PRP19_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PRP19_MOUSE
• UniProt AC: Q99KP6
• Protein Name: Pre-mRNA-processing factor 19 {ECO:0000305}
• Gene Name: Prpf19 {ECO:0000312|MGI:MGI:106247}
• Organism: Mus musculus (Mouse).
• Sequence Length: 504
• Subcellular Localization: Isoform 1: Nucleus . Nucleus, nucleoplasm . Cytoplasm, cytoskeleton, spindle . Cytoplasm . Lipid droplet . Nucleoplasmic in interphase cells. Irregularly distributed in anaphase cells. In prophase cells, uniformly distributed, but not associated with
• Protein Description: Isoform 1: Ubiquitin-protein ligase which is a core component of several complexes mainly involved in 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. Recruited to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also couple the transcriptional and spliceosomal machineries. The XAB2 complex, which contains PRPF19, is also involved in pre-mRNA splicing, transcription and transcription-coupled repair. 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. May also play a role in DNA double-strand break (DSB) repair by recruiting the repair factor SETMAR to altered DNA. As part of the PSO4 complex may also be involved in the DNA interstrand cross-links/ICLs repair process. In addition, may also mediate 'Lys-48'-linked polyubiquitination of substrates and play a role in proteasomal degradation. [PubMed: 17349974 May play a role in the biogenesis of lipid droplets]
• Protein Sequence: MSLICSISNEVPEHPCVSPVSNHVYERRLIEKYIAENGTDPINNQPLSEEQLIDIKVAHPIRPKPPSATSIPAILKALQDEWDAVMLHSFTLRQQLQTTRQELSHALYQHDAACRVIARLTKEVTAAREALATLKPQAGLIVPQAVPSSQPSVVGAGEPMDLGELVGMTPEIIQKLQDKATVLTTERKKRGKTVPEELVKPEELSKYRQVASHVGLHSASIPGILALDLCPSDTNKILTGGADKNVVVFDKSTEQILATLKGHTKKVTSVVFHPSQELVFSASPDATIRIWSVPNTSCVQVVRAHESAVTGLSLHATGDYLLSSSDDQYWAFSDIQTGRVLTKVTDETSGCSLTCAQFHPDGLIFGTGTMDSQIKIWDLKERTNVANFPGHSGPITSIAFSENGYYLATAADDSSVKLWDLRKLKNFKTLQLDNNFEVKSLIFDQSGTYLALGGTDVQIYICKQWTEILHFTEHSGLTTGVAFGHHAKFIASTGMDRSLKFYSL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSLICSISN ------CCEEEECCC	26.83	26643407
2	Acetylation	------MSLICSISN ------CCEEEECCC	26.83	-
6	Phosphorylation	--MSLICSISNEVPE --CCEEEECCCCCCC	23.27	26643407
8	Phosphorylation	MSLICSISNEVPEHP CCEEEECCCCCCCCC	15.62	26643407
18	Phosphorylation	VPEHPCVSPVSNHVY CCCCCCCCCCCCHHH	26.71	26643407
21	Phosphorylation	HPCVSPVSNHVYERR CCCCCCCCCHHHHHH	25.30	26643407
25	Phosphorylation	SPVSNHVYERRLIEK CCCCCHHHHHHHHHH	9.00	26643407
37	Ubiquitination	IEKYIAENGTDPINN HHHHHHHHCCCCCCC	50.03	27667366
48	Phosphorylation	PINNQPLSEEQLIDI CCCCCCCCHHHCEEE	45.85	29899451
64	Ubiquitination	VAHPIRPKPPSATSI ECCCCCCCCCCCCCH	60.76	22790023
114	S-nitrosocysteine	LYQHDAACRVIARLT HHHHHHHHHHHHHHH	3.70	-
114	S-nitrosylation	LYQHDAACRVIARLT HHHHHHHHHHHHHHH	3.70	20925432
122	Acetylation	RVIARLTKEVTAARE HHHHHHHHHHHHHHH	55.57	-
122	Ubiquitination	RVIARLTKEVTAARE HHHHHHHHHHHHHHH	55.57	22790023
141	Ubiquitination	LKPQAGLIVPQAVPS HCCCCCEECCCCCCC	4.09	27667366
159	Ubiquitination	SVVGAGEPMDLGELV CCCCCCCCCCHHHHC	22.22	27667366
179	Acetylation	IIQKLQDKATVLTTE HHHHHHHHCEEEECH	32.75	23806337
181	Phosphorylation	QKLQDKATVLTTERK HHHHHHCEEEECHHH	23.07	19854140
192	Malonylation	TERKKRGKTVPEELV CHHHHCCCCCCHHHC	50.84	26320211
244	Ubiquitination	ILTGGADKNVVVFDK EECCCCCCCEEEEEC	51.62	27667366
244	Acetylation	ILTGGADKNVVVFDK EECCCCCCCEEEEEC	51.62	23806337
244	Malonylation	ILTGGADKNVVVFDK EECCCCCCCEEEEEC	51.62	26320211
251	Ubiquitination	KNVVVFDKSTEQILA CCEEEEECCHHHHHH	48.06	22790023
251	Acetylation	KNVVVFDKSTEQILA CCEEEEECCHHHHHH	48.06	22826441
261	Ubiquitination	EQILATLKGHTKKVT HHHHHHHCCCCCEEE	44.27	22790023
261	Acetylation	EQILATLKGHTKKVT HHHHHHHCCCCCEEE	44.27	22826441
263	Ubiquitination	ILATLKGHTKKVTSV HHHHHCCCCCEEEEE	32.69	27667366
266	Ubiquitination	TLKGHTKKVTSVVFH HHCCCCCEEEEEEEC	52.48	22790023
503	Phosphorylation	DRSLKFYSL------ CCCCEEECC------	30.64	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PRP19_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PRP19_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PRP19_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRS8_MOUSE	Psmc5	physical	17349974

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.