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Information on EC 3.6.4.13 - RNA helicase and Organism(s) Homo sapiens

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EC Tree
IUBMB Comments
RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. Some of them unwind RNA with a 3' to 5' polarity , other show 5' to 3' polarity . Some helicases unwind DNA as well as RNA [7,8]. May be identical with EC 3.6.4.12 (DNA helicase).
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
helicase, rig-i, rna helicase, eif4a, ddx3x, dead-box rna helicase, ns3 helicase, dead-box helicase, ddx21, rna helicase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP-dependent helicase
-
ATP-dependent RNA helicase DDX5
-
Brr2 RNA helicase
-
Brr2p
-
-
ChlR1 helicase
-
DDX21 RNA helicase
-
DDX3X
DDX3Y
DEAD box RNA helicase
-
DEAD-box RNA helicase
DEAH box protein 34
-
DEAH-box protein 2
-
DEAH-box RNA helicase
DEAH/RHA RNA helicase
-
DEXD/H-box RNA helicase
-
DExH protein RNA helicase A
-
-
DExH/D-Box protein RNA helicase A
-
DExH/D-box RNA helicase
-
DHX36
-
-
GRTH/DDX25
-
intron-binding protein 160
-
p54 RNA helicase
-
p68 RNA helicase
-
-
RNA helicase A
RNA helicase Aquarius
-
RNA helicase DDX17
-
RNA helicase DDX3
-
RNA helicase DDX5
-
RNA helicase DHX34
-
RNA helicase DHX8
-
RNA Helicase p68
-
RNA helicase RHAU
-
-
RNA helicase UPF1
-
RNA-dependent ATPase
-
RNA-helicase
-
Ski2-like helicase
-
spliceosomal RNA helicase
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (RNA helix unwinding)
RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. Some of them unwind RNA with a 3' to 5' polarity [3], other show 5' to 3' polarity [8]. Some helicases unwind DNA as well as RNA [7,8]. May be identical with EC 3.6.4.12 (DNA helicase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
CTP + H2O
CDP + phosphate
show the reaction diagram
-
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
the enzyme displaces partial duplex RNA exclusively in a 5' to 3' direction. This reaction is supported by ATP and dATP at relatively high concentrations. The enzyme displays only ATPase and dATPase activity. RNA helicase catalyzes the unwinding of duplex RNA and RNA*DNA hybrids provided that single-stranded RNA is available for the helicase to bind
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
-
slight stimulation at 0.05-0.1 M, inhibition at 0.2 M
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(6Z)-6-[[5-(3-chlorophenyl)furan-2-yl]methylidene]-5-imino-2-propyl-5,6-dihydro-7H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-7-one
-
3-[5-[(Z)-(2-cyclohexyl-5-imino-7-oxo-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-6(7H)-ylidene)methyl]furan-2-yl]benzoic acid
binds an RNA-binding site inside the N-terminal cassette, mechanism of action, enzyme binding structure, overview
3-[5-[(Z)-(5-imino-7-oxo-2-propyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-6(7H)-ylidene)methyl]furan-2-yl]benzoic acid
-
4-(3,5-dimethoxyphenyl)-N-(7-fluoro-3-methoxyquinoxalin-2-yl)piperazine-1-carboxamide
i.e. supinoxin or RX-5902, intervenes in the phosphorylated p68-beta-catenin signaling pathway by interacting with Tyr593 in SK-MEL-28 (human melanoma), MDA-MB-231 (human metastatic breast cancer), and WI-38 (human normal fetal lung fibroblasts) cell lines
6-benzyl-3-[(2R)-2-(3-fluoropyridin-2-yl)-6-methyl-3,4-dihydro-2H-1-benzopyran-7-yl]-4,6-dihydropyrido[4,3-d]pyrimidine-2,7(1H,3H)-dione
binds to an unexpected allosteric site between the C-terminal and the N-terminal helicase cassettes, enzyme binding structure, overview
6-benzyl-3-[3-(benzyloxy)phenyl]-4,6-dihydropyrido[4,3-d]pyrimidine-2,7(1H,3H)-dione
enzyme binding structure, overview
ADP
the affinity for RNA is over 90fold weaker in the absence of nucleotide and in the presence of ADP, the RNA affinity is too weak to determine. These results indicate that DHX8-mediated disruption of RNA interactions occurs through a series of alternating strong and weak RNA binding events controlled by ATP hydrolysis. Both full-length fl-DHX8 and truncated DHX8DELAT547 preferentially bind the purine nucleotides ADP and GDP, but are also able to bind CDP, TDP and UDP. RNA binding triggers DEAH and P-loop movement and stimulates ADP release
AMP-PNP
structure of Aquarius in complex with AMP-PNP, modelling, overview
benzoquinoquinoxaline
BQQ, inhibits ChlR1 triplex DNA unwinding activity
EDTA
-
-
EWS-FLI1
the small molecule reduces RHA helicase activity in a dose-dependent and enantiomeric manner without affecting intrinsic ATPase activity, the RHA kinetics indicate a complex model. Only (S)-YK-4-279 reverses the EWS-FLI1 inhibition of RHA helicase activity. YK-4-279 inhibition of RHA binding to EWS-FLI1 alters the RNA binding profile of both proteins. EWS-FLI1 modulates RHA helicase activity causing changes in overall transcriptome processing
-
poly(A)10
-
-
poly(A)4
-
-
poly(A)6
-
-
poly(A)8
-
-
poly(C)10
-
-
poly(G)10
-
-
poly(U)10
-
-
poly(X) RNA
DHX8 is an RNA-specific helicase by showing that a poly(dA)10 DNA strand cannot displace Cy5-poly(A)10 from DHX8 in the presence of ADP-AlFx. The displacement of the probe with poly(A)10, poly(C)10, poly(G)10 and poly(U)10 RNA indicates that DHX8 has a preference for binding adenine-rich sequences as the rank ascending order of IC50 values is poly (A)10, poly(U)10, poly(C)10, poly(G)10
-
Prp8 protein
the Jab1 domain of the Prp8 proten can inhibit Brr2 by intermittently inserting a C-terminal tail in the enzyme's RNA-binding tunnel or activate the helicase after removal of this tail. Binding of the Prp8 Jab1 C-terminal tail at the Brr2 RNA binding tunnel is evolutionarily conserved, Brr2-Jab1 binding structure and analysis, overview. Jab1-based inhibition of Brr2 presumably takes effect in all eukaryotes but is implemented via organism-specific molecular contacts. Brr2 autoinhibition can act in concert with Jab1-mediated inhibition. The NTR and the Jab1 tail cooperate in inhibiting RNA binding by Brr2; the Jab1 domain of the Prp8 proten can inhibit Brr2 by intermittently inserting a C-terminal tail in the enzyme's RNA-binding tunnel or activate the helicase after removal of this tail. Binding of the Prp8 Jab1 C-terminal tail at the Brr2 RNA binding tunnel is evolutionarily conserved, Brr2-Jab1 binding structure and analysis, overview. Jab1-based inhibition of Brr2 presumably takes effect in all eukaryotes but is implemented via organism-specific molecular contacts. Brr2 autoinhibition can act in concert with Jab1-mediated inhibition.The NTR and the Jab1 tail cooperate in inhibiting RNA binding by Brr2
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MLN51
stimulates the RNA-helicase activity of eIF4AIII
-
poly(C)
-
stimulates ATPase and dATPase activity
Prp8 protein
the Jab1 domain of the Prp8 protein can inhibit Brr2 by intermittently inserting a C-terminal tail in the enzyme's RNA-binding tunnel or activate the helicase after removal of this tail. Binding of the Prp8 Jab1 C-terminal tail at the Brr2 RNA binding tunnel is evolutionarily conserved, Brr2-Jab1 binding structure and analysis, overview
-
RNA
Aquarius hydrolyzes ATP, and this activity is highly stimulated in the presence of a 22-nt RNA with a random sequence. Aquarius does not bind a blunt-ended RNA duplex, and correspondingly the latter does not stimulate Aquarius's ATPase activity
Single-stranded RNA
-
RNA helicase catalyzes the unwinding of duplex RNA and RNA*DNA hybrids provided that single-stranded RNA is available for the helicase to bind
ssRNA
DHX8 ATPase activity is stimulated by RNA
-
Upf2
interaction analysis. The two proteins Upf1 and Upf2 form a complex while unwinding RNA. The binding of Upf2 to CH domain activates Upf1-CH-HD unwinding and translocation
-
additional information
Brr2 can be autoinhibited via a large N-terminal region folding back onto its helicase core and autoactivated by a catalytically inactive C-terminal helicase cassette
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0157 - 0.24
ATP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0283 - 0.3
ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
(6Z)-6-[[5-(3-chlorophenyl)furan-2-yl]methylidene]-5-imino-2-propyl-5,6-dihydro-7H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-7-one
Homo sapiens
above, pH and temperature not specified in the publication
0.0053
3-[5-[(Z)-(2-cyclohexyl-5-imino-7-oxo-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-6(7H)-ylidene)methyl]furan-2-yl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0042
3-[5-[(Z)-(5-imino-7-oxo-2-propyl-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-6(7H)-ylidene)methyl]furan-2-yl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0026
ADP
Homo sapiens
pH 7.4, temperature not specified in the publication, recombinant mutant enzyme DHX8DELTA54
0.016
poly(A)10
Homo sapiens
pH 7.4, temperature not specified in the publication, recombinant mutant enzyme DHX8DELTA54
-
0.1
poly(A)4
Homo sapiens
pH 7.4, temperature not specified in the publication, recombinant mutant enzyme DHX8DELTA54
-
0.036
poly(A)6
Homo sapiens
pH 7.4, temperature not specified in the publication, recombinant mutant enzyme DHX8DELTA54
-
0.017
poly(A)8
Homo sapiens
pH 7.4, temperature not specified in the publication, recombinant mutant enzyme DHX8DELTA54
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
assay at, ATPase assay
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
26
RNA assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
p68 is highly expressed in several carcinomas, such as breast, prostate, and colon
Manually annotated by BRENDA team
fetal lung fibroblasts
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DDX27_HUMAN
796
0
89835
Swiss-Prot
Mitochondrion (Reliability: 3)
DDX28_HUMAN
540
0
59581
Swiss-Prot
Mitochondrion (Reliability: 2)
DDX31_HUMAN
851
0
94087
Swiss-Prot
other Location (Reliability: 3)
DDX3X_HUMAN
662
0
73243
Swiss-Prot
other Location (Reliability: 2)
DDX3Y_HUMAN
660
0
73154
Swiss-Prot
other Location (Reliability: 1)
DX39A_HUMAN
427
0
49130
Swiss-Prot
other Location (Reliability: 1)
MTREX_HUMAN
1042
0
117805
Swiss-Prot
other Location (Reliability: 1)
DDX51_HUMAN
666
0
72457
Swiss-Prot
other Location (Reliability: 2)
DDX52_HUMAN
599
0
67466
Swiss-Prot
other Location (Reliability: 5)
DDX53_HUMAN
631
0
71154
Swiss-Prot
other Location (Reliability: 2)
DDX54_HUMAN
881
0
98595
Swiss-Prot
other Location (Reliability: 4)
IF4A3_HUMAN
411
0
46871
Swiss-Prot
other Location (Reliability: 4)
MOV10_HUMAN
1003
0
113671
Swiss-Prot
other Location (Reliability: 5)
YTDC2_HUMAN
1430
0
160248
Swiss-Prot
other Location (Reliability: 3)
AQR_HUMAN
1485
0
171295
Swiss-Prot
other Location (Reliability: 3)
D11L8_HUMAN
907
0
101811
Swiss-Prot
other Location (Reliability: 2)
M10L1_HUMAN
1211
0
135293
Swiss-Prot
Secretory Pathway (Reliability: 4)
PRP16_HUMAN
1227
0
140503
Swiss-Prot
other Location (Reliability: 1)
TDR12_HUMAN
1177
0
132578
Swiss-Prot
other Location (Reliability: 3)
DDX55_HUMAN
600
0
68547
Swiss-Prot
other Location (Reliability: 3)
DDX56_HUMAN
547
0
61590
Swiss-Prot
other Location (Reliability: 2)
DDX58_HUMAN
925
0
106600
Swiss-Prot
other Location (Reliability: 3)
DDX59_HUMAN
619
0
68810
Swiss-Prot
other Location (Reliability: 2)
DDX5_HUMAN
614
0
69148
Swiss-Prot
other Location (Reliability: 3)
U520_HUMAN
2136
0
244508
Swiss-Prot
other Location (Reliability: 2)
DDX41_HUMAN
622
0
69838
Swiss-Prot
other Location (Reliability: 1)
DDX42_HUMAN
938
0
102975
Swiss-Prot
other Location (Reliability: 4)
DDX43_HUMAN
648
0
72844
Swiss-Prot
Mitochondrion (Reliability: 3)
DDX46_HUMAN
1031
0
117362
Swiss-Prot
other Location (Reliability: 3)
DHX32_HUMAN
743
0
84419
Swiss-Prot
other Location (Reliability: 1)
DHX33_HUMAN
707
0
78874
Swiss-Prot
other Location (Reliability: 5)
DHX34_HUMAN
1143
0
128120
Swiss-Prot
other Location (Reliability: 3)
DHX35_HUMAN
703
0
78910
Swiss-Prot
other Location (Reliability: 3)
DHX36_HUMAN
1008
0
114760
Swiss-Prot
other Location (Reliability: 1)
DHX37_HUMAN
1157
0
129545
Swiss-Prot
other Location (Reliability: 4)
DHX40_HUMAN
779
0
88560
Swiss-Prot
Mitochondrion (Reliability: 4)
FANCJ_HUMAN
1249
0
140867
Swiss-Prot
other Location (Reliability: 2)
FANCM_HUMAN
2048
1
232191
Swiss-Prot
Mitochondrion (Reliability: 2)
DDX47_HUMAN
455
0
50647
Swiss-Prot
other Location (Reliability: 2)
DDX49_HUMAN
483
0
54226
Swiss-Prot
other Location (Reliability: 2)
DDX4_HUMAN
724
0
79308
Swiss-Prot
other Location (Reliability: 1)
DDX50_HUMAN
737
0
82565
Swiss-Prot
other Location (Reliability: 2)
DHX57_HUMAN
1386
0
155604
Swiss-Prot
other Location (Reliability: 2)
DHX58_HUMAN
678
0
76613
Swiss-Prot
other Location (Reliability: 2)
DHX8_HUMAN
1220
0
139315
Swiss-Prot
other Location (Reliability: 4)
DHX9_HUMAN
1270
0
140958
Swiss-Prot
other Location (Reliability: 2)
DDX20_HUMAN
824
0
92241
Swiss-Prot
other Location (Reliability: 4)
DDX21_HUMAN
783
0
87344
Swiss-Prot
other Location (Reliability: 1)
DDX23_HUMAN
820
0
95583
Swiss-Prot
other Location (Reliability: 1)
DDX24_HUMAN
859
0
96332
Swiss-Prot
other Location (Reliability: 2)
DDX25_HUMAN
483
0
54692
Swiss-Prot
other Location (Reliability: 3)
G3BP1_HUMAN
466
0
52164
Swiss-Prot
other Location (Reliability: 2)
IF4A1_HUMAN
406
0
46154
Swiss-Prot
other Location (Reliability: 2)
IF4A2_HUMAN
407
0
46402
Swiss-Prot
other Location (Reliability: 1)
DDX60_HUMAN
1712
0
197853
Swiss-Prot
other Location (Reliability: 2)
DDX6L_HUMAN
1706
0
197674
Swiss-Prot
other Location (Reliability: 3)
DDX6_HUMAN
483
0
54417
Swiss-Prot
other Location (Reliability: 2)
DHX15_HUMAN
795
0
90933
Swiss-Prot
other Location (Reliability: 1)
DHX16_HUMAN
1041
0
119264
Swiss-Prot
other Location (Reliability: 1)
DHX29_HUMAN
1369
0
155236
Swiss-Prot
Mitochondrion (Reliability: 2)
DHX30_HUMAN
1194
0
133938
Swiss-Prot
Mitochondrion (Reliability: 4)
SMBP2_HUMAN
993
0
109149
Swiss-Prot
other Location (Reliability: 3)
TDRD9_HUMAN
1382
0
155683
Swiss-Prot
other Location (Reliability: 2)
DDX10_HUMAN
875
0
100888
Swiss-Prot
other Location (Reliability: 2)
DX39B_HUMAN
428
0
48991
Swiss-Prot
other Location (Reliability: 1)
SUV3_HUMAN
786
0
87991
Swiss-Prot
Mitochondrion (Reliability: 1)
DD19A_HUMAN
478
0
53975
Swiss-Prot
other Location (Reliability: 1)
DD19B_HUMAN
479
0
53927
Swiss-Prot
other Location (Reliability: 1)
DDX12_HUMAN
950
0
106006
Swiss-Prot
Mitochondrion (Reliability: 3)
DDX17_HUMAN
729
0
80272
Swiss-Prot
Secretory Pathway (Reliability: 3)
DDX18_HUMAN
670
0
75407
Swiss-Prot
Mitochondrion (Reliability: 4)
DDX1_HUMAN
740
0
82432
Swiss-Prot
other Location (Reliability: 3)
IFIH1_HUMAN
1025
0
116689
Swiss-Prot
other Location (Reliability: 3)
RENT1_HUMAN
1129
0
124345
Swiss-Prot
other Location (Reliability: 1)
A0A1U9X7L7_HUMAN
981
0
112455
TrEMBL
other Location (Reliability: 3)
A2A376_HUMAN
722
0
82613
TrEMBL
other Location (Reliability: 1)
A0A499FJW5_HUMAN
312
0
35541
TrEMBL
other Location (Reliability: 1)
A0A140T8Y5_HUMAN
560
0
63455
TrEMBL
other Location (Reliability: 5)
A0A0D9SFB3_HUMAN
640
0
70840
TrEMBL
other Location (Reliability: 2)
B4DV26_HUMAN
661
0
74772
TrEMBL
other Location (Reliability: 2)
B4E0S6_HUMAN
784
0
89547
TrEMBL
other Location (Reliability: 1)
A0A2R8YCW1_HUMAN
647
0
71694
TrEMBL
other Location (Reliability: 2)
A0A0D9SG12_HUMAN
647
0
71541
TrEMBL
other Location (Reliability: 2)
A4UCU0_HUMAN
182
0
19802
TrEMBL
other Location (Reliability: 1)
Q7Z2V5_HUMAN
406
0
45997
TrEMBL
other Location (Reliability: 3)
B4E102_HUMAN
146
0
15900
TrEMBL
other Location (Reliability: 1)
B3KQ43_HUMAN
417
0
46782
TrEMBL
other Location (Reliability: 1)
J3KT12_HUMAN
341
0
38862
TrEMBL
other Location (Reliability: 2)
M0R1S3_HUMAN
112
0
11720
TrEMBL
other Location (Reliability: 2)
A0A7P0T8G7_HUMAN
345
0
37645
TrEMBL
other Location (Reliability: 4)
Q53G16_HUMAN
479
0
53914
TrEMBL
other Location (Reliability: 1)
A0A7I2V4Q0_HUMAN
160
0
17421
TrEMBL
other Location (Reliability: 3)
B4DED6_HUMAN
643
0
72158
TrEMBL
other Location (Reliability: 2)
A0A7I2YQ77_HUMAN
677
0
75460
TrEMBL
other Location (Reliability: 3)
A0A024R7H0_HUMAN
316
0
35095
TrEMBL
other Location (Reliability: 1)
J3QLN6_HUMAN
163
0
18043
TrEMBL
other Location (Reliability: 2)
Q86YB2_HUMAN
1220
0
139315
TrEMBL
other Location (Reliability: 4)
Q7KYK3_HUMAN
144
0
15867
TrEMBL
other Location (Reliability: 1)
B7Z611_HUMAN
631
0
71103
TrEMBL
other Location (Reliability: 2)
B3KY11_HUMAN
800
0
93234
TrEMBL
other Location (Reliability: 1)
E7EX41_HUMAN
191
0
21615
TrEMBL
other Location (Reliability: 3)
Q59E92_HUMAN
457
0
51729
TrEMBL
Mitochondrion (Reliability: 1)
F8WEI3_HUMAN
103
0
11132
TrEMBL
other Location (Reliability: 2)
Q4ZG72_HUMAN
546
0
61595
TrEMBL
other Location (Reliability: 1)
A0A8I5KXC3_HUMAN
1023
0
115418
TrEMBL
other Location (Reliability: 5)
B2R858_HUMAN
472
0
53216
TrEMBL
other Location (Reliability: 3)
H3BQK0_HUMAN
484
0
54500
TrEMBL
Mitochondrion (Reliability: 4)
F6S4E6_HUMAN
231
0
25898
TrEMBL
other Location (Reliability: 1)
A0A2R8Y5G6_HUMAN
622
0
69048
TrEMBL
other Location (Reliability: 1)
F6S8Q4_HUMAN
629
0
69356
TrEMBL
other Location (Reliability: 2)
A0A7P0TB94_HUMAN
423
0
46890
TrEMBL
other Location (Reliability: 3)
M0QZC0_HUMAN
118
0
12286
TrEMBL
other Location (Reliability: 2)
Q86WD0_HUMAN
101
0
11017
TrEMBL
other Location (Reliability: 1)
H0YI52_HUMAN
152
0
16530
TrEMBL
other Location (Reliability: 2)
F6QDS0_HUMAN
479
0
54018
TrEMBL
other Location (Reliability: 1)
B3GQE6_HUMAN
765
0
86635
TrEMBL
other Location (Reliability: 2)
B4DR88_HUMAN
631
0
72191
TrEMBL
other Location (Reliability: 2)
A0A0D9SF53_HUMAN
733
0
81477
TrEMBL
other Location (Reliability: 2)
B7Z5N6_HUMAN
567
1
62778
TrEMBL
other Location (Reliability: 2)
A0A2R8YF78_HUMAN
641
0
70940
TrEMBL
other Location (Reliability: 2)
B4DET0_HUMAN
1220
0
139681
TrEMBL
other Location (Reliability: 1)
B4DIS6_HUMAN
766
0
85210
TrEMBL
other Location (Reliability: 1)
A0A024RAS3_HUMAN
455
0
50647
TrEMBL
other Location (Reliability: 2)
F8WDT8_HUMAN
185
0
20343
TrEMBL
other Location (Reliability: 2)
A0A384N652_HUMAN
600
0
68501
TrEMBL
other Location (Reliability: 3)
A0A5H1ZRQ2_HUMAN
731
0
80458
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0G2JJL7_HUMAN
187
0
20397
TrEMBL
other Location (Reliability: 4)
B3KM65_HUMAN
413
0
46139
TrEMBL
other Location (Reliability: 5)
Q5SQH4_HUMAN
1041
0
119264
TrEMBL
other Location (Reliability: 1)
A8K088_HUMAN
406
0
46126
TrEMBL
other Location (Reliability: 2)
B4DKX3_HUMAN
781
0
90316
TrEMBL
other Location (Reliability: 2)
B7Z8P5_HUMAN
873
0
100143
TrEMBL
other Location (Reliability: 1)
B4DH55_HUMAN
139
0
14875
TrEMBL
other Location (Reliability: 1)
J3KTB5_HUMAN
257
0
29082
TrEMBL
other Location (Reliability: 1)
Q53TP4_HUMAN
589
0
68138
TrEMBL
other Location (Reliability: 1)
J3QQP0_HUMAN
95
0
10666
TrEMBL
other Location (Reliability: 2)
A0A087X059_HUMAN
275
0
30321
TrEMBL
other Location (Reliability: 1)
Q86VR6_HUMAN
745
0
85832
TrEMBL
other Location (Reliability: 2)
A0A7P0Z4K8_HUMAN
193
0
20189
TrEMBL
other Location (Reliability: 4)
Q9NTA9_HUMAN
399
0
44076
TrEMBL
other Location (Reliability: 1)
K7EPJ3_HUMAN
189
0
21362
TrEMBL
other Location (Reliability: 1)
B5BTY4_HUMAN
662
0
73171
TrEMBL
other Location (Reliability: 2)
Q5SQH5_HUMAN
560
0
63513
TrEMBL
other Location (Reliability: 5)
F6U6E2_HUMAN
125
0
13519
TrEMBL
other Location (Reliability: 1)
B4DHI6_HUMAN
465
0
52570
TrEMBL
other Location (Reliability: 3)
Q59EC7_HUMAN
845
0
97363
TrEMBL
other Location (Reliability: 5)
B2R988_HUMAN
648
0
72776
TrEMBL
Mitochondrion (Reliability: 3)
E7EMV8_HUMAN
98
0
10697
TrEMBL
other Location (Reliability: 1)
J3QL17_HUMAN
468
0
52825
TrEMBL
other Location (Reliability: 3)
B7Z8F4_HUMAN
1181
0
133958
TrEMBL
other Location (Reliability: 4)
A0A7P0TBA6_HUMAN
294
0
31662
TrEMBL
other Location (Reliability: 4)
B7Z700_HUMAN
941
1
106519
TrEMBL
other Location (Reliability: 2)
J3KT04_HUMAN
85
0
9272
TrEMBL
other Location (Reliability: 3)
Q8IV96_HUMAN
187
0
20426
TrEMBL
other Location (Reliability: 2)
A0A0K1H1B1_HUMAN
1706
0
197696
TrEMBL
other Location (Reliability: 3)
F6SXL5_HUMAN
136
0
14718
TrEMBL
other Location (Reliability: 2)
A0A8I5KNP3_HUMAN
768
0
85797
TrEMBL
other Location (Reliability: 1)
Q9P186_HUMAN
560
0
63460
TrEMBL
other Location (Reliability: 5)
B4DX78_HUMAN
470
0
53697
TrEMBL
Mitochondrion (Reliability: 3)
A0A8I5KZ07_HUMAN
937
0
106252
TrEMBL
Mitochondrion (Reliability: 3)
F5H1N9_HUMAN
196
0
22033
TrEMBL
other Location (Reliability: 2)
A0A8I5KQZ1_HUMAN
676
0
77696
TrEMBL
other Location (Reliability: 2)
B7Z6D5_HUMAN
765
0
86605
TrEMBL
other Location (Reliability: 2)
F6TRA5_HUMAN
238
0
26708
TrEMBL
other Location (Reliability: 1)
B3KWW1_HUMAN
854
0
98058
TrEMBL
other Location (Reliability: 2)
G3V0G3_HUMAN
375
0
41653
TrEMBL
other Location (Reliability: 2)
A0A8I5KNN2_HUMAN
808
0
89956
TrEMBL
other Location (Reliability: 1)
J3QL43_HUMAN
271
0
30649
TrEMBL
other Location (Reliability: 2)
A0A8I5KSH6_HUMAN
925
0
106382
TrEMBL
other Location (Reliability: 2)
B4DM03_HUMAN
763
0
85510
TrEMBL
other Location (Reliability: 1)
A8K6G9_HUMAN
1227
0
140475
TrEMBL
other Location (Reliability: 1)
B4DYZ1_HUMAN
722
0
80931
TrEMBL
other Location (Reliability: 5)
F6S2B7_HUMAN
132
0
14348
TrEMBL
other Location (Reliability: 1)
F6R6M7_HUMAN
197
0
21915
TrEMBL
other Location (Reliability: 1)
A0A0A0MT12_HUMAN
235
0
26355
TrEMBL
other Location (Reliability: 1)
Q86X36_HUMAN
1220
0
139287
TrEMBL
other Location (Reliability: 4)
A8K6X3_HUMAN
1032
0
117471
TrEMBL
other Location (Reliability: 3)
F8WE11_HUMAN
97
0
10892
TrEMBL
other Location (Reliability: 1)
J3QRQ7_HUMAN
212
0
23488
TrEMBL
other Location (Reliability: 3)
J3QR64_HUMAN
214
0
23772
TrEMBL
other Location (Reliability: 5)
Q5JWW0_HUMAN
95
0
10604
TrEMBL
other Location (Reliability: 1)
A0A024RBS0_HUMAN
600
0
68547
TrEMBL
other Location (Reliability: 3)
A0A3B3ISR7_HUMAN
679
0
77799
TrEMBL
other Location (Reliability: 2)
M0R0K1_HUMAN
166
0
17685
TrEMBL
other Location (Reliability: 2)
Q5STU3_HUMAN
425
0
48826
TrEMBL
other Location (Reliability: 1)
F6WLT2_HUMAN
289
0
32941
TrEMBL
other Location (Reliability: 1)
B3KRK2_HUMAN
496
0
55410
TrEMBL
other Location (Reliability: 1)
J3KS25_HUMAN
187
0
20532
TrEMBL
other Location (Reliability: 1)
Q59F68_HUMAN
375
0
42417
TrEMBL
other Location (Reliability: 2)
J3KSN7_HUMAN
109
0
12071
TrEMBL
other Location (Reliability: 1)
Q58F26_HUMAN
596
0
67106
TrEMBL
other Location (Reliability: 2)
Q9H4E3_HUMAN
455
0
50635
TrEMBL
other Location (Reliability: 2)
J3KS93_HUMAN
85
0
9354
TrEMBL
other Location (Reliability: 1)
H0Y8L8_HUMAN
173
0
19486
TrEMBL
other Location (Reliability: 4)
A0A8I5KPM1_HUMAN
482
0
55379
TrEMBL
other Location (Reliability: 2)
A0A024R9A4_HUMAN
660
0
73154
TrEMBL
other Location (Reliability: 1)
M0QXD4_HUMAN
41
0
4397
TrEMBL
other Location (Reliability: 2)
A0A7I2V507_HUMAN
406
0
46027
TrEMBL
other Location (Reliability: 3)
B4DW97_HUMAN
711
0
80016
TrEMBL
other Location (Reliability: 2)
K7EL56_HUMAN
108
0
11940
TrEMBL
other Location (Reliability: 1)
Q53GJ1_HUMAN
448
0
49882
TrEMBL
other Location (Reliability: 1)
Q59G92_HUMAN
310
0
34753
TrEMBL
Mitochondrion (Reliability: 4)
Q8TDR3_HUMAN
824
0
92221
TrEMBL
other Location (Reliability: 4)
A8KA56_HUMAN
820
0
95611
TrEMBL
other Location (Reliability: 1)
I3L1L6_HUMAN
617
0
69367
TrEMBL
other Location (Reliability: 1)
A0A024RCM3_HUMAN
428
0
48991
TrEMBL
other Location (Reliability: 1)
G3V529_HUMAN
816
0
91481
TrEMBL
other Location (Reliability: 1)
A0A7I2V2S0_HUMAN
416
0
47274
TrEMBL
other Location (Reliability: 3)
H7BXY3_HUMAN
1166
0
130550
TrEMBL
other Location (Reliability: 4)
Q6ZND7_HUMAN
528
0
58926
TrEMBL
Mitochondrion (Reliability: 5)
E9PIF2_HUMAN
835
0
96455
TrEMBL
other Location (Reliability: 2)
B4DZ28_HUMAN
981
0
112455
TrEMBL
other Location (Reliability: 3)
E9PBH4_HUMAN
96
0
10805
TrEMBL
other Location (Reliability: 1)
A3RJH1_HUMAN
740
0
82432
TrEMBL
other Location (Reliability: 3)
J3KTQ4_HUMAN
181
0
19817
TrEMBL
other Location (Reliability: 2)
B4DLU5_HUMAN
532
0
58774
TrEMBL
other Location (Reliability: 2)
Q8TEC9_HUMAN
353
0
39800
TrEMBL
other Location (Reliability: 3)
A8K7F6_HUMAN
406
0
46122
TrEMBL
other Location (Reliability: 2)
Q8NEH0_HUMAN
824
0
92156
TrEMBL
other Location (Reliability: 4)
A0A8I5KXY1_HUMAN
451
0
51655
TrEMBL
other Location (Reliability: 2)
E7EQG2_HUMAN
362
0
41290
TrEMBL
other Location (Reliability: 1)
E7EWK3_HUMAN
797
0
91431
TrEMBL
other Location (Reliability: 1)
B4DYP6_HUMAN
132
0
14081
TrEMBL
other Location (Reliability: 2)
A0A2R8Y645_HUMAN
716
1
79475
TrEMBL
other Location (Reliability: 2)
B7Z455_HUMAN
578
0
65250
TrEMBL
other Location (Reliability: 2)
D6RJA6_HUMAN
471
0
53964
TrEMBL
other Location (Reliability: 3)
B4DM30_HUMAN
900
0
102185
TrEMBL
other Location (Reliability: 1)
Q53HB9_HUMAN
547
0
61565
TrEMBL
other Location (Reliability: 2)
Q2NL95_HUMAN
449
0
50644
TrEMBL
other Location (Reliability: 1)
Q53HI2_HUMAN
622
0
69839
TrEMBL
other Location (Reliability: 1)
A0A2R8Y4A4_HUMAN
662
0
73243
TrEMBL
other Location (Reliability: 2)
Q59GX6_HUMAN
674
0
74579
TrEMBL
other Location (Reliability: 5)
H3BTB3_HUMAN
129
0
14479
TrEMBL
other Location (Reliability: 1)
B4DVE4_HUMAN
411
0
46090
TrEMBL
other Location (Reliability: 3)
A0A7I2V5X8_HUMAN
319
0
35174
TrEMBL
other Location (Reliability: 3)
E9PR46_HUMAN
407
0
46514
TrEMBL
other Location (Reliability: 2)
Q5THR1_HUMAN
679
0
76047
TrEMBL
other Location (Reliability: 3)
H0YHH7_HUMAN
160
0
18478
TrEMBL
other Location (Reliability: 2)
A0A024R1Y5_HUMAN
678
0
76613
TrEMBL
other Location (Reliability: 2)
A0A0G2JHN7_HUMAN
95
0
10253
TrEMBL
other Location (Reliability: 1)
A0A8I5KND9_HUMAN
661
0
73890
TrEMBL
other Location (Reliability: 2)
A0A024R0Z3_HUMAN
820
0
95583
TrEMBL
other Location (Reliability: 1)
Q7Z4W5_HUMAN
479
0
54137
TrEMBL
other Location (Reliability: 1)
C9J081_HUMAN
250
0
27682
TrEMBL
other Location (Reliability: 2)
A0A0C4DG89_HUMAN
1032
0
117461
TrEMBL
other Location (Reliability: 3)
Q59FS7_HUMAN
676
0
75048
TrEMBL
other Location (Reliability: 3)
K0J110_HUMAN
731
0
82037
TrEMBL
other Location (Reliability: 3)
A0A8I5KUU7_HUMAN
489
0
55936
TrEMBL
other Location (Reliability: 2)
Q8IYV2_HUMAN
824
0
92156
TrEMBL
other Location (Reliability: 4)
D3DQA6_HUMAN
883
0
100393
TrEMBL
other Location (Reliability: 3)
H3BMQ5_HUMAN
233
0
26083
TrEMBL
other Location (Reliability: 2)
D6RA70_HUMAN
739
0
82989
TrEMBL
other Location (Reliability: 3)
B4E010_HUMAN
410
0
45939
TrEMBL
other Location (Reliability: 1)
Q59F66_HUMAN
737
0
81067
TrEMBL
Secretory Pathway (Reliability: 3)
A0A7P0T9T8_HUMAN
754
0
83293
TrEMBL
other Location (Reliability: 4)
F5H658_HUMAN
1181
0
134002
TrEMBL
other Location (Reliability: 4)
A8K6J9_HUMAN
1220
0
139385
TrEMBL
other Location (Reliability: 4)
J3QS69_HUMAN
300
0
33949
TrEMBL
other Location (Reliability: 2)
Q59GT8_HUMAN
67
0
7705
TrEMBL
other Location (Reliability: 1)
K7ENP6_HUMAN
92
0
10243
TrEMBL
other Location (Reliability: 1)
A0A7P0Z4A9_HUMAN
921
0
104962
TrEMBL
other Location (Reliability: 5)
D6RCM4_HUMAN
518
0
56542
TrEMBL
other Location (Reliability: 1)
A0A3B3IRK8_HUMAN
986
0
112285
TrEMBL
other Location (Reliability: 3)
Q8NI92_HUMAN
145
0
16395
TrEMBL
other Location (Reliability: 1)
Q6PJK6_HUMAN
599
0
67447
TrEMBL
other Location (Reliability: 2)
H0YD26_HUMAN
191
0
21004
TrEMBL
other Location (Reliability: 3)
B4DFD7_HUMAN
854
0
97507
TrEMBL
other Location (Reliability: 2)
F6QYI9_HUMAN
187
0
20450
TrEMBL
Mitochondrion (Reliability: 5)
B4DN41_HUMAN
603
0
67762
TrEMBL
other Location (Reliability: 2)
H0Y960_HUMAN
305
0
32970
TrEMBL
other Location (Reliability: 1)
J3QKZ9_HUMAN
134
0
14595
TrEMBL
other Location (Reliability: 2)
A0A7I2V421_HUMAN
358
0
39522
TrEMBL
other Location (Reliability: 3)
A0A2U3TZJ9_HUMAN
661
0
73214
TrEMBL
other Location (Reliability: 2)
C9J8G5_HUMAN
224
0
24975
TrEMBL
other Location (Reliability: 1)
F5H5U2_HUMAN
569
0
65191
TrEMBL
other Location (Reliability: 3)
A0A2R8YDH3_HUMAN
503
0
56248
TrEMBL
other Location (Reliability: 2)
B3KN51_HUMAN
447
0
51794
TrEMBL
other Location (Reliability: 1)
B4E047_HUMAN
173
0
18910
TrEMBL
other Location (Reliability: 2)
A0A2R8YFS5_HUMAN
661
0
73156
TrEMBL
other Location (Reliability: 2)
F8VRX4_HUMAN
208
0
22945
TrEMBL
other Location (Reliability: 3)
H3BN59_HUMAN
261
0
28982
TrEMBL
other Location (Reliability: 1)
A8KA76_HUMAN
1025
0
116630
TrEMBL
other Location (Reliability: 3)
K7EIL8_HUMAN
125
0
13793
TrEMBL
other Location (Reliability: 1)
A0A7I2V4J3_HUMAN
474
0
52357
TrEMBL
other Location (Reliability: 3)
A0A7P0TB70_HUMAN
875
0
100532
TrEMBL
Secretory Pathway (Reliability: 4)
K7EN69_HUMAN
130
0
14396
TrEMBL
other Location (Reliability: 1)
A0A7I2V2M5_HUMAN
729
0
81103
TrEMBL
other Location (Reliability: 3)
J3KTA4_HUMAN
614
0
69087
TrEMBL
other Location (Reliability: 3)
B4DL08_HUMAN
548
0
61993
TrEMBL
other Location (Reliability: 3)
Q5JR04_HUMAN
947
0
107210
TrEMBL
Mitochondrion (Reliability: 3)
A0A7P0Z4I9_HUMAN
279
0
29990
TrEMBL
other Location (Reliability: 4)
A8K7A1_HUMAN
483
0
54284
TrEMBL
other Location (Reliability: 2)
A0A024R8W0_HUMAN
411
0
46871
TrEMBL
other Location (Reliability: 4)
B4E3C4_HUMAN
308
0
33792
TrEMBL
Mitochondrion (Reliability: 5)
A0A2R8YFR4_HUMAN
660
0
73127
TrEMBL
other Location (Reliability: 2)
B5BUE6_HUMAN
614
0
69121
TrEMBL
other Location (Reliability: 3)
I3L3H2_HUMAN
390
0
44511
TrEMBL
other Location (Reliability: 5)
Q59H21_HUMAN
512
0
57757
TrEMBL
Mitochondrion (Reliability: 5)
A0A8I5KYZ4_HUMAN
729
0
81578
TrEMBL
other Location (Reliability: 1)
Q9NVY6_HUMAN
257
0
28598
TrEMBL
other Location (Reliability: 2)
Q59G60_HUMAN
733
0
82611
TrEMBL
other Location (Reliability: 2)
A0A1X7SBZ2_HUMAN
729
0
80254
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1U9X7L6_HUMAN
981
0
112397
TrEMBL
other Location (Reliability: 3)
Q9HBZ9_HUMAN
478
0
54020
TrEMBL
other Location (Reliability: 1)
A0A0U4B4U6_HUMAN
479
0
53927
TrEMBL
other Location (Reliability: 1)
B4DZQ7_HUMAN
420
0
47558
TrEMBL
other Location (Reliability: 2)
DDX11_HUMAN
970
0
108313
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
x * 100000, gel filtration
119037
x * 119037, calculated from sequence
130000
-
glycerol gradient centrifugation
140000
246000
-
calculated from sequence. Apart from an N-terminal domain of unknown function, Brr2p consists of two putative helicase domains, each connected at its C-terminus to a Sec63-like domain
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 130000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
P68 may undergo various modifications such as ubiquitylation, sumoylation, and acetylation
phosphoprotein
sumoylation
P68 may undergo various modifications such as ubiquitylation, sumoylation, and acetylation. P68 may be sumoylated on site K53 residue, which may be associated with transcriptional coactivation
ubiquitination
P68 may undergo various modifications such as ubiquitylation, sumoylation, and acetylation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of RIG-1, PDB ID 2YKG
crystal structure analysis, PDB ID 3G0H
crystals of DDX1954-475 in complex with RNA and Mg/adenosine 5'-(beta,gamma-imido)triphosphate are obtained by vapor diffusion in sitting drops incubated at 4°C by mixing 0.0001 ml of protein solution (20 mg/ml) including 10-molar excess of decauracil ssRNA, adenosine 5'-(beta,gamma-imido)triphosphate, and MgCl2 and 0.0002 ml of reservoir solution containing 14% polyethylene glycol monomethyl ether 2000, 0.25 M trimethylamine n-oxide, 0.1 M Tris, pH 8. The crystal structures of DDX19, in its RNA-bound prehydrolysis and free posthydrolysis state, reveal an alpha-helix that inserts between the conserved domains of the free protein to negatively regulate ATPase activity
hanging-drop method, crystallization of recombinant DDX3 RNA helicase domain
purified recombinant Brr2-Jab1 complex, for complex 1: yBrr2FL and yJab1 are mixed in a 1:2 molar ratio in 10 mM Tris-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, and separated by gel filtration and and concentrated to 2 mg/ml, followed by sitting drop vapor diffusion technique, mixing of 0.0013 ml of protein solution with 0.0013 ml of reservoir solution containing 0.1 M Tris-HCl, pH 7.5, 10.5% w/v PEG 3350, and 0.2 M MgCl2, 18°C. For complex 2: yBrr2T2, yJab1 and yNtr2 are mixed in a 1:5:5 molar ratio in 10 mM Tris-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, and separated by gel filtration and and concentrated to 4 mg/ml, followed by hanging drop vapor diffusion technique, mixing of 0.0005 ml of protein solution with 0.00025 ml of reservoit solution containing 0.1 M MES-NaOH, pH 6.5, 9.2% w/v PEG 4000, 0.4 M MgCl2, and with 0.00025 ml 0.33% w/v 1,5-naphthalenedisulfonic acid, 18°C. X-ray diffraction structure determination and analysis at 3.4-4.2 A resolution, molecular replacement using the yBrr2T4-Jab1 structure coordinates as the search model (PDB ID 4BGD)
purified recombinant Brr2-Jab1 complex, X-ray diffraction structure determination and analysis at 3.4-4.2 A resolution
purified recombinant detagged enzyme in complex with inhibitors 6-benzyl-3-[(2R)-2-(3-fluoropyridin-2-yl)-6-methyl-3,4-dihydro-2H-1-benzopyran-7-yl]-4,6-dihydropyrido[4,3-d]pyrimidine-2,7(1H,3H)-dione, 6-benzyl-3-[3-(benzyloxy)phenyl]-4,6-dihydropyrido[4,3-d]pyrimidine-2,7(1H,3H)-dione, and 3-[5-[(Z)-(2-cyclohexyl-5-imino-7-oxo-5H-[1,3,4]thiadiazolo[3,2-a]pyrimidin-6(7H)-ylidene)methyl]furan-2-yl]benzoic acid, X-ray diffraction structure determination and analysis at 2.75 A, 2.95 A, and 2.80 A resolution, respectivly
purified recombinant enzyme Aquanrius, X-ray diffraction structure determination and analysis at 2.3 A resolution
purified recombinant helicase core of UPF1_1 in its apo-state, X-ray diffraction structure determination and analysis at 3.34 A resolution. Analysis of the X-ray crystal structures of the different states of UPF1_2DELTACH mutant
recombinant catalytic core fragment DHX8DELTA547 bound to ADP and to poly(A)6 single-strand RNA, hanging-drop vapour-diffusion, mixing of 500 nl of protein solution consisting of 3 mg/ml DHX8DELTA547, 1 mM ADP, and 1 mM MgCl2, with 0.00015 ml of reservoir solution comprising 15% v/v 2-methyl-2,4-pentanediol, 100 mM sodium acetate, pH 5.5 and 6% v/v DMSO, and equilibration over 0.25 ml reservoir solution. For the DHX8DELTA547 structure bound to poly(A)6 RNA, a DHX8DELTA547 crystal grown in the presence of ADP is soaked with 1 mM poly(A)6 ssRNA at 4°C for 48 h, X-ray diffraction structure determination and analysis at 2.3-3.2 A resolution, molecular replacement using the structures of RecA1 and RecA2 domains of Saccharomyces cerevisiae Prp43 (PDB ID 2XAU) and of helicase-associated domain of DHX8 (PDB ID 3I4U) as two independent search models
sitting-drop vapor diffusion method at 4 °C. Crystal structures of the conserved domain 1 of the DEIH-motif-containing helicase DHX9 and of the DEAD-box helicase DDX20. Both contain a RecA-like core, but DHX9 differs from DEAD-box proteins in the arrangement of secondary structural elements and is more similar to viral helicases such as NS3. The N-terminus of the DHX9 core contains two long alpha-helices that reside on the surface of the core without contributing to nucleotide binding
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D279A
site-directed mutagenesis, the mutation affects ATP hydrolysis
DELTA53-105
-
a region within the N-terminus of RHAU, referred to as the RSM, interacts with human telomerase RNA
F192E
site-directed mutagenesis, the mutant shows slightly reduced activity compared with the wild-type enzyme. Upf1F192E definitely prefers to unwind a dsDNA than to translocate it, strand switching
K191S
site-directed mutagenesis, the mutation affects ATP binding
K235A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD2, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K236A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD2, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K236E
-
mutant exhibits relatively minor reduction in interaction with SNV PCE
K50R
site-directed mutagenesis, ATPase dead mutant, fails completely to unwind triplex substrates
K54A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD1, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K54A/K55A
-
mutant exhibits relatively minor reduction in interaction with SNV PCE
K54A/K55A/K236E
-
triple mutant shows a severe reduction in interaction with junD post-transcriptional control element (PCE) or SNV PCE compared with wild-type
K55A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD1, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K829A
site-directed mutagenesis, mutation of the invariant lysine residue from motif I involved in ATP binding and hydrolysis drastically reduced Aquarius's ability to bind ATP and ADP and to hydroxadlyze ATP, the mutant shows significantly reduced ATPase activity compared to wild-type enzyme
K897del
site-directed mutagenesis, the mutant fails in unwinding the DNA substrates
Y1196A
site-directed mutagenesis, mutation of a conserved aromatic residue located near the putative RNA-binding surface of the RecA2 inhibits Aquarius's RNA-unwinding activity without changing its RNA-binding and ATPase properties, a helicase-deficient mutant
Y593F
-
expression of the mutant enzyme in SW620 cells leads to Snail repression, E-cadherin upregulation and vimentin repression
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged and N-terminally calmodulin-binding-protein-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Rosetta by nickel and calmodulin affinity chromatography
recombinant CBP- and His-tagged wild-type and mutant isozymes from Escherichia coli strain BL21(DE3) by nickel affinity and calmodulin affinity chromatography, followed by dialysis
recombinant His-tagged enzyme by nickel affinity chromatography and anion exchange chromatography
recombinant His-tagged enzyme from Spodoptera frugiperda Sf9 cells by nickel affinity and heparin affinity chromatography
recombinant His10-tagged Brr2 fragments from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography, tag cleavage by TEV protease, and gel filtration
recombinant His6-GST-tagged full-length DHX8 and truncated mutant DHX8DELTA547 from Sf9 insect cells by nickel affinity and heparin affinity chromatography, and gel filtration
recombinant His6-tagged enzyme from Spodoptera frugiperda Sf9 cells by nickel affinity chromatography, tag cleavage by TEV protease, follwed by dialysis, another step of nickel affinity chromatography, and ultrafiltration of the flow-through
recombinant N-terminally His6-tagged mutant enzymes from HEK293E cells by nickel affinity chromatography
using affinity chromatography
-
using Ni-NTA chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL-21
-
expression in Escherichia coli
gene BRR2, recombinant expression of His10-tagged TEV-cleavable codon-optimized DNA fragments encoding selected regions of yBrr2 in Escherichia coli strain Rosetta2 (DE3)
gene DDX5, is located in the region 17q23-q25
gene SNRNP200
gene SNRNP200, recombinant expression of His10-tagged TEV-cleavable codon-optimized DNA fragments encoding selected regions of hBrr2 in Escherichia coli strain Rosetta2 (DE3)
overexpression in Escherichia coli
recombinant expression of C-terminally His-tagged and N-terminally calmodulin-binding-protein-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Rosetta
recombinant expression of C-terminally His6-GST-tagged full-length DHX8 (fl-DHX8) and truncated construct containing the complete catalytically active C-terminal helicase core region (DHX8DELTA547) in Spodoptera frugiperda Sf9 cells using the baculovirus expression system
recombinant expression of FLAG-tagged DHX34 in HEK-293T cells, co-expression with recombinant UPF1 protein, DHX34 and UPF1 interact directly, but weak interaction with UPF2 and UPF3b
recombinant expression of FLAG3-tagged wild-type and mutant enzymes in HEK293T cells
recombinant expression of His-tagged enzyme
recombinant expression of N-terminally His6-tagged enzyme in Spodooptera frugiperda Sf9 cells
recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in HEK293e cells
recombinant expression of wild-type and mutant isozymes, that are CBP-tagged at the N-terminus and His-tagged at the C-terminus, in Escherichia coli strain BL21(DE3)
recombinant His-tagged enzyme expression in Spodoptera frugiperda Sf9 cells using the baculovirus expression system
recombinantly expressed as a His-tagged fusion protein
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
an alpha-helix that inserts between the conserved domains of the free protein negatively regulate ATPase activity
polymerase II can interact with beta-actin, and this interaction is enhanced due to the overexpression of RNA helicase A
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
enzyme p68 is a drug target in the treatment of cancer, e.g. breast cancer
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rodamilans, B.; Montoya, G.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain
Acta Crystallogr. Sect. F
63
283-286
2007
Homo sapiens (O00571), Homo sapiens
Manually annotated by BRENDA team
Abdelhaleem, M.
RNA helicases: regulators of differentiation
Clin. Biochem.
38
499-503
2005
Homo sapiens (O00571), Homo sapiens (O15523), Homo sapiens (Q9NQI0), Homo sapiens (Q9UHL0), Homo sapiens, Mus musculus (Q501J6), Mus musculus (Q61656), Mus musculus (Q9QY15), Rattus norvegicus (Q9QY16)
Manually annotated by BRENDA team
Lee, C.G.; Hurwitz, J.
A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3' to 5' direction.
J. Biol. Chem.
267
4398-4407
1992
Homo sapiens
Manually annotated by BRENDA team
Flores-Rozas, H.; Hurwitz, J.
Characterization of a new RNA helicase from nuclear extracts of HeLa cells which translocates in the 5' to 3' direction.
J. Biol. Chem.
268
21372-21383
1993
Homo sapiens
Manually annotated by BRENDA team
Gutti, R.K.; Tsai-Morris, C.H.; Dufau, M.L.
Gonadotropin-regulated testicular helicase (DDX25), an essential regulator of spermatogenesis, prevents testicular germ cell apoptosis
J. Biol. Chem.
283
17055-17064
2008
Homo sapiens (Q9UHL0)
Manually annotated by BRENDA team
Imamura, O.; Saiki, K.; Tani, T.; Ohshima, Y.; Sugawara, M.; Furuichi. Y.
Cloning and characterization of a human DEAH-box RNA helicase, a functional homolog of fission yeast Cdc28/Prp8
Nucleic Acids Res.
26
2063-2068
1998
Homo sapiens (O60231), Homo sapiens
Manually annotated by BRENDA team
Vlineva, T.; Yang, J.; Silvennoinen, O.
Characterization of RNA helicase A as component of STAT6-dependent enhanceosome
Nucleic Acids Res.
34
3938-3946
2006
Homo sapiens
Manually annotated by BRENDA team
Noble, C.G.; Song, H.
MLN51 stimulates the RNA-helicase activity of eIF4AIII
PLoS One
21
e303
2007
Homo sapiens (P38919)
Manually annotated by BRENDA team
Tang, W.; You, W.; Shi, F.; Qi, T.; Wang, L.; Djouder, Z.; Liu, W.; Zeng, X.
RNA helicase A acts as a bridging factor linking nuclear beta-actin with RNA polymerase II
Biochem. J.
420
421-428
2009
Homo sapiens
Manually annotated by BRENDA team
Hahn, D.; Beggs, J.D.
Brr2p RNA helicase with a split personality: insights into structure and function
Biochem. Soc. Trans.
38
1105-1109
2010
Homo sapiens
Manually annotated by BRENDA team
Collins, R.; Karlberg, T.; Lehtioe, L.; Schuetz, P.; van den Berg, S.; Dahlgren, L.G.; Hammarstroem, M.; Weigelt, J.; Schueler, H.
The DEXD/H-box RNA helicase DDX19 is regulated by an alpha-helical switch
J. Biol. Chem.
284
10296-10300
2009
Homo sapiens (Q9UMR2), Homo sapiens
Manually annotated by BRENDA team
Schuetz, P.; Wahlberg, E.; Karlberg, T.; Hammarstroem, M.; Collins, R.; Flores, A.; Schueler, H.
Crystal structure of human RNA helicase A (DHX9): structural basis for unselective nucleotide base binding in a DEAD-box variant protein
J. Mol. Biol.
400
768-782
2010
Homo sapiens (Q08211), Homo sapiens
Manually annotated by BRENDA team
Minshall, N.; Kress, M.; Weil, D.; Standart, N.
Role of p54 RNA helicase activity and its C-terminal domain in translational repression, P-body localization and assembly
Mol. Biol. Cell
20
2464-2472
2009
Homo sapiens (P26196), Homo sapiens
Manually annotated by BRENDA team
Carter, C.L.; Lin, C.; Liu, C.Y.; Yang, L.; Liu, Z.R.
Phosphorylated p68 RNA helicase activates Snail1 transcription by promoting HDAC1 dissociation from the Snail1 promoter
Oncogene
29
5427-5436
2010
Homo sapiens
Manually annotated by BRENDA team
Ranji, A.; Shkriabai, N.; Kvaratskhelia, M.; Musier-Forsyth, K.; Boris-Lawrie, K.
Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAs
J. Biol. Chem.
286
5328-5337
2011
Homo sapiens
Manually annotated by BRENDA team
Choi, Y.J.; Lee, S.G.
The DEAD-box RNA helicase DDX3 interacts with DDX5, co-localizes with it in the cytoplasm during the G2/M phase of the cycle, and affects its shuttling during mRNP export
J. Cell. Biochem.
113
985-996
2012
Homo sapiens, Homo sapiens (P17844)
Manually annotated by BRENDA team
Kar, A.; Fushimi, K.; Zhou, X.; Ray, P.; Shi, C.; Chen, X.; Liu, Z.; Chen, S.; Wu, J.Y.
RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5 splice site
Mol. Cell. Biol.
31
1812-1821
2011
Homo sapiens (P17844)
Manually annotated by BRENDA team
Booy, E.P.; Meier, M.; Okun, N.; Novakowski, S.K.; Xiong, S.; Stetefeld, J.; McKenna, S.A.
The RNA helicase RHAU (DHX36) unwinds a G4-quadruplex in human telomerase RNA and promotes the formation of the P1 helix template boundary
Nucleic Acids Res.
40
4110-4124
2012
Homo sapiens
Manually annotated by BRENDA team
Manojlovic, Z.; Stefanovic, B.
A novel role of RNA helicase A in regulation of translation of type I collagen mRNAs
RNA
18
321-334
2012
Homo sapiens
Manually annotated by BRENDA team
Xing, L.; Niu, M.; Zhao, X.; Kleiman, L.
Different activities of the conserved lysine residues in the double-stranded RNA binding domains of RNA helicase A in vitro and in the cell
Biochim. Biophys. Acta
1840
2234-2243
2014
Homo sapiens (Q08211)
Manually annotated by BRENDA team
Chen, G.; Liu, C.H.; Zhou, L.; Krug, R.M.
Cellular DDX21 RNA helicase inhibits influenza A virus replication but is counteracted by the viral NS1 protein
Cell Host Microbe
15
484-493
2014
Homo sapiens (Q9NR30)
Manually annotated by BRENDA team
Hug, N.; Caceres, J.F.
The RNA helicase DHX34 activates NMD by promoting a transition from the surveillance to the decay-inducing complex
Cell Rep.
8
1845-1856
2014
Homo sapiens (Q14147), Homo sapiens
Manually annotated by BRENDA team
Leitao, A.L.; Costa, M.C.; Enguita, F.J.
Unzippers, resolvers and sensors: a structural and functional biochemistry tale of RNA helicases
Int. J. Mol. Sci.
16
2269-2293
2015
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P21372), Saccharomyces cerevisiae (P47047), Dengue virus, Hepacivirus C, Neurospora crassa, Yellow fever virus, Homo sapiens (O95786), Homo sapiens (Q9UMR2), Murray Valley encephalitis virus (P05769), Kunjin virus (P14335), Japanese encephalitis virus (P27395)
Manually annotated by BRENDA team
Guo, M.; Hundseth, K.; Ding, H.; Vidhyasagar, V.; Inoue, A.; Nguyen, C.H.; Zain, R.; Lee, J.S.; Wu, Y.
A distinct triplex DNA unwinding activity of ChlR1 helicase
J. Biol. Chem.
290
5174-5189
2015
Homo sapiens (Q96FC9), Homo sapiens
Manually annotated by BRENDA team
Fiorini, F.; Bagchi, D.; Le Hir, H.; Croquette, V.
Human Upf1 is a highly processive RNA helicase and translocase with RNP remodelling activities
Nat. Commun.
6
7581
2015
Homo sapiens (Q92900), Homo sapiens
Manually annotated by BRENDA team
Erkizan, H.V.; Schneider, J.A.; Sajwan, K.; Graham, G.T.; Griffin, B.; Chasovskikh, S.; Youbi, S.E.; Kallarakal, A.; Chruszcz, M.; Padmanabhan, R.; Casey, J.L.; Ueren, A.; Toretsky, J.A.
RNA helicase A activity is inhibited by oncogenic transcription factor EWS-FLI1
Nucleic Acids Res.
43
1069-1080
2015
Homo sapiens (Q08211)
Manually annotated by BRENDA team
Felisberto-Rodrigues, C.; Thomas, J.C.; McAndrew, C.; Le Bihan, Y.V.; Burke, R.; Workman, P.; van Montfort, R.L.M.
Structural and functional characterisation of human RNA helicase DHX8 provides insights into the mechanism of RNA-stimulated ADP release
Biochem. J.
476
2521-2543
2019
Homo sapiens (Q14562), Homo sapiens
Manually annotated by BRENDA team
Xie, Q.; Liu, J.; Shan, Y.; Wang, S.; Liu, F.
Substrate determinants for unwinding activity of the DExH/D-Box protein RNA helicase A
Biochemistry
57
6662-6668
2018
Homo sapiens (Q08211)
Manually annotated by BRENDA team
Giraud, G.; Terrone, S.; Bourgeois, C.F.
Functions of DEAD box RNA helicases DDX5 and DDX17 in chromatin organization and transcriptional regulation
BMB Rep.
51
613-622
2018
Drosophila melanogaster, Drosophila melanogaster (P19109), Homo sapiens (P17844), Homo sapiens (Q92841), Mus musculus (Q501J6), Mus musculus (Q61656)
Manually annotated by BRENDA team
Absmeier, E.; Santos, K.F.; Wahl, M.C.
Functions and regulation of the Brr2 RNA helicase during splicing
Cell Cycle
15
3362-3377
2016
Homo sapiens (O75643), Homo sapiens, Saccharomyces cerevisiae (P32639), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P32639)
Manually annotated by BRENDA team
Absmeier, E.; Becke, C.; Wollenhaupt, J.; Santos, K.F.; Wahl, M.C.
Interplay of cis- and trans-regulatory mechanisms in the spliceosomal RNA helicase Brr2
Cell Cycle
16
100-112
2017
Thermochaetoides thermophila (G0S0B9), Homo sapiens (O75643), Thermochaetoides thermophila IMI 039719 (G0S0B9), Thermochaetoides thermophila DSM 1495 (G0S0B9), Thermochaetoides thermophila CBS 144.50 (G0S0B9)
Manually annotated by BRENDA team
Hashemi, V.; Masjedi, A.; Hazhir-Karzar, B.; Tanomand, A.; Shotorbani, S.S.; Hojjat-Farsangi, M.; Ghalamfarsa, G.; Azizi, G.; Anvari, E.; Baradaran, B.; Jadidi-Niaragh, F.
The role of DEAD-box RNA helicase p68 (DDX5) in the development and treatment of breast cancer
J. Cell. Physiol.
234
5478-5487
2019
Homo sapiens (P17844), Homo sapiens
Manually annotated by BRENDA team
Iwatani-Yoshihara, M.; Ito, M.; Klein, M.G.; Yamamoto, T.; Yonemori, K.; Tanaka, T.; Miwa, M.; Morishita, D.; Endo, S.; Tjhen, R.; Qin, L.; Nakanishi, A.; Maezaki, H.; Kawamoto, T.
Discovery of allosteric inhibitors targeting the spliceosomal RNA helicase Brr2
J. Med. Chem.
60
5759-5771
2017
Homo sapiens (O75643)
Manually annotated by BRENDA team
De, I.; Bessonov, S.; Hofele, R.; dos Santos, K.; Will, C.L.; Urlaub, H.; Luehrmann, R.; Pena, V.
The RNA helicase Aquarius exhibits structural adaptations mediating its recruitment to spliceosomes
Nat. Struct. Mol. Biol.
22
138-144
2015
Homo sapiens (O60306), Homo sapiens
Manually annotated by BRENDA team
Gowravaram, M.; Bonneau, F.; Kanaan, J.; Maciej, V.D.; Fiorini, F.; Raj, S.; Croquette, V.; Le Hir, H.; Chakrabarti, S.
A conserved structural element in the RNA helicase UPF1 regulates its catalytic activity in an isoform-specific manner
Nucleic Acids Res.
46
2648-2659
2018
Homo sapiens (Q92900)
Manually annotated by BRENDA team