DDX50_HUMAN - dbPTM
DDX50_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX50_HUMAN
UniProt AC Q9BQ39
Protein Name ATP-dependent RNA helicase DDX50
Gene Name DDX50
Organism Homo sapiens (Human).
Sequence Length 737
Subcellular Localization Nucleus, nucleolus .
Protein Description
Protein Sequence MPGKLLWGDIMELEAPLEESESQKKERQKSDRRKSRHHYDSDEKSETRENGVTDDLDAPKAKKSKMKEKLNGDTEEGFNRLSDEFSKSHKSRRKDLPNGDIDEYEKKSKRVSSLDTSTHKSSDNKLEETLTREQKEGAFSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRKLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVDLVGKMTQKAATTVEHLAIQCHWSQRPAVIGDVLQVYSGSEGRAIIFCETKKNVTEMAMNPHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQLRYVEQKAGITFKRVGVPSTMDLVKSKSMDAIRSLASVSYAAVDFFRPSAQRLIEEKGAVDALAAALAHISGASSFEPRSLITSDKGFVTMTLESLEEIQDVSCAWKELNRKLSSNAVSQITRMCLLKGNMGVCFDVPTTESERLQAEWHDSDWILSVPAKLPEIEEYYDGNTSSNSRQRSGWSSGRSGRSGRSGGRSGGRSGRQSRQGSRSGSRQDGRRRSGNRNRSRSGGHKRSFD
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
20PhosphorylationLEAPLEESESQKKER
EECCCCCCHHHHHHH
32.9227690223
22PhosphorylationAPLEESESQKKERQK
CCCCCCHHHHHHHHH
57.4925627689
35PhosphorylationQKSDRRKSRHHYDSD
HHHHHHHHHHCCCCC
34.7321857030
39PhosphorylationRRKSRHHYDSDEKSE
HHHHHHCCCCCCCCC
15.8323927012
41PhosphorylationKSRHHYDSDEKSETR
HHHHCCCCCCCCCCH
40.2723401153
42UbiquitinationSRHHYDSDEKSETRE
HHHCCCCCCCCCCHH
65.5324816145
45PhosphorylationHYDSDEKSETRENGV
CCCCCCCCCCHHCCC
42.0028355574
47PhosphorylationDSDEKSETRENGVTD
CCCCCCCCHHCCCCC
50.8325159151
53PhosphorylationETRENGVTDDLDAPK
CCHHCCCCCCCCCHH
25.7923927012
74PhosphorylationKEKLNGDTEEGFNRL
HHHHCCCCHHHHHHH
37.0222617229
82PhosphorylationEEGFNRLSDEFSKSH
HHHHHHHHHHHHHHH
31.6830266825
86PhosphorylationNRLSDEFSKSHKSRR
HHHHHHHHHHHHHHC
31.0730266825
87UbiquitinationRLSDEFSKSHKSRRK
HHHHHHHHHHHHHCC
63.0029967540
87AcetylationRLSDEFSKSHKSRRK
HHHHHHHHHHHHHCC
63.0025953088
94AcetylationKSHKSRRKDLPNGDI
HHHHHHCCCCCCCCH
63.617822435
104PhosphorylationPNGDIDEYEKKSKRV
CCCCHHHHHHHHHCH
29.33-
106AcetylationGDIDEYEKKSKRVSS
CCHHHHHHHHHCHHC
62.5426051181
107UbiquitinationDIDEYEKKSKRVSSL
CHHHHHHHHHCHHCC
49.6324816145
112PhosphorylationEKKSKRVSSLDTSTH
HHHHHCHHCCCCCCC
29.2625159151
113PhosphorylationKKSKRVSSLDTSTHK
HHHHCHHCCCCCCCC
27.6625159151
116PhosphorylationKRVSSLDTSTHKSSD
HCHHCCCCCCCCCCC
40.6024732914
117PhosphorylationRVSSLDTSTHKSSDN
CHHCCCCCCCCCCCC
28.3424732914
118PhosphorylationVSSLDTSTHKSSDNK
HHCCCCCCCCCCCCH
35.1024732914
120UbiquitinationSLDTSTHKSSDNKLE
CCCCCCCCCCCCHHH
52.3129967540
121PhosphorylationLDTSTHKSSDNKLEE
CCCCCCCCCCCHHHH
35.01-
122PhosphorylationDTSTHKSSDNKLEET
CCCCCCCCCCHHHHH
50.43-
125AcetylationTHKSSDNKLEETLTR
CCCCCCCHHHHHHHH
63.3726051181
125UbiquitinationTHKSSDNKLEETLTR
CCCCCCCHHHHHHHH
63.3729967540
125SumoylationTHKSSDNKLEETLTR
CCCCCCCHHHHHHHH
63.3728112733
135UbiquitinationETLTREQKEGAFSNF
HHHHHHHHCCCCCCC
54.0529967540
135SumoylationETLTREQKEGAFSNF
HHHHHHHHCCCCCCC
54.05-
138UbiquitinationTREQKEGAFSNFPIS
HHHHHCCCCCCCCCC
13.0421890473
140PhosphorylationEQKEGAFSNFPISEE
HHHCCCCCCCCCCHH
36.7121082442
143UbiquitinationEGAFSNFPISEETIK
CCCCCCCCCCHHHHH
33.1824816145
150AcetylationPISEETIKLLKGRGV
CCCHHHHHHHCCCCC
56.0125953088
150UbiquitinationPISEETIKLLKGRGV
CCCHHHHHHHCCCCC
56.0132015554
150SumoylationPISEETIKLLKGRGV
CCCHHHHHHHCCCCC
56.01-
167UbiquitinationLFPIQVKTFGPVYEG
EEEEEEEEECCEECC
34.6624816145
175UbiquitinationFGPVYEGKDLIAQAR
ECCEECCCEEEEECC
37.1029967540
187UbiquitinationQARTGTGKTFSFAIP
ECCCCCCCHHHHHHH
46.35-
187AcetylationQARTGTGKTFSFAIP
ECCCCCCCHHHHHHH
46.3526051181
188PhosphorylationARTGTGKTFSFAIPL
CCCCCCCHHHHHHHH
26.3420068231
190PhosphorylationTGTGKTFSFAIPLIE
CCCCCHHHHHHHHHH
20.9920068231
208UbiquitinationRNQETIKKSRSPKVL
HCHHHHHHCCCCCEE
47.4524816145
211PhosphorylationETIKKSRSPKVLVLA
HHHHHCCCCCEEEEC
35.84-
229UbiquitinationELANQVAKDFKDITR
HHHHHHHHHHHHHHH
65.9129967540
232AcetylationNQVAKDFKDITRKLS
HHHHHHHHHHHHHHH
59.3525953088
232UbiquitinationNQVAKDFKDITRKLS
HHHHHHHHHHHHHHH
59.3524816145
244PhosphorylationKLSVACFYGGTSYQS
HHHHHHHCCCCCHHH
17.9630576142
247PhosphorylationVACFYGGTSYQSQIN
HHHHCCCCCHHHHHH
21.65-
251PhosphorylationYGGTSYQSQINHIRN
CCCCCHHHHHHHHHC
25.46-
266PhosphorylationGIDILVGTPGRIKDH
CCCEEECCCCHHHHH
18.3223401153
283UbiquitinationSGRLDLSKLRHVVLD
CCCCCHHHHHHHHHH
57.76-
322PhosphorylationDSEDNPQTLLFSATC
CCCCCCCEEEEEECC
27.04-
345PhosphorylationKKYMKSRYEQVDLVG
HHHHHHHHHHHHHHH
20.15-
353UbiquitinationEQVDLVGKMTQKAAT
HHHHHHHHHHHHHHH
31.1529967540
367UbiquitinationTTVEHLAIQCHWSQR
HHHHHHHHHCCHHCC
5.8921890473
412UbiquitinationMAMNPHIKQNAQCLH
HHCCHHHHHHHHHHC
34.1729967540
432AcetylationSQREITLKGFREGSF
HCCEEEEECCCCCCE
47.5625953088
432UbiquitinationSQREITLKGFREGSF
HCCEEEEECCCCCCE
47.5621890473
432MethylationSQREITLKGFREGSF
HCCEEEEECCCCCCE
47.56-
438PhosphorylationLKGFREGSFKVLVAT
EECCCCCCEEEEEEE
19.6923403867
445PhosphorylationSFKVLVATNVAARGL
CEEEEEEECHHHCCC
23.8124114839
461UbiquitinationIPEVDLVIQSSPPQD
CCCCCEEEECCCCCC
4.2324816145
463PhosphorylationEVDLVIQSSPPQDVE
CCCEEEECCCCCCHH
33.4228122231
464PhosphorylationVDLVIQSSPPQDVES
CCEEEECCCCCCHHH
24.9928122231
471PhosphorylationSPPQDVESYIHRSGR
CCCCCHHHHHHHCCC
29.2728122231
472PhosphorylationPPQDVESYIHRSGRT
CCCCHHHHHHHCCCC
6.2928122231
506AcetylationQLRYVEQKAGITFKR
CCEEEHHHCCCCEEE
34.7725953088
506UbiquitinationQLRYVEQKAGITFKR
CCEEEHHHCCCCEEE
34.77-
512MethylationQKAGITFKRVGVPST
HHCCCCEEECCCCCH
37.21-
512UbiquitinationQKAGITFKRVGVPST
HHCCCCEEECCCCCH
37.2129967540
518PhosphorylationFKRVGVPSTMDLVKS
EEECCCCCHHHHHHC
33.6820068231
519PhosphorylationKRVGVPSTMDLVKSK
EECCCCCHHHHHHCC
14.5020068231
524UbiquitinationPSTMDLVKSKSMDAI
CCHHHHHHCCCHHHH
60.5129967540
526UbiquitinationTMDLVKSKSMDAIRS
HHHHHHCCCHHHHHH
44.0424816145
606AcetylationQDVSCAWKELNRKLS
HHHHHHHHHHHHHHC
33.5211921489
611UbiquitinationAWKELNRKLSSNAVS
HHHHHHHHHCHHHHH
52.2029967540
613PhosphorylationKELNRKLSSNAVSQI
HHHHHHHCHHHHHHH
25.2823927012
614PhosphorylationELNRKLSSNAVSQIT
HHHHHHCHHHHHHHH
38.9623927012
618PhosphorylationKLSSNAVSQITRMCL
HHCHHHHHHHHHHHH
17.2930622161
621PhosphorylationSNAVSQITRMCLLKG
HHHHHHHHHHHHHCC
12.5230622161
630SulfoxidationMCLLKGNMGVCFDVP
HHHHCCCCEEEEECC
6.0821406390
668PhosphorylationLPEIEEYYDGNTSSN
CCCHHHHCCCCCCCC
22.2123186163
672PhosphorylationEEYYDGNTSSNSRQR
HHHCCCCCCCCCCCC
38.7825159151
673PhosphorylationEYYDGNTSSNSRQRS
HHCCCCCCCCCCCCC
31.3625159151
674PhosphorylationYYDGNTSSNSRQRSG
HCCCCCCCCCCCCCC
36.4623186163
676PhosphorylationDGNTSSNSRQRSGWS
CCCCCCCCCCCCCCC
31.5725159151
680PhosphorylationSSNSRQRSGWSSGRS
CCCCCCCCCCCCCCC
35.9523186163
683PhosphorylationSRQRSGWSSGRSGRS
CCCCCCCCCCCCCCC
26.8323401153
684PhosphorylationRQRSGWSSGRSGRSG
CCCCCCCCCCCCCCC
31.5530576142
687PhosphorylationSGWSSGRSGRSGRSG
CCCCCCCCCCCCCCC
41.9226657352
713PhosphorylationRQGSRSGSRQDGRRR
CCCCCCCCCCCCCCC
28.19-
735PhosphorylationRSGGHKRSFD-----
CCCCCCCCCC-----
38.2724719451

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 DDX50_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX50_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 DDX50_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RASK_HUMANKRASphysical
21988832
PRKRA_HUMANPRKRAphysical
24778252
TRBP2_HUMANTARBP2physical
24778252
DDX21_HUMANDDX21physical
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 DDX50_HUMAN

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Related Literatures of Post-Translational Modification
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-82, AND MASSSPECTROMETRY.
"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-45, AND MASSSPECTROMETRY.

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