Double-stranded RNA-specific editase 1

Preferred order of sections

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

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

General annotation (Comments)

Function	Editing of the messenger RNAs for glutamate receptor (GluR) subunits by site-selective adenosine deamination. Edits both the GluR-B Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently.
Cofactor	Binds 1 inositol hexakisphosphate (IP6) per subunit.
Tissue specificity	Highly expressed in brain and heart and at lower levels in placenta. Fair expression in lung, liver and kikney. Detected in brain, heart, kidney, lung and liver (at protein level). Isoform 5 is high expressed in hippocampus and colon. Ref.1 Ref.9
Sequence similarities	Contains 1 A to I editase domain. Contains 2 DRBM (double-stranded RNA-binding) domains.

Ontologies

Keywords
Biological process	mRNA processing
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 Traceable author statement. Source: Reactome base conversion or substitution editing Inferred by curator Ref.1. Source: HGNC mRNA modification Traceable author statement. Source: Reactome mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleoplasm Traceable author statement. Source: Reactome nucleus Inferred from direct assay. 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 Ref.1. Source: HGNC double-stranded RNA binding Inferred from electronic annotation. Source: InterPro 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

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.11 Ref.12

Natural variations

Alternative sequence

1

M → MKIPRMKTPCQPDRNSLRQS RNPQKYFA in isoform 4.

VSP_019597

Alternative sequence

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

.

741

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform 1 (RED1-L) (DRADA2B) [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 02B583414DD59C20 Show »	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 « Hide
Isoform 2 (RED1-S) (DRADA2A) [UniParc]. Checksum: 12D26888C1F131B6 Show »	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 « Hide
Isoform 3 (DRADA2C) [UniParc]. Checksum: 10F6C71FFB641CFE Show »	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 « Hide
Isoform 4 [UniParc]. Checksum: F1C025263B9D3F3F Show »	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 « Hide
Isoform 5 [UniParc]. Checksum: F931D8FC8850764D Show »	FASTA	64	7,778
10 20 30 40 50 60 MGTFFSVMGR RYKRRRKKRS ERKDRNSLRQ SRNPQKYFAM DIEDEENMSS SSTDVKENRN LDNV « Hide

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: 9149227] [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: 9143496] [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: 9111310] [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: 9330641] [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: 12459255] [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: 16297572] [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. Yaspo M.-L. Nature 405:311-319(2000) [PubMed: 10830953] [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. 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: 19156214] [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: 14759258] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[11]	"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) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 16141067] [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.

SMR

P78563. Positions 74-301, 306-740.

ModBase

Search...

Protein-protein interaction databases

IntAct

P78563. 1 interaction.

STRING

P78563.

PTM databases

PhosphoSite

P78563.

Polymorphism databases

DMDM

2829669.

Proteomic databases

PRIDE

P78563.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360697; ENSP00000353920; ENSG00000197381.

GeneID

104.

KEGG

hsa:104.

UCSC

uc002zgq.1. human.
uc002zgr.1. 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

prNOG15982.

GeneTree

ENSGT00550000074412.

HOVERGEN

HBG003836.

InParanoid

P78563.

OMA

DEENMSS.

PhylomeDB

P78563.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.

Gene expression databases

ArrayExpress

P78563.

Bgee

P78563.

Genevestigator

P78563.

GermOnline

ENSG00000197381. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.30.160.20. dsRNA-bd-like. 2 hits.

KO

K13194.

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

NextBio

399.

SOURCE

Search...

Entry information

Entry name

RED1_HUMAN

Accession

Primary (citable) accession number: P78563
Secondary accession number(s): A6NFK8

Q8NFD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	January 25, 2012
This is version 115 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.

Relevant documents

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families