RED1_HUMAN - dbPTM
RED1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RED1_HUMAN
UniProt AC P78563
Protein Name Double-stranded RNA-specific editase 1
Gene Name ADARB1
Organism Homo sapiens (Human).
Sequence Length 741
Subcellular Localization Nucleus. Nucleus, nucleolus. Shuttles between nucleoli and the nucleoplasm.
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 GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently. Can exert a proviral effect towards human immunodeficiency virus type 1 (HIV-1) and enhances its replication via both an editing-dependent and editing-independent mechanism. The former involves editing of adenosines in the 5'UTR while the latter occurs via suppression of EIF2AK2/PKR activation and function. Can inhibit cell proliferation and migration and can stimulate exocytosis..
Protein Sequence MDIEDEENMSSSSTDVKENRNLDNVSPKDGSTPGPGEGSQLSNGGGGGPGRKRPLEEGSNGHSKYRLKKRRKTPGPVLPKNALMQLNEIKPGLQYTLLSQTGPVHAPLFVMSVEVNGQVFEGSGPTKKKAKLHAAEKALRSFVQFPNASEAHLAMGRTLSVNTDFTSDQADFPDTLFNGFETPDKAEPPFYVGSNGDDSFSSSGDLSLSASPVPASLAQPPLPVLPPFPPPSGKNPVMILNELRPGLKYDFLSESGESHAKSFVMSVVVDGQFFEGSGRNKKLAKARAAQSALAAIFNLHLDQTPSRQPIPSEGLQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYTQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEGSRSYTQAGVQWCNHGSLQPRPPGLLSDPSTSTFQGAGTTEPADRHPNRKARGQLRTKIESGEGTIPVRSNASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTP
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
10PhosphorylationIEDEENMSSSSTDVK
CCCCCCCCCCCCCHH		38.3523663014
11PhosphorylationEDEENMSSSSTDVKE
CCCCCCCCCCCCHHH		19.9623401153
12PhosphorylationDEENMSSSSTDVKEN
CCCCCCCCCCCHHHH		29.9223663014
13PhosphorylationEENMSSSSTDVKENR
CCCCCCCCCCHHHHC		30.4923663014
14PhosphorylationENMSSSSTDVKENRN
CCCCCCCCCHHHHCC		46.9223663014
26PhosphorylationNRNLDNVSPKDGSTP
HCCCCCCCCCCCCCC		32.2729255136
31PhosphorylationNVSPKDGSTPGPGEG
CCCCCCCCCCCCCCC		41.3821815630
32PhosphorylationVSPKDGSTPGPGEGS
CCCCCCCCCCCCCCC		37.4821815630
39PhosphorylationTPGPGEGSQLSNGGG
CCCCCCCCCCCCCCC		24.5221815630
42PhosphorylationPGEGSQLSNGGGGGP
CCCCCCCCCCCCCCC		26.2820068231
59PhosphorylationKRPLEEGSNGHSKYR
CCCCCCCCCCCCCHH		42.8120068231
63PhosphorylationEEGSNGHSKYRLKKR
CCCCCCCCCHHCCCC		32.5520068231
65PhosphorylationGSNGHSKYRLKKRRK
CCCCCCCHHCCCCCC		24.9620068231
73PhosphorylationRLKKRRKTPGPVLPK
HCCCCCCCCCCCCCH		31.5028674419
149PhosphorylationFVQFPNASEAHLAMG
HHCCCCHHHHHHHCC		41.7916297572
158PhosphorylationAHLAMGRTLSVNTDF
HHHHCCCEEEECCCC		20.0428348404
160PhosphorylationLAMGRTLSVNTDFTS
HHCCCEEEECCCCCC		16.8328348404
163PhosphorylationGRTLSVNTDFTSDQA
CCEEEECCCCCCCCC		30.2728348404
191PhosphorylationDKAEPPFYVGSNGDD
CCCCCCEECCCCCCC		15.0720873877
194PhosphorylationEPPFYVGSNGDDSFS
CCCEECCCCCCCCCC		27.8220873877
199PhosphorylationVGSNGDDSFSSSGDL
CCCCCCCCCCCCCCC		31.5920873877
201PhosphorylationSNGDDSFSSSGDLSL
CCCCCCCCCCCCCEE		27.7820873877
202PhosphorylationNGDDSFSSSGDLSLS
CCCCCCCCCCCCEEC		36.0120873877
203PhosphorylationGDDSFSSSGDLSLSA
CCCCCCCCCCCEECC		34.8220873877
207PhosphorylationFSSSGDLSLSASPVP
CCCCCCCEECCCCCC		25.6420873877
209PhosphorylationSSGDLSLSASPVPAS
CCCCCEECCCCCCHH		24.2720873877
211PhosphorylationGDLSLSASPVPASLA
CCCEECCCCCCHHHC		24.0520873877
216PhosphorylationSASPVPASLAQPPLP
CCCCCCHHHCCCCCC		20.4020873877
232PhosphorylationLPPFPPPSGKNPVMI
CCCCCCCCCCCCEEE		69.0820873877
255PhosphorylationKYDFLSESGESHAKS
CEEECCCCCCCHHCE		44.4725627689
304PhosphorylationFNLHLDQTPSRQPIP
HHCCCCCCCCCCCCC		23.9320068231
306PhosphorylationLHLDQTPSRQPIPSE
CCCCCCCCCCCCCCC		47.1120068231
334AcetylationVSRLVLGKFGDLTDN
HHHHHHHHHCCCCCC		41.8526051181
339PhosphorylationLGKFGDLTDNFSSPH
HHHHCCCCCCCCCHH		33.3727134283
343PhosphorylationGDLTDNFSSPHARRK
CCCCCCCCCHHHHHH		49.5729214152
344PhosphorylationDLTDNFSSPHARRKV
CCCCCCCCHHHHHHH		19.3025159151
358PhosphorylationVLAGVVMTTGTDVKD
HHEEEEEEECCCCCC		15.5128270605
359PhosphorylationLAGVVMTTGTDVKDA
HEEEEEEECCCCCCC		21.7128270605
361PhosphorylationGVVMTTGTDVKDAKV
EEEEEECCCCCCCEE		35.2128270605
370PhosphorylationVKDAKVISVSTGTKC
CCCCEEEEEECCCEE		17.0126503514
372PhosphorylationDAKVISVSTGTKCIN
CCEEEEEECCCEEEC		17.8326503514
373PhosphorylationAKVISVSTGTKCING
CEEEEEECCCEEECC		46.8726503514
375PhosphorylationVISVSTGTKCINGEY
EEEEECCCEEECCEE		23.8826503514
384PhosphorylationCINGEYMSDRGLALN
EECCEECCCCCCCCC		24.2126503514
424PhosphorylationNKDDQKRSIFQKSER
CCHHHHHHHHHHHCC		34.4922496350
428UbiquitinationQKRSIFQKSERGGFR
HHHHHHHHHCCCCEE		43.46-
429AcetylationKRSIFQKSERGGFRL
HHHHHHHHCCCCEEC		23.0319413330
429PhosphorylationKRSIFQKSERGGFRL
HHHHHHHHCCCCEEC		23.0322496350
458PhosphorylationCGDARIFSPHEPILE
CCCCEEECCCCCCCC		23.9928674419
523SumoylationARGQLRTKIESGEGT
CCCCCCCEEECCCCE		37.73-
523SumoylationARGQLRTKIESGEGT
CCCCCCCEEECCCCE		37.73-
530PhosphorylationKIESGEGTIPVRSNA
EEECCCCEEECCCCC		20.15-
535PhosphorylationEGTIPVRSNASIQTW
CCEEECCCCCEEEEE		36.6620873877
538PhosphorylationIPVRSNASIQTWDGV
EECCCCCEEEEECCE		21.3420873877
541PhosphorylationRSNASIQTWDGVLQG
CCCCEEEEECCEECC		24.6920873877
553PhosphorylationLQGERLLTMSCSDKI
ECCCEEEEEECCHHH		16.1921712546
555PhosphorylationGERLLTMSCSDKIAR
CCEEEEEECCHHHHH		12.7723836654
557PhosphorylationRLLTMSCSDKIARWN
EEEEEECCHHHHHCC		34.3323836654
559AcetylationLTMSCSDKIARWNVV
EEEECCHHHHHCCEE		23.2126051181
615PhosphorylationEDLPPLYTLNKPLLS
CCCCCCEECCCCHHC		31.3825690035
651UbiquitinationVGDSAIEVINATTGK
ECHHHEEEEECCCCC		3.1429967540
669MethylationGRASRLCKHALYCRW
HHHHHHHHHHHHHHH		36.18115976495
691UbiquitinationPSHLLRSKITKPNVY
CHHHHHCCCCCCCCC		48.2229967540
708PhosphorylationSKLAAKEYQAAKARL
HHHHHHHHHHHHHHH		11.62-
717PhosphorylationAAKARLFTAFIKAGL
HHHHHHHHHHHHHCC		25.8328634298
732PhosphorylationGAWVEKPTEQDQFSL
CCCCCCCCCCCCCCC		58.3020873877
738PhosphorylationPTEQDQFSLTP----
CCCCCCCCCCC----		26.2120873877
740PhosphorylationEQDQFSLTP------
CCCCCCCCC------		26.2525159151
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
211SPhosphorylationKinasePRKCZQ05513
GPS
216SPhosphorylationKinasePRKCZQ05513
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RED1_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 RED1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PIN1_HUMANPIN1physical
21847096
WWP2_HUMANWWP2physical
21847096
A4_HUMANAPPphysical
21832049
BRX1_HUMANBRIX1physical
24778252
MMTA2_HUMANC1orf35physical
24778252
CG050_HUMANC7orf50physical
24778252
CC124_HUMANCCDC124physical
24778252
EBP2_HUMANEBNA1BP2physical
24778252
IFRD2_HUMANIFRD2physical
24778252
MK67I_HUMANNIFKphysical
24778252
MRT4_HUMANMRTO4physical
24778252
NOP16_HUMANNOP16physical
24778252
RRS1_HUMANRRS1physical
24778252
SDA1_HUMANSDAD1physical
24778252
STRBP_HUMANSTRBPphysical
24778252
ZFR_HUMANZFRphysical
24778252
LPPRC_HUMANLRPPRCphysical
26344197
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 RED1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory