DHX58_HUMAN - dbPTM
DHX58_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHX58_HUMAN
UniProt AC Q96C10
Protein Name Probable ATP-dependent RNA helicase DHX58
Gene Name DHX58
Organism Homo sapiens (Human).
Sequence Length 678
Subcellular Localization Cytoplasm .
Protein Description Acts as a regulator of DDX58/RIG-I and IFIH1/MDA5 mediated antiviral signaling. Cannot initiate antiviral signaling as it lacks the CARD domain required for activating MAVS/IPS1-dependent signaling events. Can have both negative and positive regulatory functions related to DDX58/RIG-I and IFIH1/MDA5 signaling and this role in regulating signaling may be complex and could probably depend on characteristics of the infecting virus or target cells, or both. Its inhibitory action on DDX58/RIG-I signaling may involve the following mechanisms: competition with DDX58/RIG-I for binding to the viral RNA, binding to DDX58/RIG-I and inhibiting its dimerization and interaction with MAVS/IPS1, competing with IKBKE in its binding to MAVS/IPS1 thereby inhibiting activation of interferon regulatory factor 3 (IRF3). Its positive regulatory role may involve unwinding or stripping nucleoproteins of viral RNA thereby facilitating their recognition by DDX58/RIG-I and IFIH1/MDA5. Involved in the innate immune response to various RNA viruses and some DNA viruses such as poxviruses, and also to the bacterial pathogen Listeria monocytogenes. Can bind both ssRNA and dsRNA, with a higher affinity for dsRNA. Shows a preference to 5'-triphosphorylated RNA, although it can recognize RNA lacking a 5'-triphosphate..
Protein Sequence MELRSYQWEVIMPALEGKNIIIWLPTGAGKTRAAAYVAKRHLETVDGAKVVVLVNRVHLVTQHGEEFRRMLDGRWTVTTLSGDMGPRAGFGHLARCHDLLICTAELLQMALTSPEEEEHVELTVFSLIVVDECHHTHKDTVYNVIMSQYLELKLQRAQPLPQVLGLTASPGTGGASKLDGAINHVLQLCANLDTWCIMSPQNCCPQLQEHSQQPCKQYNLCHRRSQDPFGDLLKKLMDQIHDHLEMPELSRKFGTQMYEQQVVKLSEAAALAGLQEQRVYALHLRRYNDALLIHDTVRAVDALAALQDFYHREHVTKTQILCAERRLLALFDDRKNELAHLATHGPENPKLEMLEKILQRQFSSSNSPRGIIFTRTRQSAHSLLLWLQQQQGLQTVDIRAQLLIGAGNSSQSTHMTQRDQQEVIQKFQDGTLNLLVATSVAEEGLDIPHCNVVVRYGLLTNEISMVQARGRARADQSVYAFVATEGSRELKRELINEALETLMEQAVAAVQKMDQAEYQAKIRDLQQAALTKRAAQAAQRENQRQQFPVEHVQLLCINCMVAVGHGSDLRKVEGTHHVNVNPNFSNYYNVSRDPVVINKVFKDWKPGGVISCRNCGEVWGLQMIYKSVKLPVLKVRSMLLETPQGRIQAKKWSRVPFSVPDFDFLQHCAENLSDLSLD
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
18AcetylationIMPALEGKNIIIWLP
EEHHHCCCEEEEEEE
35.287429273
76PhosphorylationRMLDGRWTVTTLSGD
HHHCCCEEEEEECCC
13.4530576142
79PhosphorylationDGRWTVTTLSGDMGP
CCCEEEEEECCCCCC
18.0030576142
225PhosphorylationYNLCHRRSQDPFGDL
HCCCCCCCCCHHHHH
38.6027499020
310PhosphorylationLAALQDFYHREHVTK
HHHHHHHHHHHCCCH
14.3022817900
335AcetylationLALFDDRKNELAHLA
HHHHCCCHHHHHHHH
62.867677899
350AcetylationTHGPENPKLEMLEKI
HHCCCCHHHHHHHHH
69.537677909
477PhosphorylationGRARADQSVYAFVAT
CCCCCCCCEEEEEEC
20.0425348954
479PhosphorylationARADQSVYAFVATEG
CCCCCCEEEEEECCC
10.2825348954
484PhosphorylationSVYAFVATEGSRELK
CEEEEEECCCCHHHH
35.2625348954
518PhosphorylationQKMDQAEYQAKIRDL
HCCCHHHHHHHHHHH
19.45-

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 DHX58_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHX58_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 DHX58_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AGO2_HUMANAGO2physical
21903422
DICER_HUMANDICER1physical
21903422
E2AK2_HUMANEIF2AK2physical
21903422
STAU1_HUMANSTAU1physical
21903422
STAU2_HUMANSTAU2physical
21903422
CARF_HUMANCDKN2AIPphysical
21903422
DHX30_HUMANDHX30physical
21903422
IF6_HUMANEIF6physical
21903422
NKRF_HUMANNKRFphysical
21903422
XRN2_HUMANXRN2physical
21903422
A4_HUMANAPPphysical
21832049

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 DHX58_HUMAN

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Related Literatures of Post-Translational Modification

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