Full text data of DHX29
DHX29
(DDX29)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
ATP-dependent RNA helicase DHX29; 3.6.4.13 (DEAH box protein 29; Nucleic acid helicase DDXx)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
ATP-dependent RNA helicase DHX29; 3.6.4.13 (DEAH box protein 29; Nucleic acid helicase DDXx)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q7Z478
ID DHX29_HUMAN Reviewed; 1369 AA.
AC Q7Z478; O75549; Q63HN0; Q63HN3; Q8IWW2; Q8N3A1; Q9UMH2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JUL-2006, sequence version 2.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=ATP-dependent RNA helicase DHX29;
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 29;
DE AltName: Full=Nucleic acid helicase DDXx;
GN Name=DHX29; Synonyms=DDX29;
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].
RA Abdelhaleem M.M.;
RT "Identification of a new member of the DDx subfamily of helicases.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-630.
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-1369.
RC TISSUE=Amygdala, Fetal kidney, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 561-1369.
RA Bassi M.T., Banfi S., Riboni M., Ballabio A., Borsani G.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1119-1369.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-200, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP FUNCTION, RIBOSOME-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19109895; DOI=10.1016/j.cell.2008.10.037;
RA Pisareva V.P., Pisarev A.V., Komar A.A., Hellen C.U.T., Pestova T.V.;
RT "Translation initiation on mammalian mRNAs with structured 5'UTRs
RT requires DExH-box protein DHX29.";
RL Cell 135:1237-1250(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-200, AND
RP MASS SPECTROMETRY.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-200, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASS
RP 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 [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.6 ANGSTROMS) IN COMPLEX WITH THE
RP 43S PRE-INITIATION COMPLEX, FUNCTION, AND SUBUNIT.
RX PubMed=23706745; DOI=10.1016/j.cell.2013.04.036;
RA Hashem Y., des Georges A., Dhote V., Langlois R., Liao H.Y.,
RA Grassucci R.A., Hellen C.U., Pestova T.V., Frank J.;
RT "Structure of the mammalian ribosomal 43S preinitiation complex bound
RT to the scanning factor DHX29.";
RL Cell 153:1108-1119(2013).
CC -!- FUNCTION: ATP-binding RNA helicase involved in translation
CC initiation. Part of the 43S pre-initiation complex that is
CC required for efficient initiation on mammalian mRNAs with
CC structured 5'-UTRs by promoting efficient NTPase-dependent 48S
CC complex formation. Specifically binds to the 40S ribosome near the
CC mRNA entrance. Does not possess a processive helicase activity.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Part of the 43S pre-initiation complex that contains at
CC least Met-tRNA, EIF1, EIF1A (EIF1AX or EIF1AY), EIF2S1, EIF2S2,
CC EIF2S3, EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H,
CC EIF3I, EIF3J, EIF3K, EIF3L, EIF3M, DHX29 and the 40S ribosomal
CC subunit.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC 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; AY036974; AAK64516.1; -; mRNA.
DR EMBL; BC056219; AAH56219.1; -; mRNA.
DR EMBL; AL834496; CAD39154.1; -; mRNA.
DR EMBL; BX648101; CAH56172.1; -; mRNA.
DR EMBL; BX648269; CAH56153.1; -; mRNA.
DR EMBL; AL079292; CAB45191.1; -; mRNA.
DR EMBL; AF070639; AAC25394.1; -; mRNA.
DR RefSeq; NP_061903.2; NM_019030.2.
DR UniGene; Hs.593268; -.
DR ProteinModelPortal; Q7Z478; -.
DR SMR; Q7Z478; 520-754, 868-1292.
DR IntAct; Q7Z478; 3.
DR MINT; MINT-1376685; -.
DR STRING; 9606.ENSP00000251636; -.
DR PhosphoSite; Q7Z478; -.
DR DMDM; 110278938; -.
DR PaxDb; Q7Z478; -.
DR PeptideAtlas; Q7Z478; -.
DR PRIDE; Q7Z478; -.
DR Ensembl; ENST00000251636; ENSP00000251636; ENSG00000067248.
DR GeneID; 54505; -.
DR KEGG; hsa:54505; -.
DR UCSC; uc003jpx.3; human.
DR CTD; 54505; -.
DR GeneCards; GC05M054552; -.
DR H-InvDB; HIX0004866; -.
DR HGNC; HGNC:15815; DHX29.
DR HPA; HPA038317; -.
DR HPA; HPA038318; -.
DR MIM; 612720; gene.
DR neXtProt; NX_Q7Z478; -.
DR PharmGKB; PA27215; -.
DR eggNOG; COG1643; -.
DR HOGENOM; HOG000247063; -.
DR HOVERGEN; HBG081436; -.
DR InParanoid; Q7Z478; -.
DR OMA; WLLYQEK; -.
DR OrthoDB; EOG7SV0TS; -.
DR PhylomeDB; Q7Z478; -.
DR ChiTaRS; DHX29; human.
DR GenomeRNAi; 54505; -.
DR NextBio; 56869; -.
DR PRO; PR:Q7Z478; -.
DR Bgee; Q7Z478; -.
DR CleanEx; HS_DHX29; -.
DR Genevestigator; Q7Z478; -.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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 ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Helicase;
KW Hydrolase; Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Protein biosynthesis; Reference proteome.
FT CHAIN 1 1369 ATP-dependent RNA helicase DHX29.
FT /FTId=PRO_0000245535.
FT DOMAIN 582 755 Helicase ATP-binding.
FT DOMAIN 849 1026 Helicase C-terminal.
FT NP_BIND 595 602 ATP (By similarity).
FT COILED 221 311 Potential.
FT COILED 492 519 Potential.
FT MOTIF 702 705 DEAH box.
FT COMPBIAS 10 53 Ala-rich.
FT COMPBIAS 789 793 Poly-Glu.
FT MOD_RES 71 71 Phosphoserine.
FT MOD_RES 192 192 Phosphoserine.
FT MOD_RES 200 200 Phosphoserine.
FT VARIANT 309 309 D -> A (in dbSNP:rs35874395).
FT /FTId=VAR_052180.
FT VARIANT 630 630 P -> H (in dbSNP:rs17854904).
FT /FTId=VAR_026985.
FT CONFLICT 121 121 A -> D (in Ref. 3; CAH56172).
FT CONFLICT 185 185 K -> E (in Ref. 3; CAH56153).
FT CONFLICT 356 356 D -> G (in Ref. 1; AAK64516).
FT CONFLICT 885 885 D -> G (in Ref. 3; CAH56172).
SQ SEQUENCE 1369 AA; 155236 MW; F720A77D224C7F59 CRC64;
MGGKNKKHKA PAAAVVRAAV SASRAKSAEA GIAGEAQSKK PVSRPATAAA AAAGSREPRV
KQGPKIYSFN STNDSSGPAN LDKSILKVVI NNKLEQRIIG VINEHKKQNN DKGMISGRLT
AKKLQDLYMA LQAFSFKTKD IEDAMTNTLL YGGDLHSALD WLCLNLSDDA LPEGFSQEFE
EQQPKSRPKF QSPQIQATIS PPLQPKTKTY EEDPKSKPKK EEKNMEVNMK EWILRYAEQQ
NEEEKNENSK SLEEEEKFDP NERYLHLAAK LLDAKEQAAT FKLEKNKQGQ KEAQEKIRKF
QREMETLEDH PVFNPAMKIS HQQNERKKPP VATEGESALN FNLFEKSAAA TEEEKDKKKE
PHDVRNFDYT ARSWTGKSPK QFLIDWVRKN LPKSPNPSFE KVPVGRYWKC RVRVIKSEDD
VLVVCPTILT EDGMQAQHLG ATLALYRLVK GQSVHQLLPP TYRDVWLEWS DAEKKREELN
KMETNKPRDL FIAKLLNKLK QQQQQQQQHS ENKRENSEDP EESWENLVSD EDFSALSLES
ANVEDLEPVR NLFRKLQSTP KYQKLLKERQ QLPVFKHRDS IVETLKRHRV VVVAGETGSG
KSTQVPHFLL EDLLLNEWEA SKCNIVCTQP RRISAVSLAN RVCDELGCEN GPGGRNSLCG
YQIRMESRAC ESTRLLYCTT GVLLRKLQED GLLSNVSHVI VDEVHERSVQ SDFLLIILKE
ILQKRSDLHL ILMSATVDSE KFSTYFTHCP ILRISGRSYP VEVFHLEDII EETGFVLEKD
SEYCQKFLEE EEEVTINVTS KAGGIKKYQE YIPVQTGAHA DLNPFYQKYS SRTQHAILYM
NPHKINLDLI LELLAYLDKS PQFRNIEGAV LIFLPGLAHI QQLYDLLSND RRFYSERYKV
IALHSILSTQ DQAAAFTLPP PGVRKIVLAT NIAETGITIP DVVFVIDTGR TKENKYHESS
QMSSLVETFV SKASALQRQG RAGRVRDGFC FRMYTRERFE GFMDYSVPEI LRVPLEELCL
HIMKCNLGSP EDFLSKALDP PQLQVISNAM NLLRKIGACE LNEPKLTPLG QHLAALPVNV
KIGKMLIFGA IFGCLDPVAT LAAVMTEKSP FTTPIGRKDE ADLAKSALAM ADSDHLTIYN
AYLGWKKARQ EGGYRSEITY CRRNFLNRTS LLTLEDVKQE LIKLVKAAGF SSSTTSTSWE
GNRASQTLSF QEIALLKAVL VAGLYDNVGK IIYTKSVDVT EKLACIVETA QGKAQVHPSS
VNRDLQTHGW LLYQEKIRYA RVYLRETTLI TPFPVLLFGG DIEVQHRERL LSIDGWIYFQ
APVKIAVIFK QLRVLIDSVL RKKLENPKMS LENDKILQII TELIKTENN
//
ID DHX29_HUMAN Reviewed; 1369 AA.
AC Q7Z478; O75549; Q63HN0; Q63HN3; Q8IWW2; Q8N3A1; Q9UMH2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JUL-2006, sequence version 2.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=ATP-dependent RNA helicase DHX29;
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 29;
DE AltName: Full=Nucleic acid helicase DDXx;
GN Name=DHX29; Synonyms=DDX29;
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].
RA Abdelhaleem M.M.;
RT "Identification of a new member of the DDx subfamily of helicases.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-630.
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-1369.
RC TISSUE=Amygdala, Fetal kidney, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 561-1369.
RA Bassi M.T., Banfi S., Riboni M., Ballabio A., Borsani G.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1119-1369.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-200, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP FUNCTION, RIBOSOME-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19109895; DOI=10.1016/j.cell.2008.10.037;
RA Pisareva V.P., Pisarev A.V., Komar A.A., Hellen C.U.T., Pestova T.V.;
RT "Translation initiation on mammalian mRNAs with structured 5'UTRs
RT requires DExH-box protein DHX29.";
RL Cell 135:1237-1250(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-200, AND
RP MASS SPECTROMETRY.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-200, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASS
RP 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 [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.6 ANGSTROMS) IN COMPLEX WITH THE
RP 43S PRE-INITIATION COMPLEX, FUNCTION, AND SUBUNIT.
RX PubMed=23706745; DOI=10.1016/j.cell.2013.04.036;
RA Hashem Y., des Georges A., Dhote V., Langlois R., Liao H.Y.,
RA Grassucci R.A., Hellen C.U., Pestova T.V., Frank J.;
RT "Structure of the mammalian ribosomal 43S preinitiation complex bound
RT to the scanning factor DHX29.";
RL Cell 153:1108-1119(2013).
CC -!- FUNCTION: ATP-binding RNA helicase involved in translation
CC initiation. Part of the 43S pre-initiation complex that is
CC required for efficient initiation on mammalian mRNAs with
CC structured 5'-UTRs by promoting efficient NTPase-dependent 48S
CC complex formation. Specifically binds to the 40S ribosome near the
CC mRNA entrance. Does not possess a processive helicase activity.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Part of the 43S pre-initiation complex that contains at
CC least Met-tRNA, EIF1, EIF1A (EIF1AX or EIF1AY), EIF2S1, EIF2S2,
CC EIF2S3, EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H,
CC EIF3I, EIF3J, EIF3K, EIF3L, EIF3M, DHX29 and the 40S ribosomal
CC subunit.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC 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; AY036974; AAK64516.1; -; mRNA.
DR EMBL; BC056219; AAH56219.1; -; mRNA.
DR EMBL; AL834496; CAD39154.1; -; mRNA.
DR EMBL; BX648101; CAH56172.1; -; mRNA.
DR EMBL; BX648269; CAH56153.1; -; mRNA.
DR EMBL; AL079292; CAB45191.1; -; mRNA.
DR EMBL; AF070639; AAC25394.1; -; mRNA.
DR RefSeq; NP_061903.2; NM_019030.2.
DR UniGene; Hs.593268; -.
DR ProteinModelPortal; Q7Z478; -.
DR SMR; Q7Z478; 520-754, 868-1292.
DR IntAct; Q7Z478; 3.
DR MINT; MINT-1376685; -.
DR STRING; 9606.ENSP00000251636; -.
DR PhosphoSite; Q7Z478; -.
DR DMDM; 110278938; -.
DR PaxDb; Q7Z478; -.
DR PeptideAtlas; Q7Z478; -.
DR PRIDE; Q7Z478; -.
DR Ensembl; ENST00000251636; ENSP00000251636; ENSG00000067248.
DR GeneID; 54505; -.
DR KEGG; hsa:54505; -.
DR UCSC; uc003jpx.3; human.
DR CTD; 54505; -.
DR GeneCards; GC05M054552; -.
DR H-InvDB; HIX0004866; -.
DR HGNC; HGNC:15815; DHX29.
DR HPA; HPA038317; -.
DR HPA; HPA038318; -.
DR MIM; 612720; gene.
DR neXtProt; NX_Q7Z478; -.
DR PharmGKB; PA27215; -.
DR eggNOG; COG1643; -.
DR HOGENOM; HOG000247063; -.
DR HOVERGEN; HBG081436; -.
DR InParanoid; Q7Z478; -.
DR OMA; WLLYQEK; -.
DR OrthoDB; EOG7SV0TS; -.
DR PhylomeDB; Q7Z478; -.
DR ChiTaRS; DHX29; human.
DR GenomeRNAi; 54505; -.
DR NextBio; 56869; -.
DR PRO; PR:Q7Z478; -.
DR Bgee; Q7Z478; -.
DR CleanEx; HS_DHX29; -.
DR Genevestigator; Q7Z478; -.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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 ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Helicase;
KW Hydrolase; Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Protein biosynthesis; Reference proteome.
FT CHAIN 1 1369 ATP-dependent RNA helicase DHX29.
FT /FTId=PRO_0000245535.
FT DOMAIN 582 755 Helicase ATP-binding.
FT DOMAIN 849 1026 Helicase C-terminal.
FT NP_BIND 595 602 ATP (By similarity).
FT COILED 221 311 Potential.
FT COILED 492 519 Potential.
FT MOTIF 702 705 DEAH box.
FT COMPBIAS 10 53 Ala-rich.
FT COMPBIAS 789 793 Poly-Glu.
FT MOD_RES 71 71 Phosphoserine.
FT MOD_RES 192 192 Phosphoserine.
FT MOD_RES 200 200 Phosphoserine.
FT VARIANT 309 309 D -> A (in dbSNP:rs35874395).
FT /FTId=VAR_052180.
FT VARIANT 630 630 P -> H (in dbSNP:rs17854904).
FT /FTId=VAR_026985.
FT CONFLICT 121 121 A -> D (in Ref. 3; CAH56172).
FT CONFLICT 185 185 K -> E (in Ref. 3; CAH56153).
FT CONFLICT 356 356 D -> G (in Ref. 1; AAK64516).
FT CONFLICT 885 885 D -> G (in Ref. 3; CAH56172).
SQ SEQUENCE 1369 AA; 155236 MW; F720A77D224C7F59 CRC64;
MGGKNKKHKA PAAAVVRAAV SASRAKSAEA GIAGEAQSKK PVSRPATAAA AAAGSREPRV
KQGPKIYSFN STNDSSGPAN LDKSILKVVI NNKLEQRIIG VINEHKKQNN DKGMISGRLT
AKKLQDLYMA LQAFSFKTKD IEDAMTNTLL YGGDLHSALD WLCLNLSDDA LPEGFSQEFE
EQQPKSRPKF QSPQIQATIS PPLQPKTKTY EEDPKSKPKK EEKNMEVNMK EWILRYAEQQ
NEEEKNENSK SLEEEEKFDP NERYLHLAAK LLDAKEQAAT FKLEKNKQGQ KEAQEKIRKF
QREMETLEDH PVFNPAMKIS HQQNERKKPP VATEGESALN FNLFEKSAAA TEEEKDKKKE
PHDVRNFDYT ARSWTGKSPK QFLIDWVRKN LPKSPNPSFE KVPVGRYWKC RVRVIKSEDD
VLVVCPTILT EDGMQAQHLG ATLALYRLVK GQSVHQLLPP TYRDVWLEWS DAEKKREELN
KMETNKPRDL FIAKLLNKLK QQQQQQQQHS ENKRENSEDP EESWENLVSD EDFSALSLES
ANVEDLEPVR NLFRKLQSTP KYQKLLKERQ QLPVFKHRDS IVETLKRHRV VVVAGETGSG
KSTQVPHFLL EDLLLNEWEA SKCNIVCTQP RRISAVSLAN RVCDELGCEN GPGGRNSLCG
YQIRMESRAC ESTRLLYCTT GVLLRKLQED GLLSNVSHVI VDEVHERSVQ SDFLLIILKE
ILQKRSDLHL ILMSATVDSE KFSTYFTHCP ILRISGRSYP VEVFHLEDII EETGFVLEKD
SEYCQKFLEE EEEVTINVTS KAGGIKKYQE YIPVQTGAHA DLNPFYQKYS SRTQHAILYM
NPHKINLDLI LELLAYLDKS PQFRNIEGAV LIFLPGLAHI QQLYDLLSND RRFYSERYKV
IALHSILSTQ DQAAAFTLPP PGVRKIVLAT NIAETGITIP DVVFVIDTGR TKENKYHESS
QMSSLVETFV SKASALQRQG RAGRVRDGFC FRMYTRERFE GFMDYSVPEI LRVPLEELCL
HIMKCNLGSP EDFLSKALDP PQLQVISNAM NLLRKIGACE LNEPKLTPLG QHLAALPVNV
KIGKMLIFGA IFGCLDPVAT LAAVMTEKSP FTTPIGRKDE ADLAKSALAM ADSDHLTIYN
AYLGWKKARQ EGGYRSEITY CRRNFLNRTS LLTLEDVKQE LIKLVKAAGF SSSTTSTSWE
GNRASQTLSF QEIALLKAVL VAGLYDNVGK IIYTKSVDVT EKLACIVETA QGKAQVHPSS
VNRDLQTHGW LLYQEKIRYA RVYLRETTLI TPFPVLLFGG DIEVQHRERL LSIDGWIYFQ
APVKIAVIFK QLRVLIDSVL RKKLENPKMS LENDKILQII TELIKTENN
//
MIM
612720
*RECORD*
*FIELD* NO
612720
*FIELD* TI
*612720 DEAH BOX POLYPEPTIDE 29; DHX29
*FIELD* TX
CLONING
Pisareva et al. (2008) purified Dhx29 from rabbit reticulocyte lysate
read moreand identified human DHX29 by database analysis. The deduced 1,369-amino
acid human DHX29 protein contains a central DEAH box helicase domain and
C-terminal helicase-associated HA2 and DUF1605 domains.
GENE FUNCTION
The 43S preinitiation complex containing 40S ribosomal subunits EIF3
(see 602039), EIF2 (see 603907), EIF1, EIF1A (EIF1AX; 300186), and
initiator tRNA (see 180620) binds to and scans 5-prime UTRs of mRNAs to
identify the initiation codon, where it stops to form the 48S initiation
complex. Scanning of unstructured 5-prime UTRs does not require ATP or
factors associated with ATP hydrolysis and RNA unwinding, whereas
scanning of 5-prime UTRs with even weak secondary structure requires ATP
and EIF4A (see 602641), EIF4G (see 600495), and EIF4B (603928). Pisareva
et al. (2008) showed that rabbit Dhx29 was also required for efficient
scanning of 5-prime UTRs with stable secondary structures. The extent of
the requirement for Dhx29 correlated with the degree of stability in the
secondary structure. Dhx29 bound 40S ribosomal subunits and hydrolyzed
ATP, GTP, UTP, and CTP. NTPase activity of Dhx29 was strongly stimulated
by 43S complexes, and Dhx29 stimulated 48S complex formation most
strongly when it was present in substoichiometric amounts relative to
43S complexes. Rabbit Dhx29 did not show processive helicase activity.
MAPPING
Hartz (2009) mapped the DHX29 gene to chromosome 5q11.2 based on an
alignment of the DHX29 gene (GenBank GENBANK AL079292) with the genomic
sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/1/2009.
2. Pisareva, V. P.; Pisarev, A. V.; Komar, A. A.; Hellen, C. U. T.;
Pestova, T. V.: Translation initiation on mammalian mRNAs with structured
5-prime UTRs requires DExH-box protein DHX29. Cell 135: 1237-1250,
2008.
*FIELD* CD
Patricia A. Hartz: 4/7/2009
*FIELD* ED
alopez: 10/03/2013
mgross: 4/7/2009
*RECORD*
*FIELD* NO
612720
*FIELD* TI
*612720 DEAH BOX POLYPEPTIDE 29; DHX29
*FIELD* TX
CLONING
Pisareva et al. (2008) purified Dhx29 from rabbit reticulocyte lysate
read moreand identified human DHX29 by database analysis. The deduced 1,369-amino
acid human DHX29 protein contains a central DEAH box helicase domain and
C-terminal helicase-associated HA2 and DUF1605 domains.
GENE FUNCTION
The 43S preinitiation complex containing 40S ribosomal subunits EIF3
(see 602039), EIF2 (see 603907), EIF1, EIF1A (EIF1AX; 300186), and
initiator tRNA (see 180620) binds to and scans 5-prime UTRs of mRNAs to
identify the initiation codon, where it stops to form the 48S initiation
complex. Scanning of unstructured 5-prime UTRs does not require ATP or
factors associated with ATP hydrolysis and RNA unwinding, whereas
scanning of 5-prime UTRs with even weak secondary structure requires ATP
and EIF4A (see 602641), EIF4G (see 600495), and EIF4B (603928). Pisareva
et al. (2008) showed that rabbit Dhx29 was also required for efficient
scanning of 5-prime UTRs with stable secondary structures. The extent of
the requirement for Dhx29 correlated with the degree of stability in the
secondary structure. Dhx29 bound 40S ribosomal subunits and hydrolyzed
ATP, GTP, UTP, and CTP. NTPase activity of Dhx29 was strongly stimulated
by 43S complexes, and Dhx29 stimulated 48S complex formation most
strongly when it was present in substoichiometric amounts relative to
43S complexes. Rabbit Dhx29 did not show processive helicase activity.
MAPPING
Hartz (2009) mapped the DHX29 gene to chromosome 5q11.2 based on an
alignment of the DHX29 gene (GenBank GENBANK AL079292) with the genomic
sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/1/2009.
2. Pisareva, V. P.; Pisarev, A. V.; Komar, A. A.; Hellen, C. U. T.;
Pestova, T. V.: Translation initiation on mammalian mRNAs with structured
5-prime UTRs requires DExH-box protein DHX29. Cell 135: 1237-1250,
2008.
*FIELD* CD
Patricia A. Hartz: 4/7/2009
*FIELD* ED
alopez: 10/03/2013
mgross: 4/7/2009