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Database: UniProt
Entry: Q9UMS4
LinkDB: Q9UMS4
Original site: Q9UMS4 
ID   PRP19_HUMAN             Reviewed;         504 AA.
AC   Q9UMS4;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   29-SEP-2021, entry version 193.
DE   RecName: Full=Pre-mRNA-processing factor 19 {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000269|PubMed:11435423};
DE   AltName: Full=Nuclear matrix protein 200 {ECO:0000303|PubMed:11082287};
DE   AltName: Full=PRP19/PSO4 homolog {ECO:0000303|PubMed:12960389};
DE            Short=hPso4 {ECO:0000303|PubMed:12960389};
DE   AltName: Full=RING-type E3 ubiquitin transferase PRP19 {ECO:0000305};
DE   AltName: Full=Senescence evasion factor {ECO:0000303|PubMed:16332694};
GN   Name=PRPF19 {ECO:0000312|HGNC:HGNC:17896};
GN   Synonyms=NMP200 {ECO:0000303|PubMed:11082287},
GN   PRP19 {ECO:0000303|PubMed:11435423}, SNEV {ECO:0000303|PubMed:16332694};
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], PROTEIN SEQUENCE OF 32-40; 100-115; 179-187;
RP   192-199 AND 334-342, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND CHROMOSOMAL LOCATION.
RC   TISSUE=Cervix;
RX   PubMed=11082287; DOI=10.1006/excr.2000.5025;
RA   Gotzmann J., Gerner C., Meissner M., Holzmann K., Grimm R., Mikulits W.,
RA   Sauermann G.;
RT   "hNMP 200: a novel human common nuclear matrix protein combining structural
RT   and regulatory functions.";
RL   Exp. Cell Res. 261:166-179(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP   INTERACTION WITH DNTT.
RX   PubMed=12960389; DOI=10.1073/pnas.1631060100;
RA   Mahajan K.N., Mitchell B.S.;
RT   "Role of human Pso4 in mammalian DNA repair and association with terminal
RT   deoxynucleotidyl transferase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Muscle;
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   [4]
RP   PROTEIN SEQUENCE OF 2-27; 33-56; 77-93; 101-115; 193-206; 209-236; 252-261
RP   AND 266-303, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RA   Bienvenut W.V., Waridel P., Quadroni M.;
RL   Submitted (MAR-2009) to UniProtKB.
RN   [5]
RP   PROTEIN SEQUENCE OF 2-27; 33-56; 63-93; 101-115; 193-206; 209-261; 266-303;
RP   344-375 AND 429-439, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP   SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Ovarian carcinoma;
RA   Bienvenut W.V.;
RL   Submitted (JAN-2010) to UniProtKB.
RN   [6]
RP   PROTEIN SEQUENCE OF 32-40, AND TISSUE SPECIFICITY.
RC   TISSUE=Peripheral blood;
RX   PubMed=10404385;
RX   DOI=10.1002/(sici)1097-4644(19990801)74:2<145::aid-jcb1>3.0.co;2-#;
RA   Gerner C., Holzmann K., Meissner M., Gotzmann J., Grimm R., Sauermann G.;
RT   "Reassembling proteins and chaperones in human nuclear matrix protein
RT   fractions.";
RL   J. Cell. Biochem. 74:145-151(1999).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11435423; DOI=10.1074/jbc.m102755200;
RA   Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.;
RT   "U box proteins as a new family of ubiquitin-protein ligases.";
RL   J. Biol. Chem. 276:33111-33120(2001).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA   Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA   Greco A., Hochstrasser D.F., Diaz J.-J.;
RT   "Functional proteomic analysis of human nucleolus.";
RL   Mol. Biol. Cell 13:4100-4109(2002).
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   FUNCTION, AND SUBUNIT.
RX   PubMed=16332694; DOI=10.1093/nar/gki986;
RA   Grillari J., Ajuh P., Stadler G., Loescher M., Voglauer R., Ernst W.,
RA   Chusainow J., Eisenhaber F., Pokar M., Fortschegger K., Grey M.,
RA   Lamond A.I., Katinger H.;
RT   "SNEV is an evolutionarily conserved splicing factor whose oligomerization
RT   is necessary for spliceosome assembly.";
RL   Nucleic Acids Res. 33:6868-6883(2005).
RN   [11]
RP   INTERACTION WITH PSMB4, AND FUNCTION.
RX   PubMed=15660529; DOI=10.1042/bj20041517;
RA   Loescher M., Fortschegger K., Ritter G., Wostry M., Voglauer R.,
RA   Schmid J.A., Watters S., Rivett A.J., Ajuh P., Lamond A.I., Katinger H.,
RA   Grillari J.;
RT   "Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the
RT   20 S proteasome.";
RL   Biochem. J. 388:593-603(2005).
RN   [12]
RP   FUNCTION, AND IDENTIFICATION AS A COMPONENT OF THE PSO4 COMPLEX.
RX   PubMed=16223718; DOI=10.1074/jbc.m508453200;
RA   Zhang N., Kaur R., Lu X., Shen X., Li L., Legerski R.J.;
RT   "The Pso4 mRNA splicing and DNA repair complex interacts with WRN for
RT   processing of DNA interstrand cross-links.";
RL   J. Biol. Chem. 280:40559-40567(2005).
RN   [13]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16388800; DOI=10.1016/j.yexcr.2005.11.025;
RA   Voglauer R., Chang M.W.-F., Dampier B., Wieser M., Baumann K.,
RA   Sterovsky T., Schreiber M., Katinger H., Grillari J.;
RT   "SNEV overexpression extends the life span of human endothelial cells.";
RL   Exp. Cell Res. 312:746-759(2006).
RN   [14]
RP   FUNCTION.
RX   PubMed=17349974; DOI=10.1016/j.bbrc.2007.02.134;
RA   Sihn C.R., Cho S.Y., Lee J.H., Lee T.R., Kim S.H.;
RT   "Mouse homologue of yeast Prp19 interacts with mouse SUG1, the regulatory
RT   subunit of 26S proteasome.";
RL   Biochem. Biophys. Res. Commun. 356:175-180(2007).
RN   [15]
RP   FUNCTION, AND IDENTIFICATION AS PART OF THE XAB2 COMPLEX.
RX   PubMed=17981804; DOI=10.1074/jbc.m706647200;
RA   Kuraoka I., Ito S., Wada T., Hayashida M., Lee L., Saijo M., Nakatsu Y.,
RA   Matsumoto M., Matsunaga T., Handa H., Qin J., Nakatani Y., Tanaka K.;
RT   "Isolation of XAB2 complex involved in pre-mRNA splicing, transcription,
RT   and transcription-coupled repair.";
RL   J. Biol. Chem. 283:940-950(2008).
RN   [16]
RP   FUNCTION, INTERACTION WITH SETMAR, AND SUBCELLULAR LOCATION.
RX   PubMed=18263876; DOI=10.1074/jbc.m800150200;
RA   Beck B.D., Park S.J., Lee Y.J., Roman Y., Hromas R.A., Lee S.H.;
RT   "Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase
RT   function in DNA repair.";
RL   J. Biol. Chem. 283:9023-9030(2008).
RN   [17]
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   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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   [19]
RP   SUBUNIT, AND INTERACTION WITH KHDC4.
RX   PubMed=19641227; DOI=10.1074/jbc.m109.036632;
RA   Grillari J., Loescher M., Denegri M., Lee K., Fortschegger K.,
RA   Eisenhaber F., Ajuh P., Lamond A.I., Katinger H., Grillari-Voglauer R.;
RT   "Blom7alpha is a novel heterogeneous nuclear ribonucleoprotein K homology
RT   domain protein involved in pre-mRNA splicing that interacts with SNEVPrp19-
RT   Pso4.";
RL   J. Biol. Chem. 284:29193-29204(2009).
RN   [20]
RP   INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=19188445; DOI=10.1128/mcb.01337-08;
RA   Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M.,
RA   Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A.,
RA   Quadrifoglio F., Tell G.;
RT   "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the
RT   rRNA quality control process.";
RL   Mol. Cell. Biol. 29:1834-1854(2009).
RN   [21]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122 AND LYS-261, AND
RP   IDENTIFICATION BY MASS 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   [22]
RP   FUNCTION, AND INTERACTION WITH PRPF3.
RX   PubMed=20595234; DOI=10.1101/gad.1925010;
RA   Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D.,
RA   Harper J.W., Elledge S.J., Kirschner M.W., Rape M.;
RT   "The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control
RT   reversible ubiquitination at the spliceosome.";
RL   Genes Dev. 24:1434-1447(2010).
RN   [23]
RP   IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX,
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH CDC5L; PLRG1 AND BCAS2.
RX   PubMed=20176811; DOI=10.1128/mcb.01505-09;
RA   Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A.,
RA   Fischle W., Urlaub H., Luhrmann R.;
RT   "Molecular architecture of the human Prp19/CDC5L complex.";
RL   Mol. Cell. Biol. 30:2105-2119(2010).
RN   [24]
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   [25]
RP   FUNCTION, AND INTERACTION WITH U2AF2.
RX   PubMed=21536736; DOI=10.1101/gad.2038011;
RA   David C.J., Boyne A.R., Millhouse S.R., Manley J.L.;
RT   "The RNA polymerase II C-terminal domain promotes splicing activation
RT   through recruitment of a U2AF65-Prp19 complex.";
RL   Genes Dev. 25:972-983(2011).
RN   [26]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [27]
RP   INTERACTION WITH CWC22 AND EIF4A3.
RX   PubMed=22961380; DOI=10.1038/nsmb.2380;
RA   Barbosa I., Haque N., Fiorini F., Barrandon C., Tomasetto C.,
RA   Blanchette M., Le Hir H.;
RT   "Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes
RT   exon junction complex assembly.";
RL   Nat. Struct. Mol. Biol. 19:983-990(2012).
RN   [28]
RP   FUNCTION, INTERACTION WITH RPA1 AND RPA2, DOMAIN, AND MUTAGENESIS OF
RP   TYR-405.
RX   PubMed=24332808; DOI=10.1016/j.molcel.2013.11.002;
RA   Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D., Liu S.,
RA   Jimenez A.E., Jin J., Zou L.;
RT   "PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives
RT   ATR activation via a ubiquitin-mediated circuitry.";
RL   Mol. Cell 53:235-246(2014).
RN   [29]
RP   INTERACTION WITH KNSTRN.
RX   PubMed=24718257; DOI=10.1371/journal.pone.0092712;
RA   Lu S., Wang R., Cai C., Liang J., Xu L., Miao S., Wang L., Song W.;
RT   "Small kinetochore associated protein (SKAP) promotes UV-induced cell
RT   apoptosis through negatively regulating pre-mRNA processing factor 19
RT   (Prp19).";
RL   PLoS ONE 9:E92712-E92712(2014).
RN   [30] {ECO:0007744|PDB:4LG8}
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 169-504.
RX   PubMed=28962858; DOI=10.1016/j.bbrc.2017.09.145;
RA   Zhang Y., Li Y., Liang X., Zhu Z., Sun H., He H., Min J., Liao S., Liu Y.;
RT   "Crystal structure of the WD40 domain of human PRPF19.";
RL   Biochem. Biophys. Res. Commun. 493:1250-1253(2017).
RN   [31] {ECO:0007744|PDB:5XJC}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA   Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT   "An Atomic Structure of the Human Spliceosome.";
RL   Cell 169:918-929(2017).
RN   [32] {ECO:0007744|PDB:5MQF}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=28076346; DOI=10.1038/nature21079;
RA   Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA   Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT   "Cryo-EM structure of a human spliceosome activated for step 2 of
RT   splicing.";
RL   Nature 542:318-323(2017).
RN   [33] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.10 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=29360106; DOI=10.1038/cr.2018.14;
RA   Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.;
RT   "Structure of the human activated spliceosome in three conformational
RT   states.";
RL   Cell Res. 28:307-322(2018).
RN   [34] {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).
RN   [35] {ECO:0007744|PDB:6QDV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=30705154; DOI=10.1126/science.aaw5569;
RA   Fica S.M., Oubridge C., Wilkinson M.E., Newman A.J., Nagai K.;
RT   "A human postcatalytic spliceosome structure reveals essential roles of
RT   metazoan factors for exon ligation.";
RL   Science 363:710-714(2019).
CC   -!- FUNCTION: Ubiquitin-protein ligase which is a core component of several
CC       complexes mainly involved pre-mRNA splicing and DNA repair. Required
CC       for pre-mRNA splicing as component of the spliceosome (PubMed:28502770,
CC       PubMed:28076346, PubMed:29360106, PubMed:29301961, PubMed:30705154).
CC       Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which
CC       is part of the spliceosome and participates in its assembly, its
CC       remodeling and is required for its activity. During assembly of the
CC       spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4
CC       spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its
CC       recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri-
CC       snRNP spliceosomal complex (PubMed:20595234). Recruited to RNA
CC       polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also
CC       couple the transcriptional and spliceosomal machineries
CC       (PubMed:21536736). The XAB2 complex, which contains PRPF19, is also
CC       involved in pre-mRNA splicing, transcription and transcription-coupled
CC       repair (PubMed:17981804). Beside its role in pre-mRNA splicing PRPF19,
CC       as part of the PRP19-CDC5L complex, plays a role in the DNA damage
CC       response/DDR. It is recruited to the sites of DNA damage by the RPA
CC       complex where PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'-
CC       linked polyubiquitination of the RPA complex allows the recruitment of
CC       the ATR-ATRIP complex and the activation of ATR, a master regulator of
CC       the DNA damage response (PubMed:24332808). May also play a role in DNA
CC       double-strand break (DSB) repair by recruiting the repair factor SETMAR
CC       to altered DNA (PubMed:18263876). As part of the PSO4 complex may also
CC       be involved in the DNA interstrand cross-links/ICLs repair process
CC       (PubMed:16223718). In addition, may also mediate 'Lys-48'-linked
CC       polyubiquitination of substrates and play a role in proteasomal
CC       degradation (PubMed:11435423). May play a role in the biogenesis of
CC       lipid droplets (By similarity). May play a role in neural
CC       differentiation possibly through its function as part of the
CC       spliceosome (By similarity). {ECO:0000250|UniProtKB:Q99KP6,
CC       ECO:0000250|UniProtKB:Q9JMJ4, ECO:0000269|PubMed:11082287,
CC       ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:12960389,
CC       ECO:0000269|PubMed:15660529, ECO:0000269|PubMed:16223718,
CC       ECO:0000269|PubMed:16332694, ECO:0000269|PubMed:16388800,
CC       ECO:0000269|PubMed:17349974, ECO:0000269|PubMed:18263876,
CC       ECO:0000269|PubMed:21536736, ECO:0000269|PubMed:24332808,
CC       ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC       ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106,
CC       ECO:0000269|PubMed:30705154, ECO:0000303|PubMed:17981804,
CC       ECO:0000303|PubMed:20595234}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000269|PubMed:11435423};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000269|PubMed:11435423}.
CC   -!- SUBUNIT: Homotetramer. Component of activated, catalytic and post-
CC       catalytic spliceosomes (PubMed:28502770, PubMed:28076346,
CC       PubMed:29360106, PubMed:29301961, PubMed:30705154). Component of the
CC       Prp19 complex/PRP19C/Nineteen complex/NTC and related complexes
CC       described as PRP19-CDC5L splicing complex and PSO4 complex. A
CC       homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2 constitute the core of
CC       those complexes. The interaction with CDC5L, PLRG1 and BCAS2 is direct
CC       within this core complex. At least three less stably associated
CC       proteins CTNNBL1, CWC15 and HSPA8 are found in the Prp19 complex. The
CC       Prp19 complex associates with the spliceosome during its assembly and
CC       remodeling recruiting additional proteins. Component of the XAB2
CC       complex, a multimeric protein complex composed of XAB2, PRPF19, AQR,
CC       ZNF830, ISY1, and PPIE. Interacts with CWC22 and EIF4A3 in an RNA-
CC       independent manner. Interacts with RPA1 and RPA2; the PRP19-CDC5L
CC       complex is recruited to the sites of DNA repair where it interacts with
CC       the replication protein A complex (RPA). Interacts with SETMAR;
CC       required for SETMAR recruitment to site of DNA damage. Interacts with
CC       U2AF2; the interaction is direct and recruits the Prp19 complex to RNA
CC       polymerase II C-terminal domain (CTD) and the pre-mRNA. Interacts with
CC       PRPF3. Interacts with APEX1, DNTT and PSMB4. Interacts with PSMC5 (By
CC       similarity). Interacts with KNSTRN (PubMed:24718257). Interacts (via N-
CC       terminus) with CDC5L (By similarity). Interacts with KHDC4
CC       (PubMed:19641227). {ECO:0000250|UniProtKB:Q99KP6,
CC       ECO:0000250|UniProtKB:Q9JMJ4, ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:12960389, ECO:0000269|PubMed:15660529,
CC       ECO:0000269|PubMed:16223718, ECO:0000269|PubMed:16332694,
CC       ECO:0000269|PubMed:17981804, ECO:0000269|PubMed:18263876,
CC       ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:19641227,
CC       ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:20595234,
CC       ECO:0000269|PubMed:21536736, ECO:0000269|PubMed:22961380,
CC       ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:24718257,
CC       ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC       ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106,
CC       ECO:0000269|PubMed:30705154}.
CC   -!- INTERACTION:
CC       Q9UMS4; O75934: BCAS2; NbExp=3; IntAct=EBI-395746, EBI-1050106;
CC       Q9UMS4; O60508: CDC40; NbExp=3; IntAct=EBI-395746, EBI-2557812;
CC       Q9UMS4; Q99459: CDC5L; NbExp=3; IntAct=EBI-395746, EBI-374880;
CC       Q9UMS4; Q6P2Q9: PRPF8; NbExp=2; IntAct=EBI-395746, EBI-538479;
CC       Q9UMS4; P98175: RBM10; NbExp=2; IntAct=EBI-395746, EBI-721525;
CC       Q9UMS4; P52756: RBM5; NbExp=8; IntAct=EBI-395746, EBI-714003;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11082287,
CC       ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:19188445,
CC       ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961,
CC       ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30705154}. Nucleus,
CC       nucleoplasm {ECO:0000269|PubMed:11082287}. Cytoplasm, cytoskeleton,
CC       spindle {ECO:0000269|PubMed:11082287}. Cytoplasm
CC       {ECO:0000269|PubMed:11435423}. Lipid droplet
CC       {ECO:0000250|UniProtKB:Q99KP6}. Note=Nucleoplasmic in interphase cells.
CC       Irregularly distributed in anaphase cells. In prophase cells, uniformly
CC       distributed, but not associated with condensing chromosomes. Found in
CC       extrachromosomal regions in metaphase cells. Mainly localized to the
CC       mitotic spindle apparatus when chromosomes segregate during anaphase.
CC       When nuclei reform during late telophase, uniformly distributed in
CC       daughter cells and displays no preferred association with decondensing
CC       chromatin. Recruited on damaged DNA at sites of double-strand break.
CC       {ECO:0000269|PubMed:11082287, ECO:0000269|PubMed:18263876}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Weakly expressed in senescent cells of
CC       different tissue origins. Highly expressed in tumor cell lines.
CC       {ECO:0000269|PubMed:10404385, ECO:0000269|PubMed:11082287,
CC       ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:12960389,
CC       ECO:0000269|PubMed:16388800}.
CC   -!- INDUCTION: By gamma irradiation and chemical mutagens but not by UV
CC       irradiation. {ECO:0000269|PubMed:12960389}.
CC   -!- DOMAIN: The 7 WD repeats are necessary and sufficient to support
CC       interaction with the RPA complex. {ECO:0000269|PubMed:24332808}.
CC   -!- SIMILARITY: Belongs to the WD repeat PRP19 family. {ECO:0000305}.
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DR   EMBL; AJ131186; CAB51857.1; -; mRNA.
DR   EMBL; BC008719; AAH08719.1; -; mRNA.
DR   EMBL; BC018665; AAH18665.1; -; mRNA.
DR   EMBL; BC018698; AAH18698.1; -; mRNA.
DR   CCDS; CCDS7995.1; -.
DR   RefSeq; NP_055317.1; NM_014502.4.
DR   PDB; 4LG8; X-ray; 1.89 A; A=169-504.
DR   PDB; 5MQF; EM; 5.90 A; G/H/I/J=1-504.
DR   PDB; 5XJC; EM; 3.60 A; q/r/s/t=1-504.
DR   PDB; 5YZG; EM; 4.10 A; q/r/s/t=1-504.
DR   PDB; 5Z56; EM; 5.10 A; q/r/s/t=1-504.
DR   PDB; 5Z57; EM; 6.50 A; q/r/s/t=1-504.
DR   PDB; 6FF7; EM; 4.50 A; G/H/I/J=1-504.
DR   PDB; 6ICZ; EM; 3.00 A; q/r/s/t=1-504.
DR   PDB; 6ID0; EM; 2.90 A; q/r/s/t=1-504.
DR   PDB; 6ID1; EM; 2.86 A; q/r/s/t=1-504.
DR   PDB; 6QDV; EM; 3.30 A; t/u/v/w=1-504.
DR   PDB; 7A5P; EM; 5.00 A; G/H/I/J=1-504.
DR   PDBsum; 4LG8; -.
DR   PDBsum; 5MQF; -.
DR   PDBsum; 5XJC; -.
DR   PDBsum; 5YZG; -.
DR   PDBsum; 5Z56; -.
DR   PDBsum; 5Z57; -.
DR   PDBsum; 6FF7; -.
DR   PDBsum; 6ICZ; -.
DR   PDBsum; 6ID0; -.
DR   PDBsum; 6ID1; -.
DR   PDBsum; 6QDV; -.
DR   PDBsum; 7A5P; -.
DR   SMR; Q9UMS4; -.
DR   BioGRID; 118151; 298.
DR   ComplexPortal; CPX-5824; PRP19-CDC5L complex.
DR   CORUM; Q9UMS4; -.
DR   DIP; DIP-32978N; -.
DR   IntAct; Q9UMS4; 104.
DR   MINT; Q9UMS4; -.
DR   STRING; 9606.ENSP00000227524; -.
DR   MoonDB; Q9UMS4; Predicted.
DR   GlyGen; Q9UMS4; 7 sites, 2 O-linked glycans (7 sites).
DR   iPTMnet; Q9UMS4; -.
DR   MetOSite; Q9UMS4; -.
DR   PhosphoSitePlus; Q9UMS4; -.
DR   SwissPalm; Q9UMS4; -.
DR   BioMuta; PRPF19; -.
DR   DMDM; 55976619; -.
DR   REPRODUCTION-2DPAGE; IPI00004968; -.
DR   SWISS-2DPAGE; Q9UMS4; -.
DR   CPTAC; CPTAC-576; -.
DR   CPTAC; CPTAC-577; -.
DR   EPD; Q9UMS4; -.
DR   jPOST; Q9UMS4; -.
DR   MassIVE; Q9UMS4; -.
DR   MaxQB; Q9UMS4; -.
DR   PaxDb; Q9UMS4; -.
DR   PeptideAtlas; Q9UMS4; -.
DR   PRIDE; Q9UMS4; -.
DR   ProteomicsDB; 85207; -.
DR   Antibodypedia; 3247; 313 antibodies.
DR   DNASU; 27339; -.
DR   Ensembl; ENST00000227524; ENSP00000227524; ENSG00000110107.
DR   GeneID; 27339; -.
DR   KEGG; hsa:27339; -.
DR   UCSC; uc001nqf.4; human.
DR   CTD; 27339; -.
DR   DisGeNET; 27339; -.
DR   GeneCards; PRPF19; -.
DR   HGNC; HGNC:17896; PRPF19.
DR   HPA; ENSG00000110107; Low tissue specificity.
DR   MIM; 608330; gene.
DR   neXtProt; NX_Q9UMS4; -.
DR   OpenTargets; ENSG00000110107; -.
DR   PharmGKB; PA134941355; -.
DR   VEuPathDB; HostDB:ENSG00000110107; -.
DR   eggNOG; KOG0289; Eukaryota.
DR   GeneTree; ENSGT00940000153662; -.
DR   HOGENOM; CLU_023894_1_1_1; -.
DR   InParanoid; Q9UMS4; -.
DR   OMA; QHWAFSD; -.
DR   OrthoDB; 1049599at2759; -.
DR   PhylomeDB; Q9UMS4; -.
DR   TreeFam; TF105919; -.
DR   PathwayCommons; Q9UMS4; -.
DR   Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR   Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR   Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; Q9UMS4; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 27339; 816 hits in 1027 CRISPR screens.
DR   ChiTaRS; PRPF19; human.
DR   GeneWiki; PRPF19; -.
DR   GenomeRNAi; 27339; -.
DR   Pharos; Q9UMS4; Tbio.
DR   PRO; PR:Q9UMS4; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9UMS4; protein.
DR   Bgee; ENSG00000110107; Expressed in frontal cortex and 241 other tissues.
DR   ExpressionAtlas; Q9UMS4; baseline and differential.
DR   Genevisible; Q9UMS4; HS.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000974; C:Prp19 complex; IDA:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
DR   GO; GO:0034613; P:cellular protein localization; IMP:UniProtKB.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:UniProtKB.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
DR   GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IBA:GO_Central.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:0048711; P:positive regulation of astrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IMP:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IMP:BHF-UCL.
DR   GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:UniProtKB.
DR   DisProt; DP01161; -.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR013915; Pre-mRNA_splic_Prp19.
DR   InterPro; IPR038959; Prp19.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR43995; PTHR43995; 1.
DR   Pfam; PF08606; Prp19; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00504; Ubox; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS51698; U_BOX; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; DNA damage; DNA repair; Lipid droplet;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW   Spliceosome; Transferase; Ubl conjugation pathway; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.4, ECO:0000269|Ref.5,
FT                   ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895"
FT   CHAIN           2..504
FT                   /note="Pre-mRNA-processing factor 19"
FT                   /id="PRO_0000051145"
FT   DOMAIN          2..73
FT                   /note="U-box"
FT   REPEAT          219..259
FT                   /note="WD 1"
FT   REPEAT          262..301
FT                   /note="WD 2"
FT   REPEAT          304..345
FT                   /note="WD 3"
FT   REPEAT          348..387
FT                   /note="WD 4"
FT   REPEAT          390..429
FT                   /note="WD 5"
FT   REPEAT          433..472
FT                   /note="WD 6"
FT   REPEAT          473..503
FT                   /note="WD 7"
FT   REGION          68..223
FT                   /note="May mediate interaction with PSMC5"
FT                   /evidence="ECO:0000250|UniProtKB:Q99KP6"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|Ref.4, ECO:0000269|Ref.5,
FT                   ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895"
FT   MOD_RES         122
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         179
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99KP6"
FT   MOD_RES         244
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99KP6"
FT   MOD_RES         261
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MUTAGEN         405
FT                   /note="Y->A: Loss of interaction with the RPA complex and
FT                   loss of recruitment to sites of DNA damage."
FT                   /evidence="ECO:0000269|PubMed:24332808"
FT   TURN            6..8
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          13..17
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           27..36
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   HELIX           70..74
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           76..132
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   HELIX           201..204
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          208..213
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          219..221
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          224..230
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          233..241
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          246..250
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   TURN            251..254
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          255..260
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          269..272
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          276..282
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          288..292
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   TURN            293..296
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          297..302
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          309..314
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          318..325
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          328..334
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   TURN            335..337
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          340..345
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   TURN            347..349
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          353..358
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          362..369
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          374..378
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   TURN            379..382
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          383..388
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          395..400
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          404..411
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          414..420
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   TURN            421..424
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          425..431
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          438..443
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          447..461
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   TURN            462..465
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          466..471
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          474..476
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          478..483
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   HELIX           485..487
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          490..494
FT                   /evidence="ECO:0007829|PDB:4LG8"
FT   STRAND          499..503
FT                   /evidence="ECO:0007829|PDB:4LG8"
SQ   SEQUENCE   504 AA;  55181 MW;  B34C37496E8AA032 CRC64;
     MSLICSISNE VPEHPCVSPV SNHVYERRLI EKYIAENGTD PINNQPLSEE QLIDIKVAHP
     IRPKPPSATS IPAILKALQD EWDAVMLHSF TLRQQLQTTR QELSHALYQH DAACRVIARL
     TKEVTAAREA LATLKPQAGL IVPQAVPSSQ PSVVGAGEPM DLGELVGMTP EIIQKLQDKA
     TVLTTERKKR GKTVPEELVK PEELSKYRQV ASHVGLHSAS IPGILALDLC PSDTNKILTG
     GADKNVVVFD KSSEQILATL KGHTKKVTSV VFHPSQDLVF SASPDATIRI WSVPNASCVQ
     VVRAHESAVT GLSLHATGDY LLSSSDDQYW AFSDIQTGRV LTKVTDETSG CSLTCAQFHP
     DGLIFGTGTM DSQIKIWDLK ERTNVANFPG HSGPITSIAF SENGYYLATA ADDSSVKLWD
     LRKLKNFKTL QLDNNFEVKS LIFDQSGTYL ALGGTDVQIY ICKQWTEILH FTEHSGLTTG
     VAFGHHAKFI ASTGMDRSLK FYSL
//
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