Q86XP3 (DDX42_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent RNA helicase DDX42
EC=3.6.4.13

Alternative name(s):
DEAD box protein 42
RNA helicase-like protein
Short name=RHELP
RNA helicase-related protein
Short name=RNAHP
SF3b DEAD box protein
Splicing factor 3B-associated 125 kDa protein
Short name=SF3b125

Gene names

Name:

DDX42

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	938 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ATP-dependent RNA helicase. Binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm. Ref.10 Ref.12
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Component of splicing factor SF3B which is composed of at least eight subunits; SF3B1/SAP155/SF3B155, SF3B2/SAP145/SF3B155, SF3B3/SAP130/SF3B130, SF3B4/SAP49/SF3B49, SF3B14A, PHF5A/SF3B14B, SF3B10 and SF3B125. Interacts (via the C-terminus) with TP53BP2; the interaction is not inhibitied by TP53BP2 ubiquitination and is independent of p53/TP53. Ref.8 Ref.12
Subcellular location	Cytoplasm. Nucleus speckle. Nucleus › Cajal body. Note: Isoform 2 is present in Cajal bodies (CBs) and nuclear speckles. Ref.8 Ref.10 Ref.12
Tissue specificity	Expressed in several cell lines (at protein level). Expressed in liver, lung, tonsil, thymus, muscle and pancreatic islets. Ref.1 Ref.10
Sequence similarities	Belongs to the DEAD box helicase family. DDX42 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.
Sequence caution	The sequence AAC32396.1 differs from that shown. Reason: Frameshift at position 818.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein localization Inferred from direct assay Ref.12. Source: UniProtKB
Cellular_component	Cajal body Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay Ref.12. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.12. 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 Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86XP3-1)

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.

Isoform 2 (identifier: Q86XP3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 938	938	ATP-dependent RNA helicase DDX42		PRO_0000280058
Regions
	Domain	284 – 459	176	Helicase ATP-binding
	Domain	487 – 632	146	Helicase C-terminal
	Nucleotide binding	297 – 304	8	ATP By similarity
	Region	738 – 833	96	Necessary for interaction with TP53BP2
	Coiled coil	116 – 157	42	Potential
	Motif	253 – 281	29	Q motif
	Motif	407 – 410	4	DEAD box
	Compositional bias	43 – 46	4	Poly-Ser
	Compositional bias	175 – 178	4	Poly-Glu
	Compositional bias	654 – 659	6	Poly-Gly
	Compositional bias	762 – 883	122	Gly-rich
	Compositional bias	819 – 871	53	His-rich
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.14
	Modified residue	5	1	N6-acetyllysine Ref.14
	Modified residue	104	1	Phosphoserine Ref.11
	Modified residue	109	1	Phosphoserine Ref.9 Ref.11 Ref.13 Ref.15
	Modified residue	111	1	Phosphoserine Ref.9 Ref.11 Ref.13 Ref.15
	Modified residue	185	1	Phosphoserine Ref.11
	Modified residue	754	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	1 – 119	119	Missing in isoform 2.		VSP_023518

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D89A252E095D8913	FASTA	938	102,975
	10 20 30 40 50 60 MNWNKGGPGT KRGFGFGGFA ISAGKKEEPK LPQQSHSAFG ATSSSSGFGK SAPPQLPSFY 70 80 90 100 110 120 KIGSKRANFD EENAYFEDEE EDSSNVDLPY IPAENSPTRQ QFHSKPVDSD SDDDPLEAFM 130 140 150 160 170 180 AEVEDQAARD MKRLEEKDKE RKNVKGIRDD IEEEDDQEAY FRYMAENPTA GVVQEEEEDN 190 200 210 220 230 240 LEYDSDGNPI APTKKIIDPL PPIDHSEIDY PPFEKNFYNE HEEITNLTPQ QLIDLRHKLN 250 260 270 280 290 300 LRVSGAAPPR PGSSFAHFGF DEQLMHQIRK SEYTQPTPIQ CQGVPVALSG RDMIGIAKTG 310 320 330 340 350 360 SGKTAAFIWP MLIHIMDQKE LEPGDGPIAV IVCPTRELCQ QIHAECKRFG KAYNLRSVAV 370 380 390 400 410 420 YGGGSMWEQA KALQEGAEIV VCTPGRLIDH VKKKATNLQR VSYLVFDEAD RMFDMGFEYQ 430 440 450 460 470 480 VRSIASHVRP DRQTLLFSAT FRKKIEKLAR DILIDPIRVV QGDIGEANED VTQIVEILHS 490 500 510 520 530 540 GPSKWNWLTR RLVEFTSSGS VLLFVTKKAN AEELANNLKQ EGHNLGLLHG DMDQSERNKV 550 560 570 580 590 600 ISDFKKKDIP VLVATDVAAR GLDIPSIKTV INYDVARDID THTHRIGRTG RAGEKGVAYT 610 620 630 640 650 660 LLTPKDSNFA GDLVRNLEGA NQHVSKELLD LAMQNAWFRK SRFKGGKGKK LNIGGGGLGY 670 680 690 700 710 720 RERPGLGSEN MDRGNNNVMS NYEAYKPSTG AMGDRLTAMK AAFQSQYKSH FVAASLSNQK 730 740 750 760 770 780 AGSSAAGASG WTSAGSLNSV PTNSAQQGHN SPDSPVTSAA KGIPGFGNTG NISGAPVTYP 790 800 810 820 830 840 SAGAQGVNNT ASGNNSREGT GGSNGKRERY TENRGSSRHS HGETGNRHSD SPRHGDGGRH 850 860 870 880 890 900 GDGYRHPESS SRHTDGHRHG ENRHGGSAGR HGENRGANDG RNGESRKEAF NRESKMEPKM 910 920 930 EPKVDSSKMD KVDSKTDKTA DGFAVPEPPK RKKSRWDS
	Isoform 2 [UniParc]. Checksum: F1EED814DA44F42C	FASTA	819	90,068
	10 20 30 40 50 60 MAEVEDQAAR DMKRLEEKDK ERKNVKGIRD DIEEEDDQEA YFRYMAENPT AGVVQEEEED 70 80 90 100 110 120 NLEYDSDGNP IAPTKKIIDP LPPIDHSEID YPPFEKNFYN EHEEITNLTP QQLIDLRHKL 130 140 150 160 170 180 NLRVSGAAPP RPGSSFAHFG FDEQLMHQIR KSEYTQPTPI QCQGVPVALS GRDMIGIAKT 190 200 210 220 230 240 GSGKTAAFIW PMLIHIMDQK ELEPGDGPIA VIVCPTRELC QQIHAECKRF GKAYNLRSVA 250 260 270 280 290 300 VYGGGSMWEQ AKALQEGAEI VVCTPGRLID HVKKKATNLQ RVSYLVFDEA DRMFDMGFEY 310 320 330 340 350 360 QVRSIASHVR PDRQTLLFSA TFRKKIEKLA RDILIDPIRV VQGDIGEANE DVTQIVEILH 370 380 390 400 410 420 SGPSKWNWLT RRLVEFTSSG SVLLFVTKKA NAEELANNLK QEGHNLGLLH GDMDQSERNK 430 440 450 460 470 480 VISDFKKKDI PVLVATDVAA RGLDIPSIKT VINYDVARDI DTHTHRIGRT GRAGEKGVAY 490 500 510 520 530 540 TLLTPKDSNF AGDLVRNLEG ANQHVSKELL DLAMQNAWFR KSRFKGGKGK KLNIGGGGLG 550 560 570 580 590 600 YRERPGLGSE NMDRGNNNVM SNYEAYKPST GAMGDRLTAM KAAFQSQYKS HFVAASLSNQ 610 620 630 640 650 660 KAGSSAAGAS GWTSAGSLNS VPTNSAQQGH NSPDSPVTSA AKGIPGFGNT GNISGAPVTY 670 680 690 700 710 720 PSAGAQGVNN TASGNNSREG TGGSNGKRER YTENRGSSRH SHGETGNRHS DSPRHGDGGR 730 740 750 760 770 780 HGDGYRHPES SSRHTDGHRH GENRHGGSAG RHGENRGAND GRNGESRKEA FNRESKMEPK 790 800 810 MEPKVDSSKM DKVDSKTDKT ADGFAVPEPP KRKKSRWDS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel human member of the DEAD box protein family." Suk K., Kim S., Kim Y.-H., Oh S.-H., Lee M.-K., Kim K.-W., Kim H.-D., Seo Y.-S., Lee M.-S. Biochim. Biophys. Acta 1501:63-69(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[2]	"Expression of RNA helicase-related protein in human hair follicle." Ikeda A., Tsuritani K. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"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: Trachea.
[4]	"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].
[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 (SEP-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] (ISOFORMS 1 AND 2). Tissue: Eye, Pancreas and Uterus.
[7]	"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] OF 574-938 (ISOFORMS 1/2). Tissue: Uterus.
[8]	"Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein." Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R. EMBO J. 21:4978-4988(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2), SUBCELLULAR LOCATION, IDENTIFICATION IN THE SF3B COMPLEX.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Ddx42p -- a human DEAD box protein with RNA chaperone activities." Uhlmann-Schiffler H., Jalal C., Stahl H. Nucleic Acids Res. 34:10-22(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, RNA-BINDING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[11]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-109; SER-111; SER-185 AND SER-754, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"The DEAD box protein Ddx42p modulates the function of ASPP2, a stimulator of apoptosis." Uhlmann-Schiffler H., Kiermayer S., Stahl H. Oncogene 28:2065-2073(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TP53BP2, SUBCELLULAR LOCATION.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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 MET-1 AND LYS-5, MASS SPECTROMETRY.
[15]	"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-109 AND SER-111, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF083255 mRNA. Translation: AAC32396.1. Frameshift. AB036090 mRNA. Translation: BAC66466.1. AK292908 mRNA. Translation: BAF85597.1. AC015651 Genomic DNA. No translation available. CH471109 Genomic DNA. Translation: EAW94277.1. BC008208 mRNA. Translation: AAH08208.1. BC015505 mRNA. Translation: AAH15505.1. BC078667 mRNA. Translation: AAH78667.1. BC093081 mRNA. Translation: AAH93081.1. AL050096 mRNA. Translation: CAB43268.1. BK000566 mRNA. Translation: DAA00077.1.
IPI	IPI00409671. IPI00829889.
PIR	T08745.
RefSeq	NP_031398.2. NM_007372.2. NP_987095.1. NM_203499.1.
UniGene	Hs.702010.
3D structure databases
HSSP	HSSP built from PDB template 2DB3 based on UniProtKB P09052.
ProteinModelPortal	Q86XP3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q86XP3. 5 interactions.
MINT	MINT-1427725.
STRING	9606.ENSP00000352308.
PTM databases
PhosphoSite	Q86XP3.
Polymorphism databases
DMDM	74750541.
Proteomic databases
PaxDb	Q86XP3.
PRIDE	Q86XP3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000359353; ENSP00000352308; ENSG00000198231. ENST00000389924; ENSP00000374574; ENSG00000198231. ENST00000457800; ENSP00000390121; ENSG00000198231. ENST00000578681; ENSP00000464050; ENSG00000198231. ENST00000583590; ENSP00000463561; ENSG00000198231.
GeneID	11325.
KEGG	hsa:11325.
UCSC	uc002jbu.3. human.
Organism-specific databases
CTD	11325.
GeneCards	GC17P061851.
HGNC	HGNC:18676. DDX42.
HPA	HPA023447. HPA023571. HPA025941.
MIM	613369. gene.
neXtProt	NX_Q86XP3.
PharmGKB	PA134875761.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0513.
HOVERGEN	HBG081425.
InParanoid	Q86XP3.
KO	K12835.
OMA	QGVNNTA.
OrthoDB	EOG47WNN9.
Gene expression databases
ArrayExpress	Q86XP3.
Bgee	Q86XP3.
CleanEx	HS_DDX42.
Genevestigator	Q86XP3.
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	DDX42. human.
GenomeRNAi	11325.
NextBio	43019.
SOURCE	Search...

Entry information

Entry name

DDX42_HUMAN

Accession

Primary (citable) accession number: Q86XP3
Secondary accession number(s): A6NML1 , A8KA43, O75619, Q68G51, Q96BK1, Q96HR7, Q9Y3V8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 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.