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Q92841

- DDX17_HUMAN

UniProt

Q92841 - DDX17_HUMAN

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Protein

Probable ATP-dependent RNA helicase DDX17

Gene

DDX17

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

Functioni

RNA-dependent ATPase activity. Involved in transcriptional regulation. Transcriptional coactivator for estrogen receptor ESR1. Increases ESR1 AF-1 domain-mediated transactivation. Synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and probably involved in skeletal muscle differentiation. Required for zinc-finger antiviral protein ZC3HAV1-mediated mRNA degradation.6 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi215 – 2228ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. positive regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
  3. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  4. regulation of skeletal muscle cell differentiation Source: UniProtKB
  5. RNA processing Source: ProtInc
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX17 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 17
DEAD box protein p72
RNA-dependent helicase p72
Gene namesi
Name:DDX17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:2740. DDX17.

Subcellular locationi

Nucleus 1 Publication. Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi129 – 1291K → R: Impaired sumoylation and decreased stability. 1 Publication

Organism-specific databases

PharmGKBiPA27206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 729729Probable ATP-dependent RNA helicase DDX17PRO_0000054993Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Phosphoserine1 Publication
Cross-linki129 – 129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei523 – 5231Phosphothreonine1 Publication

Post-translational modificationi

Sumoylation significantly increases stability, it also promotes interaction with HDAC1.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ92841.
PaxDbiQ92841.
PRIDEiQ92841.

2D gel databases

REPRODUCTION-2DPAGEIPI00023785.

PTM databases

PhosphoSiteiQ92841.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ92841.
CleanExiHS_DDX17.
ExpressionAtlasiQ92841. baseline and differential.
GenevestigatoriQ92841.

Organism-specific databases

HPAiCAB024908.
HPA051161.

Interactioni

Subunit structurei

Interacts with ESR1. Interacts with NCOA1, NCOA2, NCOA3, TP53 and HDAC1. Self-associates. Interacts with DDX5. Interacts with DCP1A in an RNA-independent manner. Interacts with DCP2 in an RNA-dependent manner. Interacts with ZC3HAV1 (via N-terminal domain) in an RNA-independent manner. Interacts with EXOSC3 and EXOSC5 only in the presence of ZC3HAV1 in an RNA-independent manner.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX5P178443EBI-746012,EBI-351962
ESR1P033727EBI-746012,EBI-78473
HDAC1Q135473EBI-5280703,EBI-301834
NCOA2Q155962EBI-746012,EBI-81236
NCOA3Q9Y6Q92EBI-746012,EBI-81196
NFAT5O949163EBI-746012,EBI-308320
Srek1Q9JKL73EBI-746012,EBI-6452221From a different organism.
TP53P046373EBI-746012,EBI-366083
YAP1P469377EBI-746012,EBI-1044059

Protein-protein interaction databases

BioGridi115776. 106 interactions.
DIPiDIP-29843N.
IntActiQ92841. 59 interactions.
MINTiMINT-4545892.
STRINGi9606.ENSP00000380033.

Structurei

3D structure databases

ProteinModelPortaliQ92841.
SMRiQ92841. Positions 126-546.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini202 – 377176Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini405 – 552148Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni547 – 729183Transactivation domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi171 – 19929Q motifAdd
BLAST
Motifi325 – 3284DEAD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi101 – 1044Poly-Gly
Compositional biasi556 – 5638Poly-Gly
Compositional biasi718 – 7269Poly-Pro

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0513.
HOGENOMiHOG000268804.
HOVERGENiHBG015893.
InParanoidiQ92841.
KOiK13178.

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.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. Align

Isoform 1 (identifier: Q92841-4) [UniParc]FASTAAdd to Basket

Also known as: p82

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
MPTGFVAPIL CVLLPSPTRE AATVASATGD SASERESAAP AAAPTAEAPP
60 70 80 90 100
PSVVTRPEPQ ALPSPAIRAP LPDLYPFGTM RGGGFGDRDR DRDRGGFGAR
110 120 130 140 150
GGGGLPPKKF GNPGERLRKK KWDLSELPKF EKNFYVEHPE VARLTPYEVD
160 170 180 190 200
ELRRKKEITV RGGDVCPKPV FAFHHANFPQ YVMDVLMDQH FTEPTPIQCQ
210 220 230 240 250
GFPLALSGRD MVGIAQTGSG KTLAYLLPAI VHINHQPYLE RGDGPICLVL
260 270 280 290 300
APTRELAQQV QQVADDYGKC SRLKSTCIYG GAPKGPQIRD LERGVEICIA
310 320 330 340 350
TPGRLIDFLE SGKTNLRRCT YLVLDEADRM LDMGFEPQIR KIVDQIRPDR
360 370 380 390 400
QTLMWSATWP KEVRQLAEDF LRDYTQINVG NLELSANHNI LQIVDVCMES
410 420 430 440 450
EKDHKLIQLM EEIMAEKENK TIIFVETKRR CDDLTRRMRR DGWPAMCIHG
460 470 480 490 500
DKSQPERDWV LNEFRSGKAP ILIATDVASR GLDVEDVKFV INYDYPNSSE
510 520 530 540 550
DYVHRIGRTA RSTNKGTAYT FFTPGNLKQA RELIKVLEEA NQAINPKLMQ
560 570 580 590 600
LVDHRGGGGG GGGRSRYRTT SSANNPNLMY QDECDRRLRG VKDGGRRDSA
610 620 630 640 650
SYRDRSETDR AGYANGSGYG SPNSAFGAQA GQYTYGQGTY GAAAYGTSSY
660 670 680 690 700
TAQEYGAGTY GASSTTSTGR SSQSSSQQFS GIGRSGQQPQ PLMSQQFAQP
710 720
PGATNMIGYM GQTAYQYPPP PPPPPPSRK

Note: Starts at an alternative CUG codon.

Length:729
Mass (Da):80,272
Last modified:March 21, 2012 - v2
Checksum:iC819F53515B1BC39
GO
Isoform 2 (identifier: Q92841-1) [UniParc]FASTAAdd to Basket

Also known as: p72

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.

Note: Produced by alternative initiation at Met-80 of isoform 1.

Show »
Length:650
Mass (Da):72,371
Checksum:iE58AA249D23F66F3
GO
Isoform 3 (identifier: Q92841-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     482-482: L → LGL

Note: Produced by alternative splicing of isoform 2. No experimental confirmation available.

Show »
Length:652
Mass (Da):72,542
Checksum:i71E89198BBDBF2E6
GO
Isoform 4 (identifier: Q92841-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     562-562: G → GKG

Note: Produced by alternative splicing of isoform 2. No experimental confirmation available.

Show »
Length:652
Mass (Da):72,557
Checksum:i05DFD042E4268F2C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7979Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_042527Add
BLAST
Alternative sequencei482 – 4821L → LGL in isoform 3. 1 PublicationVSP_042528
Alternative sequencei562 – 5621G → GKG in isoform 4. 1 PublicationVSP_042529

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59321 mRNA. Translation: AAC50787.1.
CR456432 mRNA. Translation: CAG30318.1.
AL713763 mRNA. Translation: CAH10627.2.
Z97056 Genomic DNA. Translation: CAQ08924.1.
Z97056 Genomic DNA. Translation: CAB09792.1.
CH471095 Genomic DNA. Translation: EAW60243.1.
BC000595 mRNA. Translation: AAH00595.2.
CCDSiCCDS33646.1. [Q92841-4]
PIRiS72367.
RefSeqiNP_006377.2. NM_006386.4. [Q92841-4]
UniGeneiHs.528305.
Hs.706116.

Genome annotation databases

EnsembliENST00000403230; ENSP00000385536; ENSG00000100201.
GeneIDi10521.
KEGGihsa:10521.
UCSCiuc003avx.4. human. [Q92841-4]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59321 mRNA. Translation: AAC50787.1 .
CR456432 mRNA. Translation: CAG30318.1 .
AL713763 mRNA. Translation: CAH10627.2 .
Z97056 Genomic DNA. Translation: CAQ08924.1 .
Z97056 Genomic DNA. Translation: CAB09792.1 .
CH471095 Genomic DNA. Translation: EAW60243.1 .
BC000595 mRNA. Translation: AAH00595.2 .
CCDSi CCDS33646.1. [Q92841-4 ]
PIRi S72367.
RefSeqi NP_006377.2. NM_006386.4. [Q92841-4 ]
UniGenei Hs.528305.
Hs.706116.

3D structure databases

ProteinModelPortali Q92841.
SMRi Q92841. Positions 126-546.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115776. 106 interactions.
DIPi DIP-29843N.
IntActi Q92841. 59 interactions.
MINTi MINT-4545892.
STRINGi 9606.ENSP00000380033.

PTM databases

PhosphoSitei Q92841.

2D gel databases

REPRODUCTION-2DPAGE IPI00023785.

Proteomic databases

MaxQBi Q92841.
PaxDbi Q92841.
PRIDEi Q92841.

Protocols and materials databases

DNASUi 10521.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000403230 ; ENSP00000385536 ; ENSG00000100201 .
GeneIDi 10521.
KEGGi hsa:10521.
UCSCi uc003avx.4. human. [Q92841-4 ]

Organism-specific databases

CTDi 10521.
GeneCardsi GC22M038879.
HGNCi HGNC:2740. DDX17.
HPAi CAB024908.
HPA051161.
MIMi 608469. gene.
neXtProti NX_Q92841.
PharmGKBi PA27206.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0513.
HOGENOMi HOG000268804.
HOVERGENi HBG015893.
InParanoidi Q92841.
KOi K13178.

Miscellaneous databases

ChiTaRSi DDX17. human.
GeneWikii DDX17.
GenomeRNAii 10521.
NextBioi 39902.
PROi Q92841.
SOURCEi Search...

Gene expression databases

Bgeei Q92841.
CleanExi HS_DDX17.
ExpressionAtlasi Q92841. baseline and differential.
Genevestigatori Q92841.

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.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[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. "p72: a human nuclear DEAD box protein highly related to p68."
    Lamm G.M., Nicol S.M., Fuller-Pace F.V., Lamond A.I.
    Nucleic Acids Res. 24:3739-3747(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Amygdala.
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Skin.
  7. "The mRNA of DEAD box protein p72 is alternatively translated into an 82-kDa RNA helicase."
    Uhlmann-Schiffler H., Rossler O.G., Stahl H.
    J. Biol. Chem. 277:1066-1075(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION (ISOFORM 1).
  8. "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.
  9. "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 DDX5.
  10. "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.
  11. "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: INTERACTION WITH TP53.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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.
  14. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF."
    Shin S., Janknecht R.
    J. Cell. Biochem. 101:1252-1265(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH EP300; CREBBP AND KAT2B.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "p72 DEAD box RNA helicase is required for optimal function of the zinc-finger antiviral protein."
    Chen G., Guo X., Lv F., Xu Y., Gao G.
    Proc. Natl. Acad. Sci. U.S.A. 105:4352-4357(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZC3HAV1; EXOSC3 AND EXOSC5.
  19. "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.
  20. "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-129, MUTAGENESIS OF LYS-129.
  21. "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-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
    Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
    Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCP1A AND DCP2.
  24. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
    Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
    Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDDX17_HUMAN
AccessioniPrimary (citable) accession number: Q92841
Secondary accession number(s): B1AHM0, Q69YT1, Q6ICD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: March 21, 2012
Last modified: October 29, 2014
This is version 154 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3