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P17844

- DDX5_HUMAN

UniProt

P17844 - DDX5_HUMAN

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Protein

Probable ATP-dependent RNA helicase DDX5

Gene

DDX5

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

Functioni

Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for estrogen receptor ESR1 and androgen receptor AR. Increases ESR1 AF-1 domain-mediated transactivation and ESR1 AF-1 and AF-2 domains transcriptional synergistic activity. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specicic manner; the function probbaly involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms.10 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei121 – 1211ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi114 – 1163ATP
Nucleotide bindingi138 – 1458ATP

GO - Molecular functioni

  1. androgen receptor binding Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. ATP-dependent RNA helicase activity Source: Ensembl
  4. estrogen receptor binding Source: UniProtKB
  5. poly(A) RNA binding Source: UniProtKB
  6. pre-mRNA binding Source: UniProtKB
  7. RNA helicase activity Source: UniProtKB
  8. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. cell growth Source: UniProtKB
  2. circadian rhythm Source: Ensembl
  3. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  4. in utero embryonic development Source: Ensembl
  5. mRNA splicing, via spliceosome Source: UniProtKB
  6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. positive regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  8. positive regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
  9. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  10. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  11. regulation of androgen receptor signaling pathway Source: UniProtKB
  12. regulation of osteoblast differentiation Source: UniProtKB
  13. regulation of skeletal muscle cell differentiation Source: UniProtKB
  14. regulation of viral genome replication Source: Ensembl
  15. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Biological rhythms, mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX5 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 5
RNA helicase p68
Gene namesi
Name:DDX5
Synonyms:G17P1, HELR, HLR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:2746. DDX5.

Subcellular locationi

Nucleusnucleolus 2 Publications

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. membrane Source: UniProtKB
  4. nucleolus Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi53 – 531K → R: Abolishes sumoylation, abolishes interaction with HDAC1, increases TP53 coactivation and promotes polyubiquitination. 2 Publications
Mutagenesisi55 – 551E → A: Abolishes sumoylation. 1 Publication
Mutagenesisi144 – 1441K → R: Abolishes RNA helicase activity, no effect on transcriptional coactivator function. 2 Publications
Mutagenesisi403 – 4031R → L: Binds to the tau stem-loop-containing RNA. Inhibits tau exon 10 inclusion and RNA cleavage. Does not inhibit interaction with RBM4. 1 Publication

Organism-specific databases

PharmGKBiPA27228.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 614614Probable ATP-dependent RNA helicase DDX5PRO_0000054991Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321N6-acetyllysine1 Publication
Modified residuei33 – 331N6-acetyllysine1 Publication
Modified residuei40 – 401N6-acetyllysine1 Publication
Cross-linki53 – 53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei236 – 2361N6-acetyllysineBy similarity
Modified residuei297 – 2971Phosphotyrosine1 Publication
Modified residuei480 – 4801Phosphoserine2 Publications

Post-translational modificationi

Arg-502 is dimethylated, probably to asymmetric dimethylarginine.
Sumoylated; sumoylation, promoted by PIAS1, promotes interaction with HDAC1 and transcriptional repression activity. Sumoylation also significantly increases stability, and reduces polyubiquitination.2 Publications
Polyubiquitinated, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP17844.
PaxDbiP17844.
PeptideAtlasiP17844.
PRIDEiP17844.

2D gel databases

SWISS-2DPAGEP17844.

PTM databases

PhosphoSiteiP17844.

Expressioni

Gene expression databases

BgeeiP17844.
CleanExiHS_DDX5.
ExpressionAtlasiP17844. baseline and differential.
GenevestigatoriP17844.

Organism-specific databases

HPAiCAB005868.
HPA020043.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Interacts with RBM4; the interaction occurs in an RNA-independent manner. Interacts with AGO1 and AGO2. Interacts with ESR1; the interaction is enhanced by phosphorylation of ESR1 AF-1 domain. Interacts with AR, NCOA1, NCOA2, NCOA3, EP300, CREBBP, POLR2A, TP53, RUNX2 and HDAC1. Self-associates. Interacts with DDX17. Interacts with BRDT. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active).16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P2795812EBI-351962,EBI-6904388From a different organism.
P299913EBI-351962,EBI-8826747From a different organism.
CHD3Q128734EBI-351962,EBI-523590
CrebbpP454813EBI-351962,EBI-296306From a different organism.
DDX17Q928413EBI-351962,EBI-746012
EBNA-LPQ8AZK72EBI-351962,EBI-1185167From a different organism.
EP300Q094724EBI-351962,EBI-447295
ESR1P033728EBI-351962,EBI-78473
FBLP220876EBI-351962,EBI-358318
HDAC1Q135474EBI-351962,EBI-301834
MBD3O959834EBI-351962,EBI-1783068
Myod1P100853EBI-351962,EBI-4405734From a different organism.
NFAT5O949164EBI-351962,EBI-308320
POLR2AP249283EBI-351962,EBI-295301
Runx2Q08775-32EBI-351962,EBI-6119991From a different organism.
TP53P046376EBI-351962,EBI-366083
TP53P04637-12EBI-351962,EBI-3895849
TP53P04637-72EBI-351962,EBI-3895873

Protein-protein interaction databases

BioGridi108021. 167 interactions.
DIPiDIP-29844N.
IntActiP17844. 83 interactions.
MINTiMINT-5000516.
STRINGi9606.ENSP00000225792.

Structurei

Secondary structure

1
614
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi64 – 663Combined sources
Helixi72 – 809Combined sources
Beta strandi82 – 876Combined sources
Turni96 – 994Combined sources
Helixi103 – 1108Combined sources
Turni111 – 1133Combined sources
Helixi119 – 13012Combined sources
Beta strandi134 – 1385Combined sources
Helixi144 – 15714Combined sources
Beta strandi169 – 1735Combined sources
Helixi177 – 19317Combined sources
Beta strandi198 – 2014Combined sources
Helixi207 – 21610Combined sources
Beta strandi219 – 2235Combined sources
Helixi225 – 2339Combined sources
Turni234 – 2363Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi244 – 2474Combined sources
Helixi250 – 2556Combined sources
Helixi259 – 2668Combined sources
Beta strandi274 – 2807Combined sources
Helixi284 – 29310Combined sources
Beta strandi298 – 3025Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FE2X-ray2.60A/B68-307[»]
4A4DX-ray2.70A52-304[»]
ProteinModelPortaliP17844.
SMRiP17844. Positions 50-473.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17844.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 300176Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini328 – 475148Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni477 – 614138Transactivation domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi94 – 12229Q motifAdd
BLAST
Motifi248 – 2514DEAD box

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00760000119219.
HOGENOMiHOG000268804.
HOVERGENiHBG015893.
InParanoidiP17844.
KOiK12823.
PhylomeDBiP17844.
TreeFamiTF300332.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR012587. P68HR.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF08061. P68HR. 2 hits.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P17844-1) [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
MSGYSSDRDR GRDRGFGAPR FGGSRAGPLS GKKFGNPGEK LVKKKWNLDE
60 70 80 90 100
LPKFEKNFYQ EHPDLARRTA QEVETYRRSK EITVRGHNCP KPVLNFYEAN
110 120 130 140 150
FPANVMDVIA RQNFTEPTAI QAQGWPVALS GLDMVGVAQT GSGKTLSYLL
160 170 180 190 200
PAIVHINHQP FLERGDGPIC LVLAPTRELA QQVQQVAAEY CRACRLKSTC
210 220 230 240 250
IYGGAPKGPQ IRDLERGVEI CIATPGRLID FLECGKTNLR RTTYLVLDEA
260 270 280 290 300
DRMLDMGFEP QIRKIVDQIR PDRQTLMWSA TWPKEVRQLA EDFLKDYIHI
310 320 330 340 350
NIGALELSAN HNILQIVDVC HDVEKDEKLI RLMEEIMSEK ENKTIVFVET
360 370 380 390 400
KRRCDELTRK MRRDGWPAMG IHGDKSQQER DWVLNEFKHG KAPILIATDV
410 420 430 440 450
ASRGLDVEDV KFVINYDYPN SSEDYIHRIG RTARSTKTGT AYTFFTPNNI
460 470 480 490 500
KQVSDLISVL REANQAINPK LLQLVEDRGS GRSRGRGGMK DDRRDRYSAG
510 520 530 540 550
KRGGFNTFRD RENYDRGYSS LLKRDFGAKT QNGVYSAANY TNGSFGSNFV
560 570 580 590 600
SAGIQTSFRT GNPTGTYQNG YDSTQQYGSN VPNMHNGMNQ QAYAYPATAA
610
APMIGYPMPT GYSQ
Length:614
Mass (Da):69,148
Last modified:August 1, 1990 - v1
Checksum:i84DF684FD6871594
GO
Isoform 2 (identifier: P17844-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-163: Missing.

Note: No experimental confirmation available.

Show »
Length:535
Mass (Da):60,563
Checksum:iA665AD0571ABC456
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti480 – 4801S → A.
Corresponds to variant rs1140409 [ dbSNP | Ensembl ].
VAR_029241

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei85 – 16379Missing in isoform 2. 1 PublicationVSP_056154Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52104 mRNA. Translation: CAA36324.1.
AF015812 Genomic DNA. Translation: AAB84094.1.
BT006943 mRNA. Translation: AAP35589.1.
AK297192 mRNA. Translation: BAG59680.1.
AB451257 mRNA. Translation: BAG70071.1.
AC009994 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94202.1.
CH471109 Genomic DNA. Translation: EAW94203.1.
BC016027 mRNA. Translation: AAH16027.1.
X15729 mRNA. Translation: CAA33751.1.
AJ010931 Genomic DNA. Translation: CAA09408.1.
CCDSiCCDS11659.1. [P17844-1]
PIRiJC1087.
RefSeqiNP_004387.1. NM_004396.3. [P17844-1]
XP_005257168.1. XM_005257111.1. [P17844-1]
XP_006721801.1. XM_006721738.1. [P17844-1]
UniGeneiHs.279806.

Genome annotation databases

EnsembliENST00000225792; ENSP00000225792; ENSG00000108654. [P17844-1]
ENST00000450599; ENSP00000403085; ENSG00000108654. [P17844-2]
GeneIDi1655.
KEGGihsa:1655.
UCSCiuc002jej.2. human. [P17844-1]

Polymorphism databases

DMDMi129383.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52104 mRNA. Translation: CAA36324.1 .
AF015812 Genomic DNA. Translation: AAB84094.1 .
BT006943 mRNA. Translation: AAP35589.1 .
AK297192 mRNA. Translation: BAG59680.1 .
AB451257 mRNA. Translation: BAG70071.1 .
AC009994 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94202.1 .
CH471109 Genomic DNA. Translation: EAW94203.1 .
BC016027 mRNA. Translation: AAH16027.1 .
X15729 mRNA. Translation: CAA33751.1 .
AJ010931 Genomic DNA. Translation: CAA09408.1 .
CCDSi CCDS11659.1. [P17844-1 ]
PIRi JC1087.
RefSeqi NP_004387.1. NM_004396.3. [P17844-1 ]
XP_005257168.1. XM_005257111.1. [P17844-1 ]
XP_006721801.1. XM_006721738.1. [P17844-1 ]
UniGenei Hs.279806.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FE2 X-ray 2.60 A/B 68-307 [» ]
4A4D X-ray 2.70 A 52-304 [» ]
ProteinModelPortali P17844.
SMRi P17844. Positions 50-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108021. 167 interactions.
DIPi DIP-29844N.
IntActi P17844. 83 interactions.
MINTi MINT-5000516.
STRINGi 9606.ENSP00000225792.

PTM databases

PhosphoSitei P17844.

Polymorphism databases

DMDMi 129383.

2D gel databases

SWISS-2DPAGE P17844.

Proteomic databases

MaxQBi P17844.
PaxDbi P17844.
PeptideAtlasi P17844.
PRIDEi P17844.

Protocols and materials databases

DNASUi 1655.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000225792 ; ENSP00000225792 ; ENSG00000108654 . [P17844-1 ]
ENST00000450599 ; ENSP00000403085 ; ENSG00000108654 . [P17844-2 ]
GeneIDi 1655.
KEGGi hsa:1655.
UCSCi uc002jej.2. human. [P17844-1 ]

Organism-specific databases

CTDi 1655.
GeneCardsi GC17M062494.
HGNCi HGNC:2746. DDX5.
HPAi CAB005868.
HPA020043.
MIMi 180630. gene.
neXtProti NX_P17844.
PharmGKBi PA27228.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0513.
GeneTreei ENSGT00760000119219.
HOGENOMi HOG000268804.
HOVERGENi HBG015893.
InParanoidi P17844.
KOi K12823.
PhylomeDBi P17844.
TreeFami TF300332.

Miscellaneous databases

ChiTaRSi DDX5. human.
EvolutionaryTracei P17844.
GeneWikii DDX5.
GenomeRNAii 1655.
NextBioi 35473161.
PROi P17844.
SOURCEi Search...

Gene expression databases

Bgeei P17844.
CleanExi HS_DDX5.
ExpressionAtlasi P17844. baseline and differential.
Genevestigatori P17844.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR012587. P68HR.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF08061. P68HR. 2 hits.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete cDNA sequence of the human p68 protein."
    Hloch P., Stahl H.
    Nucleic Acids Res. 18:3045-3045(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "p68 RNA helicase: identification of a nucleolar form and cloning of related genes containing a conserved intron in yeasts."
    Iggo R.D., Jamieson D.J., McNeill S.A., Southgate J., McPheat J., Lane D.P.
    Mol. Cell. Biol. 11:1326-1333(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
  3. "Structure and expression of the human p68 RNA helicase gene."
    Roessler O.G., Hloch P., Schutz N., Weitzenegger T., Stahl H.
    Nucleic Acids Res. 28:932-939(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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] (ISOFORM 2).
    Tissue: Brain.
  6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Muscle.
  10. "Nuclear protein with sequence homology to translation initiation factor eIF-4A."
    Ford M.J., Anton I.A., Lane D.P.
    Nature 332:736-738(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-614 (ISOFORM 1).
  11. "Molecular organization of the murine p68 RNA helicase gene promotor region."
    Petry P., Bammer S., Heinlein U.A.O.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-163.
  12. "Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor alpha."
    Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H., Yanagisawa J., Metzger D., Hashimoto S., Kato S.
    Mol. Cell. Biol. 19:5363-5372(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH ESR1, MUTAGENESIS OF LYS-144.
  13. "The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase."
    Nicol S.M., Causevic M., Prescott A.R., Fuller-Pace F.V.
    Exp. Cell Res. 257:272-280(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBL, SUBCELLULAR LOCATION.
  14. "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor alpha coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA."
    Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S., Arao Y., Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y., Kato S.
    EMBO J. 20:1341-1352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH ESR1; NCOA1; NCOA2 AND NCOA3.
  15. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  16. "The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells."
    Ogilvie V.C., Wilson B.J., Nicol S.M., Morrice N.A., Saunders L.R., Barber G.N., Fuller-Pace F.V.
    Nucleic Acids Res. 31:1470-1480(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, INTERACTION WITH DDX17.
  17. "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300."
    Rossow K.L., Janknecht R.
    Oncogene 22:151-156(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH EP300; CREBBP AND POLR2A.
  18. "The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner."
    Wilson B.J., Bates G.J., Nicol S.M., Gregory D.J., Perkins N.D., Fuller-Pace F.V.
    BMC Mol. Biol. 5:11-11(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTIONAL REPRESSION, INTERACTION WITH HDAC1.
  19. "The DEAD box protein p68: a novel transcriptional coactivator of the p53 tumour suppressor."
    Bates G.J., Nicol S.M., Wilson B.J., Jacobs A.M., Bourdon J.C., Wardrop J., Gregory D.J., Lane D.P., Perkins N.D., Fuller-Pace F.V.
    EMBO J. 24:543-553(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH TP53.
  20. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators of MyoD and skeletal muscle differentiation."
    Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P., Ogryzko V., Fuller-Pace F.V., Hoffman E.P., Tapscott S.J., Sartorelli V.
    Dev. Cell 11:547-560(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYOD1, MUTAGENESIS OF LYS-144.
  22. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
    Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
    EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AGO1 AND AGO2.
  23. "SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1."
    Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T., Fuller-Pace F.V.
    Oncogene 26:5866-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-53, INTERACTION WITH HDAC1 AND PIAS1, MUTAGENESIS OF LYS-53 AND GLU-55.
  24. "The RNA helicase p68 is a novel androgen receptor coactivator involved in splicing and is overexpressed in prostate cancer."
    Clark E.L., Coulson A., Dalgliesh C., Rajan P., Nicol S.M., Fleming S., Heer R., Gaughan L., Leung H.Y., Elliott D.J., Fuller-Pace F.V., Robson C.N.
    Cancer Res. 68:7938-7946(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH AR.
  25. Cited for: FUNCTION, INTERACTION WITH RUNX2.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "The DEAD-box protein p72 regulates ERalpha-/oestrogen-dependent transcription and cell growth, and is associated with improved survival in ERalpha-positive breast cancer."
    Wortham N.C., Ahamed E., Nicol S.M., Thomas R.S., Periyasamy M., Jiang J., Ochocka A.M., Shousha S., Huson L., Bray S.E., Coombes R.C., Ali S., Fuller-Pace F.V.
    Oncogene 28:4053-4064(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ESR1.
  28. "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-32; LYS-33 AND LYS-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Sumoylation of p68 and p72 RNA helicases affects protein stability and transactivation potential."
    Mooney S.M., Grande J.P., Salisbury J.L., Janknecht R.
    Biochemistry 49:1-10(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-53, MUTAGENESIS OF LYS-53, POLYUBIQUITINATION.
  30. "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-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5' splice site."
    Kar A., Fushimi K., Zhou X., Ray P., Shi C., Chen X., Liu Z., Chen S., Wu J.Y.
    Mol. Cell. Biol. 31:1812-1821(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RBM4, MUTAGENESIS OF ARG-403, RNA-BINDING.
  33. "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-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 68-307 IN COMPLEX WITH ADP.

Entry informationi

Entry nameiDDX5_HUMAN
AccessioniPrimary (citable) accession number: P17844
Secondary accession number(s): B4DLW8
, B5BU21, D3DU32, E7ETL9, O75681, Q53Y61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 26, 2014
This is version 170 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3