Q92841 (DDX17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

DDX17

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	729 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Nucleus › nucleolus 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative initiation Alternative splicing
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	ATP 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 transcription coactivator activity Inferred from direct assay Ref.8Ref.15. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ESR1	P03372	7	EBI-746012,EBI-78473
HDAC1	Q13547	3	EBI-5280703,EBI-301834
NCOA2	Q15596	2	EBI-746012,EBI-81236
NCOA3	Q9Y6Q9	2	EBI-746012,EBI-81196
NFAT5	O94916	3	EBI-746012,EBI-308320
Srek1	Q9JKL7	3	EBI-746012,EBI-6452221	From a different organism.
TP53	P04637	3	EBI-746012,EBI-366083

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 729	729	Probable ATP-dependent RNA helicase DDX17		PRO_0000054993
Regions
	Domain	202 – 377	176	Helicase ATP-binding
	Domain	405 – 552	148	Helicase C-terminal
	Nucleotide binding	215 – 222	8	ATP By similarity
	Region	547 – 729	183	Transactivation domain
	Motif	171 – 199	29	Q motif
	Motif	325 – 328	4	DEAD box
	Compositional bias	101 – 104	4	Poly-Gly
	Compositional bias	556 – 563	8	Poly-Gly
	Compositional bias	718 – 726	9	Poly-Pro
Amino acid modifications
	Modified residue	64	1	Phosphoserine Ref.21
	Modified residue	523	1	Phosphothreonine Ref.14
	Cross-link	129		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.20
Natural variations
	Alternative sequence	1 – 79	79	Missing in isoform 2, isoform 3 and isoform 4.		VSP_042527
	Alternative sequence	482	1	L → LGL in isoform 3.		VSP_042528
	Alternative sequence	562	1	G → GKG in isoform 4.		VSP_042529
Experimental info
	Mutagenesis	129	1	K → R: Impaired sumoylation and decreased stability. Ref.20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p82) [UniParc]. Last modified March 21, 2012. Version 2. Checksum: C819F53515B1BC39	FASTA	729	80,272
	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
	Isoform 2 (p72) [UniParc]. Checksum: E58AA249D23F66F3	FASTA	650	72,371
	10 20 30 40 50 60 MRGGGFGDRD RDRDRGGFGA RGGGGLPPKK FGNPGERLRK KKWDLSELPK FEKNFYVEHP 70 80 90 100 110 120 EVARLTPYEV DELRRKKEIT VRGGDVCPKP VFAFHHANFP QYVMDVLMDQ HFTEPTPIQC 130 140 150 160 170 180 QGFPLALSGR DMVGIAQTGS GKTLAYLLPA IVHINHQPYL ERGDGPICLV LAPTRELAQQ 190 200 210 220 230 240 VQQVADDYGK CSRLKSTCIY GGAPKGPQIR DLERGVEICI ATPGRLIDFL ESGKTNLRRC 250 260 270 280 290 300 TYLVLDEADR MLDMGFEPQI RKIVDQIRPD RQTLMWSATW PKEVRQLAED FLRDYTQINV 310 320 330 340 350 360 GNLELSANHN ILQIVDVCME SEKDHKLIQL MEEIMAEKEN KTIIFVETKR RCDDLTRRMR 370 380 390 400 410 420 RDGWPAMCIH GDKSQPERDW VLNEFRSGKA PILIATDVAS RGLDVEDVKF VINYDYPNSS 430 440 450 460 470 480 EDYVHRIGRT ARSTNKGTAY TFFTPGNLKQ ARELIKVLEE ANQAINPKLM QLVDHRGGGG 490 500 510 520 530 540 GGGGRSRYRT TSSANNPNLM YQDECDRRLR GVKDGGRRDS ASYRDRSETD RAGYANGSGY 550 560 570 580 590 600 GSPNSAFGAQ AGQYTYGQGT YGAAAYGTSS YTAQEYGAGT YGASSTTSTG RSSQSSSQQF 610 620 630 640 650 SGIGRSGQQP QPLMSQQFAQ PPGATNMIGY MGQTAYQYPP PPPPPPPSRK
	Isoform 3 [UniParc]. Checksum: 71E89198BBDBF2E6	FASTA	652	72,542
	10 20 30 40 50 60 MRGGGFGDRD RDRDRGGFGA RGGGGLPPKK FGNPGERLRK KKWDLSELPK FEKNFYVEHP 70 80 90 100 110 120 EVARLTPYEV DELRRKKEIT VRGGDVCPKP VFAFHHANFP QYVMDVLMDQ HFTEPTPIQC 130 140 150 160 170 180 QGFPLALSGR DMVGIAQTGS GKTLAYLLPA IVHINHQPYL ERGDGPICLV LAPTRELAQQ 190 200 210 220 230 240 VQQVADDYGK CSRLKSTCIY GGAPKGPQIR DLERGVEICI ATPGRLIDFL ESGKTNLRRC 250 260 270 280 290 300 TYLVLDEADR MLDMGFEPQI RKIVDQIRPD RQTLMWSATW PKEVRQLAED FLRDYTQINV 310 320 330 340 350 360 GNLELSANHN ILQIVDVCME SEKDHKLIQL MEEIMAEKEN KTIIFVETKR RCDDLTRRMR 370 380 390 400 410 420 RDGWPAMCIH GDKSQPERDW VLNEFRSGKA PILIATDVAS RGLGLDVEDV KFVINYDYPN 430 440 450 460 470 480 SSEDYVHRIG RTARSTNKGT AYTFFTPGNL KQARELIKVL EEANQAINPK LMQLVDHRGG 490 500 510 520 530 540 GGGGGGRSRY RTTSSANNPN LMYQDECDRR LRGVKDGGRR DSASYRDRSE TDRAGYANGS 550 560 570 580 590 600 GYGSPNSAFG AQAGQYTYGQ GTYGAAAYGT SSYTAQEYGA GTYGASSTTS TGRSSQSSSQ 610 620 630 640 650 QFSGIGRSGQ QPQPLMSQQF AQPPGATNMI GYMGQTAYQY PPPPPPPPPS RK
	Isoform 4 [UniParc]. Checksum: 05DFD042E4268F2C	FASTA	652	72,557
	10 20 30 40 50 60 MRGGGFGDRD RDRDRGGFGA RGGGGLPPKK FGNPGERLRK KKWDLSELPK FEKNFYVEHP 70 80 90 100 110 120 EVARLTPYEV DELRRKKEIT VRGGDVCPKP VFAFHHANFP QYVMDVLMDQ HFTEPTPIQC 130 140 150 160 170 180 QGFPLALSGR DMVGIAQTGS GKTLAYLLPA IVHINHQPYL ERGDGPICLV LAPTRELAQQ 190 200 210 220 230 240 VQQVADDYGK CSRLKSTCIY GGAPKGPQIR DLERGVEICI ATPGRLIDFL ESGKTNLRRC 250 260 270 280 290 300 TYLVLDEADR MLDMGFEPQI RKIVDQIRPD RQTLMWSATW PKEVRQLAED FLRDYTQINV 310 320 330 340 350 360 GNLELSANHN ILQIVDVCME SEKDHKLIQL MEEIMAEKEN KTIIFVETKR RCDDLTRRMR 370 380 390 400 410 420 RDGWPAMCIH GDKSQPERDW VLNEFRSGKA PILIATDVAS RGLDVEDVKF VINYDYPNSS 430 440 450 460 470 480 EDYVHRIGRT ARSTNKGTAY TFFTPGNLKQ ARELIKVLEE ANQAINPKLM QLVDHRGGGG 490 500 510 520 530 540 GGGKGGRSRY RTTSSANNPN LMYQDECDRR LRGVKDGGRR DSASYRDRSE TDRAGYANGS 550 560 570 580 590 600 GYGSPNSAFG AQAGQYTYGQ GTYGAAAYGT SSYTAQEYGA GTYGASSTTS TGRSSQSSSQ 610 620 630 640 650 QFSGIGRSGQ QPQPLMSQQF AQPPGATNMI GYMGQTAYQY PPPPPPPPPS RK

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
IPI	IPI00651653. IPI00651677. IPI00889541. IPI01022339.
PIR	S72367.
RefSeq	NP_006377.2. NM_006386.4.
UniGene	Hs.706116. Hs.725500.
3D structure databases
ProteinModelPortal	Q92841.
SMR	Q92841. Positions 148-544.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29843N.
IntAct	Q92841. 39 interactions.
MINT	MINT-4545892.
STRING	9606.ENSP00000380033.
PTM databases
PhosphoSite	Q92841.
Polymorphism databases
DMDM	3122595.
2D gel databases
REPRODUCTION-2DPAGE	IPI00023785.
Proteomic databases
PaxDb	Q92841.
PRIDE	Q92841.
Protocols and materials databases
DNASU	10521.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000403230; ENSP00000385536; ENSG00000100201.
GeneID	10521.
KEGG	hsa:10521.
UCSC	uc003avx.4. human.
Organism-specific databases
CTD	10521.
GeneCards	GC22M038879.
HGNC	HGNC:2740. DDX17.
HPA	CAB024908.
MIM	608469. gene.
neXtProt	NX_Q92841.
PharmGKB	PA27206.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0513.
HOGENOM	HOG000268804.
HOVERGEN	HBG015893.
InParanoid	Q92841.
KO	K13178.
Gene expression databases
ArrayExpress	Q92841.
Bgee	Q92841.
CleanEx	HS_DDX17.
Genevestigator	Q92841.
GermOnline	ENSG00000100201. Homo sapiens.
Family and domain databases
InterPro	IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR000629. RNA-helicase_DEAD-box_CS. IPR014014. RNA_helicase_DEAD_Q_motif. [Graphical view]
Pfam	PF00270. DEAD. 1 hit. PF00271. Helicase_C. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
PROSITE	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]
ProtoNet	Search...
Other
ChiTaRS	DDX17. human.
GenomeRNAi	10521.
NextBio	39902.
SOURCE	Search...

Entry information

Entry name

DDX17_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.