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Q14562

- DHX8_HUMAN

UniProt

Q14562 - DHX8_HUMAN

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Protein

ATP-dependent RNA helicase DHX8

Gene

DHX8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi588 – 5958ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent RNA helicase activity Source: ProtInc
  3. identical protein binding Source: IntAct
  4. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. mRNA splicing, via spliceosome Source: UniProtKB
  3. RNA processing Source: ProtInc
  4. RNA splicing Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DHX8 (EC:3.6.4.13)
Alternative name(s):
DEAH box protein 8
RNA helicase HRH1
Gene namesi
Name:DHX8
Synonyms:DDX8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:2749. DHX8.

Subcellular locationi

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. nucleus Source: HPA
  3. spliceosomal complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi594 – 5941K → E in GET; inhibition of pre-mRNA splicing and nuclear export of unspliced RNA.
Mutagenesisi717 – 7171S → L in LAT; inhibition of pre-mRNA splicing and nuclear export of unspliced RNA.

Organism-specific databases

PharmGKBiPA27231.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12201220ATP-dependent RNA helicase DHX8PRO_0000055131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei456 – 4561Phosphoserine1 Publication
Modified residuei460 – 4601Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14562.
PaxDbiQ14562.
PeptideAtlasiQ14562.
PRIDEiQ14562.

PTM databases

PhosphoSiteiQ14562.

Expressioni

Gene expression databases

BgeeiQ14562.
CleanExiHS_DHX8.
ExpressionAtlasiQ14562. baseline and differential.
GenevestigatoriQ14562.

Organism-specific databases

HPAiHPA049285.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2511477,EBI-2511477
CHERPQ8IWX82EBI-2511477,EBI-2555370
ISY1Q9ULR02EBI-2511477,EBI-2557660
NKAPQ8N5F72EBI-2511477,EBI-721539

Protein-protein interaction databases

BioGridi108024. 56 interactions.
IntActiQ14562. 20 interactions.
MINTiMINT-3029791.
STRINGi9606.ENSP00000262415.

Structurei

Secondary structure

1
1220
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi267 – 2759
Beta strandi280 – 2845
Beta strandi286 – 2894
Beta strandi292 – 2954
Helixi297 – 2993
Beta strandi301 – 3044
Helixi309 – 3124
Beta strandi318 – 32710
Beta strandi330 – 3356
Turni340 – 3423
Helixi950 – 96314
Helixi975 – 9806
Helixi987 – 99812
Helixi1002 – 101211
Helixi1022 – 10243
Helixi1025 – 10339
Helixi1041 – 105414
Turni1055 – 10573
Helixi1059 – 10646
Helixi1069 – 108820
Helixi1101 – 111111
Helixi1112 – 11143
Beta strandi1115 – 11184
Beta strandi1120 – 11267
Turni1127 – 11293
Beta strandi1132 – 11354
Turni1140 – 11434
Beta strandi1147 – 116721
Helixi1170 – 11767
Turni1178 – 11803

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQSNMR-A260-355[»]
3I4UX-ray2.10A950-1183[»]
ProteinModelPortaliQ14562.
SMRiQ14562. Positions 260-355, 556-1198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14562.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini265 – 33672S1 motifPROSITE-ProRule annotationAdd
BLAST
Domaini575 – 738164Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini756 – 936181Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi685 – 6884DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi172 – 1754Poly-Lys
Compositional biasi176 – 22853Arg/Ser-rich (RS domain)Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 S1 motif domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1643.
GeneTreeiENSGT00760000119272.
HOGENOMiHOG000175261.
HOVERGENiHBG039428.
InParanoidiQ14562.
KOiK12818.
OMAiFVQIRTL.
PhylomeDBiQ14562.
TreeFamiTF300509.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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. S1_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
PF00575. S1. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
SM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14562-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVAVAMAGA LIGSEPGPAE ELAKLEYLSL VSKVCTELDN HLGINDKDLA
60 70 80 90 100
EFVISLAEKN TTFDTFKASL VKNGAEFTDS LISNLLRLIQ TMRPPAKPST
110 120 130 140 150
SKDPVVKPKT EKEKLKELFP VLCQPDNPSV RTMLDEDDVK VAVDVLKELE
160 170 180 190 200
ALMPSAAGQE KQRDAEHRDR TKKKKRSRSR DRNRDRDRDR ERNRDRDHKR
210 220 230 240 250
RHRSRSRSRS RTRERNKVKS RYRSRSRSQS PPKDRKDRDK YGERNLDRWR
260 270 280 290 300
DKHVDRPPPE EPTIGDIYNG KVTSIMQFGC FVQLEGLRKR WEGLVHISEL
310 320 330 340 350
RREGRVANVA DVVSKGQRVK VKVLSFTGTK TSLSMKDVDQ ETGEDLNPNR
360 370 380 390 400
RRNLVGETNE ETSMRNPDRP THLSLVSAPE VEDDSLERKR LTRISDPEKW
410 420 430 440 450
EIKQMIAANV LSKEEFPDFD EETGILPKVD DEEDEDLEIE LVEEEPPFLR
460 470 480 490 500
GHTKQSMDMS PIKIVKNPDG SLSQAAMMQS ALAKERRELK QAQREAEMDS
510 520 530 540 550
IPMGLNKHWV DPLPDAEGRQ IAANMRGIGM MPNDIPEWKK HAFGGNKASY
560 570 580 590 600
GKKTQMSILE QRESLPIYKL KEQLVQAVHD NQILIVIGET GSGKTTQITQ
610 620 630 640 650
YLAEAGYTSR GKIGCTQPRR VAAMSVAKRV SEEFGCCLGQ EVGYTIRFED
660 670 680 690 700
CTSPETVIKY MTDGMLLREC LIDPDLTQYA IIMLDEAHER TIHTDVLFGL
710 720 730 740 750
LKKTVQKRQD MKLIVTSATL DAVKFSQYFY EAPIFTIPGR TYPVEILYTK
760 770 780 790 800
EPETDYLDAS LITVMQIHLT EPPGDILVFL TGQEEIDTAC EILYERMKSL
810 820 830 840 850
GPDVPELIIL PVYSALPSEM QTRIFDPAPP GSRKVVIATN IAETSLTIDG
860 870 880 890 900
IYYVVDPGFV KQKVYNSKTG IDQLVVTPIS QAQAKQRAGR AGRTGPGKCY
910 920 930 940 950
RLYTERAYRD EMLTTNVPEI QRTNLASTVL SLKAMGINDL LSFDFMDAPP
960 970 980 990 1000
METLITAMEQ LYTLGALDDE GLLTRLGRRM AEFPLEPMLC KMLIMSVHLG
1010 1020 1030 1040 1050
CSEEMLTIVS MLSVQNVFYR PKDKQALADQ KKAKFHQTEG DHLTLLAVYN
1060 1070 1080 1090 1100
SWKNNKFSNP WCYENFIQAR SLRRAQDIRK QMLGIMDRHK LDVVSCGKST
1110 1120 1130 1140 1150
VRVQKAICSG FFRNAAKKDP QEGYRTLIDQ QVVYIHPSSA LFNRQPEWVV
1160 1170 1180 1190 1200
YHELVLTTKE YMREVTTIDP RWLVEFAPAF FKVSDPTKLS KQKKQQRLEP
1210 1220
LYNRYEEPNA WRISRAFRRR
Length:1,220
Mass (Da):139,315
Last modified:November 1, 1996 - v1
Checksum:i17C1602A73A0EF24
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1069 – 10691A → G.
Corresponds to variant rs34285079 [ dbSNP | Ensembl ].
VAR_052174

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50487 mRNA. Translation: BAA09078.1.
CCDSiCCDS11464.1.
PIRiA56236.
RefSeqiNP_004932.1. NM_004941.1.
UniGeneiHs.463105.

Genome annotation databases

EnsembliENST00000262415; ENSP00000262415; ENSG00000067596.
GeneIDi1659.
KEGGihsa:1659.
UCSCiuc002idu.1. human.

Polymorphism databases

DMDMi3023637.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50487 mRNA. Translation: BAA09078.1 .
CCDSi CCDS11464.1.
PIRi A56236.
RefSeqi NP_004932.1. NM_004941.1.
UniGenei Hs.463105.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EQS NMR - A 260-355 [» ]
3I4U X-ray 2.10 A 950-1183 [» ]
ProteinModelPortali Q14562.
SMRi Q14562. Positions 260-355, 556-1198.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108024. 56 interactions.
IntActi Q14562. 20 interactions.
MINTi MINT-3029791.
STRINGi 9606.ENSP00000262415.

PTM databases

PhosphoSitei Q14562.

Polymorphism databases

DMDMi 3023637.

Proteomic databases

MaxQBi Q14562.
PaxDbi Q14562.
PeptideAtlasi Q14562.
PRIDEi Q14562.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262415 ; ENSP00000262415 ; ENSG00000067596 .
GeneIDi 1659.
KEGGi hsa:1659.
UCSCi uc002idu.1. human.

Organism-specific databases

CTDi 1659.
GeneCardsi GC17P041569.
HGNCi HGNC:2749. DHX8.
HPAi HPA049285.
MIMi 600396. gene.
neXtProti NX_Q14562.
PharmGKBi PA27231.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1643.
GeneTreei ENSGT00760000119272.
HOGENOMi HOG000175261.
HOVERGENi HBG039428.
InParanoidi Q14562.
KOi K12818.
OMAi FVQIRTL.
PhylomeDBi Q14562.
TreeFami TF300509.

Miscellaneous databases

EvolutionaryTracei Q14562.
GenomeRNAii 1659.
NextBioi 6828.
PROi Q14562.
SOURCEi Search...

Gene expression databases

Bgeei Q14562.
CleanExi HS_DHX8.
ExpressionAtlasi Q14562. baseline and differential.
Genevestigatori Q14562.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR011545. DEAD/DEAH_box_helicase_dom.
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. S1_dom.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
PF00575. S1. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
SM00316. S1. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50126. S1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiDHX8_HUMAN
AccessioniPrimary (citable) accession number: Q14562
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3