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Q7L2E3 (DHX30_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. 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:
Putative ATP-dependent RNA helicase DHX30

EC=3.6.4.13
Alternative name(s):
DEAH box protein 30
Gene names
Name:DHX30
Synonyms:DDX30, KIAA0890
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for optimal function of the zinc-finger antiviral protein ZC3HAV1 By similarity. Associates with mitochondrial DNA. Ref.4

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Identified in a complex with TFAM and SSBP1. Interacts with AGO1 and AGO2. Interacts (via N-terminus) with ZC3HAV1 (via N-terminal domain) in an RNA-independent manner By similarity. Ref.4 Ref.5

Subcellular location

Isoform 2: Cytoplasm Ref.4 Ref.6.

Isoform 1: Cytoplasm Ref.4 Ref.6.

Mitochondrion. Cytoplasm Potential. Mitochondrion matrixmitochondrion nucleoid Ref.4 Ref.6.

Post-translational modification

Isoform 2 is phosphorylated on Ser-15.

Sequence similarities

Belongs to the DEAD box helicase family. DEAH subfamily.

Contains 1 DRBM (double-stranded RNA-binding) domain.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence BAA74913.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAA92071.1 differs from that shown. Reason: Probable cloning artifact.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q7L2E3-1)

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: Q7L2E3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MFSLDSFRKD...NPTPGGTISR → MAAARRLMAL...PGEGDGSLVN
Note: Contains a phosphoserine at position 15.
Isoform 3 (identifier: Q7L2E3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     40-41: SR → MA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11941194Putative ATP-dependent RNA helicase DHX30
PRO_0000245538

Regions

Domain53 – 12169DRBM
Domain444 – 612169Helicase ATP-binding
Domain654 – 827174Helicase C-terminal
Nucleotide binding457 – 4648ATP By similarity
Motif559 – 5624DEAH box
Compositional bias188 – 19912Poly-Glu

Natural variations

Alternative sequence1 – 4141MFSLD…GTISR → MAAARRLMALAAGISPRLQP LGPRAAGRQGRSRGFSSSCA HPDHTKEAAEAESGMAPGGP GEGDGSLVN in isoform 2.
VSP_022118
Alternative sequence1 – 3939Missing in isoform 3.
VSP_036891
Alternative sequence40 – 412SR → MA in isoform 3.
VSP_036892

Experimental info

Sequence conflict5571I → T in BAF83955. Ref.2
Sequence conflict7811G → D in BAF83955. Ref.2
Sequence conflict11361R → W in AAH14237. Ref.3

Secondary structure

................. 1194
Helix Strand Turn

Details...

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: 33D9A08799FE7A02

FASTA1,194133,938
        10         20         30         40         50         60 
MFSLDSFRKD RAQHRQRQCK LPPPRLPPMC VNPTPGGTIS RASRDLLKEF PQPKNLLNSV 

        70         80         90        100        110        120 
IGRALGISHA KDKLVYVHTN GPKKKKVTLH IKWPKSVEVE GYGSKKIDAE RQAAAAACQL 

       130        140        150        160        170        180 
FKGWGLLGPR NELFDAAKYR VLADRFGSPA DSWWRPEPTM PPTSWRQLNP ESIRPGGPGG 

       190        200        210        220        230        240 
LSRSLGREEE EDEEEELEEG TIDVTDFLSM TQQDSHAPLR DSRGSSFEMT DDDSAIRALT 

       250        260        270        280        290        300 
QFPLPKNLLA KVIQIATSSS TAKNLMQFHT VGTKTKLSTL TLLWPCPMTF VAKGRRKAEA 

       310        320        330        340        350        360 
ENKAAALACK KLKSLGLVDR NNEPLTHAMY NLASLRELGE TQRRPCTIQV PEPILRKIET 

       370        380        390        400        410        420 
FLNHYPVESS WIAPELRLQS DDILPLGKDS GPLSDPITGK PYVPLLEAEE VRLSQSLLEL 

       430        440        450        460        470        480 
WRRRGPVWQE APQLPVDPHR DTILNAIEQH PVVVISGDTG CGKTTRIPQL LLERYVTEGR 

       490        500        510        520        530        540 
GARCNVIITQ PRRISAVSVA QRVSHELGPS LRRNVGFQVR LESKPPSRGG ALLFCTVGIL 

       550        560        570        580        590        600 
LRKLQSNPSL EGVSHVIVDE VHERDVNTDF LLILLKGLQR LNPALRLVLM SATGDNERFS 

       610        620        630        640        650        660 
RYFGGCPVIK VPGFMYPVKE HYLEDILAKL GKHQYLHRHR HHESEDECAL DLDLVTDLVL 

       670        680        690        700        710        720 
HIDARGEPGG ILCFLPGWQE IKGVQQRLQE ALGMHESKYL ILPVHSNIPM MDQKAIFQQP 

       730        740        750        760        770        780 
PVGVRKIVLA TNIAETSITI NDIVHVVDSG LHKEERYDLK TKVSCLETVW VSRANVIQRR 

       790        800        810        820        830        840 
GRAGRCQSGF AYHLFPRSRL EKMVPFQVPE ILRTPLENLV LQAKIHMPEK TAVEFLSKAV 

       850        860        870        880        890        900 
DSPNIKAVDE AVILLQEIGV LDQREYLTTL GQRLAHISTD PRLAKAIVLA AIFRCLHPLL 

       910        920        930        940        950        960 
VVVSCLTRDP FSSSLQNRAE VDKVKALLSH DSGSDHLAFV RAVAGWEEVL RWQDRSSREN 

       970        980        990       1000       1010       1020 
YLEENLLYAP SLRFIHGLIK QFSENIYEAF LVGKPSDCTL ASAQCNEYSE EEELVKGVLM 

      1030       1040       1050       1060       1070       1080 
AGLYPNLIQV RQGKVTRQGK FKPNSVTYRT KSGNILLHKS TINREATRLR SRWLTYFMAV 

      1090       1100       1110       1120       1130       1140 
KSNGSVFVRD SSQVHPLAVL LLTDGDVHIR DDGRRATISL SDSDLLRLEG DSRTVRLLKE 

      1150       1160       1170       1180       1190 
LRRALGRMVE RSLRSELAAL PPSVQEEHGQ LLALLAELLR GPCGSFDVRK TADD 

« Hide

Isoform 2 [UniParc].

Checksum: BEEE9D1C88DAFCA7
Show »

FASTA1,222136,115
Isoform 3 [UniParc].

Checksum: D3417B4C609F6360
Show »

FASTA1,155129,438

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"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. expand/collapse author list , 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] (ISOFORMS 2 AND 3).
Tissue: Placenta and Teratocarcinoma.
[3]"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 3).
Tissue: Brain, Lymph and Uterus.
[4]"Human mitochondrial DNA nucleoids are linked to protein folding machinery and metabolic enzymes at the mitochondrial inner membrane."
Wang Y., Bogenhagen D.F.
J. Biol. Chem. 281:25791-25802(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[5]"Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGO1 AND AGO2.
[6]"The layered structure of human mitochondrial DNA nucleoids."
Bogenhagen D.F., Rousseau D., Burke S.
J. Biol. Chem. 283:3665-3675(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH MITOCHONDRIAL DNA, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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].
[12]"Solution structure of the double-stranded RNA binding domain in KIAA0890 protein."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 42-148.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB020697 mRNA. Translation: BAA74913.2. Different initiation.
AK002076 mRNA. Translation: BAA92071.1. Sequence problems.
AK291266 mRNA. Translation: BAF83955.1.
BC014237 mRNA. Translation: AAH14237.1.
BC015029 mRNA. Translation: AAH15029.1.
BC020126 mRNA. Translation: AAH20126.1.
BC038417 mRNA. Translation: AAH38417.1.
CCDSCCDS2759.1. [Q7L2E3-1]
PIRE56236.
RefSeqNP_055781.2. NM_014966.3. [Q7L2E3-3]
NP_619520.1. NM_138615.2. [Q7L2E3-1]
XP_006713095.1. XM_006713032.1. [Q7L2E3-2]
UniGeneHs.517948.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DB2NMR-A42-147[»]
ProteinModelPortalQ7L2E3.
SMRQ7L2E3. Positions 44-152, 239-336, 427-981.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116571. 47 interactions.
IntActQ7L2E3. 40 interactions.
MINTMINT-1186537.
STRING9606.ENSP00000392601.

PTM databases

PhosphoSiteQ7L2E3.

Polymorphism databases

DMDM74758997.

Proteomic databases

MaxQBQ7L2E3.
PaxDbQ7L2E3.
PRIDEQ7L2E3.

Protocols and materials databases

DNASU22907.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000445061; ENSP00000405620; ENSG00000132153. [Q7L2E3-1]
ENST00000446256; ENSP00000392601; ENSG00000132153. [Q7L2E3-3]
ENST00000457607; ENSP00000394682; ENSG00000132153. [Q7L2E3-2]
GeneID22907.
KEGGhsa:22907.
UCSCuc003crt.3. human. [Q7L2E3-3]
uc003cru.3. human. [Q7L2E3-1]

Organism-specific databases

CTD22907.
GeneCardsGC03P047844.
HGNCHGNC:16716. DHX30.
HPAHPA034805.
HPA034806.
neXtProtNX_Q7L2E3.
PharmGKBPA27217.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1643.
HOGENOMHOG000112212.
HOVERGENHBG081437.
InParanoidQ7L2E3.
KOK13185.
OMAHKEERYD.
OrthoDBEOG7JX33D.
PhylomeDBQ7L2E3.
TreeFamTF352030.

Gene expression databases

ArrayExpressQ7L2E3.
BgeeQ7L2E3.
CleanExHS_DHX30.
GenevestigatorQ7L2E3.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ7L2E3.
GenomeRNAi22907.
NextBio43571.
PROQ7L2E3.

Entry information

Entry nameDHX30_HUMAN
AccessionPrimary (citable) accession number: Q7L2E3
Secondary accession number(s): A8K5F1 expand/collapse secondary AC list , O94965, Q7Z753, Q96CH4, Q9NUQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 102 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM