ID DHX8_HUMAN Reviewed; 1220 AA.
AC Q14562;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 01-MAY-2013, entry version 128.
DE RecName: Full=ATP-dependent RNA helicase DHX8;
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 8;
DE AltName: Full=RNA helicase HRH1;
GN Name=DHX8; Synonyms=DDX8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7935475;
RA Ono Y., Ohno M., Shimura Y.;
RT "Identification of a putative RNA helicase (HRH1), a human homolog of
RT yeast Prp22.";
RL Mol. Cell. Biol. 14:7611-7620(1994).
RN [2]
RP FUNCTION.
RX PubMed=8608946;
RA Ohno M., Shimura Y.;
RT "A human RNA helicase-like protein, HRH1, facilitates nuclear export
RT of spliced mRNA by releasing the RNA from the spliceosome.";
RL Genes Dev. 10:997-1007(1996).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [4]
RP INTERACTION WITH ARRB2.
RX PubMed=16820410; DOI=10.1242/jcs.03046;
RA Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.;
RT "Novel function of beta-arrestin2 in the nucleus of mature
RT spermatozoa.";
RL J. Cell Sci. 119:3047-3056(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND SER-460, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP STRUCTURE BY NMR OF 260-355.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the S1 RNA binding domain of human ATP-
RT dependent RNA helicase DHX8.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Facilitates nuclear export of spliced mRNA by releasing
CC the RNA from the spliceosome.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with
CC ARRB2; the interaction is detected in the nucleus upon OR1D2
CC stimulation.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The RS domain confers a nuclear localization signal, and
CC appears to facilitate the interaction with the spliceosome.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC subfamily. DDX8/PRP22 sub-subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- SIMILARITY: Contains 1 S1 motif domain.
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DR EMBL; D50487; BAA09078.1; -; mRNA.
DR IPI; IPI00031508; -.
DR PIR; A56236; A56236.
DR RefSeq; NP_004932.1; NM_004941.1.
DR UniGene; Hs.463105; -.
DR PDB; 2EQS; NMR; -; A=260-355.
DR PDB; 3I4U; X-ray; 2.10 A; A=950-1183.
DR PDBsum; 2EQS; -.
DR PDBsum; 3I4U; -.
DR ProteinModelPortal; Q14562; -.
DR IntAct; Q14562; 4.
DR STRING; 9606.ENSP00000262415; -.
DR PhosphoSite; Q14562; -.
DR DMDM; 3023637; -.
DR PaxDb; Q14562; -.
DR PeptideAtlas; Q14562; -.
DR PRIDE; Q14562; -.
DR Ensembl; ENST00000262415; ENSP00000262415; ENSG00000067596.
DR GeneID; 1659; -.
DR KEGG; hsa:1659; -.
DR UCSC; uc002idu.1; human.
DR CTD; 1659; -.
DR GeneCards; GC17P041572; -.
DR HGNC; HGNC:2749; DHX8.
DR HPA; HPA049285; -.
DR MIM; 600396; gene.
DR neXtProt; NX_Q14562; -.
DR PharmGKB; PA27231; -.
DR eggNOG; COG1643; -.
DR HOGENOM; HOG000175261; -.
DR HOVERGEN; HBG039428; -.
DR InParanoid; Q14562; -.
DR KO; K12818; -.
DR OMA; NAWCYEN; -.
DR OrthoDB; EOG4D26P2; -.
DR PhylomeDB; Q14562; -.
DR EvolutionaryTrace; Q14562; -.
DR GenomeRNAi; 1659; -.
DR NextBio; 6828; -.
DR ArrayExpress; Q14562; -.
DR Bgee; Q14562; -.
DR CleanEx; HS_DHX8; -.
DR Genevestigator; Q14562; -.
DR GermOnline; ENSG00000067596; Homo sapiens.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR011709; DUF1605.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR InterPro; IPR022967; RNA-binding_domain_S1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Complete proteome; Helicase; Hydrolase;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Spliceosome.
FT CHAIN 1 1220 ATP-dependent RNA helicase DHX8.
FT /FTId=PRO_0000055131.
FT DOMAIN 265 336 S1 motif.
FT DOMAIN 575 738 Helicase ATP-binding.
FT DOMAIN 756 936 Helicase C-terminal.
FT NP_BIND 588 595 ATP (By similarity).
FT MOTIF 685 688 DEAH box.
FT COMPBIAS 172 175 Poly-Lys.
FT COMPBIAS 176 228 Arg/Ser-rich (RS domain).
FT MOD_RES 456 456 Phosphoserine.
FT MOD_RES 460 460 Phosphoserine.
FT VARIANT 1069 1069 A -> G (in dbSNP:rs34285079).
FT /FTId=VAR_052174.
FT MUTAGEN 594 594 K->E: In GET; inhibition of pre-mRNA
FT splicing and nuclear export of unspliced
FT RNA.
FT MUTAGEN 717 717 S->L: In LAT; inhibition of pre-mRNA
FT splicing and nuclear export of unspliced
FT RNA.
FT STRAND 267 275
FT STRAND 280 284
FT STRAND 286 289
FT STRAND 292 295
FT HELIX 297 299
FT STRAND 301 304
FT HELIX 309 312
FT STRAND 318 327
FT STRAND 330 335
FT TURN 340 342
FT HELIX 950 963
FT HELIX 975 980
FT HELIX 987 998
FT HELIX 1002 1012
FT HELIX 1022 1024
FT HELIX 1025 1033
FT HELIX 1041 1054
FT TURN 1055 1057
FT HELIX 1059 1064
FT HELIX 1069 1088
FT HELIX 1101 1111
FT HELIX 1112 1114
FT STRAND 1115 1118
FT STRAND 1120 1126
FT TURN 1127 1129
FT STRAND 1132 1135
FT TURN 1140 1143
FT STRAND 1147 1167
FT HELIX 1170 1176
FT TURN 1178 1180
SQ SEQUENCE 1220 AA; 139315 MW; 17C1602A73A0EF24 CRC64;
MAVAVAMAGA LIGSEPGPAE ELAKLEYLSL VSKVCTELDN HLGINDKDLA EFVISLAEKN
TTFDTFKASL VKNGAEFTDS LISNLLRLIQ TMRPPAKPST SKDPVVKPKT EKEKLKELFP
VLCQPDNPSV RTMLDEDDVK VAVDVLKELE ALMPSAAGQE KQRDAEHRDR TKKKKRSRSR
DRNRDRDRDR ERNRDRDHKR RHRSRSRSRS RTRERNKVKS RYRSRSRSQS PPKDRKDRDK
YGERNLDRWR DKHVDRPPPE EPTIGDIYNG KVTSIMQFGC FVQLEGLRKR WEGLVHISEL
RREGRVANVA DVVSKGQRVK VKVLSFTGTK TSLSMKDVDQ ETGEDLNPNR RRNLVGETNE
ETSMRNPDRP THLSLVSAPE VEDDSLERKR LTRISDPEKW EIKQMIAANV LSKEEFPDFD
EETGILPKVD DEEDEDLEIE LVEEEPPFLR GHTKQSMDMS PIKIVKNPDG SLSQAAMMQS
ALAKERRELK QAQREAEMDS IPMGLNKHWV DPLPDAEGRQ IAANMRGIGM MPNDIPEWKK
HAFGGNKASY GKKTQMSILE QRESLPIYKL KEQLVQAVHD NQILIVIGET GSGKTTQITQ
YLAEAGYTSR GKIGCTQPRR VAAMSVAKRV SEEFGCCLGQ EVGYTIRFED CTSPETVIKY
MTDGMLLREC LIDPDLTQYA IIMLDEAHER TIHTDVLFGL LKKTVQKRQD MKLIVTSATL
DAVKFSQYFY EAPIFTIPGR TYPVEILYTK EPETDYLDAS LITVMQIHLT EPPGDILVFL
TGQEEIDTAC EILYERMKSL GPDVPELIIL PVYSALPSEM QTRIFDPAPP GSRKVVIATN
IAETSLTIDG IYYVVDPGFV KQKVYNSKTG IDQLVVTPIS QAQAKQRAGR AGRTGPGKCY
RLYTERAYRD EMLTTNVPEI QRTNLASTVL SLKAMGINDL LSFDFMDAPP METLITAMEQ
LYTLGALDDE GLLTRLGRRM AEFPLEPMLC KMLIMSVHLG CSEEMLTIVS MLSVQNVFYR
PKDKQALADQ KKAKFHQTEG DHLTLLAVYN SWKNNKFSNP WCYENFIQAR SLRRAQDIRK
QMLGIMDRHK LDVVSCGKST VRVQKAICSG FFRNAAKKDP QEGYRTLIDQ QVVYIHPSSA
LFNRQPEWVV YHELVLTTKE YMREVTTIDP RWLVEFAPAF FKVSDPTKLS KQKKQQRLEP
LYNRYEEPNA WRISRAFRRR
//
