DDX17_DROME - dbPTM
DDX17_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX17_DROME
UniProt AC P19109
Protein Name ATP-dependent RNA helicase p62
Gene Name Rm62
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 719
Subcellular Localization Nucleus . Nucleus, nucleolus . Cytoplasm, cytosol . In the course of bunyavirus infection, relocalizes from the nucleus to the cytosol where it binds viral RNA to antagonize replication.
Protein Description As an RNA helicase, unwinds RNA and alters RNA structures through ATP binding and hydrolysis. Involved in multiple cellular processes, including pre-mRNA splicing, alternative splicing, rRNA processing and miRNA processing, as well as transcription regulation (By similarity). [PubMed: 12368261 Plays a role in innate immunity. Specifically restricts bunyavirus infection, including Rift Valley fever virus (RVFV) or La Crosse virus (LACV), but not vesicular stomatitis virus (VSV), in an interferon- and DROSHA-independent manner]
Protein Sequence MLKLVQYIAPRVGGATPRPTACGWGNLLLISPRSGASSEKCITQRRHFLFSSASSSGTFASSSSLCTEQRQQFHGSRRNRETILFPSTYSSLQAQSQRAFRDSSKPDSDDYVDSIPKAEQRTRTRKSLFNDPDERTEEIKIEGVMAPHDRDFGHSGRGGRGGDRGGDDRRGGGGGGNRFGGGGGGGDYHGIRNGRVEKRRDDRGGGNRFGGGGGFGDRRGGGGGGSQDLPMRPVDFSNLAPFKKNFYQEHPNVANRSPYEVQRYREEQEITVRGQVPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLELSANHNIRQVVDVCDEFSKEEKLKTLLSDIYDTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAFFTKNNAKQAKALVDVLREANQEINPALENLARNSRYDGGGGRSRYGGGGGGGRFGGGGFKKGSLSNGRGFGGGGGGGGEGRHSRFD
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
226PhosphorylationRGGGGGGSQDLPMRP
CCCCCCCCCCCCCCC
24.6419429919
257PhosphorylationHPNVANRSPYEVQRY
CCCCCCCCHHHHHHH
31.4729892262
581PhosphorylationREFRSGKSNILVATD
HHHHCCCCCEEEEEH
32.4022817900
627AcetylationRTGRSNTKGTSFAFF
CCCCCCCCCCCEEEE
65.5221791702
636AcetylationTSFAFFTKNNAKQAK
CCEEEEECCCHHHHH
42.9421791702
696PhosphorylationGGGFKKGSLSNGRGF
CCCCCCCCCCCCCCC
37.1929892262
716PhosphorylationGGGEGRHSRFD----
CCCCCCCCCCC----
33.0321082442

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 DDX17_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX17_DROME !!

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 DDX17_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUMB_DROMEnumbphysical
14605208
LTOR3_DROMECG5110physical
14605208
DDX17_DROMERm62physical
14605208
NPLP1_DROMENplp1physical
14605208
BX42_DROMEBx42physical
14605208
EXOC2_DROMESec5physical
14605208
ANX11_DROMEAnxB11physical
14605208
FMR1_DROMEFmr1physical
12368261
AGO2_DROMEAGO2physical
12368261
DDX17_DROMERm62physical
21674064
SUV39_DROMESu(var)3-9physical
21674064

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDX17_DROME

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Related Literatures of Post-Translational Modification

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