Full text data of DHX15
DHX15
(DBP1, DDX15)
[Confidence: low (only semi-automatic identification from reviews)]
Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15; 3.6.4.13 (ATP-dependent RNA helicase #46; DEAH box protein 15)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15; 3.6.4.13 (ATP-dependent RNA helicase #46; DEAH box protein 15)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43143
ID DHX15_HUMAN Reviewed; 795 AA.
AC O43143; Q9NQT7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-FEB-2001, sequence version 2.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase #46;
DE AltName: Full=DEAH box protein 15;
GN Name=DHX15; Synonyms=DBP1, DDX15;
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=9388478; DOI=10.1006/bbrc.1997.7585;
RA Imamura O., Sugawara M., Furuichi Y.;
RT "Cloning and characterization of a putative human RNA helicase gene of
RT the DEAH-box protein family.";
RL Biochem. Biophys. Res. Commun. 240:335-340(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SSB, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Placenta;
RX PubMed=12458796; DOI=10.1017/S1355838202021076;
RA Fouraux M.A., Kolkman M.J.M., Van der Heijden A., De Jong A.S.,
RA Van Venrooij W.J., Pruijn G.J.M.;
RT "The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a
RT putative DEAH-box RNA helicase.";
RL RNA 8:1428-1443(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND MASS
RP SPECTROMETRY.
RX PubMed=15146077; DOI=10.1261/rna.7320604;
RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R.,
RA Elbashir S., Tuschl T., Luehrmann R.;
RT "The human 18S U11/U12 snRNP contains a set of novel proteins not
RT found in the U2-dependent spliceosome.";
RL RNA 10:929-941(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-488, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
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 [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=22002106; DOI=10.1074/mcp.M111.013680;
RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
RT "Systematic analysis of protein pools, isoforms, and modifications
RT affecting turnover and subcellular localization.";
RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
CC -!- FUNCTION: Pre-mRNA processing factor involved in disassembly of
CC spliceosomes after the release of mature mRNA (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Interacts with SSB/La. Component of the U11/U12 snRNPs
CC that are part of the U12-type spliceosome.
CC -!- INTERACTION:
CC P98175:RBM10; NbExp=2; IntAct=EBI-1237044, EBI-721525;
CC Q96I25:RBM17; NbExp=2; IntAct=EBI-1237044, EBI-740272;
CC P52756:RBM5; NbExp=14; IntAct=EBI-1237044, EBI-714003;
CC Q8IWZ8:SUGP1; NbExp=2; IntAct=EBI-1237044, EBI-2691671;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC subfamily. DDX15/PRP43 sub-subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB001636; BAA23987.1; -; mRNA.
DR EMBL; AF279891; AAF90182.1; -; mRNA.
DR EMBL; BC035974; AAH35974.1; -; mRNA.
DR PIR; JC5785; JC5785.
DR RefSeq; NP_001349.2; NM_001358.2.
DR UniGene; Hs.696074; -.
DR ProteinModelPortal; O43143; -.
DR SMR; O43143; 115-787.
DR DIP; DIP-38211N; -.
DR IntAct; O43143; 39.
DR MINT; MINT-5003827; -.
DR STRING; 9606.ENSP00000336741; -.
DR PhosphoSite; O43143; -.
DR SWISS-2DPAGE; O43143; -.
DR PaxDb; O43143; -.
DR PRIDE; O43143; -.
DR Ensembl; ENST00000336812; ENSP00000336741; ENSG00000109606.
DR GeneID; 1665; -.
DR KEGG; hsa:1665; -.
DR UCSC; uc003gqx.3; human.
DR CTD; 1665; -.
DR GeneCards; GC04M024519; -.
DR HGNC; HGNC:2738; DHX15.
DR HPA; HPA047047; -.
DR MIM; 603403; gene.
DR neXtProt; NX_O43143; -.
DR PharmGKB; PA27204; -.
DR eggNOG; COG1643; -.
DR HOGENOM; HOG000175261; -.
DR HOVERGEN; HBG039428; -.
DR InParanoid; O43143; -.
DR KO; K12820; -.
DR OMA; FTSKDYY; -.
DR OrthoDB; EOG7FXZXR; -.
DR GeneWiki; DHX15; -.
DR GenomeRNAi; 1665; -.
DR NextBio; 6852; -.
DR PRO; PR:O43143; -.
DR Bgee; O43143; -.
DR CleanEx; HS_DHX15; -.
DR Genevestigator; O43143; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:HGNC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0008380; P:RNA splicing; IC:HGNC.
DR InterPro; IPR003593; AAA+_ATPase.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Helicase; Hydrolase;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1 795 Putative pre-mRNA-splicing factor ATP-
FT dependent RNA helicase DHX15.
FT /FTId=PRO_0000055139.
FT DOMAIN 147 313 Helicase ATP-binding.
FT DOMAIN 338 518 Helicase C-terminal.
FT NP_BIND 160 167 ATP (By similarity).
FT MOTIF 260 263 DEAH box.
FT MOD_RES 132 132 N6-acetyllysine.
FT MOD_RES 488 488 N6-acetyllysine.
FT CONFLICT 151 151 V -> G (in Ref. 1; BAA23987).
FT CONFLICT 172 173 QW -> HR (in Ref. 1; BAA23987).
FT CONFLICT 232 234 ILK -> FFM (in Ref. 1; BAA23987).
FT CONFLICT 786 795 KLQSKEYSQY -> QTSIQGIFTVLNSVLRTEVIERTALKD
FT E (in Ref. 1; BAA23987).
SQ SEQUENCE 795 AA; 90933 MW; 9A21FBE0051CCAA9 CRC64;
MSKRHRLDLG EDYPSGKKRA GTDGKDRDRD RDREDRSKDR DRERDRGDRE REREKEKEKE
LRASTNAMLI SAGLPPLKAS HSAHSTHSAH STHSTHSAHS THAGHAGHTS LPQCINPFTN
LPHTPRYYDI LKKRLQLPVW EYKDRFTDIL VRHQSFVLVG ETGSGKTTQI PQWCVEYMRS
LPGPKRGVAC TQPRRVAAMS VAQRVADEMD VMLGQEVGYS IRFEDCSSAK TILKYMTDGM
LLREAMNDPL LERYGVIILD EAHERTLATD ILMGVLKEVV RQRSDLKVIV MSATLDAGKF
QIYFDNCPLL TIPGRTHPVE IFYTPEPERD YLEAAIRTVI QIHMCEEEEG DLLLFLTGQE
EIDEACKRIK REVDDLGPEV GDIKIIPLYS TLPPQQQQRI FEPPPPKKQN GAIGRKVVVS
TNIAETSLTI DGVVFVIDPG FAKQKVYNPR IRVESLLVTA ISKASAQQRA GRAGRTRPGK
CFRLYTEKAY KTEMQDNTYP EILRSNLGSV VLQLKKLGID DLVHFDFMDP PAPETLMRAL
ELLNYLAALN DDGDLTELGS MMAEFPLDPQ LAKMVIASCD YNCSNEVLSI TAMLSVPQCF
VRPTEAKKAA DEAKMRFAHI DGDHLTLLNV YHAFKQNHES VQWCYDNFIN YRSLMSADNV
RQQLSRIMDR FNLPRRSTDF TSRDYYINIR KALVTGYFMQ VAHLERTGHY LTVKDNQVVQ
LHPSTVLDHK PEWVLYNEFV LTTKNYIRTC TDIKPEWLVK IAPQYYDMSN FPQCEAKRQL
DRIIAKLQSK EYSQY
//
ID DHX15_HUMAN Reviewed; 795 AA.
AC O43143; Q9NQT7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-FEB-2001, sequence version 2.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase #46;
DE AltName: Full=DEAH box protein 15;
GN Name=DHX15; Synonyms=DBP1, DDX15;
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=9388478; DOI=10.1006/bbrc.1997.7585;
RA Imamura O., Sugawara M., Furuichi Y.;
RT "Cloning and characterization of a putative human RNA helicase gene of
RT the DEAH-box protein family.";
RL Biochem. Biophys. Res. Commun. 240:335-340(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SSB, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Placenta;
RX PubMed=12458796; DOI=10.1017/S1355838202021076;
RA Fouraux M.A., Kolkman M.J.M., Van der Heijden A., De Jong A.S.,
RA Van Venrooij W.J., Pruijn G.J.M.;
RT "The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a
RT putative DEAH-box RNA helicase.";
RL RNA 8:1428-1443(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND MASS
RP SPECTROMETRY.
RX PubMed=15146077; DOI=10.1261/rna.7320604;
RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R.,
RA Elbashir S., Tuschl T., Luehrmann R.;
RT "The human 18S U11/U12 snRNP contains a set of novel proteins not
RT found in the U2-dependent spliceosome.";
RL RNA 10:929-941(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-488, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
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 [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=22002106; DOI=10.1074/mcp.M111.013680;
RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
RT "Systematic analysis of protein pools, isoforms, and modifications
RT affecting turnover and subcellular localization.";
RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
CC -!- FUNCTION: Pre-mRNA processing factor involved in disassembly of
CC spliceosomes after the release of mature mRNA (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Interacts with SSB/La. Component of the U11/U12 snRNPs
CC that are part of the U12-type spliceosome.
CC -!- INTERACTION:
CC P98175:RBM10; NbExp=2; IntAct=EBI-1237044, EBI-721525;
CC Q96I25:RBM17; NbExp=2; IntAct=EBI-1237044, EBI-740272;
CC P52756:RBM5; NbExp=14; IntAct=EBI-1237044, EBI-714003;
CC Q8IWZ8:SUGP1; NbExp=2; IntAct=EBI-1237044, EBI-2691671;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC subfamily. DDX15/PRP43 sub-subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB001636; BAA23987.1; -; mRNA.
DR EMBL; AF279891; AAF90182.1; -; mRNA.
DR EMBL; BC035974; AAH35974.1; -; mRNA.
DR PIR; JC5785; JC5785.
DR RefSeq; NP_001349.2; NM_001358.2.
DR UniGene; Hs.696074; -.
DR ProteinModelPortal; O43143; -.
DR SMR; O43143; 115-787.
DR DIP; DIP-38211N; -.
DR IntAct; O43143; 39.
DR MINT; MINT-5003827; -.
DR STRING; 9606.ENSP00000336741; -.
DR PhosphoSite; O43143; -.
DR SWISS-2DPAGE; O43143; -.
DR PaxDb; O43143; -.
DR PRIDE; O43143; -.
DR Ensembl; ENST00000336812; ENSP00000336741; ENSG00000109606.
DR GeneID; 1665; -.
DR KEGG; hsa:1665; -.
DR UCSC; uc003gqx.3; human.
DR CTD; 1665; -.
DR GeneCards; GC04M024519; -.
DR HGNC; HGNC:2738; DHX15.
DR HPA; HPA047047; -.
DR MIM; 603403; gene.
DR neXtProt; NX_O43143; -.
DR PharmGKB; PA27204; -.
DR eggNOG; COG1643; -.
DR HOGENOM; HOG000175261; -.
DR HOVERGEN; HBG039428; -.
DR InParanoid; O43143; -.
DR KO; K12820; -.
DR OMA; FTSKDYY; -.
DR OrthoDB; EOG7FXZXR; -.
DR GeneWiki; DHX15; -.
DR GenomeRNAi; 1665; -.
DR NextBio; 6852; -.
DR PRO; PR:O43143; -.
DR Bgee; O43143; -.
DR CleanEx; HS_DHX15; -.
DR Genevestigator; O43143; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:HGNC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0008380; P:RNA splicing; IC:HGNC.
DR InterPro; IPR003593; AAA+_ATPase.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Helicase; Hydrolase;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1 795 Putative pre-mRNA-splicing factor ATP-
FT dependent RNA helicase DHX15.
FT /FTId=PRO_0000055139.
FT DOMAIN 147 313 Helicase ATP-binding.
FT DOMAIN 338 518 Helicase C-terminal.
FT NP_BIND 160 167 ATP (By similarity).
FT MOTIF 260 263 DEAH box.
FT MOD_RES 132 132 N6-acetyllysine.
FT MOD_RES 488 488 N6-acetyllysine.
FT CONFLICT 151 151 V -> G (in Ref. 1; BAA23987).
FT CONFLICT 172 173 QW -> HR (in Ref. 1; BAA23987).
FT CONFLICT 232 234 ILK -> FFM (in Ref. 1; BAA23987).
FT CONFLICT 786 795 KLQSKEYSQY -> QTSIQGIFTVLNSVLRTEVIERTALKD
FT E (in Ref. 1; BAA23987).
SQ SEQUENCE 795 AA; 90933 MW; 9A21FBE0051CCAA9 CRC64;
MSKRHRLDLG EDYPSGKKRA GTDGKDRDRD RDREDRSKDR DRERDRGDRE REREKEKEKE
LRASTNAMLI SAGLPPLKAS HSAHSTHSAH STHSTHSAHS THAGHAGHTS LPQCINPFTN
LPHTPRYYDI LKKRLQLPVW EYKDRFTDIL VRHQSFVLVG ETGSGKTTQI PQWCVEYMRS
LPGPKRGVAC TQPRRVAAMS VAQRVADEMD VMLGQEVGYS IRFEDCSSAK TILKYMTDGM
LLREAMNDPL LERYGVIILD EAHERTLATD ILMGVLKEVV RQRSDLKVIV MSATLDAGKF
QIYFDNCPLL TIPGRTHPVE IFYTPEPERD YLEAAIRTVI QIHMCEEEEG DLLLFLTGQE
EIDEACKRIK REVDDLGPEV GDIKIIPLYS TLPPQQQQRI FEPPPPKKQN GAIGRKVVVS
TNIAETSLTI DGVVFVIDPG FAKQKVYNPR IRVESLLVTA ISKASAQQRA GRAGRTRPGK
CFRLYTEKAY KTEMQDNTYP EILRSNLGSV VLQLKKLGID DLVHFDFMDP PAPETLMRAL
ELLNYLAALN DDGDLTELGS MMAEFPLDPQ LAKMVIASCD YNCSNEVLSI TAMLSVPQCF
VRPTEAKKAA DEAKMRFAHI DGDHLTLLNV YHAFKQNHES VQWCYDNFIN YRSLMSADNV
RQQLSRIMDR FNLPRRSTDF TSRDYYINIR KALVTGYFMQ VAHLERTGHY LTVKDNQVVQ
LHPSTVLDHK PEWVLYNEFV LTTKNYIRTC TDIKPEWLVK IAPQYYDMSN FPQCEAKRQL
DRIIAKLQSK EYSQY
//
MIM
603403
*RECORD*
*FIELD* NO
603403
*FIELD* TI
*603403 DEAH BOX POLYPEPTIDE 15; DHX15
;;DEAD/H BOX 15; DDX15;;
DEAH BOX PROTEIN 1; DBP1;;
read morePRP43, S. CEREVISIAE, HOMOLOG OF;;
RNA HELICASE 2; HRH2
*FIELD* TX
CLONING
By RT-PCR of HeLa cell mRNA with degenerate primers based on conserved
regions of DEAH box proteins, Ono et al. (1994) isolated partial cDNAs
encoding 5 members of the human DEAH box family, including HRH1 and
HRH2. They determined that HRH2 shares 61% amino acid sequence identity
with S. cerevisiae JA1. Imamura et al. (1997) isolated cDNAs
corresponding to the entire coding region of HRH2, which they called
DBP1 (DEAH box protein 1). The predicted 813-amino acid protein contains
7 consecutive motifs characteristic of ATP-dependent RNA helicases, as
well as consensus sequences for structural motifs of a DNA/RNA helicase
with a DEAH box. Northern blot analysis revealed that DBP1 was expressed
as a 3.4-kb mRNA in all tissues tested. An additional larger transcript
was observed in many tissues.
Gee et al. (1997) isolated cDNAs encoding the mouse HRH2 homolog,
mDEAH9. Gee et al. (1997) reported that mDEAH9 and Prp43 are 65%
identical over a 500-amino acid region spanning the central helicase
domain and C-terminal region, and that mDEAH9 and HRH2 were 98%
identical in the helicase domain. When expressed in yeast, mDEAH9
complemented the Prp43 mutation specifically, although with less
efficiency than the native yeast protein. Immunofluorescence experiments
showed that mDEAH9 colocalizes with splicing factor SC35 (600813) in
punctate nuclear speckles in mammalian cells, consistent with its
predicted role as a pre-mRNA splicing factor. Gee et al. (1997)
suggested that mDEAH9 represents a mammalian homolog of Prp43.
MAPPING
By fluorescence in situ hybridization, Imamura et al. (1997) mapped the
DHX15 gene to chromosome 4p15.3.
*FIELD* RF
1. Gee, S.; Krauss, S. W.; Miller, E.; Aoyagi, K.; Arenas, J.; Conboy,
J. G.: Cloning of mDEAH9, a putative RNA helicase and mammalian homologue
of Saccharomyces cerevisiae splicing factor Prp43. Proc. Nat. Acad.
Sci. 94: 11803-11807, 1997.
2. Imamura, O.; Sugawara, M.; Furuichi, Y.: Cloning and characterization
of a putative human RNA helicase gene of the DEAH-box protein family. Biochem.
Biophys. Res. Commun. 240: 335-340, 1997.
3. Ono, Y.; Ohno, M.; Shimura, Y.: Identification of a putative RNA
helicase (HRH1), a human homolog of yeast Prp22. Molec. Cell. Biol. 14:
7611-7620, 1994.
*FIELD* CD
Rebekah S. Rasooly: 1/5/1999
*FIELD* ED
wwang: 03/30/2010
wwang: 3/30/2010
alopez: 1/5/1999
*RECORD*
*FIELD* NO
603403
*FIELD* TI
*603403 DEAH BOX POLYPEPTIDE 15; DHX15
;;DEAD/H BOX 15; DDX15;;
DEAH BOX PROTEIN 1; DBP1;;
read morePRP43, S. CEREVISIAE, HOMOLOG OF;;
RNA HELICASE 2; HRH2
*FIELD* TX
CLONING
By RT-PCR of HeLa cell mRNA with degenerate primers based on conserved
regions of DEAH box proteins, Ono et al. (1994) isolated partial cDNAs
encoding 5 members of the human DEAH box family, including HRH1 and
HRH2. They determined that HRH2 shares 61% amino acid sequence identity
with S. cerevisiae JA1. Imamura et al. (1997) isolated cDNAs
corresponding to the entire coding region of HRH2, which they called
DBP1 (DEAH box protein 1). The predicted 813-amino acid protein contains
7 consecutive motifs characteristic of ATP-dependent RNA helicases, as
well as consensus sequences for structural motifs of a DNA/RNA helicase
with a DEAH box. Northern blot analysis revealed that DBP1 was expressed
as a 3.4-kb mRNA in all tissues tested. An additional larger transcript
was observed in many tissues.
Gee et al. (1997) isolated cDNAs encoding the mouse HRH2 homolog,
mDEAH9. Gee et al. (1997) reported that mDEAH9 and Prp43 are 65%
identical over a 500-amino acid region spanning the central helicase
domain and C-terminal region, and that mDEAH9 and HRH2 were 98%
identical in the helicase domain. When expressed in yeast, mDEAH9
complemented the Prp43 mutation specifically, although with less
efficiency than the native yeast protein. Immunofluorescence experiments
showed that mDEAH9 colocalizes with splicing factor SC35 (600813) in
punctate nuclear speckles in mammalian cells, consistent with its
predicted role as a pre-mRNA splicing factor. Gee et al. (1997)
suggested that mDEAH9 represents a mammalian homolog of Prp43.
MAPPING
By fluorescence in situ hybridization, Imamura et al. (1997) mapped the
DHX15 gene to chromosome 4p15.3.
*FIELD* RF
1. Gee, S.; Krauss, S. W.; Miller, E.; Aoyagi, K.; Arenas, J.; Conboy,
J. G.: Cloning of mDEAH9, a putative RNA helicase and mammalian homologue
of Saccharomyces cerevisiae splicing factor Prp43. Proc. Nat. Acad.
Sci. 94: 11803-11807, 1997.
2. Imamura, O.; Sugawara, M.; Furuichi, Y.: Cloning and characterization
of a putative human RNA helicase gene of the DEAH-box protein family. Biochem.
Biophys. Res. Commun. 240: 335-340, 1997.
3. Ono, Y.; Ohno, M.; Shimura, Y.: Identification of a putative RNA
helicase (HRH1), a human homolog of yeast Prp22. Molec. Cell. Biol. 14:
7611-7620, 1994.
*FIELD* CD
Rebekah S. Rasooly: 1/5/1999
*FIELD* ED
wwang: 03/30/2010
wwang: 3/30/2010
alopez: 1/5/1999