:1903241 |
U2-type prespliceosome assembly |
| Cellular Component |
GO:0016607 |
nuclear speck |
| Cellular Component |
GO:0071004 |
U2-type prespliceosome |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0016787 |
hydrolase activity |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:0003724 |
RNA helicase activity |
| Biological Process |
GO:0008104 |
intracellular protein localization |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.