PRP19_HUMAN - dbPTM
PRP19_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRP19_HUMAN
UniProt AC Q9UMS4
Protein Name Pre-mRNA-processing factor 19 {ECO:0000305}
Gene Name PRPF19 {ECO:0000312|HGNC:HGNC:17896}
Organism Homo sapiens (Human).
Sequence Length 504
Subcellular Localization 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 condensing
Protein Description 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]
Protein Sequence MSLICSISNEVPEHPCVSPVSNHVYERRLIEKYIAENGTDPINNQPLSEEQLIDIKVAHPIRPKPPSATSIPAILKALQDEWDAVMLHSFTLRQQLQTTRQELSHALYQHDAACRVIARLTKEVTAAREALATLKPQAGLIVPQAVPSSQPSVVGAGEPMDLGELVGMTPEIIQKLQDKATVLTTERKKRGKTVPEELVKPEELSKYRQVASHVGLHSASIPGILALDLCPSDTNKILTGGADKNVVVFDKSSEQILATLKGHTKKVTSVVFHPSQDLVFSASPDATIRIWSVPNASCVQVVRAHESAVTGLSLHATGDYLLSSSDDQYWAFSDIQTGRVLTKVTDETSGCSLTCAQFHPDGLIFGTGTMDSQIKIWDLKERTNVANFPGHSGPITSIAFSENGYYLATAADDSSVKLWDLRKLKNFKTLQLDNNFEVKSLIFDQSGTYLALGGTDVQIYICKQWTEILHFTEHSGLTTGVAFGHHAKFIASTGMDRSLKFYSL
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 Orthologous
Protein Cluster
2Acetylation------MSLICSISN
------CCEEEECCC		26.8322223895
2Phosphorylation------MSLICSISN
------CCEEEECCC		26.8328464451
18PhosphorylationVPEHPCVSPVSNHVY
CCCCCCCCCCCCHHH		26.7125159151
32UbiquitinationYERRLIEKYIAENGT
HHHHHHHHHHHHHCC		34.6629967540
32AcetylationYERRLIEKYIAENGT
HHHHHHHHHHHHHCC		34.6626051181
48PhosphorylationPINNQPLSEEQLIDI
CCCCCCCCHHHCEEE		45.8528348404
56UbiquitinationEEQLIDIKVAHPIRP
HHHCEEEEECCCCCC		29.6229967540
64UbiquitinationVAHPIRPKPPSATSI
ECCCCCCCCCCCCCH		60.7629967540
64AcetylationVAHPIRPKPPSATSI
ECCCCCCCCCCCCCH		60.7626051181
67PhosphorylationPIRPKPPSATSIPAI
CCCCCCCCCCCHHHH		53.3520068231
69PhosphorylationRPKPPSATSIPAILK
CCCCCCCCCHHHHHH		31.3720068231
70PhosphorylationPKPPSATSIPAILKA
CCCCCCCCHHHHHHH		26.7020068231
86SulfoxidationQDEWDAVMLHSFTLR
HHHHHHHHHHHHHHH		2.7430846556
91PhosphorylationAVMLHSFTLRQQLQT
HHHHHHHHHHHHHHH		24.8524719451
104PhosphorylationQTTRQELSHALYQHD
HHHHHHHHHHHHHHH		13.1328152594
108PhosphorylationQELSHALYQHDAACR
HHHHHHHHHHHHHHH		12.4628152594
114GlutathionylationLYQHDAACRVIARLT
HHHHHHHHHHHHHHH		3.7022555962
122AcetylationRVIARLTKEVTAARE
HHHHHHHHHHHHHHH		55.5719608861
122UbiquitinationRVIARLTKEVTAARE
HHHHHHHHHHHHHHH		55.5727667366
133O-linked_GlycosylationAAREALATLKPQAGL
HHHHHHHHHCCCCCE		35.8423301498
135AcetylationREALATLKPQAGLIV
HHHHHHHCCCCCEEC		30.6326051181
148PhosphorylationIVPQAVPSSQPSVVG
ECCCCCCCCCCCCCC		34.7026714015
148O-linked_GlycosylationIVPQAVPSSQPSVVG
ECCCCCCCCCCCCCC		34.7023301498
149PhosphorylationVPQAVPSSQPSVVGA
CCCCCCCCCCCCCCC		39.7922529335
149O-linked_GlycosylationVPQAVPSSQPSVVGA
CCCCCCCCCCCCCCC		39.7923301498
152PhosphorylationAVPSSQPSVVGAGEP
CCCCCCCCCCCCCCC		23.0726714015
152O-linked_GlycosylationAVPSSQPSVVGAGEP
CCCCCCCCCCCCCCC		23.0723301498
169PhosphorylationLGELVGMTPEIIQKL
HHHHCCCCHHHHHHH		16.3126714015
169O-linked_GlycosylationLGELVGMTPEIIQKL
HHHHCCCCHHHHHHH		16.3123301498
179AcetylationIIQKLQDKATVLTTE
HHHHHHHHCEEEECH		32.7523749302
1792-HydroxyisobutyrylationIIQKLQDKATVLTTE
HHHHHHHHCEEEECH		32.75-
179UbiquitinationIIQKLQDKATVLTTE
HHHHHHHHCEEEECH		32.7529967540
181PhosphorylationQKLQDKATVLTTERK
HHHHHHCEEEECHHH		23.0721406692
184PhosphorylationQDKATVLTTERKKRG
HHHCEEEECHHHHCC		23.4428509920
185PhosphorylationDKATVLTTERKKRGK
HHCEEEECHHHHCCC		29.6328509920
192MalonylationTERKKRGKTVPEELV
CHHHHCCCCCCHHHC		50.8426320211
192UbiquitinationTERKKRGKTVPEELV
CHHHHCCCCCCHHHC		50.8432015554
193PhosphorylationERKKRGKTVPEELVK
HHHHCCCCCCHHHCC		44.0822817900
200UbiquitinationTVPEELVKPEELSKY
CCCHHHCCHHHHHHH		60.3724816145
200AcetylationTVPEELVKPEELSKY
CCCHHHCCHHHHHHH		60.3726051181
206UbiquitinationVKPEELSKYRQVASH
CCHHHHHHHHHHHHH		58.0129967540
206AcetylationVKPEELSKYRQVASH
CCHHHHHHHHHHHHH		58.0123749302
2062-HydroxyisobutyrylationVKPEELSKYRQVASH
CCHHHHHHHHHHHHH		58.01-
212PhosphorylationSKYRQVASHVGLHSA
HHHHHHHHHHCCCCC		21.6128122231
218PhosphorylationASHVGLHSASIPGIL
HHHHCCCCCCCCCEE		28.8428122231
220PhosphorylationHVGLHSASIPGILAL
HHCCCCCCCCCEEEE		32.1228348404
236AcetylationLCPSDTNKILTGGAD
CCCCCCCCEECCCCC		40.9826051181
236UbiquitinationLCPSDTNKILTGGAD
CCCCCCCCEECCCCC		40.9829967540
239PhosphorylationSDTNKILTGGADKNV
CCCCCEECCCCCCCE		36.7222210691
244AcetylationILTGGADKNVVVFDK
EECCCCCCCEEEEEC		51.6223954790
244MalonylationILTGGADKNVVVFDK
EECCCCCCCEEEEEC		51.6226320211
244UbiquitinationILTGGADKNVVVFDK
EECCCCCCCEEEEEC		51.6223000965
2442-HydroxyisobutyrylationILTGGADKNVVVFDK
EECCCCCCCEEEEEC		51.62-
2512-HydroxyisobutyrylationKNVVVFDKSSEQILA
CCEEEEECCHHHHHH		44.40-
251AcetylationKNVVVFDKSSEQILA
CCEEEEECCHHHHHH		44.4025953088
251UbiquitinationKNVVVFDKSSEQILA
CCEEEEECCHHHHHH		44.4029967540
252PhosphorylationNVVVFDKSSEQILAT
CEEEEECCHHHHHHH		40.7422210691
253PhosphorylationVVVFDKSSEQILATL
EEEEECCHHHHHHHH		38.9822210691
259PhosphorylationSSEQILATLKGHTKK
CHHHHHHHHCCCCCE		26.0922210691
261AcetylationEQILATLKGHTKKVT
HHHHHHHCCCCCEEE		44.2719608861
261UbiquitinationEQILATLKGHTKKVT
HHHHHHHCCCCCEEE		44.2722817900
2612-HydroxyisobutyrylationEQILATLKGHTKKVT
HHHHHHHCCCCCEEE		44.27-
265UbiquitinationATLKGHTKKVTSVVF
HHHCCCCCEEEEEEE		39.3022817900
266MalonylationTLKGHTKKVTSVVFH
HHCCCCCEEEEEEEC		52.4826320211
266UbiquitinationTLKGHTKKVTSVVFH
HHCCCCCEEEEEEEC		52.4822817900
268PhosphorylationKGHTKKVTSVVFHPS
CCCCCEEEEEEECCC		25.3621406692
269O-linked_GlycosylationGHTKKVTSVVFHPSQ
CCCCEEEEEEECCCC		21.1923301498
269PhosphorylationGHTKKVTSVVFHPSQ
CCCCEEEEEEECCCC		21.1921406692
275PhosphorylationTSVVFHPSQDLVFSA
EEEEECCCCCEEEEC		27.9621406692
281O-linked_GlycosylationPSQDLVFSASPDATI
CCCCEEEECCCCCEE		21.9823301498
281PhosphorylationPSQDLVFSASPDATI
CCCCEEEECCCCCEE		21.9821406692
283PhosphorylationQDLVFSASPDATIRI
CCEEEECCCCCEEEE		23.3221406692
287PhosphorylationFSASPDATIRIWSVP
EECCCCCEEEEEECC		20.4021406692
297PhosphorylationIWSVPNASCVQVVRA
EEECCCCCEEEEEEH		22.8221712546
307PhosphorylationQVVRAHESAVTGLSL
EEEEHHHCCCCCCEE		20.4018669648
310PhosphorylationRAHESAVTGLSLHAT
EHHHCCCCCCEEEEC		31.9318669648
313PhosphorylationESAVTGLSLHATGDY
HCCCCCCEEEECCCE		21.3218669648
329PhosphorylationLSSSDDQYWAFSDIQ
CCCCCCCEEEEECCC		13.0018669648
342PhosphorylationIQTGRVLTKVTDETS
CCCCCEEEEEECCCC		22.1718669648
343AcetylationQTGRVLTKVTDETSG
CCCCEEEEEECCCCC		38.6926051181
375UbiquitinationGTMDSQIKIWDLKER
CCCCCEEEEEECHHC		30.0622817900
380AcetylationQIKIWDLKERTNVAN
EEEEEECHHCCCCCC		42.5526822725
380SuccinylationQIKIWDLKERTNVAN
EEEEEECHHCCCCCC		42.5523954790
380UbiquitinationQIKIWDLKERTNVAN
EEEEEECHHCCCCCC		42.5527667366
3802-HydroxyisobutyrylationQIKIWDLKERTNVAN
EEEEEECHHCCCCCC		42.55-
405PhosphorylationIAFSENGYYLATAAD
EEEECCCEEEEEECC		13.59-
423UbiquitinationVKLWDLRKLKNFKTL
CCEEEHHHCCCCCEE		71.7322817900
425UbiquitinationLWDLRKLKNFKTLQL
EEEHHHCCCCCEEEE		64.4722817900
425AcetylationLWDLRKLKNFKTLQL
EEEHHHCCCCCEEEE		64.4725953088
428AcetylationLRKLKNFKTLQLDNN
HHHCCCCCEEEECCC		58.6925953088
428MalonylationLRKLKNFKTLQLDNN
HHHCCCCCEEEECCC		58.6932601280
428UbiquitinationLRKLKNFKTLQLDNN
HHHCCCCCEEEECCC		58.6921906983
495SulfoxidationKFIASTGMDRSLKFY
HHHHCCCCCCCCEEE		3.8121406390
500UbiquitinationTGMDRSLKFYSL---
CCCCCCCEEECC---		43.4324816145
503PhosphorylationDRSLKFYSL------
CCCCEEECC------		30.6424719451
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
149SPhosphorylationKinaseATMQ13315
PSP
193TPhosphorylationKinaseAKT1P47196
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRP19_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PRP19_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TDT_HUMANDNTTphysical
12960389
IMA1_HUMANKPNA2physical
21385873
IMA5_HUMANKPNA1physical
21385873
EGLN3_HUMANEGLN3physical
20599946
PRP19_HUMANPRPF19physical
20599946
PRPF3_HUMANPRPF3physical
20595234
PSB4_HUMANPSMB4physical
15660529
EXOC7_HUMANEXOC7physical
21639856
BLOM7_HUMANKIAA0907physical
19641227
PRP19_HUMANPRPF19physical
19641227
U2AF2_HUMANU2AF2physical
21536736
PRP19_HUMANPRPF19physical
16332694
PLRG1_HUMANPLRG1physical
20176811
SPF27_HUMANBCAS2physical
20176811
CDC5L_HUMANCDC5Lphysical
20176811
PRP8_HUMANPRPF8physical
22939629
SPF27_HUMANBCAS2physical
22939629
SNRPA_HUMANSNRPAphysical
22939629
SMD2_HUMANSNRPD2physical
22939629
SF3A1_HUMANSF3A1physical
22939629
SMD1_HUMANSNRPD1physical
22939629
SRSF1_HUMANSRSF1physical
22939629
PRPF3_HUMANPRPF3physical
22939629
PRP4_HUMANPRPF4physical
22939629
RU2A_HUMANSNRPA1physical
22939629
PRP6_HUMANPRPF6physical
22939629
SF3B3_HUMANSF3B3physical
22939629
RU17_HUMANSNRNP70physical
22939629
SYF1_HUMANXAB2physical
22939629
SF3A3_HUMANSF3A3physical
22939629
SNUT1_HUMANSART1physical
22939629
U520_HUMANSNRNP200physical
22939629
SRSF5_HUMANSRSF5physical
22939629
U2AF1_HUMANU2AF1physical
22939629
RBM25_HUMANRBM25physical
22939629
U5S1_HUMANEFTUD2physical
22939629
RNPS1_HUMANRNPS1physical
22939629
SRS11_HUMANSRSF11physical
22939629
RBM39_HUMANRBM39physical
22939629
SON_HUMANSONphysical
22939629
RS10_HUMANRPS10physical
22939629
UT14A_HUMANUTP14Aphysical
22939629
VTNC_HUMANVTNphysical
22939629
TRI55_HUMANTRIM55physical
22939629
RBM14_HUMANRBM14physical
22939629
SRP14_HUMANSRP14physical
22939629
RS24_HUMANRPS24physical
22939629
U2AF1_HUMANU2AF1physical
22365833
RBM10_HUMANRBM10physical
22365833
RBM5_HUMANRBM5physical
22365833
PRP8_HUMANPRPF8physical
22365833
SPF27_HUMANBCAS2physical
22365833
PRCC_HUMANPRCCphysical
22365833
HSPB1_HUMANHSPB1physical
22365833
PRP17_HUMANCDC40physical
22365833
DDX42_HUMANDDX42physical
22365833
RBM5_HUMANRBM5physical
22569250
UCHL5_HUMANUCHL5physical
23220010
RFA2_HUMANRPA2physical
24332808
RFA1_HUMANRPA1physical
24332808
RFA3_HUMANRPA3physical
24332808
EXOC3_HUMANEXOC3physical
21639856
UBP4_HUMANUSP4physical
20595234
UB2D3_HUMANUBE2D3physical
20595234
SKAP_HUMANKNSTRNphysical
24718257
SPF27_HUMANBCAS2physical
26344197
DHX8_HUMANDHX8physical
26344197
LTN1_HUMANLTN1physical
26344197
MTCH1_HUMANMTCH1physical
26344197
PRP4_HUMANPRPF4physical
26344197
R113B_HUMANRNF113Bphysical
26344197
RPN1_HUMANRPN1physical
26344197
SF3B1_HUMANSF3B1physical
26344197
U520_HUMANSNRNP200physical
26344197
SMD1_HUMANSNRPD1physical
26344197
SMD2_HUMANSNRPD2physical
26344197
SNW1_HUMANSNW1physical
26344197
CHIP_HUMANSTUB1physical
26344197
UBXN1_HUMANUBXN1physical
26344197
SNUT2_HUMANUSP39physical
26344197
PTN11_HUMANPTPN11physical
27213290
SKAP_HUMANKNSTRNphysical
28514442
GCC1_HUMANGCC1physical
28514442
SENP6_HUMANSENP6physical
28514442
ZDBF2_HUMANZDBF2physical
28514442
GPTC1_HUMANGPATCH1physical
28514442
C19L2_HUMANCWF19L2physical
28514442
CDC5L_HUMANCDC5Lphysical
28514442
AQR_HUMANAQRphysical
28514442
SPF27_HUMANBCAS2physical
28514442
SYF1_HUMANXAB2physical
28514442
DHX35_HUMANDHX35physical
28514442
CCD18_HUMANCCDC18physical
28514442
CCD12_HUMANCCDC12physical
28514442
PRP17_HUMANCDC40physical
28514442
CTBL1_HUMANCTNNBL1physical
28514442
SNW1_HUMANSNW1physical
28514442
ISY1_HUMANISY1physical
28514442
TFP11_HUMANTFIP11physical
28514442
C19L1_HUMANCWF19L1physical
28514442
SLMAP_HUMANSLMAPphysical
28514442
ASPP2_HUMANTP53BP2physical
28514442
CRNL1_HUMANCRNKL1physical
28514442
RBM22_HUMANRBM22physical
28514442
BUD31_HUMANBUD31physical
28514442
ZN830_HUMANZNF830physical
28514442
STRN_HUMANSTRNphysical
28514442
U520_HUMANSNRNP200physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRP19_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122 AND LYS-261, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; THR-310; SER-313;TYR-329 AND THR-342, AND MASS SPECTROMETRY.

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