Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP-dependent RNA helicase DDX1

Gene

DDX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB: together with archease (ZBTB8OS), acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation (PubMed:24870230). Required for HIV-1 Rev function as well as for HIV-1 replication. Binds to the RRE sequence of HIV-1 mRNAs.6 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 538ATPCurated

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent helicase activity Source: UniProtKB
  • ATP-dependent RNA helicase activity Source: GO_Central
  • chromatin binding Source: UniProtKB
  • DNA/RNA helicase activity Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • double-stranded RNA binding Source: Ensembl
  • exonuclease activity Source: UniProtKB-KW
  • nuclease activity Source: UniProtKB
  • poly(A) binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA helicase activity Source: ProtInc
  • transcription cofactor activity Source: UniProtKB

GO - Biological processi

  • DNA duplex unwinding Source: UniProtKB
  • double-strand break repair Source: UniProtKB
  • multicellular organism development Source: UniProtKB
  • protein localization to cytoplasmic stress granule Source: AgBase
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • regulation of translational initiation Source: UniProtKB
  • response to exogenous dsRNA Source: Ensembl
  • response to virus Source: Ensembl
  • RNA secondary structure unwinding Source: GO_Central
  • spliceosomal complex assembly Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • tRNA splicing, via endonucleolytic cleavage and ligation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Exonuclease, Helicase, Hydrolase, Nuclease

Keywords - Biological processi

mRNA processing, Transcription, Transcription regulation, tRNA processing

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-6784531. tRNA processing in the nucleus.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DDX1 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 1
DEAD box protein retinoblastoma
Short name:
DBP-RB
Gene namesi
Name:DDX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2734. DDX1.

Subcellular locationi

  • Nucleus
  • Cytoplasm
  • Cytoplasmic granule

  • Note: Localized with MBNL1, TIAL1 and YBX1 in stress granules upon stress. Localized with CSTF2 in cleavage bodies. Forms large aggregates called DDX1 bodies. Relocalized into multiple foci (IR-induced foci or IRIF) after IR treatment, a process that depends on the presence of chromosomal DNA and/or RNA-DNA duplexes. Relocalized at sites of DNA double-strand breaks (DSBs) in an ATM-dependent manner after IR treatment. Colocalized with RELA in the nucleus upon TNF-alpha induction. Relocalized to the cytoplasm with a perinuclear staining pattern in avian infectious bronchitis virus (IBV)-infected cells. Required for proper localization of HIV-1 Rev. Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low (PubMed:24608264).1 Publication

GO - Cellular componenti

  • cleavage body Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic stress granule Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: MGI
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • tRNA-splicing ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521K → N: Abolishes ability to promote guanylylation of RTCB. 1 Publication
Mutagenesisi371 – 3711E → G: Inhibits the transcriptional activity of RELA and attenuates NF-kappa-B-mediated gene expression. 2 Publications
Mutagenesisi371 – 3711E → Q: Abolishes ability to promote guanylylation of RTCB. 2 Publications

Organism-specific databases

PharmGKBiPA27199.

Chemistry

ChEMBLiCHEMBL2010634.

Polymorphism and mutation databases

BioMutaiDDX1.
DMDMi6919862.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740ATP-dependent RNA helicase DDX1PRO_0000054986Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391N6-acetyllysineCombined sources
Modified residuei268 – 2681N6-acetyllysineCombined sources
Modified residuei281 – 2811N6-acetyllysineCombined sources
Modified residuei481 – 4811PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated. Phosphorylated by ATM kinase; phosphorylation is increased in response to ionizing radiation (IR).1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ92499.
MaxQBiQ92499.
PaxDbiQ92499.
PeptideAtlasiQ92499.
PRIDEiQ92499.

2D gel databases

REPRODUCTION-2DPAGEIPI00293655.

PTM databases

iPTMnetiQ92499.
PhosphoSiteiQ92499.
SwissPalmiQ92499.

Expressioni

Tissue specificityi

Highest levels of transcription in 2 retinoblastoma cell lines and in tissues of neuroectodermal origin including the retina, brain, and spinal cord.1 Publication

Gene expression databases

BgeeiQ92499.
CleanExiHS_DDX1.
ExpressionAtlasiQ92499. baseline and differential.
GenevisibleiQ92499. HS.

Organism-specific databases

HPAiCAB012280.
HPA034502.
HPA034503.

Interactioni

Subunit structurei

Interacts with PHF5A (via C-terminus) (By similarity). Interacts with MBNL1. Interacts with CSTF2. Interacts with HNRNPK. Interacts with ATM. Interacts with RELA (via C-terminus). Interacts (via C-terminus) with the replicase polyprotein 1ab Nsp14 of the avian infectious bronchitis virus (IBV). Interacts with Rev of HIV-1. Interacts with severe acute respiratory syndrome coronavirus (SARS-CoV) (via N-terminus). Component of the tRNA-splicing ligase complex.By similarity9 Publications

Protein-protein interaction databases

BioGridi108019. 136 interactions.
DIPiDIP-38163N.
IntActiQ92499. 30 interactions.
MINTiMINT-5005493.
STRINGi9606.ENSP00000233084.

Chemistry

BindingDBiQ92499.

Structurei

Secondary structure

1
740
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi90 – 989Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi120 – 13920Combined sources
Beta strandi141 – 15010Combined sources
Beta strandi164 – 1685Combined sources
Turni169 – 1713Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi191 – 1977Combined sources
Turni198 – 2014Combined sources
Beta strandi202 – 2076Combined sources
Beta strandi210 – 2178Combined sources
Helixi220 – 2223Combined sources
Beta strandi227 – 24519Combined sources
Helixi258 – 2603Combined sources
Helixi263 – 2653Combined sources
Beta strandi266 – 2683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XW3X-ray2.00A/B72-283[»]
ProteinModelPortaliQ92499.
SMRiQ92499. Positions 25-70, 86-674.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 428427Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini70 – 247178B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST
Domaini493 – 681189Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 525525Necessary for interaction with RELAAdd
BLAST
Regioni1 – 295295Necessary for interaction with HNRNPKAdd
BLAST
Regioni525 – 740216Necessary for interaction with HNRNPKAdd
BLAST
Regioni536 – 63196Necessary for interaction with replicase polyprotein 1ab nsp14 of IBVAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi370 – 3734DEAD box

Domaini

The helicase domain is involved in the stimulation of RELA transcriptional activity.

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0349. Eukaryota.
COG0513. LUCA.
GeneTreeiENSGT00770000120531.
HOGENOMiHOG000251633.
HOVERGENiHBG005462.
InParanoidiQ92499.
KOiK13177.
OMAiTLNNVKQ.
OrthoDBiEOG7RNJZJ.
PhylomeDBiQ92499.
TreeFamiTF106114.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF52540. SSF52540. 3 hits.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 2 hits.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92499-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAFSEMGVM PEIAQAVEEM DWLLPTDIQA ESIPLILGGG DVLMAAETGS
60 70 80 90 100
GKTGAFSIPV IQIVYETLKD QQEGKKGKTT IKTGASVLNK WQMNPYDRGS
110 120 130 140 150
AFAIGSDGLC CQSREVKEWH GCRATKGLMK GKHYYEVSCH DQGLCRVGWS
160 170 180 190 200
TMQASLDLGT DKFGFGFGGT GKKSHNKQFD NYGEEFTMHD TIGCYLDIDK
210 220 230 240 250
GHVKFSKNGK DLGLAFEIPP HMKNQALFPA CVLKNAELKF NFGEEEFKFP
260 270 280 290 300
PKDGFVALSK APDGYIVKSQ HSGNAQVTQT KFLPNAPKAL IVEPSRELAE
310 320 330 340 350
QTLNNIKQFK KYIDNPKLRE LLIIGGVAAR DQLSVLENGV DIVVGTPGRL
360 370 380 390 400
DDLVSTGKLN LSQVRFLVLD EADGLLSQGY SDFINRMHNQ IPQVTSDGKR
410 420 430 440 450
LQVIVCSATL HSFDVKKLSE KIMHFPTWVD LKGEDSVPDT VHHVVVPVNP
460 470 480 490 500
KTDRLWERLG KSHIRTDDVH AKDNTRPGAN SPEMWSEAIK ILKGEYAVRA
510 520 530 540 550
IKEHKMDQAI IFCRTKIDCD NLEQYFIQQG GGPDKKGHQF SCVCLHGDRK
560 570 580 590 600
PHERKQNLER FKKGDVRFLI CTDVAARGID IHGVPYVINV TLPDEKQNYV
610 620 630 640 650
HRIGRVGRAE RMGLAISLVA TEKEKVWYHV CSSRGKGCYN TRLKEDGGCT
660 670 680 690 700
IWYNEMQLLS EIEEHLNCTI SQVEPDIKVP VDEFDGKVTY GQKRAAGGGS
710 720 730 740
YKGHVDILAP TVQELAALEK EAQTSFLHLG YLPNQLFRTF
Length:740
Mass (Da):82,432
Last modified:August 1, 1998 - v2
Checksum:iC6D0179F83BD8C73
GO
Isoform 2 (identifier: Q92499-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     98-113: Missing.
     630-740: VCSSRGKGCY...YLPNQLFRTF → MVQRDAVTI

Note: No experimental confirmation available.
Show »
Length:622
Mass (Da):69,556
Checksum:iF0DC36DB1DAA09F8
GO
Isoform 3 (identifier: Q92499-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: Missing.

Note: No experimental confirmation available.
Show »
Length:612
Mass (Da):68,712
Checksum:i511B121802355812
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 128128Missing in isoform 3. 1 PublicationVSP_055453Add
BLAST
Alternative sequencei98 – 11316Missing in isoform 2. 1 PublicationVSP_055454Add
BLAST
Alternative sequencei630 – 740111VCSSR…LFRTF → MVQRDAVTI in isoform 2. 1 PublicationVSP_055455Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70649 mRNA. Translation: CAA49992.1.
AK297432 mRNA. Translation: BAG59860.1.
AK298426 mRNA. Translation: BAG60648.1.
BC012132 mRNA. Translation: AAH12132.1.
BC053673 mRNA. Translation: AAH53673.1.
CCDSiCCDS1686.1. [Q92499-1]
RefSeqiNP_004930.1. NM_004939.2. [Q92499-1]
UniGeneiHs.440599.

Genome annotation databases

EnsembliENST00000233084; ENSP00000233084; ENSG00000079785. [Q92499-1]
ENST00000381341; ENSP00000370745; ENSG00000079785. [Q92499-1]
GeneIDi1653.
KEGGihsa:1653.
UCSCiuc002rce.5. human. [Q92499-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70649 mRNA. Translation: CAA49992.1.
AK297432 mRNA. Translation: BAG59860.1.
AK298426 mRNA. Translation: BAG60648.1.
BC012132 mRNA. Translation: AAH12132.1.
BC053673 mRNA. Translation: AAH53673.1.
CCDSiCCDS1686.1. [Q92499-1]
RefSeqiNP_004930.1. NM_004939.2. [Q92499-1]
UniGeneiHs.440599.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XW3X-ray2.00A/B72-283[»]
ProteinModelPortaliQ92499.
SMRiQ92499. Positions 25-70, 86-674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108019. 136 interactions.
DIPiDIP-38163N.
IntActiQ92499. 30 interactions.
MINTiMINT-5005493.
STRINGi9606.ENSP00000233084.

Chemistry

BindingDBiQ92499.
ChEMBLiCHEMBL2010634.

PTM databases

iPTMnetiQ92499.
PhosphoSiteiQ92499.
SwissPalmiQ92499.

Polymorphism and mutation databases

BioMutaiDDX1.
DMDMi6919862.

2D gel databases

REPRODUCTION-2DPAGEIPI00293655.

Proteomic databases

EPDiQ92499.
MaxQBiQ92499.
PaxDbiQ92499.
PeptideAtlasiQ92499.
PRIDEiQ92499.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233084; ENSP00000233084; ENSG00000079785. [Q92499-1]
ENST00000381341; ENSP00000370745; ENSG00000079785. [Q92499-1]
GeneIDi1653.
KEGGihsa:1653.
UCSCiuc002rce.5. human. [Q92499-1]

Organism-specific databases

CTDi1653.
GeneCardsiDDX1.
HGNCiHGNC:2734. DDX1.
HPAiCAB012280.
HPA034502.
HPA034503.
MIMi601257. gene.
neXtProtiNX_Q92499.
PharmGKBiPA27199.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0349. Eukaryota.
COG0513. LUCA.
GeneTreeiENSGT00770000120531.
HOGENOMiHOG000251633.
HOVERGENiHBG005462.
InParanoidiQ92499.
KOiK13177.
OMAiTLNNVKQ.
OrthoDBiEOG7RNJZJ.
PhylomeDBiQ92499.
TreeFamiTF106114.

Enzyme and pathway databases

ReactomeiR-HSA-6784531. tRNA processing in the nucleus.

Miscellaneous databases

ChiTaRSiDDX1. human.
GeneWikiiDDX1.
GenomeRNAii1653.
PROiQ92499.
SOURCEiSearch...

Gene expression databases

BgeeiQ92499.
CleanExiHS_DDX1.
ExpressionAtlasiQ92499. baseline and differential.
GenevisibleiQ92499. HS.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF52540. SSF52540. 3 hits.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 2 hits.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amplification of a DEAD box protein gene in retinoblastoma cell lines."
    Godbout R., Squire J.
    Proc. Natl. Acad. Sci. U.S.A. 90:7578-7582(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Retinoblastoma.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Brain and Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung and Uterus.
  4. "Association of human DEAD box protein DDX1 with a cleavage stimulation factor involved in 3'-end processing of pre-MRNA."
    Bleoo S., Sun X., Hendzel M.J., Rowe J.M., Packer M., Godbout R.
    Mol. Biol. Cell 12:3046-3059(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSTF2, SUBCELLULAR LOCATION.
  5. "An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous nuclear ribonucleoprotein K."
    Chen H.C., Lin W.C., Tsay Y.G., Lee S.C., Chang C.J.
    J. Biol. Chem. 277:40403-40409(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HNRNPK, RNA-BINDING.
  6. "A DEAD box protein facilitates HIV-1 replication as a cellular co-factor of Rev."
    Fang J., Kubota S., Yang B., Zhou N., Zhang H., Godbout R., Pomerantz R.J.
    Virology 330:471-480(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH REV OF HIV-1, RNA-BINDING, SUBCELLULAR LOCATION.
  7. "MBNL1 associates with YB-1 in cytoplasmic stress granules."
    Onishi H., Kino Y., Morita T., Futai E., Sasagawa N., Ishiura S.
    J. Neurosci. Res. 86:1994-2002(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MBNL1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "A role for DEAD box 1 at DNA double-strand breaks."
    Li L., Monckton E.A., Godbout R.
    Mol. Cell. Biol. 28:6413-6425(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATM, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  9. "The DEAD-box RNA helicase DDX1 interacts with RelA and enhances nuclear factor kappaB-mediated transcription."
    Ishaq M., Ma L., Wu X., Mu Y., Pan J., Hu J., Hu T., Fu Q., Guo D.
    J. Cell. Biochem. 106:296-305(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RELA, MUTAGENESIS OF GLU-371, SUBCELLULAR LOCATION.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239; LYS-268 AND LYS-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "The cellular RNA helicase DDX1 interacts with coronavirus nonstructural protein 14 and enhances viral replication."
    Xu L., Khadijah S., Fang S., Wang L., Tay F.P., Liu D.X.
    J. Virol. 84:8571-8583(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH REPLICASE POLYPROTEIN 1AB NSP14 OF IBV AND SARS-COV, SUBCELLULAR LOCATION.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX.
  16. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing factors."
    Popow J., Jurkin J., Schleiffer A., Martinez J.
    Nature 511:104-107(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX, MUTAGENESIS OF LYS-52 AND GLU-371.
  19. "hCLE/C14orf166 associates with DDX1-HSPC117-FAM98B in a novel transcription-dependent shuttling RNA-transporting complex."
    Perez-Gonzalez A., Pazo A., Navajas R., Ciordia S., Rodriguez-Frandsen A., Nieto A.
    PLoS ONE 9:E90957-E90957(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDDX1_HUMAN
AccessioniPrimary (citable) accession number: Q92499
Secondary accession number(s): B4DME8, B4DPN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: July 6, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

According to some authors the unwinding activity is ADP-dependent and not ATP-dependent.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.