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 29-MAY-2024, entry version 216. 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}; 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; 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. 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 EMDB; EMD-11569; -. DR EMDB; EMD-6864; -. DR SMR; Q92620; -. DR BioGRID; 115129; 172. DR CORUM; Q92620; -. DR IntAct; Q92620; 38. DR MINT; Q92620; -. DR STRING; 9606.ENSP00000268482; -. DR GlyGen; Q92620; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000268482; -. DR PeptideAtlas; Q92620; -. DR ProteomicsDB; 5268; -. DR ProteomicsDB; 75373; -. [Q92620-1] DR Pumba; Q92620; -. DR Antibodypedia; 16682; 165 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 AGR; HGNC:17211; -. 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; VDVMFHR; -. DR OrthoDB; 5488182at2759; -. 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; 406 hits in 1171 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 168 other cell types or tissues. DR ExpressionAtlas; Q92620; baseline and differential. 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:0034458; F:3'-5' RNA helicase activity; 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; TAS:Reactome. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR CDD; cd17983; DEXHc_DHX38; 1. DR CDD; cd18791; SF2_C_RHA; 1. DR Gene3D; 1.20.120.1080; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR048333; HA2_WH. DR InterPro; IPR007502; Helicase-assoc_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C-like. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1. DR PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF21010; HA2_C; 1. DR Pfam; PF04408; HA2_N; 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; P-loop containing nucleoside triphosphate hydrolases; 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; uncertain 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 //