Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Serine/threonine-protein kinase PRP4 homolog  

UniProtKB / Swiss-Prot ID :  PRP4B_MOUSE

Gene Name (Synonyms) : 
Prpf4b, Cbp143, Prp4h, Prp4k, Prp4m, Prpk  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Nucleus. 

Protein Function :  Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF. 

Protein Sequence MAATEPPSLREQAEMDDADNSEKSVNEENGEVSEDQSQNKHSRHKKKKHKHRSKHKKHKHSSEEDRDKKH...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHCCCCCCCCCCCCCCHHHHCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
8PhosphoserineTEPPSLREQ
CCCCCCCCC
51.26Phosphositeplus
Link-
21PhosphoserineDADNSEKSV
CCCCCCCCC
47.12Phosphositeplus
Link-
24PhosphoserineNSEKSVNEE
CCCCCCCCC
26.56Phosphositeplus
Link-
33PhosphoserineNGEVSEDQS
CCCCCCCCC
31.02Phosphositeplus
Link-
37PhosphoserineSEDQSQNKH
CCCCCCCCC
48.30Phosphositeplus
Link-
88PhosphoserineVIEASDKEG
CCCCCCCCC
36.10Phosphositeplus
Link-
88PhosphoserineVIEASDKEG
CCCCCCCCC
36.10SysPTM
Link-
88Phosphoserine.VIEASDKEG
CCCCCCCCC
36.10UniProtKB
Link-
94PhosphoserineKEGLSPAKR
CCCCCCCCC
33.40Phosphositeplus
Link-
94PhosphoserineKEGLSPAKR
CCCCCCCCC
33.40SysPTM
Link-
94Phosphoserine.KEGLSPAKR
CCCCCCCCC
33.40UniProtKB
Link-
134Methionine sulfoneVQSGMGLIL
CCCCCCCCC
4.83SysPTM
Link-
141PhosphotyrosineILQGYESGS
CCCCCCCCC
8.25Phosphositeplus
Link-
143PhosphoserineQGYESGSEE
CCCCCCCCC
38.85Phosphositeplus
Link-
143PhosphoserineQGYESGSEE
CCCCCCCCC
38.85SysPTM
Link-
145PhosphoserineYESGSEEEG
CCCCCCCCC
51.63Phosphositeplus
Link-
145PhosphoserineYESGSEEEG
CCCCCCCCC
51.63SysPTM
Link-
165PhosphoserineSSTRSSSTR
CCCCCCCCC
28.82Phosphositeplus
Link-
240PhosphoserineQARKSKSPP
HHHHCCCCC
32.58Phosphositeplus
Link-
242PhosphoserineRKSKSPPLR
HHCCCCCCC
38.55Phosphositeplus
Link-
258PhosphoserineGKARSPAEE
CCCCCCCCC
33.06Phosphositeplus
Link-
278PhosphoserineDRKKSPIVN
CCCCCCCCC
23.93Phosphositeplus
Link-
278Phosphoserine.DRKKSPIVN
CCCCCCCCC
23.93UniProtKB
Link-
292PhosphoserineRSKKSKSPV
CCCCCCCCC
41.94Phosphositeplus
Link-
292PhosphoserineRSKKSKSPV
CCCCCCCCC
41.94SysPTM
Link-
292Phosphoserine.RSKKSKSPV
CCCCCCCCC
41.94UniProtKB
Link-
294PhosphoserineKKSKSPVDL
CCCCCCCCC
36.93Phosphositeplus
Link-
294PhosphoserineKKSKSPVDL
CCCCCCCCC
36.93SysPTM
Link-
294Phosphoserine.KKSKSPVDL
CCCCCCCCC
36.93UniProtKB
Link-
328PhosphoserineKPIKSPSKD
CCCCCCCCC
34.82Phosphositeplus
Link-
330PhosphoserineIKSPSKDAS
CCCCCCCCC
50.70Phosphositeplus
Link-
354PhosphoserinePKRRSLSPK
CCCCCCCCC
36.91Phosphositeplus
Link-
356PhosphoserineRRSLSPKLR
CCCCCCCCC
22.64Phosphositeplus
Link-
366PhosphoserineKSRRSRSPL
CCCCCCCCC
35.68Phosphositeplus
Link-
366PhosphoserineKSRRSRSPL
CCCCCCCCC
35.68SysPTM
Link-
366Phosphoserine.KSRRSRSPL
CCCCCCCCC
35.68UniProtKB
Link-
368PhosphoserineRRSRSPLLN
CCCCCCCCC
22.58Phosphositeplus
Link-
368PhosphoserineRRSRSPLLN
CCCCCCCCC
22.58SysPTM
Link-
368Phosphoserine.RRSRSPLLN
CCCCCCCCC
22.58UniProtKB
Link-
381PhosphoserineKQSKSPSRT
CCCCCCCCC
33.10Phosphositeplus
Link-
383PhosphoserineSKSPSRTLS
CCCCCCCCC
45.01Phosphositeplus
Link-
385PhosphothreonineSPSRTLSPG
CCCCCCCCC
35.61Phosphositeplus
Link-
387PhosphoserineSRTLSPGRR
CCCCCCCCC
25.37Phosphositeplus
Link-
410PhosphoserineRRRLSSPRT
CCCCCCCCC
36.16Phosphositeplus
Link-
411PhosphoserineRRLSSPRTR
CCCCCCCCC
24.00Phosphositeplus
Link-
427PhosphoserineRCERSKDAS
CCCCCCCCC
16.76PhosphoELM
Link-
427PhosphoserineRCERSKDAS
CCCCCCCCC
16.76Phosphositeplus
Link-
427PhosphoserineRCERSKDAS
CCCCCCCCC
16.76SysPTM
Link-
427Phosphoserine.RCERSKDAS
CCCCCCCCC
16.76UniProtKB
Link-
431PhosphoserineSKDASPINR
CCCCCCCCC
36.12PhosphoELM
Link-
431PhosphoserineSKDASPINR
CCCCCCCCC
36.12Phosphositeplus
Link-
431PhosphoserineSKDASPINR
CCCCCCCCC
36.12SysPTM
Link-
431Phosphoserine.SKDASPINR
CCCCCCCCC
36.12UniProtKB
Link-
437PhosphoserineINRWSPTRR
CCCCCCCCH
17.10PhosphoELM
Link-
437PhosphoserineINRWSPTRR
CCCCCCCCH
17.10Phosphositeplus
Link-
437PhosphoserineINRWSPTRR
CCCCCCCCH
17.10SysPTM
Link-
437Phosphoserine.INRWSPTRR
CCCCCCCCH
17.10UniProtKB
Link-
439PhosphothreonineRWSPTRRRS
CCCCCCHHH
31.15Phosphositeplus
Link-
443PhosphoserineTRRRSRSPI
CCHHHCCCC
34.99Phosphositeplus
Link-
445PhosphoserineRRSRSPIRR
HHHCCCCCC
26.40Phosphositeplus
Link-
458PhosphoserinePLRRSRSPR
CCCCCCCCC
30.58Phosphositeplus
Link-
460PhosphoserineRRSRSPRRR
CCCCCCCCC
24.81Phosphositeplus
Link-
518PhosphoserineVEQESSSDD
CCCCCCCCC
34.53Phosphositeplus
Link-
519PhosphoserineEQESSSDDN
CCCCCCCCH
36.71Phosphositeplus
Link-
520PhosphoserineQESSSDDNL
CCCCCCCHH
59.26Phosphositeplus
Link-
576PhosphoserineSSTRSRSPS
CCCCCCCCC
36.88Phosphositeplus
Link-
576PhosphoserineSSTRSRSPS
CCCCCCCCC
36.88SysPTM
Link-
576Phosphoserine.SSTRSRSPS
CCCCCCCCC
36.88UniProtKB
Link-
578PhosphoserineTRSRSPSPD
CCCCCCCCC
30.86Phosphositeplus
Link-
578PhosphoserineTRSRSPSPD
CCCCCCCCC
30.86SysPTM
Link-
578Phosphoserine.TRSRSPSPD
CCCCCCCCC
30.86UniProtKB
Link-
580PhosphoserineSRSPSPDDI
CCCCCCCCC
42.05PhosphoELM
Link-
580PhosphoserineSRSPSPDDI
CCCCCCCCC
42.05Phosphositeplus
Link-
580PhosphoserineSRSPSPDDI
CCCCCCCCC
42.05SysPTM
Link-
580Phosphoserine.SRSPSPDDI
CCCCCCCCC
42.05UniProtKB
Link-
794PhosphoserineKAVRSYSQQ
HHHHHHHHH
23.65Phosphositeplus
Link-
795PhosphotyrosineAVRSYSQQL
HHHHHHHHH
10.43Phosphositeplus
Link-
837PhosphoserineCDFGSASHV
EECCEEEEC
26.96Phosphositeplus
Link-
839PhosphoserineFGSASHVAD
CCEEEECCC
21.86Phosphositeplus
Link-
849PhosphotyrosineDITPYLVSR
CEEEEEECC
15.87PhosphoELM
Link-
849PhosphotyrosineDITPYLVSR
CEEEEEECC
15.87Phosphositeplus
Link-
849PhosphotyrosineDITPYLVSR
CEEEEEECC
15.87SysPTM
Link-
849Phosphotyrosine.DITPYLVSR
CEEEEEECC
15.87UniProtKB
Link-
852PhosphoserinePYLVSRFYR
EEEECCCCC
17.68PhosphoELM
Link-
852PhosphoserinePYLVSRFYR
EEEECCCCC
17.68Phosphositeplus
Link-
852Phosphoserine.PYLVSRFYR
EEEECCCCC
17.68UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427; SER-431; SER-437;SER-580; TYR-849 AND SER-852, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278; SER-292; SER-294;SER-366; SER-368; SER-576; SER-578 AND SER-580, AND MASS SPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-94; SER-431;SER-437 AND TYR-849, AND MASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576; SER-578 ANDSER-580, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures