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Q92841 (DDX17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DDX17
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.10 Ref.13 Ref.15 Ref.18 Ref.19

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.18 Ref.19 Ref.23

Subcellular location

Nucleus. Nucleusnucleolus Ref.25.

Tissue specificity

Ubiquitous.

Post-translational modification

Sumoylation significantly increases stability, it also promotes interaction with HDAC1. Ref.20

Sequence similarities

Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Traceable author statement Ref.1. Source: GOC

RNA processing

Traceable author statement Ref.1. Source: ProtInc

positive regulation of intracellular estrogen receptor signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.8Ref.15. Source: UniProtKB

regulation of skeletal muscle cell differentiation

Inferred from mutant phenotype Ref.13. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA binding

Traceable author statement Ref.1. Source: ProtInc

RNA helicase activity

Traceable author statement Ref.1. Source: ProtInc

RNA-dependent ATPase activity

Traceable author statement Ref.1. Source: ProtInc

estrogen receptor binding

Inferred from direct assay Ref.8. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.8Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: Q92841-4)

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.
Note: Starts at an alternative CUG codon.
Isoform 2 (identifier: Q92841-1)

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.
Isoform 3 (identifier: Q92841-2)

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.
Isoform 4 (identifier: Q92841-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 729729Probable ATP-dependent RNA helicase DDX17
PRO_0000054993

Regions

Domain202 – 377176Helicase ATP-binding
Domain405 – 552148Helicase C-terminal
Nucleotide binding215 – 2228ATP By similarity
Region547 – 729183Transactivation domain
Motif171 – 19929Q motif
Motif325 – 3284DEAD box
Compositional bias101 – 1044Poly-Gly
Compositional bias556 – 5638Poly-Gly
Compositional bias718 – 7269Poly-Pro

Amino acid modifications

Modified residue641Phosphoserine Ref.21
Modified residue5231Phosphothreonine Ref.14
Cross-link129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.20

Natural variations

Alternative sequence1 – 7979Missing in isoform 2, isoform 3 and isoform 4.
VSP_042527
Alternative sequence4821L → LGL in isoform 3.
VSP_042528
Alternative sequence5621G → GKG in isoform 4.
VSP_042529

Experimental info

Mutagenesis1291K → R: Impaired sumoylation and decreased stability. Ref.20

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p82) [UniParc].

Last modified March 21, 2012. Version 2.
Checksum: C819F53515B1BC39

FASTA72980,272
        10         20         30         40         50         60 
MPTGFVAPIL CVLLPSPTRE AATVASATGD SASERESAAP AAAPTAEAPP PSVVTRPEPQ 

        70         80         90        100        110        120 
ALPSPAIRAP LPDLYPFGTM RGGGFGDRDR DRDRGGFGAR GGGGLPPKKF GNPGERLRKK 

       130        140        150        160        170        180 
KWDLSELPKF EKNFYVEHPE VARLTPYEVD ELRRKKEITV RGGDVCPKPV FAFHHANFPQ 

       190        200        210        220        230        240 
YVMDVLMDQH FTEPTPIQCQ GFPLALSGRD MVGIAQTGSG KTLAYLLPAI VHINHQPYLE 

       250        260        270        280        290        300 
RGDGPICLVL APTRELAQQV QQVADDYGKC SRLKSTCIYG GAPKGPQIRD LERGVEICIA 

       310        320        330        340        350        360 
TPGRLIDFLE SGKTNLRRCT YLVLDEADRM LDMGFEPQIR KIVDQIRPDR QTLMWSATWP 

       370        380        390        400        410        420 
KEVRQLAEDF LRDYTQINVG NLELSANHNI LQIVDVCMES EKDHKLIQLM EEIMAEKENK 

       430        440        450        460        470        480 
TIIFVETKRR CDDLTRRMRR DGWPAMCIHG DKSQPERDWV LNEFRSGKAP ILIATDVASR 

       490        500        510        520        530        540 
GLDVEDVKFV INYDYPNSSE DYVHRIGRTA RSTNKGTAYT FFTPGNLKQA RELIKVLEEA 

       550        560        570        580        590        600 
NQAINPKLMQ LVDHRGGGGG GGGRSRYRTT SSANNPNLMY QDECDRRLRG VKDGGRRDSA 

       610        620        630        640        650        660 
SYRDRSETDR AGYANGSGYG SPNSAFGAQA GQYTYGQGTY GAAAYGTSSY TAQEYGAGTY 

       670        680        690        700        710        720 
GASSTTSTGR SSQSSSQQFS GIGRSGQQPQ PLMSQQFAQP PGATNMIGYM GQTAYQYPPP 


PPPPPPSRK 

« Hide

Isoform 2 (p72) [UniParc].

Checksum: E58AA249D23F66F3
Show »

FASTA65072,371
Isoform 3 [UniParc].

Checksum: 71E89198BBDBF2E6
Show »

FASTA65272,542
Isoform 4 [UniParc].

Checksum: 05DFD042E4268F2C
Show »

FASTA65272,557

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS72367.
RefSeqNP_006377.2. NM_006386.4.
UniGeneHs.528305.
Hs.706116.

3D structure databases

ProteinModelPortalQ92841.
SMRQ92841. Positions 148-552.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115776. 94 interactions.
DIPDIP-29843N.
IntActQ92841. 54 interactions.
MINTMINT-4545892.
STRING9606.ENSP00000380033.

PTM databases

PhosphoSiteQ92841.

2D gel databases

REPRODUCTION-2DPAGEIPI00023785.

Proteomic databases

PaxDbQ92841.
PRIDEQ92841.

Protocols and materials databases

DNASU10521.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000403230; ENSP00000385536; ENSG00000100201.
GeneID10521.
KEGGhsa:10521.
UCSCuc003avx.4. human. [Q92841-4]

Organism-specific databases

CTD10521.
GeneCardsGC22M038879.
HGNCHGNC:2740. DDX17.
HPACAB024908.
HPA051161.
MIM608469. gene.
neXtProtNX_Q92841.
PharmGKBPA27206.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000268804.
HOVERGENHBG015893.
InParanoidQ92841.
KOK13178.

Gene expression databases

ArrayExpressQ92841.
BgeeQ92841.
CleanExHS_DDX17.
GenevestigatorQ92841.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
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]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDDX17. human.
GeneWikiDDX17.
GenomeRNAi10521.
NextBio39902.
PROQ92841.
SOURCESearch...

Entry information

Entry nameDDX17_HUMAN
AccessionPrimary (citable) accession number: Q92841
Secondary accession number(s): B1AHM0, Q69YT1, Q6ICD6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: March 21, 2012
Last modified: April 16, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM