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Pre-mRNA-processing factor 19 (EC 2.3.2.27) (Nuclear matrix protein 200) (PRP19/PSO4 homolog) (hPso4) (RING-type E3 ubiquitin transferase PRP19) (Senescence evasion factor)

 PRP19_HUMAN             Reviewed;         504 AA.
Q9UMS4;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 161.
RecName: Full=Pre-mRNA-processing factor 19 {ECO:0000305};
EC=2.3.2.27 {ECO:0000269|PubMed:11435423};
AltName: Full=Nuclear matrix protein 200 {ECO:0000303|PubMed:11082287};
AltName: Full=PRP19/PSO4 homolog {ECO:0000303|PubMed:12960389};
Short=hPso4 {ECO:0000303|PubMed:12960389};
AltName: Full=RING-type E3 ubiquitin transferase PRP19 {ECO:0000305};
AltName: Full=Senescence evasion factor {ECO:0000303|PubMed:16332694};
Name=PRPF19 {ECO:0000312|HGNC:HGNC:17896};
Synonyms=NMP200 {ECO:0000303|PubMed:11082287},
PRP19 {ECO:0000303|PubMed:11435423},
SNEV {ECO:0000303|PubMed:16332694};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-40; 100-115;
179-187; 192-199 AND 334-342, FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND CHROMOSOMAL LOCATION.
TISSUE=Cervix;
PubMed=11082287; DOI=10.1006/excr.2000.5025;
Gotzmann J., Gerner C., Meissner M., Holzmann K., Grimm R.,
Mikulits W., Sauermann G.;
"hNMP 200: a novel human common nuclear matrix protein combining
structural and regulatory functions.";
Exp. Cell Res. 261:166-179(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION,
AND INTERACTION WITH DNTT.
PubMed=12960389; DOI=10.1073/pnas.1631060100;
Mahajan K.N., Mitchell B.S.;
"Role of human Pso4 in mammalian DNA repair and association with
terminal deoxynucleotidyl transferase.";
Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-27; 33-56; 77-93; 101-115; 193-206; 209-236;
252-261 AND 266-303, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 2-27; 33-56; 63-93; 101-115; 193-206; 209-261;
266-303; 344-375 AND 429-439, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V.;
Submitted (JAN-2010) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 32-40, AND TISSUE SPECIFICITY.
TISSUE=Peripheral blood;
PubMed=10404385;
DOI=10.1002/(SICI)1097-4644(19990801)74:2<145::AID-JCB1>3.3.CO;2-R;
Gerner C., Holzmann K., Meissner M., Gotzmann J., Grimm R.,
Sauermann G.;
"Reassembling proteins and chaperones in human nuclear matrix protein
fractions.";
J. Cell. Biochem. 74:145-151(1999).
[7]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=11435423; DOI=10.1074/jbc.M102755200;
Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.;
"U box proteins as a new family of ubiquitin-protein ligases.";
J. Biol. Chem. 276:33111-33120(2001).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[10]
FUNCTION, AND SUBUNIT.
PubMed=16332694; DOI=10.1093/nar/gki986;
Grillari J., Ajuh P., Stadler G., Loescher M., Voglauer R., Ernst W.,
Chusainow J., Eisenhaber F., Pokar M., Fortschegger K., Grey M.,
Lamond A.I., Katinger H.;
"SNEV is an evolutionarily conserved splicing factor whose
oligomerization is necessary for spliceosome assembly.";
Nucleic Acids Res. 33:6868-6883(2005).
[11]
INTERACTION WITH PSMB4, AND FUNCTION.
PubMed=15660529; DOI=10.1042/BJ20041517;
Loescher M., Fortschegger K., Ritter G., Wostry M., Voglauer R.,
Schmid J.A., Watters S., Rivett A.J., Ajuh P., Lamond A.I.,
Katinger H., Grillari J.;
"Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of
the 20 S proteasome.";
Biochem. J. 388:593-603(2005).
[12]
FUNCTION, AND IDENTIFICATION AS A COMPONENT OF THE PSO4 COMPLEX.
PubMed=16223718; DOI=10.1074/jbc.M508453200;
Zhang N., Kaur R., Lu X., Shen X., Li L., Legerski R.J.;
"The Pso4 mRNA splicing and DNA repair complex interacts with WRN for
processing of DNA interstrand cross-links.";
J. Biol. Chem. 280:40559-40567(2005).
[13]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16388800; DOI=10.1016/j.yexcr.2005.11.025;
Voglauer R., Chang M.W.-F., Dampier B., Wieser M., Baumann K.,
Sterovsky T., Schreiber M., Katinger H., Grillari J.;
"SNEV overexpression extends the life span of human endothelial
cells.";
Exp. Cell Res. 312:746-759(2006).
[14]
FUNCTION.
PubMed=17349974; DOI=10.1016/j.bbrc.2007.02.134;
Sihn C.R., Cho S.Y., Lee J.H., Lee T.R., Kim S.H.;
"Mouse homologue of yeast Prp19 interacts with mouse SUG1, the
regulatory subunit of 26S proteasome.";
Biochem. Biophys. Res. Commun. 356:175-180(2007).
[15]
FUNCTION, AND IDENTIFICATION AS PART OF THE XAB2 COMPLEX.
PubMed=17981804; DOI=10.1074/jbc.M706647200;
Kuraoka I., Ito S., Wada T., Hayashida M., Lee L., Saijo M.,
Nakatsu Y., Matsumoto M., Matsunaga T., Handa H., Qin J., Nakatani Y.,
Tanaka K.;
"Isolation of XAB2 complex involved in pre-mRNA splicing,
transcription, and transcription-coupled repair.";
J. Biol. Chem. 283:940-950(2008).
[16]
FUNCTION, INTERACTION WITH SETMAR, AND SUBCELLULAR LOCATION.
PubMed=18263876; DOI=10.1074/jbc.M800150200;
Beck B.D., Park S.J., Lee Y.J., Roman Y., Hromas R.A., Lee S.H.;
"Human Pso4 is a metnase (SETMAR)-binding partner that regulates
metnase function in DNA repair.";
J. Biol. Chem. 283:9023-9030(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
SUBUNIT, AND INTERACTION WITH BLOM7.
PubMed=19641227; DOI=10.1074/jbc.M109.036632;
Grillari J., Loescher M., Denegri M., Lee K., Fortschegger K.,
Eisenhaber F., Ajuh P., Lamond A.I., Katinger H.,
Grillari-Voglauer R.;
"Blom7alpha is a novel heterogeneous nuclear ribonucleoprotein K
homology domain protein involved in pre-mRNA splicing that interacts
with SNEVPrp19-Pso4.";
J. Biol. Chem. 284:29193-29204(2009).
[20]
INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBCELLULAR LOCATION.
PubMed=19188445; DOI=10.1128/MCB.01337-08;
Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M.,
Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A.,
Quadrifoglio F., Tell G.;
"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in
the rRNA quality control process.";
Mol. Cell. Biol. 29:1834-1854(2009).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122 AND LYS-261, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[22]
FUNCTION, AND INTERACTION WITH PRPF3.
PubMed=20595234; DOI=10.1101/gad.1925010;
Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D.,
Harper J.W., Elledge S.J., Kirschner M.W., Rape M.;
"The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control
reversible ubiquitination at the spliceosome.";
Genes Dev. 24:1434-1447(2010).
[23]
IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX,
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
INTERACTION WITH CDC5L; PLRG1 AND BCAS2.
PubMed=20176811; DOI=10.1128/MCB.01505-09;
Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A.,
Fischle W., Urlaub H., Luhrmann R.;
"Molecular architecture of the human Prp19/CDC5L complex.";
Mol. Cell. Biol. 30:2105-2119(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
FUNCTION, AND INTERACTION WITH U2AF2.
PubMed=21536736; DOI=10.1101/gad.2038011;
David C.J., Boyne A.R., Millhouse S.R., Manley J.L.;
"The RNA polymerase II C-terminal domain promotes splicing activation
through recruitment of a U2AF65-Prp19 complex.";
Genes Dev. 25:972-983(2011).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[27]
INTERACTION WITH CWC22 AND EIF4A3.
PubMed=22961380; DOI=10.1038/nsmb.2380;
Barbosa I., Haque N., Fiorini F., Barrandon C., Tomasetto C.,
Blanchette M., Le Hir H.;
"Human CWC22 escorts the helicase eIF4AIII to spliceosomes and
promotes exon junction complex assembly.";
Nat. Struct. Mol. Biol. 19:983-990(2012).
[28]
FUNCTION, INTERACTION WITH RPA1 AND RPA2, DOMAIN, AND MUTAGENESIS OF
TYR-405.
PubMed=24332808; DOI=10.1016/j.molcel.2013.11.002;
Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D.,
Liu S., Jimenez A.E., Jin J., Zou L.;
"PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and
drives ATR activation via a ubiquitin-mediated circuitry.";
Mol. Cell 53:235-246(2014).
[29]
X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 169-504.
Structural genomics consortium (SGC);
"Crystal structure of PRPF19 WD40 repeats.";
Submitted (JUN-2013) to the PDB data bank.
[30]
INTERACTION WITH KNSTRN.
PubMed=24718257; DOI=10.1371/journal.pone.0092712;
Lu S., Wang R., Cai C., Liang J., Xu L., Miao S., Wang L., Song W.;
"Small kinetochore associated protein (SKAP) promotes UV-induced cell
apoptosis through negatively regulating pre-mRNA processing factor 19
(Prp19).";
PLoS ONE 9:E92712-E92712(2014).
-!- FUNCTION: Ubiquitin-protein ligase which is a core component of
several complexes mainly involved pre-mRNA splicing and DNA
repair. Core component of the PRP19C/Prp19 complex/NTC/Nineteen
complex which is part of the spliceosome and participates in its
assembly, its remodeling and is required for its activity. During
assembly of the spliceosome, mediates 'Lys-63'-linked
polyubiquitination of the U4 spliceosomal protein PRPF3.
Ubiquitination of PRPF3 allows its recognition by the U5 component
PRPF8 and stabilizes the U4/U5/U6 tri-snRNP spliceosomal complex
(PubMed:20595234). Recruited to RNA polymerase II C-terminal
domain (CTD) and the pre-mRNA, it may also couple the
transcriptional and spliceosomal machineries (PubMed:21536736).
The XAB2 complex, which contains PRPF19, is also involved in pre-
mRNA splicing, transcription and transcription-coupled repair
(PubMed:17981804). Beside its role in pre-mRNA splicing PRPF19, as
part of the PRP19-CDC5L complex, plays a role in the DNA damage
response/DDR. It is recruited to the sites of DNA damage by the
RPA complex where PRPF19 directly ubiquitinates RPA1 and RPA2.
'Lys-63'-linked polyubiquitination of the RPA complex allows the
recruitment of the ATR-ATRIP complex and the activation of ATR, a
master regulator of the DNA damage response (PubMed:24332808). May
also play a role in DNA double-strand break (DSB) repair by
recruiting the repair factor SETMAR to altered DNA
(PubMed:18263876). As part of the PSO4 complex may also be
involved in the DNA interstrand cross-links/ICLs repair process
(PubMed:16223718). In addition, may also mediate 'Lys-48'-linked
polyubiquitination of substrates and play a role in proteasomal
degradation (PubMed:11435423). May play a role in the biogenesis
of lipid droplets (By similarity). May play a role in neural
differentiation possibly through its function as part of the
spliceosome (By similarity). {ECO:0000250|UniProtKB:Q99KP6,
ECO:0000250|UniProtKB:Q9JMJ4, ECO:0000269|PubMed:11082287,
ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:12960389,
ECO:0000269|PubMed:15660529, ECO:0000269|PubMed:16223718,
ECO:0000269|PubMed:16332694, ECO:0000269|PubMed:16388800,
ECO:0000269|PubMed:17349974, ECO:0000269|PubMed:18263876,
ECO:0000269|PubMed:21536736, ECO:0000269|PubMed:24332808,
ECO:0000303|PubMed:17981804, ECO:0000303|PubMed:20595234}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:11435423}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:11435423}.
-!- SUBUNIT: Homotetramer. Component of the Prp19
complex/PRP19C/Nineteen complex/NTC and related complexes
described as PRP19-CDC5L splicing complex and PSO4 complex. A
homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2 constitute the core
of those complexes. The interaction with CDC5L, PLRG1 and BCAS2 is
direct within this core complex. At least three less stably
associated proteins CTNNBL1, CWC15 and HSPA8 are found in the
Prp19 complex. The Prp19 complex associates with the spliceosome
during its assembly and remodeling recruiting additional proteins.
Component of the XAB2 complex, a multimeric protein complex
composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Interacts
with CWC22 and EIF4A3 in an RNA-independent manner. Interacts with
RPA1 and RPA2; the PRP19-CDC5L complex is recruited to the sites
of DNA repair where it interacts with the replication protein A
complex (RPA). Interacts with SETMAR; required for SETMAR
recruitment to site of DNA damage. Interacts with U2AF2; the
interaction is direct and recruits the Prp19 complex to RNA
polymerase II C-terminal domain (CTD) and the pre-mRNA. Interacts
with PRPF3. Interacts with APEX1, DNTT and PSMB4. Interacts with
PSMC5 (By similarity). Interacts with KNSTRN (PubMed:24718257).
Interacts (via N-terminus) with CDC5L (By similarity). Interacts
with BLOM7 (PubMed:19641227). {ECO:0000250|UniProtKB:Q99KP6,
ECO:0000250|UniProtKB:Q9JMJ4, ECO:0000269|PubMed:11991638,
ECO:0000269|PubMed:12960389, ECO:0000269|PubMed:15660529,
ECO:0000269|PubMed:16223718, ECO:0000269|PubMed:16332694,
ECO:0000269|PubMed:17981804, ECO:0000269|PubMed:18263876,
ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:19641227,
ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:20595234,
ECO:0000269|PubMed:21536736, ECO:0000269|PubMed:22961380,
ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:24718257}.
-!- INTERACTION:
O75934:BCAS2; NbExp=2; IntAct=EBI-395746, EBI-1050106;
O60508:CDC40; NbExp=2; IntAct=EBI-395746, EBI-2557812;
Q99459:CDC5L; NbExp=2; IntAct=EBI-395746, EBI-374880;
Q6P2Q9:PRPF8; NbExp=2; IntAct=EBI-395746, EBI-538479;
P98175:RBM10; NbExp=2; IntAct=EBI-395746, EBI-721525;
P52756:RBM5; NbExp=8; IntAct=EBI-395746, EBI-714003;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11082287,
ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:19188445,
ECO:0000269|PubMed:20176811}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:11082287}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:11082287}. Cytoplasm
{ECO:0000269|PubMed:11435423}. Lipid droplet
{ECO:0000250|UniProtKB:Q99KP6}. Note=Nucleoplasmic in interphase
cells. Irregularly distributed in anaphase cells. In prophase
cells, uniformly distributed, but not associated with condensing
chromosomes. Found in extrachromosomal regions in metaphase cells.
Mainly localized to the mitotic spindle apparatus when chromosomes
segregate during anaphase. When nuclei reform during late
telophase, uniformly distributed in daughter cells and displays no
preferred association with decondensing chromatin. Recruited on
damaged DNA at sites of double-strand break.
{ECO:0000269|PubMed:11082287, ECO:0000269|PubMed:18263876}.
-!- TISSUE SPECIFICITY: Ubiquitous. Weakly expressed in senescent
cells of different tissue origins. Highly expressed in tumor cell
lines. {ECO:0000269|PubMed:10404385, ECO:0000269|PubMed:11082287,
ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:12960389,
ECO:0000269|PubMed:16388800}.
-!- INDUCTION: By gamma irradiation and chemical mutagens but not by
UV irradiation. {ECO:0000269|PubMed:12960389}.
-!- DOMAIN: The 7 WD repeats are necessary and sufficient to support
interaction with the RPA complex. {ECO:0000269|PubMed:24332808}.
-!- SIMILARITY: Belongs to the WD repeat PRP19 family. {ECO:0000305}.
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EMBL; AJ131186; CAB51857.1; -; mRNA.
EMBL; BC008719; AAH08719.1; -; mRNA.
EMBL; BC018665; AAH18665.1; -; mRNA.
EMBL; BC018698; AAH18698.1; -; mRNA.
CCDS; CCDS7995.1; -.
RefSeq; NP_055317.1; NM_014502.4.
UniGene; Hs.502705; -.
PDB; 4LG8; X-ray; 1.89 A; A=169-504.
PDB; 5MQF; EM; 5.90 A; G/H/I/J=1-504.
PDB; 5XJC; EM; 3.60 A; q/r/s/t=1-504.
PDBsum; 4LG8; -.
PDBsum; 5MQF; -.
PDBsum; 5XJC; -.
ProteinModelPortal; Q9UMS4; -.
SMR; Q9UMS4; -.
BioGrid; 118151; 176.
CORUM; Q9UMS4; -.
DIP; DIP-32978N; -.
IntAct; Q9UMS4; 45.
MINT; MINT-1454442; -.
STRING; 9606.ENSP00000227524; -.
iPTMnet; Q9UMS4; -.
PhosphoSitePlus; Q9UMS4; -.
SwissPalm; Q9UMS4; -.
BioMuta; PRPF19; -.
DMDM; 55976619; -.
REPRODUCTION-2DPAGE; IPI00004968; -.
SWISS-2DPAGE; Q9UMS4; -.
EPD; Q9UMS4; -.
MaxQB; Q9UMS4; -.
PaxDb; Q9UMS4; -.
PeptideAtlas; Q9UMS4; -.
PRIDE; Q9UMS4; -.
DNASU; 27339; -.
Ensembl; ENST00000227524; ENSP00000227524; ENSG00000110107.
GeneID; 27339; -.
KEGG; hsa:27339; -.
UCSC; uc001nqf.4; human.
CTD; 27339; -.
DisGeNET; 27339; -.
EuPathDB; HostDB:ENSG00000110107.8; -.
GeneCards; PRPF19; -.
HGNC; HGNC:17896; PRPF19.
HPA; CAB012448; -.
HPA; HPA038051; -.
HPA; HPA059070; -.
MIM; 608330; gene.
neXtProt; NX_Q9UMS4; -.
OpenTargets; ENSG00000110107; -.
PharmGKB; PA134941355; -.
eggNOG; KOG0289; Eukaryota.
eggNOG; ENOG410XPQV; LUCA.
GeneTree; ENSGT00900000140925; -.
HOGENOM; HOG000177308; -.
HOVERGEN; HBG053697; -.
InParanoid; Q9UMS4; -.
KO; K10599; -.
OMA; KPQAGIV; -.
OrthoDB; EOG091G05AH; -.
PhylomeDB; Q9UMS4; -.
TreeFam; TF105919; -.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
SignaLink; Q9UMS4; -.
UniPathway; UPA00143; -.
ChiTaRS; PRPF19; human.
GeneWiki; PRPF19; -.
GenomeRNAi; 27339; -.
PRO; PR:Q9UMS4; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110107; -.
CleanEx; HS_PRPF19; -.
ExpressionAtlas; Q9UMS4; baseline and differential.
Genevisible; Q9UMS4; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000974; C:Prp19 complex; IDA:UniProtKB.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
GO; GO:0034613; P:cellular protein localization; IMP:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IBA:GO_Central.
GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
GO; GO:0008610; P:lipid biosynthetic process; IEA:Ensembl.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; IEA:Ensembl.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:0010498; P:proteasomal protein catabolic process; IMP:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; IMP:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
GO; GO:0072422; P:signal transduction involved in DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0000245; P:spliceosomal complex assembly; IMP:BHF-UCL.
GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:UniProtKB.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
Gene3D; 2.130.10.10; -; 2.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR013915; Pre-mRNA_splic_Prp19.
InterPro; IPR000772; Ricin_B_lectin.
InterPro; IPR003613; Ubox_domain.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF08606; Prp19; 1.
Pfam; PF04564; U-box; 1.
Pfam; PF00400; WD40; 5.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00504; Ubox; 1.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS51698; U_BOX; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 4.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; DNA damage; DNA repair; Lipid droplet;
mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
Spliceosome; Transferase; Ubl conjugation pathway; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
CHAIN 2 504 Pre-mRNA-processing factor 19.
/FTId=PRO_0000051145.
DOMAIN 2 73 U-box.
REPEAT 219 259 WD 1.
REPEAT 262 301 WD 2.
REPEAT 304 345 WD 3.
REPEAT 348 387 WD 4.
REPEAT 390 429 WD 5.
REPEAT 433 472 WD 6.
REPEAT 473 503 WD 7.
REGION 68 223 May mediate interaction with PSMC5.
{ECO:0000250|UniProtKB:Q99KP6}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
MOD_RES 122 122 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 179 179 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99KP6}.
MOD_RES 244 244 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99KP6}.
MOD_RES 261 261 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MUTAGEN 405 405 Y->A: Loss of interaction with the RPA
complex and loss of recruitment to sites
of DNA damage.
{ECO:0000269|PubMed:24332808}.
HELIX 201 204 {ECO:0000244|PDB:4LG8}.
STRAND 208 213 {ECO:0000244|PDB:4LG8}.
STRAND 219 221 {ECO:0000244|PDB:4LG8}.
STRAND 224 230 {ECO:0000244|PDB:4LG8}.
STRAND 233 241 {ECO:0000244|PDB:4LG8}.
STRAND 246 250 {ECO:0000244|PDB:4LG8}.
TURN 251 254 {ECO:0000244|PDB:4LG8}.
STRAND 255 260 {ECO:0000244|PDB:4LG8}.
STRAND 269 272 {ECO:0000244|PDB:4LG8}.
STRAND 276 282 {ECO:0000244|PDB:4LG8}.
STRAND 288 292 {ECO:0000244|PDB:4LG8}.
TURN 293 296 {ECO:0000244|PDB:4LG8}.
STRAND 297 302 {ECO:0000244|PDB:4LG8}.
STRAND 309 314 {ECO:0000244|PDB:4LG8}.
STRAND 318 325 {ECO:0000244|PDB:4LG8}.
STRAND 328 334 {ECO:0000244|PDB:4LG8}.
TURN 335 337 {ECO:0000244|PDB:4LG8}.
STRAND 340 345 {ECO:0000244|PDB:4LG8}.
TURN 347 349 {ECO:0000244|PDB:4LG8}.
STRAND 353 358 {ECO:0000244|PDB:4LG8}.
STRAND 362 369 {ECO:0000244|PDB:4LG8}.
STRAND 374 378 {ECO:0000244|PDB:4LG8}.
TURN 379 382 {ECO:0000244|PDB:4LG8}.
STRAND 383 388 {ECO:0000244|PDB:4LG8}.
STRAND 395 400 {ECO:0000244|PDB:4LG8}.
STRAND 404 411 {ECO:0000244|PDB:4LG8}.
STRAND 414 420 {ECO:0000244|PDB:4LG8}.
TURN 421 424 {ECO:0000244|PDB:4LG8}.
STRAND 425 431 {ECO:0000244|PDB:4LG8}.
STRAND 438 443 {ECO:0000244|PDB:4LG8}.
STRAND 447 461 {ECO:0000244|PDB:4LG8}.
TURN 462 465 {ECO:0000244|PDB:4LG8}.
STRAND 466 471 {ECO:0000244|PDB:4LG8}.
STRAND 474 476 {ECO:0000244|PDB:4LG8}.
STRAND 478 483 {ECO:0000244|PDB:4LG8}.
HELIX 485 487 {ECO:0000244|PDB:4LG8}.
STRAND 490 494 {ECO:0000244|PDB:4LG8}.
STRAND 499 503 {ECO:0000244|PDB:4LG8}.
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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