PR38B_HUMAN - dbPTM
PR38B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PR38B_HUMAN
UniProt AC Q5VTL8
Protein Name Pre-mRNA-splicing factor 38B
Gene Name PRPF38B
Organism Homo sapiens (Human).
Sequence Length 546
Subcellular Localization Nucleus .
Protein Description May be required for pre-mRNA splicing..
Protein Sequence MANNSPALTGNSQPQHQAAAAAAQQQQQCGGGGATKPAVSGKQGNVLPLWGNEKTMNLNPMILTNILSSPYFKVQLYELKTYHEVVDEIYFKVTHVEPWEKGSRKTAGQTGMCGGVRGVGTGGIVSTAFCLLYKLFTLKLTRKQVMGLITHTDSPYIRALGFMYIRYTQPPTDLWDWFESFLDDEEDLDVKAGGGCVMTIGEMLRSFLTKLEWFSTLFPRIPVPVQKNIDQQIKTRPRKIKKDGKEGAEEIDRHVERRRSRSPRRSLSPRRSPRRSRSRSHHREGHGSSSFDRELEREKERQRLEREAKEREKERRRSRSIDRGLERRRSRSRERHRSRSRSRDRKGDRRDRDREREKENERGRRRDRDYDKERGNEREKERERSRERSKEQRSRGEVEEKKHKEDKDDRRHRDDKRDSKKEKKHSRSRSRERKHRSRSRSRNAGKRSRSRSKEKSSKHKNESKEKSNKRSRSGSQGRTDSVEKSKKREHSPSKEKSRKRSRSKERSHKRDHSDSKDQSDKHDRRRSQSIEQESQEKQHKNKDETV
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------MANNSPALT
------CCCCCCCCC		24.7419413330
5Phosphorylation---MANNSPALTGNS
---CCCCCCCCCCCC		16.0323401153
9PhosphorylationANNSPALTGNSQPQH
CCCCCCCCCCCCHHH		36.1029255136
12PhosphorylationSPALTGNSQPQHQAA
CCCCCCCCCHHHHHH		44.5829255136
30UbiquitinationAQQQQQCGGGGATKP
HHHHHHCCCCCCCCC		33.1833845483
35PhosphorylationQCGGGGATKPAVSGK
HCCCCCCCCCCCCCC		40.6123663014
36AcetylationCGGGGATKPAVSGKQ
CCCCCCCCCCCCCCC		30.3723954790
40PhosphorylationGATKPAVSGKQGNVL
CCCCCCCCCCCCCEE		42.2423927012
43UbiquitinationKPAVSGKQGNVLPLW
CCCCCCCCCCEECCC		52.8233845483
45UbiquitinationAVSGKQGNVLPLWGN
CCCCCCCCEECCCCC		29.6533845483
48UbiquitinationGKQGNVLPLWGNEKT
CCCCCEECCCCCCCC		23.0624816145
61UbiquitinationKTMNLNPMILTNILS
CCCCCCHHHHHHHHC		3.6924816145
68PhosphorylationMILTNILSSPYFKVQ
HHHHHHHCCCCCEEE		26.01-
69PhosphorylationILTNILSSPYFKVQL
HHHHHHCCCCCEEEE		21.85-
77PhosphorylationPYFKVQLYELKTYHE
CCCEEEEEECCCHHH		11.3428152594
82UbiquitinationQLYELKTYHEVVDEI
EEEECCCHHHHHHHC		8.3933845483
90PhosphorylationHEVVDEIYFKVTHVE
HHHHHHCEEEEECCC		8.69-
100UbiquitinationVTHVEPWEKGSRKTA
EECCCCCCCCCCCCC		59.2524816145
101UbiquitinationTHVEPWEKGSRKTAG
ECCCCCCCCCCCCCC		59.3119413330
101AcetylationTHVEPWEKGSRKTAG
ECCCCCCCCCCCCCC		59.3119413330
105UbiquitinationPWEKGSRKTAGQTGM
CCCCCCCCCCCCCCC		44.41-
116UbiquitinationQTGMCGGVRGVGTGG
CCCCCCCCCCCCCCH		2.6733845483
121PhosphorylationGGVRGVGTGGIVSTA
CCCCCCCCCHHHHHH		29.8119413330
150PhosphorylationKQVMGLITHTDSPYI
HHHHHHHCCCCCHHH		24.6220068231
152PhosphorylationVMGLITHTDSPYIRA
HHHHHCCCCCHHHHH		29.5320068231
154PhosphorylationGLITHTDSPYIRALG
HHHCCCCCHHHHHHC		22.2820068231
156PhosphorylationITHTDSPYIRALGFM
HCCCCCHHHHHHCCE		13.6420068231
227UbiquitinationRIPVPVQKNIDQQIK
CCCCCCCCCHHHHHH		56.9833845483
227MalonylationRIPVPVQKNIDQQIK
CCCCCCCCCHHHHHH		56.9832601280
227AcetylationRIPVPVQKNIDQQIK
CCCCCCCCCHHHHHH		56.9819608861
234AcetylationKNIDQQIKTRPRKIK
CCHHHHHHHCCCCCC		33.8625953088
234UbiquitinationKNIDQQIKTRPRKIK
CCHHHHHHHCCCCCC		33.8629967540
245UbiquitinationRKIKKDGKEGAEEID
CCCCCCCHHHHHHHH		64.2124816145
245AcetylationRKIKKDGKEGAEEID
CCCCCCCHHHHHHHH		64.2126051181
253MethylationEGAEEIDRHVERRRS
HHHHHHHHHHHHHHH		41.22115488991
260PhosphorylationRHVERRRSRSPRRSL
HHHHHHHHCCCCCCC		34.9930576142
262PhosphorylationVERRRSRSPRRSLSP
HHHHHHCCCCCCCCC		24.8130576142
266PhosphorylationRSRSPRRSLSPRRSP
HHCCCCCCCCCCCCC		34.1823927012
268PhosphorylationRSPRRSLSPRRSPRR
CCCCCCCCCCCCCCC		20.0130278072
272PhosphorylationRSLSPRRSPRRSRSR
CCCCCCCCCCCCCCC		24.8417081983
276PhosphorylationPRRSPRRSRSRSHHR
CCCCCCCCCCCCCCC		35.5717081983
280PhosphorylationPRRSRSRSHHREGHG
CCCCCCCCCCCCCCC		25.5421406692
288PhosphorylationHHREGHGSSSFDREL
CCCCCCCCCHHHHHH		19.6823401153
289PhosphorylationHREGHGSSSFDRELE
CCCCCCCCHHHHHHH		39.3523401153
290PhosphorylationREGHGSSSFDRELER
CCCCCCCHHHHHHHH		32.6323401153
318PhosphorylationREKERRRSRSIDRGL
HHHHHHHHHHHHHHH		28.6823401153
320PhosphorylationKERRRSRSIDRGLER
HHHHHHHHHHHHHHH		30.0425159151
330PhosphorylationRGLERRRSRSRERHR
HHHHHHHHHHHHHHH		32.5620068231
332PhosphorylationLERRRSRSRERHRSR
HHHHHHHHHHHHHHH		39.4832645325
338PhosphorylationRSRERHRSRSRSRDR
HHHHHHHHHHHHHHC		28.6017081983
340PhosphorylationRERHRSRSRSRDRKG
HHHHHHHHHHHHCCC		35.5420068231
342PhosphorylationRHRSRSRSRDRKGDR
HHHHHHHHHHCCCCH		39.5220068231
345PhosphorylationSRSRSRDRKGDRRDR
HHHHHHHCCCCHHHH		43.6932645325
347PhosphorylationSRSRDRKGDRRDRDR
HHHHHCCCCHHHHHH		34.2532645325
384PhosphorylationEREKERERSRERSKE
HHHHHHHHHHHHHHH		47.4332645325
385PhosphorylationREKERERSRERSKEQ
HHHHHHHHHHHHHHH		33.4720068231
394PhosphorylationERSKEQRSRGEVEEK
HHHHHHHHHHHHHHH		44.3128102081
418PhosphorylationRHRDDKRDSKKEKKH
CCCHHHHHHHHHHHH		71.2332645325
428PhosphorylationKEKKHSRSRSRERKH
HHHHHHHHHHHHHHH		37.3120068231
430PhosphorylationKKHSRSRSRERKHRS
HHHHHHHHHHHHHHH		39.4820068231
437PhosphorylationSRERKHRSRSRSRNA
HHHHHHHHHHHHHHH		34.0417081983
439PhosphorylationERKHRSRSRSRNAGK
HHHHHHHHHHHHHHH		35.5422210691
448PhosphorylationSRNAGKRSRSRSKEK
HHHHHHHHHHHHHHH		37.7920068231
467PhosphorylationKNESKEKSNKRSRSG
HHHHHHHHCHHCCCC		48.9923532336
471PhosphorylationKEKSNKRSRSGSQGR
HHHHCHHCCCCCCCC		32.1926055452
473PhosphorylationKSNKRSRSGSQGRTD
HHCHHCCCCCCCCHH		44.0025159151
475PhosphorylationNKRSRSGSQGRTDSV
CHHCCCCCCCCHHHH		30.6125159151
479PhosphorylationRSGSQGRTDSVEKSK
CCCCCCCHHHHHHHH		39.1828176443
481PhosphorylationGSQGRTDSVEKSKKR
CCCCCHHHHHHHHCC		31.4028176443
485PhosphorylationRTDSVEKSKKREHSP
CHHHHHHHHCCCCCC		29.8822817900
491PhosphorylationKSKKREHSPSKEKSR
HHHCCCCCCCHHHHH		26.5628176443
493PhosphorylationKKREHSPSKEKSRKR
HCCCCCCCHHHHHHH		57.3620068231
503PhosphorylationKSRKRSRSKERSHKR
HHHHHHHHHHHHHCC		39.8622817900
513PhosphorylationRSHKRDHSDSKDQSD
HHHCCCCCCCCCCHH		48.1229632367
515PhosphorylationHKRDHSDSKDQSDKH
HCCCCCCCCCCHHHH		40.9424144214
519PhosphorylationHSDSKDQSDKHDRRR
CCCCCCCHHHHHHHH		59.7824144214
527PhosphorylationDKHDRRRSQSIEQES
HHHHHHHHHHHHHHH		26.8629255136
529PhosphorylationHDRRRSQSIEQESQE
HHHHHHHHHHHHHHH		29.3729255136
534PhosphorylationSQSIEQESQEKQHKN
HHHHHHHHHHHHHCC		43.2522167270
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

Oops, there are no upstream regulatory protein records of PR38B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PR38B_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 PR38B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PR38B_HUMAN !!
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 PR38B_HUMAN

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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
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.

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