DSRAD_MOUSE - dbPTM
DSRAD_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DSRAD_MOUSE
UniProt AC Q99MU3
Protein Name Double-stranded RNA-specific adenosine deaminase
Gene Name Adar
Organism Mus musculus (Mouse).
Sequence Length 1178
Subcellular Localization Isoform 1: Cytoplasm. Nucleus, nucleolus. Long forms starting at Met-1 are found predominantly in cytoplasm. Shuttles between the cytoplasm and nucleus.
Isoform 2: Cytoplasm. Nucleus, nucleolus. Long forms starting at Met-1 are found predominan
Protein Description Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Does not affect polyomavirus replication but provides protection against virus-induced cytopathic effects. Essential for embryonic development and cell survival and plays a critical role in the maintenance of hematopoietic stem cells..
Protein Sequence MSQGFRGPTGVFPHQTQSYLDPSHEHSKWRYPQPQGPESYPRSFQLQQIEFLKGRLPEAPLIGIQTQSLPPFLPGHWPRFPGPPAQDRQLEIWEFPRSVTLRNQGFHIGPPLPPPHSRGTPWRGADGLCSHFRELSISQSPEQKVLNRLEELGEGKATTAHVLARELRIPKRDINRILYSLEKKGKLHRGRGKPPLWSLVPLSQAWTQPPGVVNPDSCIQEFPRGEPGLDSEDGDPASDLEGPSEPLDMAEIKEKICDYLFNVSNSSALNLAKNIGLTKARDVTSVLIDLERQGDVYRQGATPPIWYLTDKKRERLQMKRSTHSAPAPTPTAVPEATRSPSFPACHPPPAGASSSVAASKRVENGQEPAIKHESRHEARPGPMRLRPHAYHNGPSRAGYVASENGQWATDDIPDNLNSIHTAPGEFRAIMEMPSFYSPTLPRCSPYKKLTECQLKNPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILLREAKAKDSGQPEDLSHCPMEEDSEKPAEAQAPSSSATSLFSGKSPVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPPVSAPSKKVAKQMAAEEAMKALQEEAASSADDQSGGANTDSLDESMAPNKIRRIGELVRYLNTNPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVLIGESEKAEQLGFAEVTPVTGASLRRTMLLLSRSPDAHPKTLPLSGSTFHDQIAMLSHRCFNALTNSFQPSLLGRKILAAIIMKRDPEDMGVVVSLGTGNRCVKGDSLSLKGETVNDCHAEIISRRGFIRFLYSELMKYNHHTAKNSIFELARGGEKLQIKKTVSFHLYISTAPCGDGALFDKSCSDRAVESTESRHYPVFENPKQGKLRTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFLQPVYLKSVTLGYLFSQGHLTRAICCRVTRDGKAFEDGLRYPFIVNHPKVGRVSVYDSKRQSGKTKETSVNWCMADGYDLEILDGTRGTVDGPGKELSRVSKKNIFLQFKKLCSFRARRDLLQLSYGEAKKAARDYDLAKNYFKKSLRDMGYGNWISKPQEEKNFYLCPVPND
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
30MethylationSHEHSKWRYPQPQGP
CCCCCCCCCCCCCCC
36.6724129315
30Asymmetric dimethylarginineSHEHSKWRYPQPQGP
CCCCCCCCCCCCCCC
36.67-
42Asymmetric dimethylarginineQGPESYPRSFQLQQI
CCCCCCCCCEEHHHH
41.70-
42MethylationQGPESYPRSFQLQQI
CCCCCCCCCEEHHHH
41.7024129315
53UbiquitinationLQQIEFLKGRLPEAP
HHHHHHHCCCCCCCC
47.5122790023
55DimethylationQIEFLKGRLPEAPLI
HHHHHCCCCCCCCEE
45.54-
79DimethylationFLPGHWPRFPGPPAQ
CCCCCCCCCCCCCCC
45.24-
100PhosphorylationWEFPRSVTLRNQGFH
EECCCCEECCCCCCC
22.6524719451
136PhosphorylationCSHFRELSISQSPEQ
HHHHHHCCCCCCHHH
18.5525521595
138PhosphorylationHFRELSISQSPEQKV
HHHHCCCCCCHHHHH
22.6425521595
140PhosphorylationRELSISQSPEQKVLN
HHCCCCCCHHHHHHH
24.5063809353
179PhosphorylationRDINRILYSLEKKGK
HHHHHHHHHHHHCCC
14.6121743459
180PhosphorylationDINRILYSLEKKGKL
HHHHHHHHHHHCCCC
26.9721743459
231PhosphorylationRGEPGLDSEDGDPAS
CCCCCCCCCCCCCHH
42.5025159016
238PhosphorylationSEDGDPASDLEGPSE
CCCCCCHHHCCCCCC
48.3825159016
244PhosphorylationASDLEGPSEPLDMAE
HHHCCCCCCCCCHHH
63.8030635358
321PhosphorylationERLQMKRSTHSAPAP
HHHHHCCCCCCCCCC
25.5925777480
322PhosphorylationRLQMKRSTHSAPAPT
HHHHCCCCCCCCCCC
24.7125777480
324PhosphorylationQMKRSTHSAPAPTPT
HHCCCCCCCCCCCCC
35.7225777480
329PhosphorylationTHSAPAPTPTAVPEA
CCCCCCCCCCCCCCC
35.0625777480
331PhosphorylationSAPAPTPTAVPEATR
CCCCCCCCCCCCCCC
42.6425777480
337PhosphorylationPTAVPEATRSPSFPA
CCCCCCCCCCCCCCC
29.9825777480
339PhosphorylationAVPEATRSPSFPACH
CCCCCCCCCCCCCCC
22.1228066266
341PhosphorylationPEATRSPSFPACHPP
CCCCCCCCCCCCCCC
45.1428066266
353PhosphorylationHPPPAGASSSVAASK
CCCCCCCCCCHHHHH
23.4125777480
354PhosphorylationPPPAGASSSVAASKR
CCCCCCCCCHHHHHC
28.4425777480
355PhosphorylationPPAGASSSVAASKRV
CCCCCCCCHHHHHCH
17.1825777480
359PhosphorylationASSSVAASKRVENGQ
CCCCHHHHHCHHCCC
15.9725777480
360AcetylationSSSVAASKRVENGQE
CCCHHHHHCHHCCCC
56.5930985433
434PhosphorylationRAIMEMPSFYSPTLP
HHHHCCCCCCCCCCC
35.19-
437PhosphorylationMEMPSFYSPTLPRCS
HCCCCCCCCCCCCCC
14.9229514104
444PhosphorylationSPTLPRCSPYKKLTE
CCCCCCCCCCCCCCH
32.3226745281
446PhosphorylationTLPRCSPYKKLTECQ
CCCCCCCCCCCCHHH
12.4026745281
511UbiquitinationAGSKKVAKQDAAVKA
CCCHHHHHHHHHHHH
52.2622790023
567PhosphorylationTSLFSGKSPVTTLLE
HHHHCCCCHHHHHHH
28.2928066266
570PhosphorylationFSGKSPVTTLLECMH
HCCCCHHHHHHHHHH
18.3428066266
571PhosphorylationSGKSPVTTLLECMHK
CCCCHHHHHHHHHHH
29.5828066266
582PhosphorylationCMHKLGNSCEFRLLS
HHHHHCCCCEEEEEC
17.1522324799
589PhosphorylationSCEFRLLSKEGPAHD
CCEEEEECCCCCCCC
33.00-
639PhosphorylationALQEEAASSADDQSG
HHHHHHHHCCCCCCC
32.8630635358
640PhosphorylationLQEEAASSADDQSGG
HHHHHHHCCCCCCCC
30.8730635358
645PhosphorylationASSADDQSGGANTDS
HHCCCCCCCCCCCCC
46.3030635358
650PhosphorylationDQSGGANTDSLDESM
CCCCCCCCCCCCHHH
26.8230635358
652PhosphorylationSGGANTDSLDESMAP
CCCCCCCCCCHHHCC
35.3630635358
656PhosphorylationNTDSLDESMAPNKIR
CCCCCCHHHCCHHHH
21.6630635358
757PhosphorylationQLGFAEVTPVTGASL
HHCCCEEECCCCHHH
11.98-
763PhosphorylationVTPVTGASLRRTMLL
EECCCCHHHHHHHHH
24.61-
772PhosphorylationRRTMLLLSRSPDAHP
HHHHHHHHCCCCCCC
30.5924719451
774PhosphorylationTMLLLSRSPDAHPKT
HHHHHHCCCCCCCCC
24.6125266776
847PhosphorylationNRCVKGDSLSLKGET
CCCCCCCCCCCCCCC
28.6423737553
849PhosphorylationCVKGDSLSLKGETVN
CCCCCCCCCCCCCHH
31.8023737553
1046PhosphorylationAFEDGLRYPFIVNHP
CCCCCCCCCEEECCC
13.92166897

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 DSRAD_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DSRAD_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 DSRAD_MOUSE !!

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

Oops, there are no PPI records of DSRAD_MOUSE !!

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

loading...

Related Literatures of Post-Translational Modification

TOP