Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Pre-mRNA-splicing factor 38B  

UniProtKB / Swiss-Prot ID :  PR38B_HUMAN

Gene Name (Synonyms) : 
PRPF38B  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (Potential). 

Protein Function :  May be required for pre-mRNA splicing (Potential). 

Protein Sequence MANNSPALTGNSQPQHQAAAAAAQQQQQCGGGGATKPAVSGKQGNVLPLWGNEKTMNLNPMILTNILSSP...
Predicted Secondary Structure CCCCCCCCCCCCCHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHCCC...
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
2N-acetylalanine.---MANNSP
---CCCCCC
24.74UniProtKB
Link-
5PhosphoserineMANNSPALT
CCCCCCCCC
16.03HPRD
Link-
5Phosphoserine.MANNSPALT
CCCCCCCCC
16.03UniProtKB
Link-
40PhosphoserineKPAVSGKQG
CCCCCCCCC
42.24HPRD
Link-
101N6-acetyllysineEPWEKGSRK
CHHHHCCCC
59.31HPRD
Link-
121PhosphothreonineRGVGTGGIV
CCCCCCCCC
29.81HPRD
Link-
150PhosphothreonineMGLITHTDS
HHHHHCCCC
24.62HPRD
Link-
150PhosphothreonineMGLITHTDS
HHHHHCCCC
24.62Phosphositeplus
Link-
152PhosphothreonineLITHTDSPY
HHHCCCCHH
29.53HPRD
Link-
154PhosphoserineTHTDSPYIR
HCCCCHHHH
22.28HPRD
Link-
227N6-acetyllysineVPVQKNIDQ
CCCCCCCCC
56.98HPRD
Link-
227N6-acetyllysineVPVQKNIDQ
CCCCCCCCC
56.98Phosphositeplus
Link-
227N6-acetyllysine.VPVQKNIDQ
CCCCCCCCC
56.98UniProtKB
Link-
266PhosphoserineSPRRSLSPR
CCCCCCCCC
34.18HPRD
Link-
266PhosphoserineSPRRSLSPR
CCCCCCCCC
34.18PhosphoELM
Link-
266PhosphoserineSPRRSLSPR
CCCCCCCCC
34.18Phosphositeplus
Link-
266PhosphoserineSPRRSLSPR
CCCCCCCCC
34.18SysPTM
Link-
266Phosphoserine.SPRRSLSPR
CCCCCCCCC
34.18UniProtKB
Link-
268PhosphoserineRRSLSPRRS
CCCCCCCCC
20.01HPRD
Link-
268PhosphoserineRRSLSPRRS
CCCCCCCCC
20.01PhosphoELM
Link-
268PhosphoserineRRSLSPRRS
CCCCCCCCC
20.01Phosphositeplus
Link-
268PhosphoserineRRSLSPRRS
CCCCCCCCC
20.01SysPTM
Link-
268Phosphoserine.RRSLSPRRS
CCCCCCCCC
20.01UniProtKB
Link-
272PhosphoserineSPRRSPRRS
CCCCCCCCC
24.84PhosphoELM
Link-
272PhosphoserineSPRRSPRRS
CCCCCCCCC
24.84Phosphositeplus
Link-
272PhosphoserineSPRRSPRRS
CCCCCCCCC
24.84SysPTM
Link-
272Phosphoserine.SPRRSPRRS
CCCCCCCCC
24.84UniProtKB
Link-
280PhosphoserineSRSRSHHRE
CCCCCCCCC
25.54Phosphositeplus
Link-
288PhosphoserineEGHGSSSFD
CCCCCCCCC
19.68HPRD
Link-
288PhosphoserineEGHGSSSFD
CCCCCCCCC
19.68SysPTM
Link-
289PhosphoserineGHGSSSFDR
CCCCCCCCC
39.35HPRD
Link-
290PhosphoserineHGSSSFDRE
CCCCCCCCC
32.63HPRD
Link-
290PhosphoserineHGSSSFDRE
CCCCCCCCC
32.63PhosphoELM
Link-
290PhosphoserineHGSSSFDRE
CCCCCCCCC
32.63Phosphositeplus
Link-
290PhosphoserineHGSSSFDRE
CCCCCCCCC
32.63SysPTM
Link-
290Phosphoserine.HGSSSFDRE
CCCCCCCCC
32.63UniProtKB
Link-
318PhosphoserineERRRSRSID
CCCCCCCCC
28.68HPRD
Link-
318PhosphoserineERRRSRSID
CCCCCCCCC
28.68PhosphoELM
Link-
318PhosphoserineERRRSRSID
CCCCCCCCC
28.68Phosphositeplus
Link-
318PhosphoserineERRRSRSID
CCCCCCCCC
28.68SysPTM
Link-
318Phosphoserine.ERRRSRSID
CCCCCCCCC
28.68UniProtKB
Link-
320PhosphoserineRRSRSIDRG
CCCCCCCCC
30.04HPRD
Link-
320PhosphoserineRRSRSIDRG
CCCCCCCCC
30.04PhosphoELM
Link-
320PhosphoserineRRSRSIDRG
CCCCCCCCC
30.04Phosphositeplus
Link-
320PhosphoserineRRSRSIDRG
CCCCCCCCC
30.04SysPTM
Link-
320Phosphoserine.RRSRSIDRG
CCCCCCCCC
30.04UniProtKB
Link-
385PhosphoserineERERSRERS
CCCCCCCCC
33.47PhosphoELM
Link-
385PhosphoserineERERSRERS
CCCCCCCCC
33.47Phosphositeplus
Link-
385PhosphoserineERERSRERS
CCCCCCCCC
33.47SysPTM
Link-
385Phosphoserine.ERERSRERS
CCCCCCCCC
33.47UniProtKB
Link-
448PhosphoserineAGKRSRSRS
CCCCHHHCC
37.79HPRD
Link-
448PhosphoserineAGKRSRSRS
CCCCHHHCC
37.79Phosphositeplus
Link-
471PhosphoserineSNKRSRSGS
CCCCCCCCC
32.19HPRD
Link-
471PhosphoserineSNKRSRSGS
CCCCCCCCC
32.19Phosphositeplus
Link-
473PhosphoserineKRSRSGSQG
CCCCCCCCC
44.00HPRD
Link-
473PhosphoserineKRSRSGSQG
CCCCCCCCC
44.00Phosphositeplus
Link-
475PhosphoserineSRSGSQGRT
CCCCCCCCC
30.61HPRD
Link-
475PhosphoserineSRSGSQGRT
CCCCCCCCC
30.61Phosphositeplus
Link-
481PhosphoserineGRTDSVEKS
CCCCCCCCC
31.40HPRD
Link-
481PhosphoserineGRTDSVEKS
CCCCCCCCC
31.40Phosphositeplus
Link-
491PhosphoserineKREHSPSKE
CCCCCCCCC
26.56HPRD
Link-
491PhosphoserineKREHSPSKE
CCCCCCCCC
26.56SysPTM
Link-
493PhosphoserineEHSPSKEKS
CCCCCCCCC
57.36HPRD
Link-
493PhosphoserineEHSPSKEKS
CCCCCCCCC
57.36PhosphoELM
Link-
493PhosphoserineEHSPSKEKS
CCCCCCCCC
57.36Phosphositeplus
Link-
493PhosphoserineEHSPSKEKS
CCCCCCCCC
57.36SysPTM
Link-
527PhosphoserineDRRRSQSIE
CCCCCCCCC
26.86HPRD
Link-
527PhosphoserineDRRRSQSIE
CCCCCCCCC
26.86PhosphoELM
Link-
527PhosphoserineDRRRSQSIE
CCCCCCCCC
26.86Phosphositeplus
Link-
527PhosphoserineDRRRSQSIE
CCCCCCCCC
26.86SysPTM
Link-
527Phosphoserine.DRRRSQSIE
CCCCCCCCC
26.86UniProtKB
Link-
529PhosphoserineRRSQSIEQE
CCCCCCCCC
29.37HPRD
Link-
529PhosphoserineRRSQSIEQE
CCCCCCCCC
29.37PhosphoELM
Link-
529PhosphoserineRRSQSIEQE
CCCCCCCCC
29.37Phosphositeplus
Link-
529PhosphoserineRRSQSIEQE
CCCCCCCCC
29.37SysPTM
Link-
529Phosphoserine.RRSQSIEQE
CCCCCCCCC
29.37UniProtKB
Link-
534PhosphoserineIEQESQEKQ
CCCCHHHHC
43.25HPRD
Link-
534PhosphoserineIEQESQEKQ
CCCCHHHHC
43.25PhosphoELM
Link-
534PhosphoserineIEQESQEKQ
CCCCHHHHC
43.25Phosphositeplus
Link-
534PhosphoserineIEQESQEKQ
CCCCHHHHC
43.25SysPTM
Link-
534Phosphoserine.IEQESQEKQ
CCCCHHHHC
43.25UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433G_HUMANin vivoHPRD:07664HPRD15324660
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-5, AND MASS SPECTROMETRY.
"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-227, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-527; SER-529 ANDSER-534, AND MASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-5, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, AND MASSSPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-529, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-268; SER-272;SER-290; SER-318; SER-320; SER-385; SER-527 AND SER-529, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-529, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-534, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures