PRP16_HUMAN
ID PRP16_HUMAN Reviewed; 1227 AA.
AC Q92620; B4DVG8; D3DWS7; O75212; Q96HN7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase DHX38;
DE AltName: Full=DEAH box protein 38;
GN Name=DHX38; Synonyms=DDX38, KIAA0224, PRP16;
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] (ISOFORM 1), FUNCTION, AND VARIANT ALA-1217.
RX PubMed=9524131; DOI=10.1093/emboj/17.7.2095;
RA Zhou Z., Reed R.;
RT "Human homologs of yeast prp16 and prp17 reveal conservation of the
RT mechanism for catalytic step II of pre-mRNA splicing.";
RL EMBO J. 17:2095-2106(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-1217.
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
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 [8]
RP PROTEIN SEQUENCE OF 2-12 AND 692-707, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT GLY-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1194, AND IDENTIFICATION BY
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-260, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; THR-117 AND SER-224, AND
RP IDENTIFICATION BY 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 [16]
RP INVOLVEMENT IN RP84, AND VARIANT RP84 ASP-332.
RX PubMed=24737827; DOI=10.1136/jmedgenet-2014-102316;
RA Ajmal M., Khan M.I., Neveling K., Khan Y.M., Azam M., Waheed N.K.,
RA Hamel C.P., Ben-Yosef T., De Baere E., Koenekoop R.K., Collin R.W.,
RA Qamar R., Cremers F.P.;
RT "A missense mutation in the splicing factor gene DHX38 is associated with
RT early-onset retinitis pigmentosa with macular coloboma.";
RL J. Med. Genet. 51:444-448(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-482, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-482; LYS-483; LYS-504 AND
RP LYS-1166, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [19]
RP INVOLVEMENT IN RP84, AND VARIANT RP84 GLN-324.
RX PubMed=30208423; DOI=10.1167/iovs.18-23849;
RG University of Washington Center for Mendelian Genomics (UWCMG) Study Group;
RA Latif Z., Chakchouk I., Schrauwen I., Lee K., Santos-Cortez R.L.P.,
RA Abbe I., Acharya A., Jarral A., Ali I., Ullah E., Khan M.N., Ali G.,
RA Tahir T.H., Bamshad M.J., Nickerson D.A., Ahmad W., Ansar M., Leal S.M.;
RT "Confirmation of the role of DHX38 in the etiology of early-onset retinitis
RT pigmentosa.";
RL Invest. Ophthalmol. Vis. Sci. 59:4552-4557(2018).
RN [20] {ECO:0007744|PDB:5YZG}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=29301961; DOI=10.1126/science.aar6401;
RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.;
RT "Structure of a human catalytic step I spliceosome.";
RL Science 359:537-545(2018).
CC -!- FUNCTION: Probable ATP-binding RNA helicase (Probable). Involved in
CC pre-mRNA splicing as component of the spliceosome (PubMed:29301961,
CC PubMed:9524131). {ECO:0000269|PubMed:29301961,
CC ECO:0000269|PubMed:9524131, ECO:0000305}.
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 -!- SUBUNIT: Identified in the spliceosome C complex.
CC {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:29301961}.
CC -!- INTERACTION:
CC Q92620; O60231: DHX16; NbExp=2; IntAct=EBI-1043041, EBI-311446;
CC Q92620; Q92917: GPKOW; NbExp=2; IntAct=EBI-1043041, EBI-746309;
CC Q92620; Q96RS6: NUDCD1; NbExp=2; IntAct=EBI-1043041, EBI-2512429;
CC Q92620; P98175: RBM10; NbExp=2; IntAct=EBI-1043041, EBI-721525;
CC Q92620; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-1043041, EBI-750109;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29301961}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92620-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92620-2; Sequence=VSP_056045;
CC -!- DISEASE: Retinitis pigmentosa 84 (RP84) [MIM:618220]: A form of
CC retinitis pigmentosa, a retinal dystrophy belonging to the group of
CC pigmentary retinopathies. Retinitis pigmentosa is characterized by
CC retinal pigment deposits visible on fundus examination and primary loss
CC of rod photoreceptor cells followed by secondary loss of cone
CC photoreceptors. Patients typically have night vision blindness and loss
CC of midperipheral visual field. As their condition progresses, they lose
CC their far peripheral visual field and eventually central vision as
CC well. RP84 is an autosomal recessive, early onset form characterized by
CC night blindness by age 4 and complete blindness by age 8. Funduscopy
CC shows severely attenuated retinal vessels, severe macular atrophy, and
CC prominent and deep macular colobomas lacking neuroretinal tissue.
CC {ECO:0000269|PubMed:24737827, ECO:0000269|PubMed:30208423}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13213.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF038391; AAC39729.1; -; mRNA.
DR EMBL; D86977; BAA13213.2; ALT_INIT; mRNA.
DR EMBL; AK301074; BAG62680.1; -; mRNA.
DR EMBL; AC009087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004682; AAC27431.1; -; Genomic_DNA.
DR EMBL; CH471166; EAW59180.1; -; Genomic_DNA.
DR EMBL; CH471166; EAW59190.1; -; Genomic_DNA.
DR EMBL; BC004235; AAH04235.1; -; mRNA.
DR EMBL; BC008340; AAH08340.1; -; mRNA.
DR CCDS; CCDS10907.1; -. [Q92620-1]
DR RefSeq; NP_054722.2; NM_014003.3. [Q92620-1]
DR RefSeq; XP_011521786.1; XM_011523484.1. [Q92620-1]
DR RefSeq; XP_011521787.1; XM_011523485.1. [Q92620-1]
DR PDB; 5YZG; EM; 4.10 A; Z=1-1227.
DR PDB; 6ZYM; EM; 3.40 A; r=1-1227.
DR PDB; 7A5P; EM; 5.00 A; r=1-1227.
DR PDBsum; 5YZG; -.
DR PDBsum; 6ZYM; -.
DR PDBsum; 7A5P; -.
DR AlphaFoldDB; Q92620; -.
DR BMRB; Q92620; -.
DR SMR; Q92620; -.
DR BioGRID; 115129; 133.
DR CORUM; Q92620; -.
DR IntAct; Q92620; 36.
DR MINT; Q92620; -.
DR STRING; 9606.ENSP00000268482; -.
DR GlyGen; Q92620; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92620; -.
DR MetOSite; Q92620; -.
DR PhosphoSitePlus; Q92620; -.
DR BioMuta; DHX38; -.
DR DMDM; 85700389; -.
DR EPD; Q92620; -.
DR jPOST; Q92620; -.
DR MassIVE; Q92620; -.
DR MaxQB; Q92620; -.
DR PaxDb; Q92620; -.
DR PeptideAtlas; Q92620; -.
DR PRIDE; Q92620; -.
DR ProteomicsDB; 5268; -.
DR ProteomicsDB; 75373; -. [Q92620-1]
DR Antibodypedia; 16682; 145 antibodies from 27 providers.
DR DNASU; 9785; -.
DR Ensembl; ENST00000268482.8; ENSP00000268482.3; ENSG00000140829.12. [Q92620-1]
DR GeneID; 9785; -.
DR KEGG; hsa:9785; -.
DR MANE-Select; ENST00000268482.8; ENSP00000268482.3; NM_014003.4; NP_054722.2.
DR UCSC; uc002fcb.4; human. [Q92620-1]
DR CTD; 9785; -.
DR DisGeNET; 9785; -.
DR GeneCards; DHX38; -.
DR HGNC; HGNC:17211; DHX38.
DR HPA; ENSG00000140829; Low tissue specificity.
DR MalaCards; DHX38; -.
DR MIM; 605584; gene.
DR MIM; 618220; phenotype.
DR neXtProt; NX_Q92620; -.
DR OpenTargets; ENSG00000140829; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA27225; -.
DR VEuPathDB; HostDB:ENSG00000140829; -.
DR eggNOG; KOG0924; Eukaryota.
DR GeneTree; ENSGT00940000156898; -.
DR HOGENOM; CLU_001832_6_2_1; -.
DR InParanoid; Q92620; -.
DR OMA; VMFHRSP; -.
DR OrthoDB; 354219at2759; -.
DR PhylomeDB; Q92620; -.
DR TreeFam; TF105793; -.
DR PathwayCommons; Q92620; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q92620; -.
DR BioGRID-ORCS; 9785; 384 hits in 1088 CRISPR screens.
DR ChiTaRS; DHX38; human.
DR GeneWiki; DHX38; -.
DR GenomeRNAi; 9785; -.
DR Pharos; Q92620; Tbio.
DR PRO; PR:Q92620; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q92620; protein.
DR Bgee; ENSG00000140829; Expressed in sural nerve and 166 other tissues.
DR ExpressionAtlas; Q92620; baseline and differential.
DR Genevisible; Q92620; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Direct protein sequencing; Disease variant; Helicase; Hydrolase;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Retinitis pigmentosa;
KW Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330"
FT CHAIN 2..1227
FT /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase
FT PRP16"
FT /id="PRO_0000055147"
FT DOMAIN 542..705
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 727..902
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 60..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 652..655
FT /note="DEAH box"
FT COMPBIAS 60..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 555..562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 260
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 482
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 483
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 504
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 99..786
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056045"
FT VARIANT 324
FT /note="R -> Q (in RP84; dbSNP:rs766053952)"
FT /evidence="ECO:0000269|PubMed:30208423"
FT /id="VAR_081338"
FT VARIANT 332
FT /note="G -> D (in RP84; unknown pathological significance;
FT dbSNP:rs587777554)"
FT /evidence="ECO:0000269|PubMed:24737827"
FT /id="VAR_081339"
FT VARIANT 1217
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:9039502,
FT ECO:0000269|PubMed:9524131"
FT /id="VAR_015518"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:6ZYM"
FT HELIX 371..384
FT /evidence="ECO:0007829|PDB:6ZYM"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:6ZYM"
SQ SEQUENCE 1227 AA; 140503 MW; 80D06118D0D465E5 CRC64;
MGDTSEDASI HRLEGTDLDC QVGGLICKSK SAASEQHVFK APAPRPSLLG LDLLASLKRR
EREEKDDGED KKKSKVSSYK DWEESKDDQK DAEEEGGDQA GQNIRKDRHY RSARVETPSH
PGGVSEEFWE RSRQRERERR EHGVYASSKE EKDWKKEKSR DRDYDRKRDR DERDRSRHSS
RSERDGGSER SSRRNEPESP RHRPKDAATP SRSTWEEEDS GYGSSRRSQW ESPSPTPSYR
DSERSHRLST RDRDRSVRGK YSDDTPLPTP SYKYNEWADD RRHLGSTPRL SRGRGRREEG
EEGISFDTEE ERQQWEDDQR QADRDWYMMD EGYDEFHNPL AYSSEDYVRR REQHLHKQKQ
KRISAQRRQI NEDNERWETN RMLTSGVVHR LEVDEDFEED NAAKVHLMVH NLVPPFLDGR
IVFTKQPEPV IPVKDATSDL AIIARKGSQT VRKHREQKER KKAQHKHWEL AGTKLGDIMG
VKKEEEPDKA VTEDGKVDYR TEQKFADHMK RKSEASSEFA KKKSILEQRQ YLPIFAVQQE
LLTIIRDNSI VIVVGETGSG KTTQLTQYLH EDGYTDYGMI GCTQPRRVAA MSVAKRVSEE
MGGNLGEEVG YAIRFEDCTS ENTLIKYMTD GILLRESLRE ADLDHYSAII MDEAHERSLN
TDVLFGLLRE VVARRSDLKL IVTSATMDAE KFAAFFGNVP IFHIPGRTFP VDILFSKTPQ
EDYVEAAVKQ SLQVHLSGAP GDILIFMPGQ EDIEVTSDQI VEHLEELENA PALAVLPIYS
QLPSDLQAKI FQKAPDGVRK CIVATNIAET SLTVDGIMFV IDSGYCKLKV FNPRIGMDAL
QIYPISQANA NQRSGRAGRT GPGQCFRLYT QSAYKNELLT TTVPEIQRTN LANVVLLLKS
LGVQDLLQFH FMDPPPEDNM LNSMYQLWIL GALDNTGGLT STGRLMVEFP LDPALSKMLI
VSCDMGCSSE ILLIVSMLSV PAIFYRPKGR EEESDQIREK FAVPESDHLT YLNVYLQWKN
NNYSTIWCND HFIHAKAMRK VREVRAQLKD IMVQQRMSLA SCGTDWDIVR KCICAAYFHQ
AAKLKGIGEY VNIRTGMPCH LHPTSSLFGM GYTPDYIVYH ELVMTTKEYM QCVTAVDGEW
LAELGPMFYS VKQAGKSRQE NRRRAKEEAS AMEEEMALAE EQLRARRQEQ EKRSPLGSVR
STKIYTPGRK EQGEPMTPRR TPARFGL
