Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
ADAR (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
ADAR Converts multiple adenosines to inosines and creates I/U mismatched base pairs in double-helical RNA substrates without apparent sequence specificity. Has been found to modify more frequently adenosines in AU-rich regions, probably due to the relative ease of melting A/U base pairs as compared to G/C pairs. Functions to modify viral RNA genomes and may be responsible for hypermutation of certain negative-stranded viruses. Edits the messenger RNAs for glutamate receptor (GLUR) subunits by site- selective adenosine deamination. Produces low-level editing at the GLUR-B Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Binds to short interfering RNAs (siRNA) without editing them and suppresses siRNA-mediated RNA interference. Binds to ILF3/NF90 and up-regulates ILF3-mediated gene expression. Isoform 1 is induced by interferon alpha. Isoform 5 is constitutively expressed. Homodimer. Isoform 1 interacts with ILF2/NF45 and ILF3/NF90. 5 isoforms of the human protein are produced by alternative promoter. Note: This description may include information from UniProtKB.
Protein type: EC 3.5.4.-; Hydrolase; RNA processing
Cellular Component: nucleoplasm; cytoplasm; nucleolus; nucleus
Molecular Function: double-stranded RNA adenosine deaminase activity; protein binding; DNA binding; metal ion binding; double-stranded RNA binding
Biological Process: base conversion or substitution editing; positive regulation of viral genome replication; cytokine and chemokine mediated signaling pathway; response to virus; adenosine to inosine editing; protein import into nucleus; mRNA modification; innate immune response; gene expression; RNA-mediated gene silencing; protein export from nucleus; mRNA processing; negative regulation of apoptosis
Reference #:  P55265 (UniProtKB)
Alt. Names/Synonyms: 136 kDa double-stranded RNA binding protein; 136 kDa double-stranded RNA-binding protein; ADAR; ADAR1; adenosine deaminase acting on RNA 1-A; adenosine deaminase, RNA-specific; Double-stranded RNA-specific adenosine deaminase; DRADA; DSH; DSRAD; G1P1; IFI-4; IFI4; interferon-induced protein 4; Interferon-inducible protein 4; K88DSRBP; p136
Gene Symbols: ADAR
Molecular weight: 136,066 Da
Basal Isoelectric point: 8.86  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ADAR
Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

 
0 1 S10-p PRQGYSLsGYYtHPF
0 3 T14-p YSLsGYYtHPFQGYE
0 5 R26-m2 GYEHRQLrYQQPGPG
0 1 K48 LKQIEFLKGQLPEAP
0 4 Y136-p HFQELSIyQDQEQRI
0 1 Y177-p KEINRVLySLAKKGK
0 1 T191-p KLQKEAGtPPLWKIA
0 1 D214-ca HSGVVRPdGHSQGAP
0 1 S285 PEDSNSTSALEDPLE
0 1 K366-u KRERMQIkRNTNSVP
0 1 K384-u PAAIPETkRNAEFLT
0 8 E407 SNNMVTTEKVENGQE
1 1 K418-s NGQEPVIkLENRQEA
0 4 Y438-p RLKPPVHyNGPSKAG
0 2 Y446-p NGPSKAGyVDFENGQ
0 2 S465-p DIPDDLNsIRAAPGE
0 8 Y483-p IMEMPSFysHGLPRC
0 3 S484-p MEMPSFysHGLPRCS
0 1 K495-u PRCSPYKkLTECQLK
0 1 S553-p FPPAEAGsKKVAKQD
0 1 K558 AGsKKVAKQDAAMKA
0 1 T567-p DAAMKAMtILLEEAk
0 1 K574-a tILLEEAkAKDSGKS
0 1 Y587-p KSEESSHySTEKESE
0 1 K595-u STEKESEktAEsQtP
0 1 T596-p TEKESEktAEsQtPt
0 1 S599-p ESEktAEsQtPtPsA
0 10 T601-p EktAEsQtPtPsATS
0 3 T603-p tAEsQtPtPsATSFF
0 1 S605-p EsQtPtPsATSFFsG
0 1 S611-p PsATSFFsGKsPVTT
0 3 S614-p TSFFsGKsPVTTLLE
0 2 S629-p CMHKLGNsCEFRLLS
0 2 K637-u CEFRLLSkEGPAHEP
0 12 Y648-p AHEPKFQyCVAVGAQ
0 21 K665-a PSVSAPSkkVAKQMA
0 1 K665-u PSVSAPSkkVAKQMA
0 3 K666-a SVSAPSkkVAKQMAA
0 2 K666-u SVSAPSkkVAKQMAA
0 1 Y722-p KIGELVRyLNTNPVG
0 1 Y734-p PVGGLLEyARSHGFA
0 1 K757-u SGPPHEPkFVYQAKV
0 5 T808-p RMGFTEVtPVTGAsL
0 6 S814-p VtPVTGAsLRRTMLL
0 3 S823-p RRTMLLLsRsPEAQP
0 7 S825-p TMLLLsRsPEAQPKT
0 1 S975-p DGALFDKsCSDRAME
0 1 S986-p RAMESTEsRHYPVFE
0 3 H1097 AFEDGLRHPFIVNHP
0 1 K1105-a PFIVNHPkVGRVSIY
0 2 K1115-a RVSIYDSkRQSGKTK
0 2 K1166-a KNIFLLFkKLCSFRY
  mouse

 
- gap
T16 TGVFPHQTQSYLDPS
R30 SHEHSKWRYPQPQGP
K53-u LQQIEFLkGRLPEAP
S138 HFRELSISQSPEQKV
Y179 RDINRILYSLEKKGK
K193 KLHRGRGKPPLWSLV
- gap
S238-p SEDGDPAsDLEGPSE
K319 KRERLQMKRSTHSAP
T337 PTAVPEATRSPSFPA
K360-a SSSVAASkRVENGQE
K371 NGQEPAIKHESRHEA
H391 RLRPHAYHNGPSRAG
Y399 NGPSRAGYVASENGQ
S418 DIPDNLNSIHTAPGE
Y436 IMEMPSFYSPTLPRC
S437 MEMPSFYSPTLPRCS
K448 PRCSPYKKLTECQLK
S506 FPPAEAGSKKVAkQD
K511-u AGSKKVAkQDAAVKA
A520 DAAVKAMAILLREAK
K527 AILLREAKAKDSGQP
C540 QPEDLSHCPMEEDSE
K548 PMEEDSEKPAEAQAP
P549 MEEDSEKPAEAQAPS
A552 DSEKPAEAQAPSSSA
A554 EKPAEAQAPSSSATS
S556 PAEAQAPSSSATSLF
S558 EAQAPSSSATSLFSG
S564 SSATSLFSGKSPVTT
S567 TSLFSGKSPVTTLLE
S582-p CMHKLGNsCEFRLLS
K590 CEFRLLSKEGPAHDP
Y601 AHDPKFQYCVAVGAQ
K618 PPVSAPSKKVAKQMA
K618 PPVSAPSKKVAKQMA
K619 PVSAPSKKVAKQMAA
K619 PVSAPSKKVAKQMAA
Y671 RIGELVRYLNTNPVG
Y683 PVGGLLEYARSHGFA
K706 SGPPHEPKFVYQAKV
T757 QLGFAEVTPVTGASL
S763 VTPVTGASLRRTMLL
S772 RRTMLLLSRSPDAHP
S774 TMLLLSRSPDAHPKT
S924 DGALFDKSCSDRAVE
S935 RAVESTESRHYPVFE
Y1046-p AFEDGLRyPFIVNHP
K1054 PFIVNHPKVGRVSVY
K1064 RVSVYDSKRQSGKTK
K1115 KNIFLQFKKLCSFRA
  rat

 
- gap
T16 TGVFPHQTQPCLDPS
R30 SYEHSKWRYLQPRGS
K53 LQQIEFLKGRLPEAP
S138 HFQELSISQNPEQKV
Y179 KDINRILYSLERKGK
K193 KLHRGVGKPPLWSLV
- gap
S235 SEDGDPASDLEGPSE
K316 KRERLQMKRSTHSGP
T334 PAAVSEATQSTSFPT
K357 SSSMATSKRVENGQE
K368 NGQEPVTKYESRHEA
H388 RLRPHAYHNGPSRAG
Y396 NGPSRAGYVASENGP
S415 DIPDNLNSIHTAPGE
Y433 IMEMPSFYSPTLPRC
S434 MEMPSFYSPTLPRCS
K445 PRCSPYKKLTECQLK
S503 FPPAEAGSKKVAKQD
K508 AGSKKVAKQDAAVKA
A517 DAAVKAMAILLREAK
K524 AILLREAKAKDSGQP
C537 QPEELSNCPMEEDPE
K545 PMEEDPEKPAESQPP
P546 MEEDPEKPAESQPPS
S549 DPEKPAESQPPSSSA
P551 EKPAESQPPSSSATS
S553 PAESQPPSSSATSLF
S555 ESQPPSSSATSLFSG
S561 SSATSLFSGKSPVTT
S564 TSLFSGKSPVTTLLE
S579 CMHKLGNSCEFRLLS
K587 CEFRLLSKEGPAHDP
Y598 AHDPKFQYCVAVGAQ
K615 PSVSAPSKKVAKQMA
K615 PSVSAPSKKVAKQMA
K616 SVSAPSKKVAKQMAA
K616 SVSAPSKKVAKQMAA
Y668 RIGELVRYLNTNPVG
Y680 PVGGLLEYARSHGFA
K703 SGPPHEPKFVYQAKV
T754 QLGFAEVTPVTGASL
S760 VTPVTGASLRRTMLL
S769 RRTMLLLSRSPDAHP
S771 TMLLLSRSPDAHPKT
S921 DGAHFDKSCSDRAVE
S932 RAVESTESRHYPVFE
Y1043 AFEDGLRYPFIVNHP
K1051 PFIVNHPKVGRVSVY
K1061 RVSVYDSKRQSGKTK
K1112 KNIFLQFKKLCSFRA
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.