PRPF19
entrez
27339
canonical
uniprot
Q9UMS4
canonical
ensembl
ENSG00000110107
resolver
ensp
ENSP00000227524
resolver
enst
ENST00000227524
resolver
genesymbol
PRPF19
resolver
genesymbol_syn
NMP200
resolver
genesymbol_syn
PRP19
resolver
genesymbol_syn
SNEV
resolver
hgnc
HGNC:17896
resolver
uniprot_entry
PRP19_HUMAN
resolver
amino_acid_sequence
MSLICSISNEVPEHPCVSPVSNHVYERRLIEKYIAENGTDPINNQPLSEEQLIDIKVAHPIRPKPPSATSIPAILKALQDEWDAVMLHSFTLRQQLQTTRQELSHALYQHDAACRVIARLTKEVTAAREALATLKPQAGLIVPQAVPSSQPSVVGAGEPMDLGELVGMTPEIIQKLQDKATVLTTERKKRGKTVPEELVKPEELSKYRQVASHVGLHSASIPGILALDLCPSDTNKILTGGADKNVVVFDKSSEQILATLKGHTKKVTSVVFHPSQDLVFSASPDATIRIWSVPNASCVQVVRAHESAVTGLSLHATGDYLLSSSDDQYWAFSDIQTGRVLTKVTDETSGCSLTCAQFHPDGLIFGTGTMDSQIKIWDLKERTNVANFPGHSGPITSIAFSENGYYLATAADDSSVKLWDLRKLKNFKTLQLDNNFEVKSLIFDQSGTYLALGGTDVQIYICKQWTEILHFTEHSGLTTGVAFGHHAKFIASTGMDRSLKFYSL
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: Ubiquitin-protein ligase which is a core component of several complexes mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome (PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106, PubMed:30705154). 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:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30705154, ECO:0000303|PubMed:17981804, ECO:0000303|PubMed:20595234}.
uniprot
proteins
mass_dalton
55181
uniprot
proteins
mutagenesis
MUTAGEN 405; /note="Y->A: Loss of interaction with the RPA complex and loss of recruitment to sites of DNA damage."; /evidence="ECO:0000269|PubMed:24332808
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:11435423}.
uniprot
proteins
protein_family
WD repeat PRP19 family
uniprot
proteins
pubmed
10404385
uniprot
proteins
pubmed
11082287
uniprot
proteins
pubmed
11435423
uniprot
proteins
pubmed
11991638
uniprot
proteins
pubmed
12429849
uniprot
proteins
pubmed
12960389
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15660529
uniprot
proteins
pubmed
16223718
uniprot
proteins
pubmed
16332694
uniprot
proteins
pubmed
16388800
uniprot
proteins
pubmed
17349974
uniprot
proteins
pubmed
17981804
uniprot
proteins
pubmed
18263876
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19188445
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19641227
uniprot
proteins
pubmed
20176811
uniprot
proteins
pubmed
20595234
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21536736
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22961380
uniprot
proteins
pubmed
23022480
uniprot
proteins
pubmed
24332808
uniprot
proteins
pubmed
24718257
uniprot
proteins
pubmed
28076346
uniprot
proteins
pubmed
28502770
uniprot
proteins
pubmed
28962858
uniprot
proteins
pubmed
29301961
uniprot
proteins
pubmed
29360106
uniprot
proteins
pubmed
30705154
uniprot
proteins
pubmed
36229594
uniprot
proteins
sequence_length
504
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11082287, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30705154}. 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}.
uniprot
proteins