RRP44_MOUSE - dbPTM
RRP44_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRP44_MOUSE
UniProt AC Q9CSH3
Protein Name Exosome complex exonuclease RRP44
Gene Name Dis3
Organism Mus musculus (Mouse).
Sequence Length 958
Subcellular Localization Cytoplasm . Nucleus, nucleolus . Nucleus, nucleoplasm . Nucleus . Predominantly located in the nucleus. According to, found in the nucleolus. According to, excluded from nucleolus supporting the existence of a nucleolar RNA exosome complex devoid of
Protein Description Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. DIS3 has both 3'-5' exonuclease and endonuclease activities..
Protein Sequence MLRSKTFLKKTRAGGVVKIVREHYLRDDIGCGAPACSACGGAHAGPALELQPRDQASSLCPWPHYLLPDTNVLLHQIDVLEHPAIRNVIVLQTVMQEVRNRSAPIYKRIRDVTNNQEKHFYTFTNEHHKETYIEQEQGENANDRNDRAIRVAAKWYNEHLKRVAADSQLQVILITNDRKNKEKAVQEGIPAFTCEEYVKSLTANPELIDRLAYLSDEMNEIESGKIIFSEHLPLSKLQQGIKSGSYLQGTFRASRENYLEATVWIHGDKEEEKEILIQGIKHLNRAVHEDIVAVELLPRSQWVAPSSVVLDDEGQNEDDVEKDEERELLLKTAVSEKMLRPTGRVVGIIKRNWRPYCGMLSKSDIKESRRHLFTPADKRIPRIRIETRQASALEGRRIIVAIDGWPRNSRYPNGHFVKNLGDVGEKETETEVLLLEHDVPHQPFSQAVLSFLPRMPWSITEEDMKNREDLRHLCVCSVDPPGCTDIDDALHCRELSNGNLEVGVHIADVSHFIRPGNALDQESARRGTTVYLCEKRIDMVPELLSSNLCSLRSNVDRLAFSCIWEMNHNAEILKTRFTKSVINSKASLTYAEAQMRIDSAAMNDDITTSLRGLNQLAKILKKGRIEKGALTLSSPEIRFHMDSETHDPIDLQTKELRETNSMVEEFMLLANISVAKKIHEEFSEHALLRKHPAPPPSNYDILVKAAKSKNLQIKTDTAKSLADSLDRAESPDFPYLNTLLRILATRCMMQAVYFCSGMDNDFHHYGLASPIYTHFTSPIRRYADIIVHRLLAVAIGADCTYPELTDKHKLSDICKNLNFRHKMAQYAQRASVAFHTQLFFKSKGIVSEEAYILFVRKNAIVVLIPKYGLEGTVFFEEKDKPKPRLAYDDEIPSLRIEGTVFHVFDKVKVKITLDSSNLQHQKIRMALVEPQIPGINIPPNVADKALTAPGGKKRKLEK
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
1Acetylation-------MLRSKTFL
-------CCCCHHHH
6.73-
18AcetylationTRAGGVVKIVREHYL
HCCCCCEEEEEHHHC
32.8323806337
213PhosphorylationELIDRLAYLSDEMNE
HHHHHHHHHCHHHHH
16.0128833060
215PhosphorylationIDRLAYLSDEMNEIE
HHHHHHHCHHHHHHH
20.8821082442
223PhosphorylationDEMNEIESGKIIFSE
HHHHHHHCCCEEEEC
51.5626745281
236UbiquitinationSEHLPLSKLQQGIKS
ECCCCHHHHHHHHHC
58.9822790023
242UbiquitinationSKLQQGIKSGSYLQG
HHHHHHHHCCCHHHE
56.4422790023
561PhosphorylationNVDRLAFSCIWEMNH
CHHHHHHHHHHHCCC
10.0930165576
633PhosphorylationEKGALTLSSPEIRFH
CCCCEECCCCCEEEE
38.3122006019
634PhosphorylationKGALTLSSPEIRFHM
CCCEECCCCCEEEEC
29.6626824392
730PhosphorylationDSLDRAESPDFPYLN
HHHHHHHCCCCHHHH
28.8726239621
922AcetylationSSNLQHQKIRMALVE
CCCCCCCEEHHHHCC
30.1023236377

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 RRP44_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRP44_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 RRP44_MOUSE !!

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

Oops, there are no PPI records of RRP44_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RRP44_MOUSE

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Related Literatures of Post-Translational Modification

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