PRP19_MOUSE
ID PRP19_MOUSE Reviewed; 504 AA.
AC Q99KP6; Q3TP64; Q4ADG5; Q8BKZ5; Q8BVQ4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Pre-mRNA-processing factor 19 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9UMS4};
DE AltName: Full=Nuclear matrix protein 200 {ECO:0000303|Ref.2};
DE AltName: Full=PRP19/PSO4 homolog;
DE AltName: Full=RING-type E3 ubiquitin transferase PRP19 {ECO:0000305};
DE AltName: Full=Senescence evasion factor {ECO:0000303|Ref.2};
GN Name=Prpf19 {ECO:0000312|MGI:MGI:106247};
GN Synonyms=Prp19, Snev {ECO:0000303|Ref.2};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAE16340.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH PPIA,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ICR {ECO:0000312|EMBL:BAE16340.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAE16340.1};
RX PubMed=16352598; DOI=10.1074/jbc.m510881200;
RA Urano Y., Iiduka M., Sugiyama A., Akiyama H., Uzawa K., Matsumoto G.,
RA Kawasaki Y., Tashiro F.;
RT "Involvement of the mouse Prp19 gene in neuronal/astroglial cell fate
RT decisions.";
RL J. Biol. Chem. 281:7498-7514(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Swiss albino;
RA Grillari J., Gross S., Katinger H.;
RT "Cloning of mSNEV, the mouse homologue of the human nuclear matrix protein
RT NMP200.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=129/SvJ;
RA Fortschegger K., Grillari J., Katinger H.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Corpus striatum, Stomach, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [6]
RP FUNCTION, AND INTERACTION WITH PSMC5.
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=17118936; DOI=10.1074/jbc.m608042200;
RA Cho S.Y., Shin E.S., Park P.J., Shin D.W., Chang H.K., Kim D., Lee H.H.,
RA Lee J.H., Kim S.H., Song M.J., Chang I.S., Lee O.S., Lee T.R.;
RT "Identification of mouse Prp19p as a lipid droplet-associated protein and
RT its possible involvement in the biogenesis of lipid droplets.";
RL J. Biol. Chem. 282:2456-2465(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: [Isoform 1]: Ubiquitin-protein ligase which is a core
CC component of several complexes mainly involved in pre-mRNA splicing and
CC DNA repair. Required for pre-mRNA splicing as component of the
CC spliceosome. Core component of the PRP19C/Prp19 complex/NTC/Nineteen
CC complex which is part of the spliceosome and participates in its
CC assembly, its remodeling and is required for its activity. During
CC assembly of the spliceosome, mediates 'Lys-63'-linked
CC polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination
CC of PRPF3 allows its recognition by the U5 component PRPF8 and
CC stabilizes the U4/U5/U6 tri-snRNP spliceosomal complex. Recruited to
CC RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also
CC couple the transcriptional and spliceosomal machineries. The XAB2
CC complex, which contains PRPF19, is also involved in pre-mRNA splicing,
CC transcription and transcription-coupled repair. Beside its role in pre-
CC mRNA splicing PRPF19, as part of the PRP19-CDC5L complex, plays a role
CC in the DNA damage response/DDR. It is recruited to the sites of DNA
CC damage by the RPA complex where PRPF19 directly ubiquitinates RPA1 and
CC RPA2. 'Lys-63'-linked polyubiquitination of the RPA complex allows the
CC recruitment of the ATR-ATRIP complex and the activation of ATR, a
CC master regulator of the DNA damage response. May also play a role in
CC DNA double-strand break (DSB) repair by recruiting the repair factor
CC SETMAR to altered DNA. As part of the PSO4 complex may also be involved
CC in the DNA interstrand cross-links/ICLs repair process. In addition,
CC may also mediate 'Lys-48'-linked polyubiquitination of substrates and
CC play a role in proteasomal degradation (PubMed:17349974). May play a
CC role in the biogenesis of lipid droplets (PubMed:17118936). May play a
CC role in neural differentiation possibly through its function as part of
CC the spliceosome (By similarity). {ECO:0000250|UniProtKB:Q9JMJ4,
CC ECO:0000250|UniProtKB:Q9UMS4, ECO:0000269|PubMed:17118936,
CC ECO:0000269|PubMed:17349974}.
CC -!- FUNCTION: [Isoform 2]: Forced expression leads to suppression of
CC neuronal differentiation, and on the contrary to stimulation of
CC astroglial cell differentiation in retinoic acid-primed P19 cells
CC (PubMed:16352598). {ECO:0000269|PubMed:16352598}.
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:0000250|UniProtKB:Q9UMS4};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9UMS4}.
CC -!- SUBUNIT: Homotetramer. Component of activated, catalytic and post-
CC catalytic spliceosomes. Component of the Prp19 complex/PRP19C/Nineteen
CC complex/NTC and related complexes described as PRP19-CDC5L splicing
CC complex and PSO4 complex. A homotetramer of PRPF19, CDC5L, PLRG1 and
CC BCAS2 constitute the core of those complexes. The interaction with
CC CDC5L, PLRG1 and BCAS2 is direct within this core complex. At least
CC three less stably associated proteins CTNNBL1, CWC15 and HSPA8 are
CC found in the Prp19 complex. The Prp19 complex associates with the
CC spliceosome during its assembly and remodeling recruiting additional
CC proteins. Component of the XAB2 complex, a multimeric protein complex
CC composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Interacts with
CC CWC22 and EIF4A3 in an RNA-independent manner. Interacts with RPA1 and
CC RPA2; the PRP19-CDC5L complex is recruited to the sites of DNA repair
CC where it interacts with the replication protein A complex (RPA).
CC Interacts with SETMAR; required for SETMAR recruitment to site of DNA
CC damage. Interacts with U2AF2; the interaction is direct and recruits
CC the Prp19 complex to RNA polymerase II C-terminal domain (CTD) and the
CC pre-mRNA. Interacts with PRPF3. Interacts with APEX1, DNTT and PSMB4.
CC Interacts with KNSTRN (By similarity). Interacts with PSMC5
CC (PubMed:17349974). Isoform 2 (via N-terminus) interacts with PPIA.
CC Isoform 2 does not interact with CDC5L (PubMed:16352598). Interacts
CC with KHDC4 (By similarity). Interacts with USB1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UMS4, ECO:0000269|PubMed:16352598,
CC ECO:0000269|PubMed:17349974}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:16352598}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9UMS4}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9UMS4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UMS4}. Lipid droplet
CC {ECO:0000269|PubMed:17118936}. 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 (By
CC similarity). {ECO:0000250|UniProtKB:Q9UMS4}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:16352598}. Nucleus {ECO:0000269|PubMed:16352598}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99KP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99KP6-2; Sequence=VSP_011945;
CC Name=3;
CC IsoId=Q99KP6-3; Sequence=VSP_012192;
CC -!- TISSUE SPECIFICITY: Expressed in white and brown adipose tissues, brain
CC and to a lower extent in liver, kidney, muscle, lung and spleen (at
CC protein level). {ECO:0000269|PubMed:17118936}.
CC -!- INDUCTION: Up-regulated in differentiating adipocytes
CC (PubMed:17118936). Isoform 2 maximal expression level during the neural
CC differentiation of P19 cells treated with retinoic acid (RA) is
CC estimated to be 2.5-fold of the expression level of the untreated cells
CC and it is detected 1-2 days after RA treatment and it decreases steeply
CC thereafter to the basal level. Isoform 2 expression level increases
CC steeply after 1 day of RA treatment and is estimated to be 4.2-fold of
CC the original level at 0 hours (PubMed:16352598).
CC {ECO:0000269|PubMed:16352598, ECO:0000269|PubMed:17118936}.
CC -!- DOMAIN: The 7 WD repeats are necessary and sufficient to support
CC interaction with the RPA complex. {ECO:0000250|UniProtKB:Q9UMS4}.
CC -!- SIMILARITY: Belongs to the WD repeat PRP19 family. {ECO:0000305}.
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DR EMBL; AB222602; BAE16340.1; -; mRNA.
DR EMBL; AF251503; AAK49039.1; -; mRNA.
DR EMBL; AF386760; AAM21468.1; -; Genomic_DNA.
DR EMBL; AK047693; BAC33127.1; -; mRNA.
DR EMBL; AK076998; BAC36557.1; -; mRNA.
DR EMBL; AK088769; BAC40560.1; -; mRNA.
DR EMBL; AK164681; BAE37873.1; -; mRNA.
DR EMBL; BC004070; AAH04070.1; -; mRNA.
DR CCDS; CCDS57135.1; -. [Q99KP6-2]
DR CCDS; CCDS79687.1; -. [Q99KP6-1]
DR RefSeq; NP_001240772.1; NM_001253843.1. [Q99KP6-2]
DR RefSeq; NP_001240773.1; NM_001253844.1. [Q99KP6-3]
DR RefSeq; NP_598890.1; NM_134129.4. [Q99KP6-1]
DR AlphaFoldDB; Q99KP6; -.
DR SMR; Q99KP6; -.
DR BioGRID; 205709; 57.
DR ComplexPortal; CPX-5825; PRP19-CDC5L complex.
DR IntAct; Q99KP6; 8.
DR MINT; Q99KP6; -.
DR STRING; 10090.ENSMUSP00000136858; -.
DR iPTMnet; Q99KP6; -.
DR PhosphoSitePlus; Q99KP6; -.
DR SwissPalm; Q99KP6; -.
DR REPRODUCTION-2DPAGE; Q99KP6; -.
DR EPD; Q99KP6; -.
DR jPOST; Q99KP6; -.
DR MaxQB; Q99KP6; -.
DR PaxDb; Q99KP6; -.
DR PeptideAtlas; Q99KP6; -.
DR PRIDE; Q99KP6; -.
DR ProteomicsDB; 291890; -. [Q99KP6-1]
DR ProteomicsDB; 291891; -. [Q99KP6-2]
DR ProteomicsDB; 291892; -. [Q99KP6-3]
DR Antibodypedia; 3247; 319 antibodies from 34 providers.
DR DNASU; 28000; -.
DR Ensembl; ENSMUST00000025642; ENSMUSP00000025642; ENSMUSG00000024735. [Q99KP6-1]
DR Ensembl; ENSMUST00000179297; ENSMUSP00000136858; ENSMUSG00000024735. [Q99KP6-2]
DR GeneID; 28000; -.
DR KEGG; mmu:28000; -.
DR UCSC; uc008grf.2; mouse. [Q99KP6-1]
DR UCSC; uc008grg.2; mouse. [Q99KP6-2]
DR CTD; 27339; -.
DR MGI; MGI:106247; Prpf19.
DR VEuPathDB; HostDB:ENSMUSG00000024735; -.
DR eggNOG; KOG0289; Eukaryota.
DR GeneTree; ENSGT00940000153662; -.
DR HOGENOM; CLU_023894_1_1_1; -.
DR InParanoid; Q99KP6; -.
DR OMA; VTRVIYH; -.
DR OrthoDB; 1049599at2759; -.
DR PhylomeDB; Q99KP6; -.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 28000; 41 hits in 116 CRISPR screens.
DR ChiTaRS; Prpf19; mouse.
DR PRO; PR:Q99KP6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q99KP6; protein.
DR Bgee; ENSMUSG00000024735; Expressed in floor plate of midbrain and 256 other tissues.
DR Genevisible; Q99KP6; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005662; C:DNA replication factor A complex; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISO:MGI.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0008610; P:lipid biosynthetic process; IDA:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISO:MGI.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI.
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; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0000245; P:spliceosomal complex assembly; ISO:MGI.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:UniProtKB.
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 Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA repair; Lipid droplet; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Spliceosome; Transferase;
KW Ubl conjugation pathway; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS4"
FT CHAIN 2..504
FT /note="Pre-mRNA-processing factor 19"
FT /id="PRO_0000051146"
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:0000269|PubMed:17349974"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS4"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS4"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 244
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 261
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS4"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012192"
FT VAR_SEQ 82
FT /note="W -> WGWPNSPALPQSSQWPTLSQ (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:16352598,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011945"
SQ SEQUENCE 504 AA; 55239 MW; B2918188A0651024 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 KSTEQILATL KGHTKKVTSV VFHPSQELVF SASPDATIRI WSVPNTSCVQ
VVRAHESAVT GLSLHATGDY LLSSSDDQYW AFSDIQTGRV LTKVTDETSG CSLTCAQFHP
DGLIFGTGTM DSQIKIWDLK ERTNVANFPG HSGPITSIAF SENGYYLATA ADDSSVKLWD
LRKLKNFKTL QLDNNFEVKS LIFDQSGTYL ALGGTDVQIY ICKQWTEILH FTEHSGLTTG
VAFGHHAKFI ASTGMDRSLK FYSL
