DX39A_HUMAN - dbPTM
DX39A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DX39A_HUMAN
UniProt AC O00148
Protein Name ATP-dependent RNA helicase DDX39A
Gene Name DDX39A
Organism Homo sapiens (Human).
Sequence Length 427
Subcellular Localization Nucleus . Cytoplasm . Can translocate to the cytoplasm in the presence of MX1.
Protein Description Isoform 1: Involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus..
Protein Sequence MAEQDVENDLLDYDEEEEPQAPQESTPAPPKKDIKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQIEPVNGQVTVLVMCHTRELAFQISKEYERFSKYMPSVKVSVFFGGLSIKKDEEVLKKNCPHVVVGTPGRILALVRNRSFSLKNVKHFVLDECDKMLEQLDMRRDVQEIFRLTPHEKQCMMFSATLSKDIRPVCRKFMQDPMEVFVDDETKLTLHGLQQYYVKLKDSEKNRKLFDLLDVLEFNQVIIFVKSVQRCMALAQLLVEQNFPAIAIHRGMAQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNVAELPEEIDISTYIEQSR
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------MAEQDVEND
------CCCCHHHCC
24.1322223895
13PhosphorylationVENDLLDYDEEEEPQ
HHCCCCCCCCCCCCC
25.8128355574
25PhosphorylationEPQAPQESTPAPPKK
CCCCCCCCCCCCCCC
34.1523401153
26PhosphorylationPQAPQESTPAPPKKD
CCCCCCCCCCCCCCC
23.7925159151
31UbiquitinationESTPAPPKKDIKGSY
CCCCCCCCCCCCCCE
63.1223000965
31SumoylationESTPAPPKKDIKGSY
CCCCCCCCCCCCCCE
63.1228112733
32UbiquitinationSTPAPPKKDIKGSYV
CCCCCCCCCCCCCEE
71.1523000965
32AcetylationSTPAPPKKDIKGSYV
CCCCCCCCCCCCCEE
71.1525953088
35AcetylationAPPKKDIKGSYVSIH
CCCCCCCCCCEEEEE
52.5219608861
35SumoylationAPPKKDIKGSYVSIH
CCCCCCCCCCEEEEE
52.52-
35UbiquitinationAPPKKDIKGSYVSIH
CCCCCCCCCCEEEEE
52.5223000965
35SumoylationAPPKKDIKGSYVSIH
CCCCCCCCCCEEEEE
52.5228112733
35AcetylationAPPKKDIKGSYVSIH
CCCCCCCCCCEEEEE
52.52-
35UbiquitinationAPPKKDIKGSYVSIH
CCCCCCCCCCEEEEE
52.52-
37PhosphorylationPKKDIKGSYVSIHSS
CCCCCCCCEEEEECC
19.8423927012
38PhosphorylationKKDIKGSYVSIHSSG
CCCCCCCEEEEECCC
13.5923927012
40PhosphorylationDIKGSYVSIHSSGFR
CCCCCEEEEECCCCH
13.3223401153
43PhosphorylationGSYVSIHSSGFRDFL
CCEEEEECCCCHHHH
30.4123927012
44PhosphorylationSYVSIHSSGFRDFLL
CEEEEECCCCHHHHC
27.9923927012
50UbiquitinationSSGFRDFLLKPELLR
CCCCHHHHCCHHHHH
7.6222817900
52AcetylationGFRDFLLKPELLRAI
CCHHHHCCHHHHHHH
38.3025825284
52UbiquitinationGFRDFLLKPELLRAI
CCHHHHCCHHHHHHH
38.3023000965
52AcetylationGFRDFLLKPELLRAI
CCHHHHCCHHHHHHH
38.30-
52UbiquitinationGFRDFLLKPELLRAI
CCHHHHCCHHHHHHH
38.3021890473
52SuccinylationGFRDFLLKPELLRAI
CCHHHHCCHHHHHHH
38.3023954790
52UbiquitinationGFRDFLLKPELLRAI
CCHHHHCCHHHHHHH
38.3021890473
57MethylationLLKPELLRAIVDCGF
HCCHHHHHHHHHCCC
34.59-
62UbiquitinationLLRAIVDCGFEHPSE
HHHHHHHCCCCCCHH
4.6921890473
64UbiquitinationRAIVDCGFEHPSEVQ
HHHHHCCCCCCHHHH
11.0923503661
68UbiquitinationDCGFEHPSEVQHECI
HCCCCCCHHHHHCHH
52.9223503661
78UbiquitinationQHECIPQAILGMDVL
HHCHHCHHHHCHHHH
8.1321890473
89UbiquitinationMDVLCQAKSGMGKTA
HHHHHHHCCCCCHHH
22.9729967540
89UbiquitinationMDVLCQAKSGMGKTA
HHHHHHHCCCCCHHH
22.97-
89AcetylationMDVLCQAKSGMGKTA
HHHHHHHCCCCCHHH
22.9725953088
95UbiquitinationAKSGMGKTAVFVLAT
HCCCCCHHHHHHEEE
23.4821890473
128UbiquitinationTRELAFQISKEYERF
HHHHHHHHHHHHHHH
5.2623000965
130UbiquitinationELAFQISKEYERFSK
HHHHHHHHHHHHHHH
66.9821906983
130UbiquitinationELAFQISKEYERFSK
HHHHHHHHHHHHHHH
66.9821890473
130AcetylationELAFQISKEYERFSK
HHHHHHHHHHHHHHH
66.9826051181
137UbiquitinationKEYERFSKYMPSVKV
HHHHHHHHHCCCCEE
42.7421890473
137UbiquitinationKEYERFSKYMPSVKV
HHHHHHHHHCCCCEE
42.74-
137AcetylationKEYERFSKYMPSVKV
HHHHHHHHHCCCCEE
42.7425953088
138PhosphorylationEYERFSKYMPSVKVS
HHHHHHHHCCCCEEE
17.0429759185
145PhosphorylationYMPSVKVSVFFGGLS
HCCCCEEEEEECCCC
13.9021712546
154SumoylationFFGGLSIKKDEEVLK
EECCCCCCCCHHHHH
51.28-
154UbiquitinationFFGGLSIKKDEEVLK
EECCCCCCCCHHHHH
51.2821890473
154SumoylationFFGGLSIKKDEEVLK
EECCCCCCCCHHHHH
51.2828112733
154UbiquitinationFFGGLSIKKDEEVLK
EECCCCCCCCHHHHH
51.28-
155UbiquitinationFGGLSIKKDEEVLKK
ECCCCCCCCHHHHHH
69.56-
155AcetylationFGGLSIKKDEEVLKK
ECCCCCCCCHHHHHH
69.5626051181
161AcetylationKKDEEVLKKNCPHVV
CCCHHHHHHCCCEEE
47.3023749302
161UbiquitinationKKDEEVLKKNCPHVV
CCCHHHHHHCCCEEE
47.3021906983
161AcetylationKKDEEVLKKNCPHVV
CCCHHHHHHCCCEEE
47.30-
161UbiquitinationKKDEEVLKKNCPHVV
CCCHHHHHHCCCEEE
47.3021890473
162UbiquitinationKDEEVLKKNCPHVVV
CCHHHHHHCCCEEEE
60.6721906983
162UbiquitinationKDEEVLKKNCPHVVV
CCHHHHHHCCCEEEE
60.67-
162SumoylationKDEEVLKKNCPHVVV
CCHHHHHHCCCEEEE
60.6728112733
171PhosphorylationCPHVVVGTPGRILAL
CCEEEECCHHHHHHH
15.8023927012
173UbiquitinationHVVVGTPGRILALVR
EEEECCHHHHHHHHH
29.1521890473
178UbiquitinationTPGRILALVRNRSFS
CHHHHHHHHHCCCCC
3.1322505724
180UbiquitinationGRILALVRNRSFSLK
HHHHHHHHCCCCCCC
33.4221890473
183PhosphorylationLALVRNRSFSLKNVK
HHHHHCCCCCCCCCC
23.8023401153
185PhosphorylationLVRNRSFSLKNVKHF
HHHCCCCCCCCCCEE
39.4130108239
187AcetylationRNRSFSLKNVKHFVL
HCCCCCCCCCCEEHH
59.5019608861
187UbiquitinationRNRSFSLKNVKHFVL
HCCCCCCCCCCEEHH
59.5021906983
187UbiquitinationRNRSFSLKNVKHFVL
HCCCCCCCCCCEEHH
59.50-
190UbiquitinationSFSLKNVKHFVLDEC
CCCCCCCCEEHHHHH
40.4929967540
190UbiquitinationSFSLKNVKHFVLDEC
CCCCCCCCEEHHHHH
40.49-
190AcetylationSFSLKNVKHFVLDEC
CCCCCCCCEEHHHHH
40.4926822725
199UbiquitinationFVLDECDKMLEQLDM
EHHHHHHHHHHHHHH
57.9829967540
199AcetylationFVLDECDKMLEQLDM
EHHHHHHHHHHHHHH
57.9826051181
204UbiquitinationCDKMLEQLDMRRDVQ
HHHHHHHHHHHHHHH
4.0021890473
205UbiquitinationDKMLEQLDMRRDVQE
HHHHHHHHHHHHHHH
28.3921890473
207MethylationMLEQLDMRRDVQEIF
HHHHHHHHHHHHHHH
31.17-
217PhosphorylationVQEIFRLTPHEKQCM
HHHHHHCCCCHHHHH
20.5323312004
221UbiquitinationFRLTPHEKQCMMFSA
HHCCCCHHHHHHEEE
45.8521906983
221UbiquitinationFRLTPHEKQCMMFSA
HHCCCCHHHHHHEEE
45.85-
221AcetylationFRLTPHEKQCMMFSA
HHCCCCHHHHHHEEE
45.8526051181
227PhosphorylationEKQCMMFSATLSKDI
HHHHHHEEEECCCCC
11.4921406692
229PhosphorylationQCMMFSATLSKDIRP
HHHHEEEECCCCCHH
30.3021406692
230UbiquitinationCMMFSATLSKDIRPV
HHHEEEECCCCCHHH
6.3121890473
231PhosphorylationMMFSATLSKDIRPVC
HHEEEECCCCCHHHH
24.7521406692
232UbiquitinationMFSATLSKDIRPVCR
HEEEECCCCCHHHHH
61.36-
240SumoylationDIRPVCRKFMQDPME
CCHHHHHHHCCCCCE
39.81-
240UbiquitinationDIRPVCRKFMQDPME
CCHHHHHHHCCCCCE
39.8123000965
240SumoylationDIRPVCRKFMQDPME
CCHHHHHHHCCCCCE
39.8128112733
240AcetylationDIRPVCRKFMQDPME
CCHHHHHHHCCCCCE
39.8125953088
255AcetylationVFVDDETKLTLHGLQ
EEECCCCEEEEHHHH
37.11156717
255UbiquitinationVFVDDETKLTLHGLQ
EEECCCCEEEEHHHH
37.1122817900
255SumoylationVFVDDETKLTLHGLQ
EEECCCCEEEEHHHH
37.1128112733
264PhosphorylationTLHGLQQYYVKLKDS
EEHHHHHEEEEECCC
9.3928152594
264UbiquitinationTLHGLQQYYVKLKDS
EEHHHHHEEEEECCC
9.3921890473
265PhosphorylationLHGLQQYYVKLKDSE
EHHHHHEEEEECCCH
6.1828152594
267UbiquitinationGLQQYYVKLKDSEKN
HHHHEEEEECCCHHH
33.4333845483
267AcetylationGLQQYYVKLKDSEKN
HHHHEEEEECCCHHH
33.4325953088
269UbiquitinationQQYYVKLKDSEKNRK
HHEEEEECCCHHHHH
54.1923503661
273UbiquitinationVKLKDSEKNRKLFDL
EEECCCHHHHHHHHH
67.0423503661
283UbiquitinationKLFDLLDVLEFNQVI
HHHHHHHHHHHCCCH
5.7921890473
310UbiquitinationAQLLVEQNFPAIAIH
HHHHHHCCCCHHHHH
31.2221890473
329PhosphorylationQEERLSRYQQFKDFQ
HHHHHHHHHHHHHHH
11.8626074081
333AcetylationLSRYQQFKDFQRRIL
HHHHHHHHHHHHHHH
53.9823236377
333UbiquitinationLSRYQQFKDFQRRIL
HHHHHHHHHHHHHHH
53.9823000965
333SumoylationLSRYQQFKDFQRRIL
HHHHHHHHHHHHHHH
53.98-
333SuccinylationLSRYQQFKDFQRRIL
HHHHHHHHHHHHHHH
53.9823954790
338MethylationQFKDFQRRILVATNL
HHHHHHHHHHHHHCC
18.79-
343PhosphorylationQRRILVATNLFGRGM
HHHHHHHHCCCCCCC
25.6021712546
348MethylationVATNLFGRGMDIERV
HHHCCCCCCCCCEEE
29.90-
361PhosphorylationRVNIVFNYDMPEDSD
EEEEEEECCCCCCCC
11.3626552605
367PhosphorylationNYDMPEDSDTYLHRV
ECCCCCCCCCHHHHH
30.1426552605
369PhosphorylationDMPEDSDTYLHRVAR
CCCCCCCCHHHHHHH
31.7526552605
370PhosphorylationMPEDSDTYLHRVARA
CCCCCCCHHHHHHHC
12.9026552605
382PhosphorylationARAGRFGTKGLAITF
HHCCCCCCCCEEEEE
21.16-
383UbiquitinationRAGRFGTKGLAITFV
HCCCCCCCCEEEEEE
52.9133845483
383AcetylationRAGRFGTKGLAITFV
HCCCCCCCCEEEEEE
52.9126051181
391PhosphorylationGLAITFVSDENDAKI
CEEEEEECCCCHHHH
34.7121712546
397AcetylationVSDENDAKILNDVQD
ECCCCHHHHHHHHHH
51.0611793901
397SumoylationVSDENDAKILNDVQD
ECCCCHHHHHHHHHH
51.06-
420PhosphorylationLPEEIDISTYIEQSR
CCCCCCHHHHHHCCC
16.0623663014
421PhosphorylationPEEIDISTYIEQSR-
CCCCCHHHHHHCCC-
28.9323663014
422PhosphorylationEEIDISTYIEQSR--
CCCCHHHHHHCCC--
8.8223663014
426PhosphorylationISTYIEQSR------
HHHHHHCCC------
27.4525159151
426UbiquitinationISTYIEQSR------
HHHHHHCCC------
27.4521890473

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 DX39A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DX39A_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 DX39A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SARNP_HUMANSARNPphysical
16189514
THOC4_HUMANALYREFphysical
17196963
SARNP_HUMANSARNPphysical
17196963
DX39A_HUMANDDX39Aphysical
25416956
SARNP_HUMANSARNPphysical
25416956
CELR1_HUMANCELSR1physical
26186194
FAT3_HUMANFAT3physical
26186194
FAT4_HUMANFAT4physical
26186194
TBA4A_HUMANTUBA4Aphysical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
WDR19_HUMANWDR19physical
26186194
FREM2_HUMANFREM2physical
26186194
GANP_HUMANMCM3APphysical
26186194
PCDH7_HUMANPCDH7physical
26186194
TERF2_HUMANTERF2physical
26186194
CELR2_HUMANCELSR2physical
26186194
BBS7_HUMANBBS7physical
26186194
OST48_HUMANDDOSTphysical
26344197
DX39B_HUMANDDX39Bphysical
26344197
IF6_HUMANEIF6physical
26344197
ETFA_HUMANETFAphysical
26344197
PHOCN_HUMANMOB4physical
26344197
PABP1_HUMANPABPC1physical
26344197
PABP4_HUMANPABPC4physical
26344197
PAWR_HUMANPAWRphysical
26344197
RPN1_HUMANRPN1physical
26344197
TMCO1_HUMANTMCO1physical
26344197
SARNP_HUMANSARNPphysical
21516116
TERF2_HUMANTERF2physical
28514442
FAT4_HUMANFAT4physical
28514442
FAT3_HUMANFAT3physical
28514442
CELR2_HUMANCELSR2physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
TBB3_HUMANTUBB3physical
28514442

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 DX39A_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, 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-35 AND LYS-187, AND MASSSPECTROMETRY.
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-40 AND THR-171, AND MASSSPECTROMETRY.

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