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 29-SEP-2021, entry version 165. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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 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 SMR; Q7Z478; -. DR BioGRID; 120001; 58. DR IntAct; Q7Z478; 23. 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; 93 antibodies. DR DNASU; 54505; -. DR Ensembl; ENST00000251636; ENSP00000251636; ENSG00000067248. DR GeneID; 54505; -. DR KEGG; hsa:54505; -. 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; WGASKCN; -. DR OrthoDB; 278674at2759; -. DR PhylomeDB; Q7Z478; -. DR TreeFam; TF324744; -. DR PathwayCommons; Q7Z478; -. DR BioGRID-ORCS; 54505; 105 hits in 1033 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 female gonad and 246 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:0140603; 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; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR034730; DHX29. 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; 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 NP_BIND 595..602 FT /note="ATP" 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 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 //