DDX3Y_HUMAN - dbPTM
DDX3Y_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX3Y_HUMAN
UniProt AC O15523
Protein Name ATP-dependent RNA helicase DDX3Y
Gene Name DDX3Y
Organism Homo sapiens (Human).
Sequence Length 660
Subcellular Localization Cytoplasm . Nucleus . Shuttles between the nucleus and the cytoplasm in an XPO1-dependent manner.
Protein Description Probable ATP-dependent RNA helicase. May play a role in spermatogenesis..
Protein Sequence MSHVVVKNDPELDQQLANLDLNSEKQSGGASTASKGRYIPPHLRNREASKGFHDKDSSGWSCSKDKDAYSSFGSRDSRGKPGYFSERGSGSRGRFDDRGRSDYDGIGNRERPGFGRFERSGHSRWCDKSVEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALKAVKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLVEAKQEVPSWLENMAYEHHYKGGSRGRSKSNRFSGGFGARDYRQSSGSSSSGFGASRGSSSRSGGGGYGNSRGFGGGGYGGFYNSDGYGGNYNSQGVDWWGN
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------MSHVVVKND
------CCCEEECCC
25.62-
23PhosphorylationLANLDLNSEKQSGGA
HHCCCCCCCCCCCCC
54.1730622161
25UbiquitinationNLDLNSEKQSGGAST
CCCCCCCCCCCCCCC
49.97-
34PhosphorylationSGGASTASKGRYIPP
CCCCCCCCCCCCCCH
35.4122210691
38PhosphorylationSTASKGRYIPPHLRN
CCCCCCCCCCHHHCC
26.8422210691
49PhosphorylationHLRNREASKGFHDKD
HHCCCHHHCCCCCCC
28.6720068231
55AcetylationASKGFHDKDSSGWSC
HHCCCCCCCCCCCCC
51.44-
66MalonylationGWSCSKDKDAYSSFG
CCCCCCCHHHHHCCC
48.2526320211
66MethylationGWSCSKDKDAYSSFG
CCCCCCCHHHHHCCC
48.25-
66UbiquitinationGWSCSKDKDAYSSFG
CCCCCCCHHHHHCCC
48.25-
69PhosphorylationCSKDKDAYSSFGSRD
CCCCHHHHHCCCCCC
18.2525159151
70PhosphorylationSKDKDAYSSFGSRDS
CCCHHHHHCCCCCCC
22.4027273156
71PhosphorylationKDKDAYSSFGSRDSR
CCHHHHHCCCCCCCC
22.4323401153
74PhosphorylationDAYSSFGSRDSRGKP
HHHHCCCCCCCCCCC
30.7923401153
75MethylationAYSSFGSRDSRGKPG
HHHCCCCCCCCCCCC
46.43-
77PhosphorylationSSFGSRDSRGKPGYF
HCCCCCCCCCCCCCC
41.6529083192
78MethylationSFGSRDSRGKPGYFS
CCCCCCCCCCCCCCC
62.54-
85PhosphorylationRGKPGYFSERGSGSR
CCCCCCCCCCCCCCC
20.2123401153
87MethylationKPGYFSERGSGSRGR
CCCCCCCCCCCCCCC
43.30-
89PhosphorylationGYFSERGSGSRGRFD
CCCCCCCCCCCCCCC
39.5524961811
98MethylationSRGRFDDRGRSDYDG
CCCCCCCCCCCCCCC
44.24-
100MethylationGRFDDRGRSDYDGIG
CCCCCCCCCCCCCCC
27.52-
101PhosphorylationRFDDRGRSDYDGIGN
CCCCCCCCCCCCCCC
43.2623401153
103PhosphorylationDDRGRSDYDGIGNRE
CCCCCCCCCCCCCCC
19.8121609022
109MethylationDYDGIGNRERPGFGR
CCCCCCCCCCCCCCC
35.77-
129PhosphorylationHSRWCDKSVEDDWSK
CCCCCCCCCCCCCCC
19.93-
135PhosphorylationKSVEDDWSKPLPPSE
CCCCCCCCCCCCHHH
31.2424719451
150PhosphorylationRLEQELFSGGNTGIN
HHHHHHHCCCCCCCC
59.4221815630
154PhosphorylationELFSGGNTGINFEKY
HHHCCCCCCCCCCCC
42.5920873877
161PhosphorylationTGINFEKYDDIPVEA
CCCCCCCCCCCCCCC
16.20-
181PhosphorylationPPHIENFSDIDMGEI
CCCCCCCCCCCCCHH
45.28-
198PhosphorylationGNIELTRYTRPTPVQ
EEEEEEEECCCCCCH
11.2328152594
199PhosphorylationNIELTRYTRPTPVQK
EEEEEEECCCCCCHH
27.2121406692
202PhosphorylationLTRYTRPTPVQKHAI
EEEECCCCCCHHCCC
32.5728152594
203UbiquitinationTRYTRPTPVQKHAIP
EEECCCCCCHHCCCC
29.26-
206UbiquitinationTRPTPVQKHAIPIIK
CCCCCCHHCCCCEEC
34.9321890473
206UbiquitinationTRPTPVQKHAIPIIK
CCCCCCHHCCCCEEC
34.9321890473
213UbiquitinationKHAIPIIKGKRDLMA
HCCCCEECCCHHHHH
60.13-
221GlutathionylationGKRDLMACAQTGSGK
CCHHHHHHCCCCCCH
1.4722555962
224PhosphorylationDLMACAQTGSGKTAA
HHHHHCCCCCCHHHH
18.1320873877
226PhosphorylationMACAQTGSGKTAAFL
HHHCCCCCCHHHHHH
40.2720873877
229PhosphorylationAQTGSGKTAAFLLPI
CCCCCCHHHHHHHHH
27.09-
247UbiquitinationIYTDGPGEALKAVKE
HHCCCCCHHHHHHHH
54.7021890473
250UbiquitinationDGPGEALKAVKENGR
CCCCHHHHHHHHHCC
59.1721890473
258PhosphorylationAVKENGRYGRRKQYP
HHHHHCCCCCCCCCC
19.18-
259UbiquitinationVKENGRYGRRKQYPI
HHHHCCCCCCCCCCC
22.89-
262UbiquitinationNGRYGRRKQYPISLV
HCCCCCCCCCCCEEE
53.4721890473
262UbiquitinationNGRYGRRKQYPISLV
HCCCCCCCCCCCEEE
53.4721890473
264PhosphorylationRYGRRKQYPISLVLA
CCCCCCCCCCEEEEC
12.9320090780
267PhosphorylationRRKQYPISLVLAPTR
CCCCCCCEEEECCCH
14.1228152594
281PhosphorylationRELAVQIYEEARKFS
HHHHHHHHHHHHHCC
7.2228152594
288PhosphorylationYEEARKFSYRSRVRP
HHHHHHCCHHHCCCC
23.7524144214
289PhosphorylationEEARKFSYRSRVRPC
HHHHHCCHHHCCCCE
18.7524144214
291PhosphorylationARKFSYRSRVRPCVV
HHHCCHHHCCCCEEE
27.2224144214
296GlutathionylationYRSRVRPCVVYGGAD
HHHCCCCEEEECCCC
1.9622555962
299PhosphorylationRVRPCVVYGGADIGQ
CCCCEEEECCCCHHH
6.8828152594
313MethylationQQIRDLERGCHLLVA
HHHHHHHCCCEEEEE
61.41-
315S-nitrosocysteineIRDLERGCHLLVATP
HHHHHCCCEEEEECC
2.27-
315GlutathionylationIRDLERGCHLLVATP
HHHHHCCCEEEEECC
2.2722555962
315S-nitrosylationIRDLERGCHLLVATP
HHHHHCCCEEEEECC
2.2719483679
315S-palmitoylationIRDLERGCHLLVATP
HHHHHCCCEEEEECC
2.2726865113
321PhosphorylationGCHLLVATPGRLVDM
CCEEEEECCCHHHHH
20.8525159151
330UbiquitinationGRLVDMMERGKIGLD
CHHHHHHHCCCCCHH
52.20-
333UbiquitinationVDMMERGKIGLDFCK
HHHHHCCCCCHHHHH
39.5621890473
337UbiquitinationERGKIGLDFCKYLVL
HCCCCCHHHHHHHHC
41.50-
339GlutathionylationGKIGLDFCKYLVLDE
CCCCHHHHHHHHCCH
2.5722555962
340UbiquitinationKIGLDFCKYLVLDEA
CCCHHHHHHHHCCHH
41.43-
341PhosphorylationIGLDFCKYLVLDEAD
CCHHHHHHHHCCHHH
11.8328152594
360MethylationMGFEPQIRRIVEQDT
CCCHHHHHHHHHHCC
19.61-
368UbiquitinationRIVEQDTMPPKGVRH
HHHHHCCCCCCCCCE
7.81-
371UbiquitinationEQDTMPPKGVRHTMM
HHCCCCCCCCCEEEE
65.25-
380PhosphorylationVRHTMMFSATFPKEI
CCEEEEEECCCCHHH
14.4328450419
382PhosphorylationHTMMFSATFPKEIQM
EEEEEECCCCHHHHH
38.9928450419
408PhosphorylationLAVGRVGSTSENITQ
HHCCCCCCCCCCCCE
26.3825159151
409PhosphorylationAVGRVGSTSENITQK
HCCCCCCCCCCCCEE
33.8528450419
410PhosphorylationVGRVGSTSENITQKV
CCCCCCCCCCCCEEE
30.2828450419
414PhosphorylationGSTSENITQKVVWVE
CCCCCCCCEEEEEEC
33.6430108239
436PhosphorylationLLDILGATGSDSLTL
HHHHHCCCCCCEEEE
35.11-
438PhosphorylationDILGATGSDSLTLVF
HHHCCCCCCEEEEEE
21.48-
440PhosphorylationLGATGSDSLTLVFVE
HCCCCCCEEEEEEEE
25.58-
447UbiquitinationSLTLVFVETKKGADS
EEEEEEEEECCCCCC
43.37-
450UbiquitinationLVFVETKKGADSLED
EEEEEECCCCCCHHH
67.75-
454PhosphorylationETKKGADSLEDFLYH
EECCCCCCHHHHHHC
32.8828450419
460PhosphorylationDSLEDFLYHEGYACT
CCHHHHHHCCCCCCC
9.6020090780
464PhosphorylationDFLYHEGYACTSIHG
HHHHCCCCCCCCCCC
8.7730108239
467PhosphorylationYHEGYACTSIHGDRS
HCCCCCCCCCCCCCC
23.6520873877
468PhosphorylationHEGYACTSIHGDRSQ
CCCCCCCCCCCCCCH
16.6920873877
486UbiquitinationEEALHQFRSGKSPIL
HHHHHHHHCCCCCHH
37.62-
487PhosphorylationEALHQFRSGKSPILV
HHHHHHHCCCCCHHH
52.4330108239
489UbiquitinationLHQFRSGKSPILVAT
HHHHHCCCCCHHHHH
55.06-
490PhosphorylationHQFRSGKSPILVATA
HHHHCCCCCHHHHHH
22.2430108239
496PhosphorylationKSPILVATAVAARGL
CCCHHHHHHHHHCCC
17.7428857561
518PhosphorylationVINFDLPSDIEEYVH
EEECCCCCCHHHHHH
59.5228450419
541PhosphorylationGNLGLATSFFNEKNM
CCCHHCHHHHCCCCC
23.4128857561
543UbiquitinationLGLATSFFNEKNMNI
CHHCHHHHCCCCCCC
13.30-
546UbiquitinationATSFFNEKNMNITKD
CHHHHCCCCCCCCHH
63.7021890473
549UbiquitinationFFNEKNMNITKDLLD
HHCCCCCCCCHHHHH
48.44-
552UbiquitinationEKNMNITKDLLDLLV
CCCCCCCHHHHHHHH
42.4521890473
567PhosphorylationEAKQEVPSWLENMAY
HHHHHCCHHHHHHHH
49.8520873877
574PhosphorylationSWLENMAYEHHYKGG
HHHHHHHHHCCCCCC
12.6729978859
578PhosphorylationNMAYEHHYKGGSRGR
HHHHHCCCCCCCCCC
17.1528796482
588PhosphorylationGSRGRSKSNRFSGGF
CCCCCCCCCCCCCCC
34.1923403867
590MethylationRGRSKSNRFSGGFGA
CCCCCCCCCCCCCCC
33.91-
592PhosphorylationRSKSNRFSGGFGARD
CCCCCCCCCCCCCCC
34.4729255136
598MethylationFSGGFGARDYRQSSG
CCCCCCCCCCCCCCC
41.70-
600PhosphorylationGGFGARDYRQSSGSS
CCCCCCCCCCCCCCC
12.6622210691
603PhosphorylationGARDYRQSSGSSSSG
CCCCCCCCCCCCCCC
27.8923312004
604PhosphorylationARDYRQSSGSSSSGF
CCCCCCCCCCCCCCC
34.0620164059
606PhosphorylationDYRQSSGSSSSGFGA
CCCCCCCCCCCCCCC
29.0628857561
607PhosphorylationYRQSSGSSSSGFGAS
CCCCCCCCCCCCCCC
31.8628857561
608PhosphorylationRQSSGSSSSGFGASR
CCCCCCCCCCCCCCC
35.8625278378
609PhosphorylationQSSGSSSSGFGASRG
CCCCCCCCCCCCCCC
39.8422210691
614PhosphorylationSSSGFGASRGSSSRS
CCCCCCCCCCCCCCC
37.2425278378
615MethylationSSGFGASRGSSSRSG
CCCCCCCCCCCCCCC
48.78-
629PhosphorylationGGGGYGNSRGFGGGG
CCCCCCCCCCCCCCC
29.4425367160
630MethylationGGGYGNSRGFGGGGY
CCCCCCCCCCCCCCC
48.75-
637PhosphorylationRGFGGGGYGGFYNSD
CCCCCCCCCCCCCCC
19.83-
643PhosphorylationGYGGFYNSDGYGGNY
CCCCCCCCCCCCCCC
22.4928348404
646PhosphorylationGFYNSDGYGGNYNSQ
CCCCCCCCCCCCCCC
27.1824719451
650PhosphorylationSDGYGGNYNSQGVDW
CCCCCCCCCCCCCCC
21.3327251275
652PhosphorylationGYGGNYNSQGVDWWG
CCCCCCCCCCCCCCC
20.2528348404

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
592SPhosphorylationKinaseAURKBQ96GD4
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX3Y_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 DDX3Y_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNB2_HUMANCCNB2physical
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 DDX3Y_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-592, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-69, AND MASSSPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-69, AND MASSSPECTROMETRY.

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