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Q14562 (DHX8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent RNA helicase DHX8

EC=3.6.4.13
Alternative name(s):
DEAH box protein 8
RNA helicase HRH1
Gene names
Name:DHX8
Synonyms:DDX8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. Ref.2

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Identified in the spliceosome C complex. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. Ref.3 Ref.4

Subcellular location

Nucleus.

Domain

The RS domain confers a nuclear localization signal, and appears to facilitate the interaction with the spliceosome.

Sequence similarities

Belongs to the DEAD box helicase family. DEAH subfamily. DDX8/PRP22 sub-subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 S1 motif domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12201220ATP-dependent RNA helicase DHX8
PRO_0000055131

Regions

Domain265 – 33672S1 motif
Domain575 – 738164Helicase ATP-binding
Domain756 – 936181Helicase C-terminal
Nucleotide binding588 – 5958ATP By similarity
Motif685 – 6884DEAH box
Compositional bias172 – 1754Poly-Lys
Compositional bias176 – 22853Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue4561Phosphoserine Ref.8
Modified residue4601Phosphoserine Ref.6 Ref.8

Natural variations

Natural variant10691A → G.
Corresponds to variant rs34285079 [ dbSNP | Ensembl ].
VAR_052174

Experimental info

Mutagenesis5941K → E in GET; inhibition of pre-mRNA splicing and nuclear export of unspliced RNA.
Mutagenesis7171S → L in LAT; inhibition of pre-mRNA splicing and nuclear export of unspliced RNA.

Secondary structure

........................................................ 1220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14562 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 17C1602A73A0EF24

FASTA1,220139,315
        10         20         30         40         50         60 
MAVAVAMAGA LIGSEPGPAE ELAKLEYLSL VSKVCTELDN HLGINDKDLA EFVISLAEKN 

        70         80         90        100        110        120 
TTFDTFKASL VKNGAEFTDS LISNLLRLIQ TMRPPAKPST SKDPVVKPKT EKEKLKELFP 

       130        140        150        160        170        180 
VLCQPDNPSV RTMLDEDDVK VAVDVLKELE ALMPSAAGQE KQRDAEHRDR TKKKKRSRSR 

       190        200        210        220        230        240 
DRNRDRDRDR ERNRDRDHKR RHRSRSRSRS RTRERNKVKS RYRSRSRSQS PPKDRKDRDK 

       250        260        270        280        290        300 
YGERNLDRWR DKHVDRPPPE EPTIGDIYNG KVTSIMQFGC FVQLEGLRKR WEGLVHISEL 

       310        320        330        340        350        360 
RREGRVANVA DVVSKGQRVK VKVLSFTGTK TSLSMKDVDQ ETGEDLNPNR RRNLVGETNE 

       370        380        390        400        410        420 
ETSMRNPDRP THLSLVSAPE VEDDSLERKR LTRISDPEKW EIKQMIAANV LSKEEFPDFD 

       430        440        450        460        470        480 
EETGILPKVD DEEDEDLEIE LVEEEPPFLR GHTKQSMDMS PIKIVKNPDG SLSQAAMMQS 

       490        500        510        520        530        540 
ALAKERRELK QAQREAEMDS IPMGLNKHWV DPLPDAEGRQ IAANMRGIGM MPNDIPEWKK 

       550        560        570        580        590        600 
HAFGGNKASY GKKTQMSILE QRESLPIYKL KEQLVQAVHD NQILIVIGET GSGKTTQITQ 

       610        620        630        640        650        660 
YLAEAGYTSR GKIGCTQPRR VAAMSVAKRV SEEFGCCLGQ EVGYTIRFED CTSPETVIKY 

       670        680        690        700        710        720 
MTDGMLLREC LIDPDLTQYA IIMLDEAHER TIHTDVLFGL LKKTVQKRQD MKLIVTSATL 

       730        740        750        760        770        780 
DAVKFSQYFY EAPIFTIPGR TYPVEILYTK EPETDYLDAS LITVMQIHLT EPPGDILVFL 

       790        800        810        820        830        840 
TGQEEIDTAC EILYERMKSL GPDVPELIIL PVYSALPSEM QTRIFDPAPP GSRKVVIATN 

       850        860        870        880        890        900 
IAETSLTIDG IYYVVDPGFV KQKVYNSKTG IDQLVVTPIS QAQAKQRAGR AGRTGPGKCY 

       910        920        930        940        950        960 
RLYTERAYRD EMLTTNVPEI QRTNLASTVL SLKAMGINDL LSFDFMDAPP METLITAMEQ 

       970        980        990       1000       1010       1020 
LYTLGALDDE GLLTRLGRRM AEFPLEPMLC KMLIMSVHLG CSEEMLTIVS MLSVQNVFYR 

      1030       1040       1050       1060       1070       1080 
PKDKQALADQ KKAKFHQTEG DHLTLLAVYN SWKNNKFSNP WCYENFIQAR SLRRAQDIRK 

      1090       1100       1110       1120       1130       1140 
QMLGIMDRHK LDVVSCGKST VRVQKAICSG FFRNAAKKDP QEGYRTLIDQ QVVYIHPSSA 

      1150       1160       1170       1180       1190       1200 
LFNRQPEWVV YHELVLTTKE YMREVTTIDP RWLVEFAPAF FKVSDPTKLS KQKKQQRLEP 

      1210       1220 
LYNRYEEPNA WRISRAFRRR 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a putative RNA helicase (HRH1), a human homolog of yeast Prp22."
Ono Y., Ohno M., Shimura Y.
Mol. Cell. Biol. 14:7611-7620(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A human RNA helicase-like protein, HRH1, facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome."
Ohno M., Shimura Y.
Genes Dev. 10:997-1007(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[3]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[4]"Novel function of beta-arrestin2 in the nucleus of mature spermatozoa."
Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.
J. Cell Sci. 119:3047-3056(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[5]"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.
[6]"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-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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].
[8]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Solution structure of the S1 RNA binding domain of human ATP-dependent RNA helicase DHX8."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 260-355.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50487 mRNA. Translation: BAA09078.1.
PIRA56236.
RefSeqNP_004932.1. NM_004941.1.
UniGeneHs.463105.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQSNMR-A260-355[»]
3I4UX-ray2.10A950-1183[»]
ProteinModelPortalQ14562.
SMRQ14562. Positions 260-355, 556-1198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108024. 29 interactions.
IntActQ14562. 19 interactions.
MINTMINT-3029791.
STRING9606.ENSP00000262415.

PTM databases

PhosphoSiteQ14562.

Polymorphism databases

DMDM3023637.

Proteomic databases

PaxDbQ14562.
PeptideAtlasQ14562.
PRIDEQ14562.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262415; ENSP00000262415; ENSG00000067596.
GeneID1659.
KEGGhsa:1659.
UCSCuc002idu.1. human.

Organism-specific databases

CTD1659.
GeneCardsGC17P041572.
HGNCHGNC:2749. DHX8.
HPAHPA049285.
MIM600396. gene.
neXtProtNX_Q14562.
PharmGKBPA27231.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1643.
HOGENOMHOG000175261.
HOVERGENHBG039428.
InParanoidQ14562.
KOK12818.
OMAFVQIRTL.
PhylomeDBQ14562.
TreeFamTF300509.

Gene expression databases

ArrayExpressQ14562.
BgeeQ14562.
CleanExHS_DHX8.
GenevestigatorQ14562.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.40.50.300. 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.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR022967. RNA-binding_domain_S1.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
PF00575. S1. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
SM00316. S1. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14562.
GenomeRNAi1659.
NextBio6828.
PROQ14562.
SOURCESearch...

Entry information

Entry nameDHX8_HUMAN
AccessionPrimary (citable) accession number: Q14562
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 138 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM