DDX17_MOUSE - dbPTM
DDX17_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX17_MOUSE
UniProt AC Q501J6
Protein Name Probable ATP-dependent RNA helicase DDX17
Gene Name Ddx17
Organism Mus musculus (Mouse).
Sequence Length 650
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, ribosomal RNA processing and miRNA processing, as well as transcription regulation. Regulates the alternative splicing of exons exhibiting specific features. This function requires the RNA helicase activity. Affects NFAT5 and histone macro-H2A.1/H2AFY alternative splicing in a CDK9-dependent manner. Affects splicing of mediators of steroid hormone signaling pathway, including kinases that phosphorylates ESR1 and transcriptional regulators. By acting splicing of regulatory factors, participates in ESR1 and AR stabilization. Promotes the inclusion of specific AC-rich alternative exons in CD44 transcripts. In myoblasts and epithelial cells, cooperates with HNRNPH1 to control the splicing of specific subsets of exons. In addition to binding mature mRNAs, also interacts with certain pri-microRNAs, including MIR132/miR-132, and stabilizes the primary transcript. Also participates in the MIR132 processing, resulting in significantly higher levels of mature MIR132 than MIR212 despite the fact that both are cotranscribed and co-regulated. [PubMed: 26947125 Binding of pri-microRNAs may occur on the 3' segment flanking the stem loop via the 5'-[ACG]CAUC[ACU]-3' consensus sequence (By similarity Participates in MYC down-regulation at high cell density through the production of MYC-targeting microRNAs. Along with DDX5, may be involved in the processing of the 32S intermediate into the mature 28S rRNA. Promoter-specific transcription regulator, functioning as a coactivator or corepressor depending on the context of the promoter and the transcriptional complex in which it exists. Enhances NFAT5 transcriptional activity. Synergizes with TP53 in the activation of the MDM2 promoter; this activity requires acetylation on lysine residues. May also coactivate MDM2 transcription through a TP53-independent pathway. Coactivates MMP7 transcription. Along with CTNNB1, coactivates MYC, JUN, FOSL1 and cyclin D1/CCND1 transcription. Alone or in combination with DDX5 and/or SRA1 non-coding RNA, plays a critical role in promoting the assembly of proteins required for the formation of the transcription initiation complex and chromatin remodeling leading to coactivation of MYOD1-dependent transcription. This helicase-independent activity is required for skeletal muscle cells to properly differentiate into myotubes]
Protein Sequence MRGGGFGDRDRDRDRGGFGARGGSGLPPKKFGNPGERLRKKKWDLSELPKFEKNFYVEHPEVARLTPYEVDELRRKKEITVRGGDVCPKPVFAFHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNLELSANHNILQIVDVCMESEKDHKLIQLMEEIMAEKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRIGRTARSTNKGTAYTFFTPGNLKQARELIKVLEEANQAINPKLMQLVDHRGGGGGGGGRSRYRTTSSANNPNLMYQDECDRRLRGVKDGGRRDSTSYRDRSETDRASYANGSGYGSPNSAFGAQAGQYTYAQGTYGAAAYGTSGYTAQEYAAGTYGASSTASAGRSSQSSSQQFSGIGRSGQQPQPLMSQQFAQPPGATNMIGYMGQTAYQYPPPPPPPPPSRK
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
2Methylation------MRGGGFGDR
------CCCCCCCCC
53.08-
21MethylationDRGGFGARGGSGLPP
CCCCCCCCCCCCCCC
50.84-
29AcetylationGGSGLPPKKFGNPGE
CCCCCCCHHHCCHHH
59.81-
30AcetylationGSGLPPKKFGNPGER
CCCCCCHHHCCHHHH
65.36-
42AcetylationGERLRKKKWDLSELP
HHHHHHCCCCHHHCC
49.31-
50SumoylationWDLSELPKFEKNFYV
CCHHHCCCCCCCEEC
77.95-
50AcetylationWDLSELPKFEKNFYV
CCHHHCCCCCCCEEC
77.9515609695
53AcetylationSELPKFEKNFYVEHP
HHCCCCCCCEECCCH
56.3315609701
168GlutathionylationERGDGPICLVLAPTR
CCCCCCEEEEEECHH
2.1224333276
168S-nitrosylationERGDGPICLVLAPTR
CCCCCCEEEEEECHH
2.1220925432
168S-nitrosocysteineERGDGPICLVLAPTR
CCCCCCEEEEEECHH
2.12-
196PhosphorylationGKCSRLKSTCIYGGA
CCCHHCCCCEEECCC
32.8622499769
197PhosphorylationKCSRLKSTCIYGGAP
CCHHCCCCEEECCCC
11.0122499769
198GlutathionylationCSRLKSTCIYGGAPK
CHHCCCCEEECCCCC
2.6624333276
200PhosphorylationRLKSTCIYGGAPKGP
HCCCCEEECCCCCCC
16.2022499769
205UbiquitinationCIYGGAPKGPQIRDL
EEECCCCCCCCCCCH
80.72-
219S-nitrosylationLERGVEICIATPGRL
HHCCEEEEEECCCHH
0.8020925432
219S-nitrosocysteineLERGVEICIATPGRL
HHCCEEEEEECCCHH
0.80-
222PhosphorylationGVEICIATPGRLIDF
CEEEEEECCCHHHHH
13.3326745281
282UbiquitinationMWSATWPKEVRQLAE
EEECCCCHHHHHHHH
61.47-
374PhosphorylationMCIHGDKSQPERDWV
EEECCCCCCCHHHHH
56.5620139300
400PhosphorylationLIATDVASRGLDVED
EEEECHHHCCCCHHH
27.0829514104
436UbiquitinationRTARSTNKGTAYTFF
CCCCCCCCCCEEEEE
58.70-
444PhosphorylationGTAYTFFTPGNLKQA
CCEEEEECCCCHHHH
26.54-
449UbiquitinationFFTPGNLKQARELIK
EECCCCHHHHHHHHH
46.00-
488PhosphorylationGGGGRSRYRTTSSAN
CCCCCCCCCCCCCCC
17.3526060331
490PhosphorylationGGRSRYRTTSSANNP
CCCCCCCCCCCCCCC
23.3026643407
491PhosphorylationGRSRYRTTSSANNPN
CCCCCCCCCCCCCCC
16.2226643407
492PhosphorylationRSRYRTTSSANNPNL
CCCCCCCCCCCCCCC
27.1724453211
493PhosphorylationSRYRTTSSANNPNLM
CCCCCCCCCCCCCCC
32.6826643407
501PhosphorylationANNPNLMYQDECDRR
CCCCCCCCCCHHHHH
18.9125777480
520PhosphorylationKDGGRRDSTSYRDRS
CCCCCCCCCCCCCCC
19.9026824392
521PhosphorylationDGGRRDSTSYRDRSE
CCCCCCCCCCCCCCC
33.7825521595
522PhosphorylationGGRRDSTSYRDRSET
CCCCCCCCCCCCCCC
23.3225266776
523PhosphorylationGRRDSTSYRDRSETD
CCCCCCCCCCCCCCC
19.3429899451
527PhosphorylationSTSYRDRSETDRASY
CCCCCCCCCCCCCHH
49.4929899451
592PhosphorylationSTASAGRSSQSSSQQ
CCCCCCCCCCCCCCC
31.6329472430
593PhosphorylationTASAGRSSQSSSQQF
CCCCCCCCCCCCCCC
32.4929472430
595PhosphorylationSAGRSSQSSSQQFSG
CCCCCCCCCCCCCCC
33.6329514104
596PhosphorylationAGRSSQSSSQQFSGI
CCCCCCCCCCCCCCC
25.2429514104
597PhosphorylationGRSSQSSSQQFSGIG
CCCCCCCCCCCCCCC
32.9929514104
605MethylationQQFSGIGRSGQQPQP
CCCCCCCCCCCCCCC
35.3824129315

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX17_MOUSE !!

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_MOUSE !!

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

Oops, there are no PPI records of DDX17_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDX17_MOUSE

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Related Literatures of Post-Translational Modification

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