DHX29_HUMAN
ID DHX29_HUMAN Reviewed; 1369 AA.
AC Q7Z478; O75549; Q63HN0; Q63HN3; Q8IWW2; Q8N3A1; Q9UMH2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=ATP-dependent RNA helicase DHX29 {ECO:0000255|HAMAP-Rule:MF_03068};
DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_03068};
DE AltName: Full=DEAH box protein 29 {ECO:0000255|HAMAP-Rule:MF_03068};
DE AltName: Full=Nucleic acid helicase DDXx;
GN Name=DHX29 {ECO:0000255|HAMAP-Rule:MF_03068}; Synonyms=DDX29;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 project:
RT 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphorylation
RT 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 requires
RT 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 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 [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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT 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
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.6 ANGSTROMS) IN COMPLEX WITH THE 43S
RP 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 to
RT the scanning factor DHX29.";
RL Cell 153:1108-1119(2013).
CC -!- FUNCTION: ATP-binding RNA helicase involved in translation initiation.
CC Part of the 43S pre-initiation complex that is required for efficient
CC initiation on mRNAs of higher eukaryotes with structured 5'-UTRs by
CC promoting efficient NTPase-dependent 48S complex formation.
CC Specifically binds to the 40S ribosome near the mRNA entrance. Does not
CC possess a processive helicase activity. {ECO:0000255|HAMAP-
CC Rule:MF_03068, ECO:0000269|PubMed:19109895,
CC ECO:0000269|PubMed:23706745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03068};
CC -!- SUBUNIT: Part of the 43S pre-initiation complex (PIC) that contains at
CC least Met-tRNA, EIF1, EIF1A (EIF1AX or EIF1AY), EIF2S1, EIF2S2, EIF2S3,
CC EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J,
CC EIF3K, EIF3L, EIF3M, DHX29 and the 40S ribosomal subunit.
CC {ECO:0000255|HAMAP-Rule:MF_03068, ECO:0000269|PubMed:23706745}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03068}.
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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 CCDS; CCDS34158.1; -.
DR RefSeq; NP_001332893.1; NM_001345964.1.
DR RefSeq; NP_001332894.1; NM_001345965.1.
DR RefSeq; NP_061903.2; NM_019030.3.
DR AlphaFoldDB; Q7Z478; -.
DR SMR; Q7Z478; -.
DR BioGRID; 120001; 124.
DR IntAct; Q7Z478; 28.
DR MINT; Q7Z478; -.
DR STRING; 9606.ENSP00000251636; -.
DR BindingDB; Q7Z478; -.
DR ChEMBL; CHEMBL4105909; -.
DR GlyGen; Q7Z478; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z478; -.
DR PhosphoSitePlus; Q7Z478; -.
DR BioMuta; DHX29; -.
DR DMDM; 110278938; -.
DR EPD; Q7Z478; -.
DR jPOST; Q7Z478; -.
DR MassIVE; Q7Z478; -.
DR MaxQB; Q7Z478; -.
DR PaxDb; Q7Z478; -.
DR PeptideAtlas; Q7Z478; -.
DR PRIDE; Q7Z478; -.
DR ProteomicsDB; 69161; -.
DR Antibodypedia; 11081; 95 antibodies from 21 providers.
DR DNASU; 54505; -.
DR Ensembl; ENST00000251636.10; ENSP00000251636.5; ENSG00000067248.11.
DR GeneID; 54505; -.
DR KEGG; hsa:54505; -.
DR MANE-Select; ENST00000251636.10; ENSP00000251636.5; NM_019030.4; NP_061903.2.
DR UCSC; uc003jpx.4; human.
DR CTD; 54505; -.
DR DisGeNET; 54505; -.
DR GeneCards; DHX29; -.
DR HGNC; HGNC:15815; DHX29.
DR HPA; ENSG00000067248; Low tissue specificity.
DR MIM; 612720; gene.
DR neXtProt; NX_Q7Z478; -.
DR OpenTargets; ENSG00000067248; -.
DR PharmGKB; PA27215; -.
DR VEuPathDB; HostDB:ENSG00000067248; -.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000157286; -.
DR HOGENOM; CLU_001832_1_4_1; -.
DR InParanoid; Q7Z478; -.
DR OMA; HQQNEKK; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; Q7Z478; -.
DR TreeFam; TF324744; -.
DR PathwayCommons; Q7Z478; -.
DR SignaLink; Q7Z478; -.
DR BioGRID-ORCS; 54505; 112 hits in 1096 CRISPR screens.
DR ChiTaRS; DHX29; human.
DR GenomeRNAi; 54505; -.
DR Pharos; Q7Z478; Tbio.
DR PRO; PR:Q7Z478; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q7Z478; protein.
DR Bgee; ENSG00000067248; Expressed in esophagus squamous epithelium and 212 other tissues.
DR ExpressionAtlas; Q7Z478; baseline and differential.
DR Genevisible; Q7Z478; HS.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:CACAO.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IMP:CACAO.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008494; F:translation activator activity; IMP:CACAO.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IMP:CACAO.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0042255; P:ribosome assembly; IMP:CACAO.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_03068; DHX29; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR034730; DHX29.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; 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 ATP-binding; Coiled coil; Cytoplasm; Helicase; Hydrolase;
KW Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..1369
FT /note="ATP-dependent RNA helicase DHX29"
FT /id="PRO_0000245535"
FT DOMAIN 582..755
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT DOMAIN 849..1026
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT REGION 27..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 222..256
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT COILED 283..310
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT COILED 492..519
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT MOTIF 702..705
FT /note="DEAH box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT COMPBIAS 186..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 595..602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VARIANT 309
FT /note="D -> A (in dbSNP:rs35874395)"
FT /id="VAR_052180"
FT VARIANT 630
FT /note="P -> H (in dbSNP:rs17854904)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026985"
FT CONFLICT 121
FT /note="A -> D (in Ref. 3; CAH56172)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="K -> E (in Ref. 3; CAH56153)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="D -> G (in Ref. 1; AAK64516)"
FT /evidence="ECO:0000305"
FT CONFLICT 885
FT /note="D -> G (in Ref. 3; CAH56172)"
FT /evidence="ECO:0000305"
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
