PRP16_HUMAN - dbPTM
PRP16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRP16_HUMAN
UniProt AC Q92620
Protein Name Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
Gene Name DHX38
Organism Homo sapiens (Human).
Sequence Length 1227
Subcellular Localization Nucleus.
Protein Description Probable ATP-binding RNA helicase involved in pre-mRNA splicing..
Protein Sequence MGDTSEDASIHRLEGTDLDCQVGGLICKSKSAASEQHVFKAPAPRPSLLGLDLLASLKRREREEKDDGEDKKKSKVSSYKDWEESKDDQKDAEEEGGDQAGQNIRKDRHYRSARVETPSHPGGVSEEFWERSRQRERERREHGVYASSKEEKDWKKEKSRDRDYDRKRDRDERDRSRHSSRSERDGGSERSSRRNEPESPRHRPKDAATPSRSTWEEEDSGYGSSRRSQWESPSPTPSYRDSERSHRLSTRDRDRSVRGKYSDDTPLPTPSYKYNEWADDRRHLGSTPRLSRGRGRREEGEEGISFDTEEERQQWEDDQRQADRDWYMMDEGYDEFHNPLAYSSEDYVRRREQHLHKQKQKRISAQRRQINEDNERWETNRMLTSGVVHRLEVDEDFEEDNAAKVHLMVHNLVPPFLDGRIVFTKQPEPVIPVKDATSDLAIIARKGSQTVRKHREQKERKKAQHKHWELAGTKLGDIMGVKKEEEPDKAVTEDGKVDYRTEQKFADHMKRKSEASSEFAKKKSILEQRQYLPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVGYAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATMDAEKFAAFFGNVPIFHIPGRTFPVDILFSKTPQEDYVEAAVKQSLQVHLSGAPGDILIFMPGQEDIEVTSDQIVEHLEELENAPALAVLPIYSQLPSDLQAKIFQKAPDGVRKCIVATNIAETSLTVDGIMFVIDSGYCKLKVFNPRIGMDALQIYPISQANANQRSGRAGRTGPGQCFRLYTQSAYKNELLTTTVPEIQRTNLANVVLLLKSLGVQDLLQFHFMDPPPEDNMLNSMYQLWILGALDNTGGLTSTGRLMVEFPLDPALSKMLIVSCDMGCSSEILLIVSMLSVPAIFYRPKGREEESDQIREKFAVPESDHLTYLNVYLQWKNNNYSTIWCNDHFIHAKAMRKVREVRAQLKDIMVQQRMSLASCGTDWDIVRKCICAAYFHQAAKLKGIGEYVNIRTGMPCHLHPTSSLFGMGYTPDYIVYHELVMTTKEYMQCVTAVDGEWLAELGPMFYSVKQAGKSRQENRRRAKEEASAMEEEMALAEEQLRARRQEQEKRSPLGSVRSTKIYTPGRKEQGEPMTPRRTPARFGL
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------MGDTSEDAS
------CCCCCHHCC
59.2019413330
30AcetylationGGLICKSKSAASEQH
CCEEECCCCCCCCCC
29.6127452117
31PhosphorylationGLICKSKSAASEQHV
CEEECCCCCCCCCCC
35.8422210691
34PhosphorylationCKSKSAASEQHVFKA
ECCCCCCCCCCCCCC
37.1924719451
47PhosphorylationKAPAPRPSLLGLDLL
CCCCCCHHHHHHHHH
37.1924719451
56PhosphorylationLGLDLLASLKRRERE
HHHHHHHHHHHHHHH
34.1028450419
58AcetylationLDLLASLKRREREEK
HHHHHHHHHHHHHHC
47.0830588135
74PhosphorylationDGEDKKKSKVSSYKD
CCCCCCHHHCHHHHC
47.3629449344
77PhosphorylationDKKKSKVSSYKDWEE
CCCHHHCHHHHCHHH
31.5229449344
78PhosphorylationKKKSKVSSYKDWEES
CCHHHCHHHHCHHHC
38.9129449344
79PhosphorylationKKSKVSSYKDWEESK
CHHHCHHHHCHHHCH
12.8829449344
85PhosphorylationSYKDWEESKDDQKDA
HHHCHHHCHHHHHHH
29.8422468782
105UbiquitinationDQAGQNIRKDRHYRS
CHHHHHHHCCCCCCC
42.23-
112PhosphorylationRKDRHYRSARVETPS
HCCCCCCCCCEECCC
17.1723312004
117PhosphorylationYRSARVETPSHPGGV
CCCCCEECCCCCCCC
27.5123927012
119PhosphorylationSARVETPSHPGGVSE
CCCEECCCCCCCCCH
50.1323403867
125PhosphorylationPSHPGGVSEEFWERS
CCCCCCCCHHHHHHH
34.3823403867
141UbiquitinationQRERERREHGVYASS
HHHHHHHHHCCCCCC
51.74-
145PhosphorylationERREHGVYASSKEEK
HHHHHCCCCCCHHHH
12.83-
149SumoylationHGVYASSKEEKDWKK
HCCCCCCHHHHHHHH
68.35-
149SumoylationHGVYASSKEEKDWKK
HCCCCCCHHHHHHHH
68.35-
176PhosphorylationDRDERDRSRHSSRSE
CHHHHHHHHHHCHHC
38.3417081983
179PhosphorylationERDRSRHSSRSERDG
HHHHHHHHCHHCCCC
26.7420068231
180PhosphorylationRDRSRHSSRSERDGG
HHHHHHHCHHCCCCC
33.4320068231
182O-linked_GlycosylationRSRHSSRSERDGGSE
HHHHHCHHCCCCCCC
38.6430379171
187UbiquitinationSRSERDGGSERSSRR
CHHCCCCCCCCCCCC
30.53-
188O-linked_GlycosylationRSERDGGSERSSRRN
HHCCCCCCCCCCCCC
35.0530379171
199PhosphorylationSRRNEPESPRHRPKD
CCCCCCCCCCCCCCC
37.6427794612
209PhosphorylationHRPKDAATPSRSTWE
CCCCCCCCCCCCCCC
24.4227422710
211PhosphorylationPKDAATPSRSTWEEE
CCCCCCCCCCCCCCC
34.2128450419
213PhosphorylationDAATPSRSTWEEEDS
CCCCCCCCCCCCCCC
42.0628450419
214PhosphorylationAATPSRSTWEEEDSG
CCCCCCCCCCCCCCC
35.4730576142
220PhosphorylationSTWEEEDSGYGSSRR
CCCCCCCCCCCCCCC
36.8830576142
222PhosphorylationWEEEDSGYGSSRRSQ
CCCCCCCCCCCCCCC
20.1327642862
224PhosphorylationEEDSGYGSSRRSQWE
CCCCCCCCCCCCCCC
16.5230576142
225PhosphorylationEDSGYGSSRRSQWES
CCCCCCCCCCCCCCC
27.6130576142
228PhosphorylationGYGSSRRSQWESPSP
CCCCCCCCCCCCCCC
38.2428450419
232PhosphorylationSRRSQWESPSPTPSY
CCCCCCCCCCCCCCC
27.9325159151
234PhosphorylationRSQWESPSPTPSYRD
CCCCCCCCCCCCCCC
51.1625159151
236PhosphorylationQWESPSPTPSYRDSE
CCCCCCCCCCCCCCH
29.2428450419
238PhosphorylationESPSPTPSYRDSERS
CCCCCCCCCCCCHHH
34.9730576142
239PhosphorylationSPSPTPSYRDSERSH
CCCCCCCCCCCHHHH
21.4628450419
242PhosphorylationPTPSYRDSERSHRLS
CCCCCCCCHHHHCCC
26.3828450419
260AcetylationRDRSVRGKYSDDTPL
CCCCCCCCCCCCCCC
30.8919608861
260MethylationRDRSVRGKYSDDTPL
CCCCCCCCCCCCCCC
30.8919608861
261PhosphorylationDRSVRGKYSDDTPLP
CCCCCCCCCCCCCCC
21.8423312004
262PhosphorylationRSVRGKYSDDTPLPT
CCCCCCCCCCCCCCC
32.2827732954
265PhosphorylationRGKYSDDTPLPTPSY
CCCCCCCCCCCCCCC
31.5421815630
269PhosphorylationSDDTPLPTPSYKYNE
CCCCCCCCCCCCCCC
32.3328387310
271PhosphorylationDTPLPTPSYKYNEWA
CCCCCCCCCCCCCCC
36.4123312004
272PhosphorylationTPLPTPSYKYNEWAD
CCCCCCCCCCCCCCC
20.78-
286PhosphorylationDDRRHLGSTPRLSRG
CCCCCCCCCCCCCCC
41.4123312004
287PhosphorylationDRRHLGSTPRLSRGR
CCCCCCCCCCCCCCC
15.6120068231
289MethylationRHLGSTPRLSRGRGR
CCCCCCCCCCCCCCC
45.44-
291PhosphorylationLGSTPRLSRGRGRRE
CCCCCCCCCCCCCCC
33.6925159151
305PhosphorylationEEGEEGISFDTEEER
CCCCCCCCCCCHHHH
28.1129457462
327PhosphorylationRQADRDWYMMDEGYD
HHHHHCHHHCCCCCC
6.2024043423
333PhosphorylationWYMMDEGYDEFHNPL
HHHCCCCCCCCCCCC
15.3924043423
342PhosphorylationEFHNPLAYSSEDYVR
CCCCCCCCCCHHHHH
22.0324043423
343PhosphorylationFHNPLAYSSEDYVRR
CCCCCCCCCHHHHHH
22.9624043423
344PhosphorylationHNPLAYSSEDYVRRR
CCCCCCCCHHHHHHH
23.0824043423
347PhosphorylationLAYSSEDYVRRREQH
CCCCCHHHHHHHHHH
7.5724043423
361UbiquitinationHLHKQKQKRISAQRR
HHHHHHHHHHHHHHH
59.75-
384PhosphorylationWETNRMLTSGVVHRL
HHHHHHHHHCCEEEE
17.68-
385PhosphorylationETNRMLTSGVVHRLE
HHHHHHHHCCEEEEE
26.1528555341
425SumoylationDGRIVFTKQPEPVIP
CCEEEEECCCCCCEE
53.01-
425SumoylationDGRIVFTKQPEPVIP
CCEEEEECCCCCCEE
53.01-
425UbiquitinationDGRIVFTKQPEPVIP
CCEEEEECCCCCCEE
53.0133845483
434UbiquitinationPEPVIPVKDATSDLA
CCCCEECCCCCCCEE
35.9729967540
437PhosphorylationVIPVKDATSDLAIIA
CEECCCCCCCEEHHH
32.6720873877
438PhosphorylationIPVKDATSDLAIIAR
EECCCCCCCEEHHHH
32.1420873877
448PhosphorylationAIIARKGSQTVRKHR
EHHHHCCCHHHHHHH
26.2223882029
450PhosphorylationIARKGSQTVRKHREQ
HHHCCCHHHHHHHHH
24.7923882029
466UbiquitinationERKKAQHKHWELAGT
HHHHHHHHHHHHHCC
38.0329967540
478UbiquitinationAGTKLGDIMGVKKEE
HCCHHHHHCCCCCCC
2.16-
482SumoylationLGDIMGVKKEEEPDK
HHHHCCCCCCCCCCC
49.06-
482SumoylationLGDIMGVKKEEEPDK
HHHHCCCCCCCCCCC
49.0628112733
483SumoylationGDIMGVKKEEEPDKA
HHHCCCCCCCCCCCC
68.8728112733
488UbiquitinationVKKEEEPDKAVTEDG
CCCCCCCCCCCCCCC
55.6224816145
504SumoylationVDYRTEQKFADHMKR
CCHHHHHHHHHHHHH
35.97-
504SumoylationVDYRTEQKFADHMKR
CCHHHHHHHHHHHHH
35.9728112733
504UbiquitinationVDYRTEQKFADHMKR
CCHHHHHHHHHHHHH
35.9729967540
510UbiquitinationQKFADHMKRKSEASS
HHHHHHHHHHHHHHH
53.94-
513PhosphorylationADHMKRKSEASSEFA
HHHHHHHHHHHHHHH
42.2926462736
516PhosphorylationMKRKSEASSEFAKKK
HHHHHHHHHHHHHHH
26.7526270265
517PhosphorylationKRKSEASSEFAKKKS
HHHHHHHHHHHHHHH
43.7226270265
521AcetylationEASSEFAKKKSILEQ
HHHHHHHHHHHHHHH
67.0819608861
5232-HydroxyisobutyrylationSSEFAKKKSILEQRQ
HHHHHHHHHHHHHHC
41.86-
523UbiquitinationSSEFAKKKSILEQRQ
HHHHHHHHHHHHHHC
41.8624816145
560UbiquitinationVVGETGSGKTTQLTQ
EEECCCCCCHHHHHH
32.4524816145
562PhosphorylationGETGSGKTTQLTQYL
ECCCCCCHHHHHHHH
24.2526552605
563PhosphorylationETGSGKTTQLTQYLH
CCCCCCHHHHHHHHC
25.6826552605
566PhosphorylationSGKTTQLTQYLHEDG
CCCHHHHHHHHCCCC
12.8326552605
568PhosphorylationKTTQLTQYLHEDGYT
CHHHHHHHHCCCCCC
12.5626552605
574PhosphorylationQYLHEDGYTDYGMIG
HHHCCCCCCCCCEEC
14.5726552605
575PhosphorylationYLHEDGYTDYGMIGC
HHCCCCCCCCCEECC
28.4226552605
577PhosphorylationHEDGYTDYGMIGCTQ
CCCCCCCCCEECCCC
10.7826552605
583PhosphorylationDYGMIGCTQPRRVAA
CCCEECCCCHHHHHH
36.0726552605
595AcetylationVAAMSVAKRVSEEMG
HHHHHHHHHHHHHHC
51.6926051181
595UbiquitinationVAAMSVAKRVSEEMG
HHHHHHHHHHHHHHC
51.6924816145
637PhosphorylationDGILLRESLREADLD
HCHHHCHHHHHCCCC
26.7128188228
679AcetylationVARRSDLKLIVTSAT
HHHHCCCEEEEEECC
40.9519820289
687SulfoxidationLIVTSATMDAEKFAA
EEEEECCCCHHHHHH
4.6121406390
708PhosphorylationIFHIPGRTFPVDILF
EEECCCCCCCCEEEE
37.90-
716PhosphorylationFPVDILFSKTPQEDY
CCCEEEEECCCCHHH
31.9724719451
717UbiquitinationPVDILFSKTPQEDYV
CCEEEEECCCCHHHH
57.82-
758UbiquitinationEDIEVTSDQIVEHLE
CCCEECHHHHHHHHH
32.6222505724
793UbiquitinationLQAKIFQKAPDGVRK
HHHHHHHHCCCCHHE
51.6522505724
794UbiquitinationQAKIFQKAPDGVRKC
HHHHHHHCCCCHHEE
9.1627667366
805PhosphorylationVRKCIVATNIAETSL
HHEEEEEECCCCCEE
19.10-
829UbiquitinationDSGYCKLKVFNPRIG
ECCCEEEEECCCCCC
30.2127667366
860PhosphorylationRSGRAGRTGPGQCFR
CCCCCCCCCCCHHHH
46.9724719451
875UbiquitinationLYTQSAYKNELLTTT
EEECCHHCCCCCCCC
43.60-
1014UbiquitinationDHLTYLNVYLQWKNN
CCCEEEEEEEEECCC
4.6924816145
1049UbiquitinationREVRAQLKDIMVQQR
HHHHHHHHHHHHHHH
32.8824816145
1058PhosphorylationIMVQQRMSLASCGTD
HHHHHHHHHHHCCCC
23.9918491316
1064PhosphorylationMSLASCGTDWDIVRK
HHHHHCCCCHHHHHH
37.94-
1083AcetylationAYFHQAAKLKGIGEY
HHHHHHHHCCCCCCC
54.4719820299
1166SumoylationQENRRRAKEEASAME
HHHHHHHHHHHHHHH
55.03-
1166SumoylationQENRRRAKEEASAME
HHHHHHHHHHHHHHH
55.0328112733
1166UbiquitinationQENRRRAKEEASAME
HHHHHHHHHHHHHHH
55.03-
1172SulfoxidationAKEEASAMEEEMALA
HHHHHHHHHHHHHHH
6.5321406390
1194PhosphorylationRQEQEKRSPLGSVRS
HHHHHHCCCCCCCCC
35.2325159151
1198PhosphorylationEKRSPLGSVRSTKIY
HHCCCCCCCCCCEEE
23.2620873877
1201PhosphorylationSPLGSVRSTKIYTPG
CCCCCCCCCEEECCC
31.7125137130
1202PhosphorylationPLGSVRSTKIYTPGR
CCCCCCCCEEECCCC
15.7625137130
1206PhosphorylationVRSTKIYTPGRKEQG
CCCCEEECCCCCCCC
23.8021815630
1217PhosphorylationKEQGEPMTPRRTPAR
CCCCCCCCCCCCCCC
25.1021815630
1221PhosphorylationEPMTPRRTPARFGL-
CCCCCCCCCCCCCC-
23.6828555341

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 PRP16_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRP16_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 PRP16_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBM8A_HUMANRBM8Aphysical
22939629
SLU7_HUMANSLU7physical
22939629
DX39B_HUMANDDX39Bphysical
22939629
SNW1_HUMANSNW1physical
22939629
CWC27_HUMANCWC27physical
22939629
RS20_HUMANRPS20physical
22939629
RBBP5_HUMANRBBP5physical
22939629
U2AF1_HUMANU2AF1physical
22365833
RBM10_HUMANRBM10physical
22365833
MFAP1_HUMANMFAP1physical
22365833
DHX16_HUMANDHX16physical
22365833
GPKOW_HUMANGPKOWphysical
22365833
COPA_HUMANCOPAphysical
22863883
PSB8_HUMANPSMB8physical
22863883
CLH1_HUMANCLTCphysical
26344197
PITH1_HUMANPITHD1physical
26344197

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 PRP16_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-260, 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-1194, AND MASSSPECTROMETRY.

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