P78563 (RED1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Double-stranded RNA-specific editase 1
EC=3.5.-.-

Alternative name(s):
RNA-editing deaminase 1
RNA-editing enzyme 1
dsRNA adenosine deaminase

Gene names

Name:	ADARB1
Synonyms:	ADAR2, DRADA2, RED1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	741 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.11 Ref.15 Ref.18
Cofactor	Binds 1 inositol hexakisphosphate (IP6) per subunit.
Subunit structure	Homodimer. Homodimerization is essential for its catalytic activity. Can form heterodimers with isoform 5 of ADAR/ADAR1. Ref.11
Subcellular location	Nucleus. Nucleus › nucleolus. Note: Shuttles between nucleoli and the nucleoplasm. Ref.11 Ref.18
Tissue specificity	Highly expressed in brain and heart and at lower levels in placenta. Fair expression in lung, liver and kidney. Detected in brain, heart, kidney, lung and liver (at protein level). Isoform 5 is high expressed in hippocampus and colon. Isoform 5 is expressed in pediatric astrocytomas and the protein has a decreased RNA-editing activity. The decrease in RNA editing correlates with the grade of malignancy of the tumors, with the high grade tumors showing lower editing is seen. Ref.1 Ref.9 Ref.11
Sequence similarities	Contains 1 A to I editase domain. Contains 2 DRBM (double-stranded RNA-binding) domains.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Metal-binding RNA-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA processing Inferred from direct assay Ref.1. Source: HGNC adenosine to inosine editing Inferred from direct assay Ref.11Ref.18. Source: UniProtKB base conversion or substitution editing Inferred by curator Ref.1. Source: HGNC defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW gene expression Traceable author statement. Source: Reactome innate immune response Inferred from electronic annotation. Source: UniProtKB-KW mRNA modification Traceable author statement. Source: Reactome mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell migration Inferred from direct assay Ref.11. Source: UniProtKB negative regulation of cell proliferation Inferred from direct assay Ref.11. Source: UniProtKB negative regulation of protein kinase activity by regulation of protein phosphorylation Inferred from direct assay Ref.18. Source: UniProtKB positive regulation of viral genome replication Inferred from mutant phenotype Ref.18. Source: UniProtKB regulation of cell cycle Inferred from direct assay Ref.11. Source: UniProtKB
Cellular_component	nucleolus Inferred from direct assay Ref.11Ref.18. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome nucleus Inferred from direct assay PubMed 8995285. Source: HGNC
Molecular_function	RNA binding Inferred from direct assay Ref.3. Source: HGNC adenosine deaminase activity Inferred from electronic annotation. Source: InterPro double-stranded RNA adenosine deaminase activity Inferred from direct assay PubMed 8995285Ref.1. Source: HGNC double-stranded RNA binding Inferred from direct assay PubMed 8995285. Source: HGNC mRNA binding Traceable author statement Ref.1. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P78563-1)

Also known as: RED1-L; DRADA2B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Alu insert from position 465 to 505. Has a lower catalytic activity than isoform 2. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 2 (identifier: P78563-2)

Also known as: RED1-S; DRADA2A;

The sequence of this isoform differs from the canonical sequence as follows:
     466-505: Missing.

Note: Has a higher catalytic activity than isoform 1.

Isoform 3 (identifier: P78563-3)

Also known as: DRADA2C;

The sequence of this isoform differs from the canonical sequence as follows:
     713-741: ARLFTAFIKAGLGAWVEKPTEQDQFSLTP → VH

Isoform 4 (identifier: P78563-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKIPRMKTPCQPDRNSLRQSRNPQKYFA
     466-505: Missing.

Isoform 5 (identifier: P78563-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGTFFSVMGRRYKRRRKKRSERKDRNSLRQSRNPQKYFAM
     26-741: Missing.

Note: Incomplete sequence. Alternative 5'exon.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 741

741

Double-stranded RNA-specific editase 1

PRO_0000171779

Regions

Domain

78 – 144

67

DRBM 1

Domain

231 – 298

68

DRBM 2

Domain

370 – 737

368

A to I editase

Region

83 – 88

6

Interaction with substrate RNA By similarity

Region

104 – 105

2

Interaction with substrate RNA By similarity

Region

237 – 242

6

Interaction with substrate RNA By similarity

Region

259

1

Interaction with substrate RNA By similarity

Sites

Active site

396

1

Proton donor

Metal binding

394

1

Zinc

Metal binding

451

1

Zinc

Metal binding

556

1

Zinc

Binding site

400

1

Inositol hexakisphosphate

Binding site

401

1

Inositol hexakisphosphate

Binding site

559

1

Inositol hexakisphosphate

Binding site

562

1

Inositol hexakisphosphate

Binding site

669

1

Inositol hexakisphosphate

Binding site

702

1

Inositol hexakisphosphate

Binding site

712

1

Inositol hexakisphosphate

Binding site

730

1

Inositol hexakisphosphate

Amino acid modifications

Modified residue

26

1

Phosphoserine Ref.16

Natural variations

Alternative sequence

1

1

M → MKIPRMKTPCQPDRNSLRQS RNPQKYFA in isoform 4.

VSP_019597

Alternative sequence

1

1

M → MGTFFSVMGRRYKRRRKKRS ERKDRNSLRQSRNPQKYFAM in isoform 5.

VSP_041421

Alternative sequence

26 – 741

716

Missing in isoform 5.

VSP_041422

Alternative sequence

466 – 505

40

Missing in isoform 2 and isoform 4.

VSP_000865

Alternative sequence

713 – 741

29

ARLFT…FSLTP → VH in isoform 3.

VSP_000866

Experimental info

Sequence conflict

30

1

G → A in AAB58300. Ref.4

Sequence conflict

30

1

G → A in AAM83100. Ref.5

Sequence conflict

30

1

G → A in AAN10291. Ref.5

Sequence conflict

423

1

R → E in AAB58300. Ref.4

Sequence conflict

423

1

R → E in AAM83100. Ref.5

Sequence conflict

423

1

R → E in AAN10291. Ref.5

Sequence conflict

475

1

V → L in AAM83100. Ref.5

Sequence conflict

475

1

V → L in AAN10291. Ref.5

Secondary structure

1

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741

Helix Strand Turn

Details...

Helix

320 – 338

19

Turn

339 – 343

5

Helix

345 – 347

3

Beta strand

352 – 361

10

Helix

363 – 365

3

Beta strand

367 – 373

7

Helix

380 – 382

3

Helix

395 – 416

22

Helix

418 – 423

6

Beta strand

425 – 428

4

Beta strand

432 – 436

5

Beta strand

440 – 448

9

Helix

453 – 456

4

Beta strand

521 – 524

4

Helix

542 – 546

5

Beta strand

552 – 554

3

Helix

556 – 566

11

Helix

570 – 574

5

Beta strand

582 – 589

8

Helix

593 – 600

8

Helix

602 – 604

3

Beta strand

620 – 623

4

Beta strand

637 – 643

7

Beta strand

650 – 653

4

Turn

654 – 657

4

Helix

669 – 680

12

Helix

685 – 687

3

Helix

698 – 703

6

Helix

706 – 721

16

Helix

732 – 735

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (RED1-L) (DRADA2B) [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 02B583414DD59C20	FASTA	741	80,763
	10 20 30 40 50 60 MDIEDEENMS SSSTDVKENR NLDNVSPKDG STPGPGEGSQ LSNGGGGGPG RKRPLEEGSN 70 80 90 100 110 120 GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYTLLSQ TGPVHAPLFV MSVEVNGQVF 130 140 150 160 170 180 EGSGPTKKKA KLHAAEKALR SFVQFPNASE AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF 190 200 210 220 230 240 ETPDKAEPPF YVGSNGDDSF SSSGDLSLSA SPVPASLAQP PLPVLPPFPP PSGKNPVMIL 250 260 270 280 290 300 NELRPGLKYD FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALAAIFNLH 310 320 330 340 350 360 LDQTPSRQPI PSEGLQLHLP QVLADAVSRL VLGKFGDLTD NFSSPHARRK VLAGVVMTTG 370 380 390 400 410 420 TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR RSLLRFLYTQ LELYLNNKDD 430 440 450 460 470 480 QKRSIFQKSE RGGFRLKENV QFHLYISTSP CGDARIFSPH EPILEGSRSY TQAGVQWCNH 490 500 510 520 530 540 GSLQPRPPGL LSDPSTSTFQ GAGTTEPADR HPNRKARGQL RTKIESGEGT IPVRSNASIQ 550 560 570 580 590 600 TWDGVLQGER LLTMSCSDKI ARWNVVGIQG SLLSIFVEPI YFSSIILGSL YHGDHLSRAM 610 620 630 640 650 660 YQRISNIEDL PPLYTLNKPL LSGISNAEAR QPGKAPNFSV NWTVGDSAIE VINATTGKDE 670 680 690 700 710 720 LGRASRLCKH ALYCRWMRVH GKVPSHLLRS KITKPNVYHE SKLAAKEYQA AKARLFTAFI 730 740 KAGLGAWVEK PTEQDQFSLT P
	Isoform 2 (RED1-S) (DRADA2A) [UniParc]. Checksum: 12D26888C1F131B6	FASTA	701	76,633
	10 20 30 40 50 60 MDIEDEENMS SSSTDVKENR NLDNVSPKDG STPGPGEGSQ LSNGGGGGPG RKRPLEEGSN 70 80 90 100 110 120 GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYTLLSQ TGPVHAPLFV MSVEVNGQVF 130 140 150 160 170 180 EGSGPTKKKA KLHAAEKALR SFVQFPNASE AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF 190 200 210 220 230 240 ETPDKAEPPF YVGSNGDDSF SSSGDLSLSA SPVPASLAQP PLPVLPPFPP PSGKNPVMIL 250 260 270 280 290 300 NELRPGLKYD FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALAAIFNLH 310 320 330 340 350 360 LDQTPSRQPI PSEGLQLHLP QVLADAVSRL VLGKFGDLTD NFSSPHARRK VLAGVVMTTG 370 380 390 400 410 420 TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR RSLLRFLYTQ LELYLNNKDD 430 440 450 460 470 480 QKRSIFQKSE RGGFRLKENV QFHLYISTSP CGDARIFSPH EPILEEPADR HPNRKARGQL 490 500 510 520 530 540 RTKIESGEGT IPVRSNASIQ TWDGVLQGER LLTMSCSDKI ARWNVVGIQG SLLSIFVEPI 550 560 570 580 590 600 YFSSIILGSL YHGDHLSRAM YQRISNIEDL PPLYTLNKPL LSGISNAEAR QPGKAPNFSV 610 620 630 640 650 660 NWTVGDSAIE VINATTGKDE LGRASRLCKH ALYCRWMRVH GKVPSHLLRS KITKPNVYHE 670 680 690 700 SKLAAKEYQA AKARLFTAFI KAGLGAWVEK PTEQDQFSLT P
	Isoform 3 (DRADA2C) [UniParc]. Checksum: 10F6C71FFB641CFE	FASTA	714	77,795
	10 20 30 40 50 60 MDIEDEENMS SSSTDVKENR NLDNVSPKDG STPGPGEGSQ LSNGGGGGPG RKRPLEEGSN 70 80 90 100 110 120 GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYTLLSQ TGPVHAPLFV MSVEVNGQVF 130 140 150 160 170 180 EGSGPTKKKA KLHAAEKALR SFVQFPNASE AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF 190 200 210 220 230 240 ETPDKAEPPF YVGSNGDDSF SSSGDLSLSA SPVPASLAQP PLPVLPPFPP PSGKNPVMIL 250 260 270 280 290 300 NELRPGLKYD FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALAAIFNLH 310 320 330 340 350 360 LDQTPSRQPI PSEGLQLHLP QVLADAVSRL VLGKFGDLTD NFSSPHARRK VLAGVVMTTG 370 380 390 400 410 420 TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR RSLLRFLYTQ LELYLNNKDD 430 440 450 460 470 480 QKRSIFQKSE RGGFRLKENV QFHLYISTSP CGDARIFSPH EPILEGSRSY TQAGVQWCNH 490 500 510 520 530 540 GSLQPRPPGL LSDPSTSTFQ GAGTTEPADR HPNRKARGQL RTKIESGEGT IPVRSNASIQ 550 560 570 580 590 600 TWDGVLQGER LLTMSCSDKI ARWNVVGIQG SLLSIFVEPI YFSSIILGSL YHGDHLSRAM 610 620 630 640 650 660 YQRISNIEDL PPLYTLNKPL LSGISNAEAR QPGKAPNFSV NWTVGDSAIE VINATTGKDE 670 680 690 700 710 LGRASRLCKH ALYCRWMRVH GKVPSHLLRS KITKPNVYHE SKLAAKEYQA AKVH
	Isoform 4 [UniParc]. Checksum: F1C025263B9D3F3F	FASTA	728	79,876
	10 20 30 40 50 60 MKIPRMKTPC QPDRNSLRQS RNPQKYFADI EDEENMSSSS TDVKENRNLD NVSPKDGSTP 70 80 90 100 110 120 GPGEGSQLSN GGGGGPGRKR PLEEGSNGHS KYRLKKRRKT PGPVLPKNAL MQLNEIKPGL 130 140 150 160 170 180 QYTLLSQTGP VHAPLFVMSV EVNGQVFEGS GPTKKKAKLH AAEKALRSFV QFPNASEAHL 190 200 210 220 230 240 AMGRTLSVNT DFTSDQADFP DTLFNGFETP DKAEPPFYVG SNGDDSFSSS GDLSLSASPV 250 260 270 280 290 300 PASLAQPPLP VLPPFPPPSG KNPVMILNEL RPGLKYDFLS ESGESHAKSF VMSVVVDGQF 310 320 330 340 350 360 FEGSGRNKKL AKARAAQSAL AAIFNLHLDQ TPSRQPIPSE GLQLHLPQVL ADAVSRLVLG 370 380 390 400 410 420 KFGDLTDNFS SPHARRKVLA GVVMTTGTDV KDAKVISVST GTKCINGEYM SDRGLALNDC 430 440 450 460 470 480 HAEIISRRSL LRFLYTQLEL YLNNKDDQKR SIFQKSERGG FRLKENVQFH LYISTSPCGD 490 500 510 520 530 540 ARIFSPHEPI LEEPADRHPN RKARGQLRTK IESGEGTIPV RSNASIQTWD GVLQGERLLT 550 560 570 580 590 600 MSCSDKIARW NVVGIQGSLL SIFVEPIYFS SIILGSLYHG DHLSRAMYQR ISNIEDLPPL 610 620 630 640 650 660 YTLNKPLLSG ISNAEARQPG KAPNFSVNWT VGDSAIEVIN ATTGKDELGR ASRLCKHALY 670 680 690 700 710 720 CRWMRVHGKV PSHLLRSKIT KPNVYHESKL AAKEYQAAKA RLFTAFIKAG LGAWVEKPTE QDQFSLTP
	Isoform 5 [UniParc]. Checksum: F931D8FC8850764D	FASTA	64	7,778
	10 20 30 40 50 60 MGTFFSVMGR RYKRRRKKRS ERKDRNSLRQ SRNPQKYFAM DIEDEENMSS SSTDVKENRN LDNV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two forms of human double-stranded RNA-specific editase 1 (hRED1) generated by the insertion of an Alu cassette." Gerber A., O'Connell M.A., Keller W. RNA 3:453-463(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, CATALYTIC ACTIVITY. Tissue: Brain.
[2]	"Cloning of a human RNA editing deaminase (ADARB1) of glutamate receptors that maps to chromosome 21q22.3." Mittaz L., Scott H.S., Rossier C., Seeburg P.H., Higuchi M., Antonarakis S.E. Genomics 41:210-217(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Fetal brain.
[3]	"Editing of glutamate receptor B subunit ion channel RNAs by four alternatively spliced DRADA2 double-stranded RNA adenosine deaminases." Lai F., Chen C.-X., Carter K.C., Nishikura K. Mol. Cell. Biol. 17:2413-2424(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
[4]	"Map location, genomic organization and expression patterns of the human RED1 RNA editase." Villard L., Tassone F., Haymowicz M., Welborn R., Gardiner K. Somat. Cell Mol. Genet. 23:135-145(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Phylogenetic comparison of the pre-mRNA adenosine deaminase ADAR2 genes and transcripts: conservation and diversity in editing site sequence and alternative splicing patterns." Slavov D., Gardiner K. Gene 299:83-94(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[6]	"Novel splice variants of human ADAR2 mRNA: skipping of the exon encoding the dsRNA-binding domains, and multiple C-terminal splice sites." Kawahara Y., Ito K., Ito M., Tsuji S., Kwak S. Gene 363:193-201(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[7]	"The DNA sequence of human chromosome 21." Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L. Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"Novel exon of mammalian ADAR2 extends open reading frame." Maas S., Gommans W.M. PLoS ONE 4:E4225-E4225(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY.
[10]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[11]	"Down-regulation of RNA editing in pediatric astrocytomas: ADAR2 editing activity inhibits cell migration and proliferation." Cenci C., Barzotti R., Galeano F., Corbelli S., Rota R., Massimi L., Di Rocco C., O'Connell M.A., Gallo A. J. Biol. Chem. 283:7251-7260(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[14]	"Functions and regulation of RNA editing by ADAR deaminases." Nishikura K. Annu. Rev. Biochem. 79:321-349(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[15]	"Human BLCAP transcript: new editing events in normal and cancerous tissues." Galeano F., Leroy A., Rossetti C., Gromova I., Gautier P., Keegan L.P., Massimi L., Di Rocco C., O'Connell M.A., Gallo A. Int. J. Cancer 127:127-137(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"RNA editing catalyzed by ADAR1 and its function in mammalian cells." Wang Q. Biokhimiia 76:900-911(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[18]	"ADAR2 editing enzyme is a novel human immunodeficiency virus-1 proviral factor." Doria M., Tomaselli S., Neri F., Ciafre S.A., Farace M.G., Michienzi A., Gallo A. J. Gen. Virol. 92:1228-1232(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[19]	"Adenosine deaminases acting on RNA, RNA editing, and interferon action." George C.X., Gan Z., Liu Y., Samuel C.E. J. Interferon Cytokine Res. 31:99-117(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[20]	"Adenosine deaminases acting on RNA (ADARs) are both antiviral and proviral." Samuel C.E. Virology 411:180-193(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[21]	"A-to-I editing of protein coding and noncoding RNAs." Mallela A., Nishikura K. Crit. Rev. Biochem. Mol. Biol. 47:493-501(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[22]	"ADAR proteins: structure and catalytic mechanism." Goodman R.A., Macbeth M.R., Beal P.A. Curr. Top. Microbiol. Immunol. 353:1-33(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[23]	"Activity regulation of adenosine deaminases acting on RNA (ADARs)." Orlandi C., Barbon A., Barlati S. Mol. Neurobiol. 45:61-75(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[24]	"Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing." Macbeth M.R., Schubert H.L., Vandemark A.P., Lingam A.T., Hill C.P., Bass B.L. Science 309:1534-1539(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 299-741 IN COMPLEX WITH IP6.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U82120 mRNA. Translation: AAB61686.1.
U82121 mRNA. Translation: AAB61687.1.
X99227 mRNA. Translation: CAA67611.1.
X99383 mRNA. Translation: CAA67762.1.
U76420 mRNA. Translation: AAC51240.1.
U76421 mRNA. Translation: AAC51241.1.
U76422 mRNA. Translation: AAC51242.1.
AF001042 mRNA. Translation: AAB58300.1.
AF525422 mRNA. Translation: AAM83100.1.
AY135659 mRNA. Translation: AAN10291.1.
AB194370 mRNA. Translation: BAE16326.1.
AB194371 mRNA. Translation: BAE16327.1.
AB194372 mRNA. Translation: BAE16328.1.
AL163301 Genomic DNA. Translation: CAB90493.1.
AP001579 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09359.1.
CH471079 Genomic DNA. Translation: EAX09360.1.
FJ169505 mRNA. Translation: ACN49026.1.

IPI

IPI00020368.
IPI00184874.
IPI00334613.
IPI00477012.
IPI01019091.

RefSeq

NP_001103.1. NM_001112.3.
NP_056648.1. NM_015833.3.
NP_056649.1. NM_015834.3.

UniGene

Hs.474018.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZY7	X-ray	1.70	A/B	299-741	[»]

ProteinModelPortal

P78563.

ModBase

Search...

Protein-protein interaction databases

IntAct

P78563. 1 interaction.

PTM databases

PhosphoSite

P78563.

Polymorphism databases

DMDM

2829669.

Proteomic databases

PaxDb

P78563.

PRIDE

P78563.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000348831; ENSP00000015877; ENSG00000197381.
ENST00000360697; ENSP00000353920; ENSG00000197381.
ENST00000389863; ENSP00000374513; ENSG00000197381.
ENST00000492414; ENSP00000436367; ENSG00000197381.
ENST00000496664; ENSP00000435381; ENSG00000197381.
ENST00000539173; ENSP00000441897; ENSG00000197381.

GeneID

104.

KEGG

hsa:104.

UCSC

uc002zgr.2. human.
uc002zgt.2. human.
uc002zgy.2. human.

Organism-specific databases

CTD

104.

GeneCards

GC21P046493.

HGNC

HGNC:226. ADARB1.

HPA

HPA018277.
HPA029645.

MIM

601218. gene.

neXtProt

NX_P78563.

PharmGKB

PA24556.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG292433.

HOVERGEN

HBG003836.

InParanoid

P78563.

KO

K13194.

OMA

PPLYTLN.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P78563.

Bgee

P78563.

Genevestigator

P78563.

GermOnline

ENSG00000197381. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.20. 2 hits.

InterPro

IPR002466. A_deamin.
IPR008996. Cytokine_IL1-like.
IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like_dom.
[Graphical view]

Pfam

PF02137. A_deamin. 1 hit.
PF00035. dsrm. 2 hits.
[Graphical view]

SMART

SM00552. ADEAMc. 1 hit.
SM00358. DSRM. 2 hits.
[Graphical view]

SUPFAM

SSF50353. Cytok_IL1_like. 1 hit.

PROSITE

PS50141. A_DEAMIN_EDITASE. 1 hit.
PS50137. DS_RBD. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P78563.

GenomeRNAi

104.

NextBio

399.

SOURCE

Search...

Entry information

Entry name

RED1_HUMAN

Accession

Primary (citable) accession number: P78563
Secondary accession number(s): A6NFK8 , A6NJ84, C3TTQ1, O00395, O00465, O00691, O00692, P78555, Q4AE79, Q8NFD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.