PR38A_HUMAN - dbPTM
PR38A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PR38A_HUMAN
UniProt AC Q8NAV1
Protein Name Pre-mRNA-splicing factor 38A
Gene Name PRPF38A
Organism Homo sapiens (Human).
Sequence Length 312
Subcellular Localization Nucleus .
Protein Description May be required for pre-mRNA splicing..
Protein Sequence MANRTVKDAHSIHGTNPQYLVEKIIRTRIYESKYWKEECFGLTAELVVDKAMELRFVGGVYGGNIKPTPFLCLTLKMLQIQPEKDIIVEFIKNEDFKYVRMLGALYMRLTGTAIDCYKYLEPLYNDYRKIKSQNRNGEFELMHVDEFIDELLHSERVCDIILPRLQKRYVLEEAEQLEPRVSALEEDMDDVESSEEEEEEDEKLERVPSPDHRRRSYRDLDKPRRSPTLRYRRSRSRSPRRRSRSPKRRSPSPRRERHRSKSPRRHRSRSRDRRHRSRSKSPGHHRSHRHRSHSKSPERSKKSHKKSRRGNE
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
7Ubiquitination-MANRTVKDAHSIHG
-CCCCCCCCCHHHCC		48.8929967540
7Methylation-MANRTVKDAHSIHG
-CCCCCCCCCHHHCC		48.89115975741
11PhosphorylationRTVKDAHSIHGTNPQ
CCCCCCHHHCCCCHH		20.2823401153
15PhosphorylationDAHSIHGTNPQYLVE
CCHHHCCCCHHHHHH		29.5720873877
22 (in isoform 2)Phosphorylation-35.62-
23AcetylationNPQYLVEKIIRTRIY
CHHHHHHHHHHHHHH		35.6319608861
23UbiquitinationNPQYLVEKIIRTRIY
CHHHHHHHHHHHHHH		35.6322817900
23 (in isoform 1)Ubiquitination-35.6321890473
39 (in isoform 2)Phosphorylation-3.25-
66UbiquitinationGVYGGNIKPTPFLCL
CCCCCCCCCCHHHHE		47.00-
68PhosphorylationYGGNIKPTPFLCLTL
CCCCCCCCHHHHEEH		22.9820068231
73 (in isoform 2)Phosphorylation-7.36-
74PhosphorylationPTPFLCLTLKMLQIQ
CCHHHHEEHHHHHCC		24.2820068231
75 (in isoform 2)Phosphorylation-1.66-
92 (in isoform 2)Phosphorylation-60.65-
92SumoylationDIIVEFIKNEDFKYV
CEEEEECCCCCHHHH		60.65-
92AcetylationDIIVEFIKNEDFKYV
CEEEEECCCCCHHHH		60.6526051181
92SumoylationDIIVEFIKNEDFKYV
CEEEEECCCCCHHHH		60.65-
94 (in isoform 2)Phosphorylation-60.88-
97UbiquitinationFIKNEDFKYVRMLGA
ECCCCCHHHHHHHHH		55.98-
97AcetylationFIKNEDFKYVRMLGA
ECCCCCHHHHHHHHH		55.9825825284
105 (in isoform 2)Phosphorylation-3.07-
107 (in isoform 2)Phosphorylation-2.70-
109 (in isoform 2)Phosphorylation-2.70-
118AcetylationGTAIDCYKYLEPLYN
CCHHHHHHHHHHHHH		50.0926051181
118UbiquitinationGTAIDCYKYLEPLYN
CCHHHHHHHHHHHHH		50.09-
129UbiquitinationPLYNDYRKIKSQNRN
HHHHCHHHHHHCCCC		48.5429967540
158GlutathionylationLLHSERVCDIILPRL
HHCHHCCHHHHHHHH		3.7822555962
169PhosphorylationLPRLQKRYVLEEAEQ
HHHHHHHHHHHHHHH		19.2018452278
182PhosphorylationEQLEPRVSALEEDMD
HHHCHHHHHHHHCHH		28.5423927012
193PhosphorylationEDMDDVESSEEEEEE
HCHHHHHCCHHHHHH		42.7923927012
194PhosphorylationDMDDVESSEEEEEED
CHHHHHCCHHHHHHH		35.2123927012
209PhosphorylationEKLERVPSPDHRRRS
HHHHCCCCCCHHCCC		39.8529255136
216PhosphorylationSPDHRRRSYRDLDKP
CCCHHCCCCCCCCCC		23.7828355574
217PhosphorylationPDHRRRSYRDLDKPR
CCHHCCCCCCCCCCC		13.3129214152
226PhosphorylationDLDKPRRSPTLRYRR
CCCCCCCCCCHHHHH		24.4222167270
228PhosphorylationDKPRRSPTLRYRRSR
CCCCCCCCHHHHHHH		25.7222167270
231PhosphorylationRRSPTLRYRRSRSRS
CCCCCHHHHHHHCCC		17.3126074081
234PhosphorylationPTLRYRRSRSRSPRR
CCHHHHHHHCCCCCC		26.1322468782
236PhosphorylationLRYRRSRSRSPRRRS
HHHHHHHCCCCCCCC		38.0530576142
238PhosphorylationYRRSRSRSPRRRSRS
HHHHHCCCCCCCCCC		24.8130576142
243PhosphorylationSRSPRRRSRSPKRRS
CCCCCCCCCCCCCCC		34.9930576142
245PhosphorylationSPRRRSRSPKRRSPS
CCCCCCCCCCCCCCC		35.7030576142
250PhosphorylationSRSPKRRSPSPRRER
CCCCCCCCCCHHHHH		33.4927273156
252PhosphorylationSPKRRSPSPRRERHR
CCCCCCCCHHHHHHH		32.0827273156
260PhosphorylationPRRERHRSKSPRRHR
HHHHHHHCCCCHHHH		31.2130576142
262PhosphorylationRERHRSKSPRRHRSR
HHHHHCCCCHHHHHH		25.5330576142
268PhosphorylationKSPRRHRSRSRDRRH
CCCHHHHHHHHHHHH		28.6020068231
270PhosphorylationPRRHRSRSRDRRHRS
CHHHHHHHHHHHHHH		39.5220068231
277PhosphorylationSRDRRHRSRSKSPGH
HHHHHHHHHCCCCCC		34.4830576142
279PhosphorylationDRRHRSRSKSPGHHR
HHHHHHHCCCCCCCH		38.4422167270
281PhosphorylationRHRSRSKSPGHHRSH
HHHHHCCCCCCCHHH		37.0422167270
287PhosphorylationKSPGHHRSHRHRSHS
CCCCCCHHHHCCCCC		22.1020068231
292PhosphorylationHRSHRHRSHSKSPER
CHHHHCCCCCCCHHH		26.4524300666
294PhosphorylationSHRHRSHSKSPERSK
HHHCCCCCCCHHHHH		35.7524300666
296PhosphorylationRHRSHSKSPERSKKS
HCCCCCCCHHHHHHH		34.7024300666
300PhosphorylationHSKSPERSKKSHKKS
CCCCHHHHHHHHHCC		42.6530622161
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 PR38A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PR38A_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 PR38A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF3C1_HUMANGTF3C1physical
16169070
DPOA2_HUMANPOLA2physical
16169070
A4_HUMANAPPphysical
21832049
U2AF1_HUMANU2AF1physical
22365833
CHERP_HUMANCHERPphysical
22365833
RBM39_HUMANRBM39physical
22365833
SRSF3_HUMANSRSF3physical
22365833
PR38A_HUMANPRPF38Aphysical
22365833
DHX8_HUMANDHX8physical
22365833
RNPS1_HUMANRNPS1physical
22365833
PPIG_HUMANPPIGphysical
22365833
SRSF4_HUMANSRSF4physical
22365833
ZCH10_HUMANZCCHC10physical
22365833
SRPK1_HUMANSRPK1physical
22365833
SRPK2_HUMANSRPK2physical
22365833
JMJD6_HUMANJMJD6physical
23455924
ANM5_HUMANPRMT5physical
23455924
CSK2B_HUMANCSNK2Bphysical
26344197
MFAP1_HUMANMFAP1physical
26344197
SRSF3_HUMANSRSF3physical
27173435
MFAP1_HUMANMFAP1physical
27173435
KTU_HUMANDNAAF2physical
27173435
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 PR38A_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-23, 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-193 AND SER-194, ANDMASS 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-194, ANDMASS 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-193; SER-194 ANDSER-209, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-194, 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-209 AND SER-226, 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-193; SER-194; SER-209;THR-228; SER-260; SER-262; SER-279 AND SER-281, AND MASS SPECTROMETRY.

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