DDX59_HUMAN - dbPTM
DDX59_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX59_HUMAN
UniProt AC Q5T1V6
Protein Name Probable ATP-dependent RNA helicase DDX59
Gene Name DDX59
Organism Homo sapiens (Human).
Sequence Length 619
Subcellular Localization Cytoplasm . Nucleus . Exhibits granular localization in the nucleus, as well as in the cytoplasm.
Protein Description
Protein Sequence MFVPRSLKIKRNANDDGKSCVAKIIKPDPEDLQLDKSRDVPVDAVATEAATIDRHISESCPFPSPGGQLAEVHSVSPEQGAKDSHPSEEPVKSFSKTQRWAEPGEPICVVCGRYGEYICDKTDEDVCSLECKAKHLLQVKEKEEKSKLSNPQKADSEPESPLNASYVYKEHPFILNLQEDQIENLKQQLGILVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKELMSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRIITGEKNLPCANVRQIILWVEDPAKKKKLFEILNDKKLFKPPVLVFVDCKLGADLLSEAVQKITGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAKRVKPTGSILPPQLLNSPYLHDQKRKEQQKDKQTQNDLVTGANLMDIIRKHDKSNSQK
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
6Phosphorylation--MFVPRSLKIKRNA
--CCCCCCCCCCCCC
28.1326074081
19PhosphorylationNANDDGKSCVAKIIK
CCCCCCCCEEEEECC
21.25-
23AcetylationDGKSCVAKIIKPDPE
CCCCEEEEECCCCHH
25.2725953088
26AcetylationSCVAKIIKPDPEDLQ
CEEEEECCCCHHHCC
47.0166726701
26SumoylationSCVAKIIKPDPEDLQ
CEEEEECCCCHHHCC
47.0128112733
26SumoylationSCVAKIIKPDPEDLQ
CEEEEECCCCHHHCC
47.01-
37PhosphorylationEDLQLDKSRDVPVDA
HHCCCCCCCCCCCCH
33.1225159151
57PhosphorylationATIDRHISESCPFPS
HHHHHHHHHCCCCCC
19.8229255136
59PhosphorylationIDRHISESCPFPSPG
HHHHHHHCCCCCCCC
21.9429255136
64PhosphorylationSESCPFPSPGGQLAE
HHCCCCCCCCCCEEE
36.2323401153
74PhosphorylationGQLAEVHSVSPEQGA
CCEEEEEECCHHCCC
29.4823401153
76PhosphorylationLAEVHSVSPEQGAKD
EEEEEECCHHCCCCC
26.2423401153
93PhosphorylationPSEEPVKSFSKTQRW
CCCCCCCCCCCCCCC
34.6824719451
149PhosphorylationKEEKSKLSNPQKADS
HHHHHHCCCCCCCCC
50.6428450419
156PhosphorylationSNPQKADSEPESPLN
CCCCCCCCCCCCCCC
60.9725159151
160PhosphorylationKADSEPESPLNASYV
CCCCCCCCCCCHHHE
45.4625159151
165PhosphorylationPESPLNASYVYKEHP
CCCCCCHHHEECCCC
17.6621815630
166PhosphorylationESPLNASYVYKEHPF
CCCCCHHHEECCCCE
12.8523403867
168PhosphorylationPLNASYVYKEHPFIL
CCCHHHEECCCCEEE
11.4823403867
169UbiquitinationLNASYVYKEHPFILN
CCHHHEECCCCEEEE
39.23-
221PhosphorylationLNHNLKKSGYEVPTP
HCCCHHHCCCCCCCC
45.0522964224
223PhosphorylationHNLKKSGYEVPTPIQ
CCHHHCCCCCCCCCE
22.3522964224
227PhosphorylationKSGYEVPTPIQMQMI
HCCCCCCCCCEEEEE
37.8922964224
246PhosphorylationLGRDILASADTGSGK
HCHHHHHCCCCCCCH
24.1918669648
253UbiquitinationSADTGSGKTAAFLLP
CCCCCCCHHHHHHHH
36.37-
270AcetylationMRALFESKTPSALIL
HHHHHHCCCCCEEEE
58.2023954790
270UbiquitinationMRALFESKTPSALIL
HHHHHHCCCCCEEEE
58.20-
278PhosphorylationTPSALILTPTRELAI
CCCEEEECCHHHHHH
18.6724719451
303PhosphorylationSGLPRMKTVLLVGGL
CCCCCCCEEEEECCC
13.67-
317PhosphorylationLPLPPQLYRLQQHVK
CCCCHHHHHHHHCCE
12.20-
410AcetylationVRIITGEKNLPCANV
EEEEECCCCCCCCCE
66.1925953088
410UbiquitinationVRIITGEKNLPCANV
EEEEECCCCCCCCCE
66.19-
432AcetylationEDPAKKKKLFEILND
CCHHHHHHHHHHHCC
68.25164187
440AcetylationLFEILNDKKLFKPPV
HHHHHCCCCCCCCCE
50.75164191
440UbiquitinationLFEILNDKKLFKPPV
HHHHHCCCCCCCCCE
50.75-
466UbiquitinationLLSEAVQKITGLKSI
HHHHHHHHHHCCCCE
35.32-
471UbiquitinationVQKITGLKSISIHSE
HHHHHCCCCEEECCC
47.27-
479UbiquitinationSISIHSEKSQIERKN
CEEECCCCHHHHHHH
51.15-
513 (in isoform 2)Phosphorylation-14.4223663014
524 (in isoform 2)Phosphorylation-31.4923663014
525 (in isoform 2)Phosphorylation-25.1223663014
529 (in isoform 2)Phosphorylation-10.0423663014
535 (in isoform 2)Phosphorylation-29.3723663014
536 (in isoform 2)Phosphorylation-4.3923663014
562UbiquitinationRLFWDIAKRVKPTGS
EEEHHHHHHCCCCCC
59.04-
578PhosphorylationLPPQLLNSPYLHDQK
CCHHHHCCCCCCHHH
18.1925159151
593UbiquitinationRKEQQKDKQTQNDLV
HHHHHHCHHHHHHHH
63.38-

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 DDX59_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX59_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 DDX59_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX59_HUMANDDX59physical
28561026
HS90A_HUMANHSP90AA1physical
28561026
HS90B_HUMANHSP90AB1physical
28561026
HSP7C_HUMANHSPA8physical
28561026
STIP1_HUMANSTIP1physical
28561026

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
174300Orofaciodigital syndrome 5 (OFD5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDX59_HUMAN

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Related Literatures of Post-Translational Modification
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-160, AND MASSSPECTROMETRY.
"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-64 AND SER-76, AND MASSSPECTROMETRY.

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