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RISC-loading complex subunit TARBP2 (TAR RNA-binding protein 2) (Trans-activation-responsive RNA-binding protein)

 TRBP2_HUMAN             Reviewed;         366 AA.
Q15633; Q12878; Q8WY32; Q8WY33; Q9BRY2;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
14-OCT-2008, sequence version 3.
30-AUG-2017, entry version 168.
RecName: Full=RISC-loading complex subunit TARBP2 {ECO:0000255|HAMAP-Rule:MF_03034};
AltName: Full=TAR RNA-binding protein 2;
AltName: Full=Trans-activation-responsive RNA-binding protein;
Name=TARBP2 {ECO:0000255|HAMAP-Rule:MF_03034}; Synonyms=TRBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT PHE-251.
PubMed=2011739; DOI=10.1126/science.2011739;
Gatignol A., Buckler-White A.J., Berkhout B., Jeang K.T.;
"Characterization of a human TAR RNA-binding protein that activates
the HIV-1 LTR.";
Science 251:1597-1600(1991).
[2]
SEQUENCE REVISION.
Gatignol A., Duarte M.;
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PHE-251.
PubMed=7774957; DOI=10.1016/0888-7543(95)80110-8;
Kozak C.A., Gatignol A., Graham K., Jeang K.T., McBride O.W.;
"Genetic mapping in human and mouse of the locus encoding TRBP, a
protein that binds the TAR region of the human immunodeficiency virus
(HIV-1).";
Genomics 25:66-72(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74, AND ALTERNATIVE PROMOTER
USAGE.
PubMed=11641396; DOI=10.1074/jbc.M104645200;
Bannwarth S., Talakoub L., Letourneur F., Duarte M., Purcell D.F.,
Hiscott J., Gatignol A.;
"Organization of the human tarbp2 gene reveals two promoters that are
repressed in an astrocytic cell line.";
J. Biol. Chem. 276:48803-48813(2001).
[8]
CHARACTERIZATION OF RNA-BINDING.
PubMed=8455607; DOI=10.1128/MCB.13.4.2193;
Gatignol A., Buckler C., Jeang K.T.;
"Relatedness of an RNA-binding motif in human immunodeficiency virus
type 1 TAR RNA-binding protein TRBP to human P1/dsI kinase and
Drosophila staufen.";
Mol. Cell. Biol. 13:2193-2202(1993).
[9]
SELF-ASSOCIATION, AND INTERACTION WITH EIF2AK2.
PubMed=11438532; DOI=10.1074/jbc.M103584200;
Daher A., Longuet M., Dorin D., Bois F., Segeral E., Bannwarth S.,
Battisti P.-L., Purcell D.F., Benarous R., Vaquero C., Meurs E.F.,
Gatignol A.;
"Two dimerization domains in the trans-activation response RNA-binding
protein (TRBP) individually reverse the protein kinase R inhibition of
HIV-1 long terminal repeat expression.";
J. Biol. Chem. 276:33899-33905(2001).
[10]
FUNCTION.
PubMed=12475984; DOI=10.1074/jbc.M208954200;
Dorin D., Bonnet M.C., Bannwarth S., Gatignol A., Meurs E.F.,
Vaquero C.;
"The TAR RNA-binding protein, TRBP, stimulates the expression of TAR-
containing RNAs in vitro and in vivo independently of its ability to
inhibit the dsRNA-dependent kinase PKR.";
J. Biol. Chem. 278:4440-4448(2003).
[11]
FUNCTION, AND INTERACTION WITH DICER1 AND AGO2.
PubMed=16271387; DOI=10.1016/j.cell.2005.10.022;
Gregory R.I., Chendrimada T.P., Cooch N., Shiekhattar R.;
"Human RISC couples microRNA biogenesis and posttranscriptional gene
silencing.";
Cell 123:631-640(2005).
[12]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SELF-ASSOCIATION, AND
INTERACTION WITH DICER1.
PubMed=16142218; DOI=10.1038/sj.embor.7400509;
Haase A.D., Jaskiewicz L., Zhang H., Laine S., Sack R., Gatignol A.,
Filipowicz W.;
"TRBP, a regulator of cellular PKR and HIV-1 virus expression,
interacts with Dicer and functions in RNA silencing.";
EMBO Rep. 6:961-967(2005).
[13]
FUNCTION, AND INTERACTION WITH DICER1 AND AGO2.
PubMed=16357216; DOI=10.1101/gad.1384005;
Maniataki E., Mourelatos Z.;
"A human, ATP-independent, RISC assembly machine fueled by pre-
miRNA.";
Genes Dev. 19:2979-2990(2005).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH DICER1
AND AGO2, AND RNA-BINDING.
PubMed=15973356; DOI=10.1038/nature03868;
Chendrimada T.P., Gregory R.I., Kumaraswamy E., Norman J., Cooch N.,
Nishikura K., Shiekhattar R.;
"TRBP recruits the Dicer complex to Ago2 for microRNA processing and
gene silencing.";
Nature 436:740-744(2005).
[15]
FUNCTION, INTERACTION WITH DICER1; AGO2 AND PRKRA, AND SUBCELLULAR
LOCATION.
PubMed=16424907; DOI=10.1038/sj.emboj.7600942;
Lee Y., Hur I., Park S.-Y., Kim Y.-K., Suh M.R., Kim V.N.;
"The role of PACT in the RNA silencing pathway.";
EMBO J. 25:522-532(2006).
[16]
FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DICER1 AND PRKRA, AND
SUBCELLULAR LOCATION.
PubMed=17452327; DOI=10.1074/jbc.M611768200;
Kok K.H., Ng M.-H., Ching Y.-P., Jin D.-Y.;
"Human TRBP and PACT directly interact with each other and associate
with dicer to facilitate the production of small interfering RNA.";
J. Biol. Chem. 282:17649-17657(2007).
[17]
INTERACTION WITH DHX9.
PubMed=17531811; DOI=10.1016/j.molcel.2007.04.016;
Robb G.B., Rana T.M.;
"RNA helicase A interacts with RISC in human cells and functions in
RISC loading.";
Mol. Cell 26:523-537(2007).
[18]
INTERACTION WITH DICER1; AGO2; EIF6; RPL7A AND MOV10, AND ASSOCIATION
WITH THE 60S RIBOSOME.
PubMed=17507929; DOI=10.1038/nature05841;
Chendrimada T.P., Finn K.J., Ji X., Baillat D., Gregory R.I.,
Liebhaber S.A., Pasquinelli A.E., Shiekhattar R.;
"MicroRNA silencing through RISC recruitment of eIF6.";
Nature 447:823-828(2007).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
DICER1 AND AGO2.
PubMed=18178619; DOI=10.1073/pnas.0710869105;
MacRae I.J., Ma E., Zhou M., Robinson C.V., Doudna J.A.;
"In vitro reconstitution of the human RISC-loading complex.";
Proc. Natl. Acad. Sci. U.S.A. 105:512-517(2008).
[21]
SELF-ASSOCIATION, INTERACTION WITH EIF2AK2 AND PRKRA, AND SUBCELLULAR
LOCATION.
PubMed=18421256; DOI=10.4161/rna.5.2.6069;
Laraki G., Clerzius G., Daher A., Melendez-Pena C., Daniels S.,
Gatignol A.;
"Interactions between the double-stranded RNA-binding proteins TRBP
and PACT define the Medipal domain that mediates protein-protein
interactions.";
RNA Biol. 5:92-103(2008).
[22]
FUNCTION.
PubMed=19219043; DOI=10.1038/ng.317;
Melo S.A., Ropero S., Moutinho C., Aaltonen L.A., Yamamoto H.,
Calin G.A., Rossi S., Fernandez A.F., Carneiro F., Oliveira C.,
Ferreira B., Liu C.-G., Villanueva A., Capella G., Schwartz S. Jr.,
Shiekhattar R., Esteller M.;
"A TARBP2 mutation in human cancer impairs microRNA processing and
DICER1 function.";
Nat. Genet. 41:365-370(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
STRUCTURE BY NMR OF 150-225.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the second DSRBD of TAR RNA-binding protein
2.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: Required for formation of the RNA induced silencing
complex (RISC). Component of the RISC loading complex (RLC), also
known as the micro-RNA (miRNA) loading complex (miRLC), which is
composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1
and TARBP2 are required to process precursor miRNAs (pre-miRNAs)
to mature miRNAs and then load them onto AGO2. AGO2 bound to the
mature miRNA constitutes the minimal RISC and may subsequently
dissociate from DICER1 and TARBP2. May also play a role in the
production of short interfering RNAs (siRNAs) from double-stranded
RNA (dsRNA) by DICER1. Binds to the HIV-1 TAR RNA which is located
in the long terminal repeat (LTR) of HIV-1, and stimulates
translation of TAR-containing RNAs. This is achieved in part at
least by binding to and inhibiting EIF2AK2/PKR, thereby reducing
phosphorylation and inhibition of EIF2S1/eIF-2-alpha. May also
promote translation of TAR-containing RNAs independently of
EIF2AK2/PKR. {ECO:0000255|HAMAP-Rule:MF_03034,
ECO:0000269|PubMed:12475984, ECO:0000269|PubMed:15973356,
ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387,
ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16424907,
ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:18178619,
ECO:0000269|PubMed:19219043}.
-!- SUBUNIT: Self-associates. Component of the RISC loading complex
(RLC), or micro-RNA (miRNA) loading complex (miRLC), which is
composed of DICER1, AGO2 and TARBP2. Note that the trimeric
RLC/miRLC is also referred to as RISC. Interacts with EIF2AK2/PKR
and inhibits its protein kinase activity. Interacts with DHX9 and
PRKRA. Interacts with DICER1, AGO2, MOV10, EIF6 and RPL7A (60S
ribosome subunit); they form a large RNA-induced silencing complex
(RISC) (PubMed:17507929). {ECO:0000255|HAMAP-Rule:MF_03034,
ECO:0000269|PubMed:11438532, ECO:0000269|PubMed:15973356,
ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387,
ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16424907,
ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:17507929,
ECO:0000269|PubMed:17531811, ECO:0000269|PubMed:18178619,
ECO:0000269|PubMed:18421256}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-978581, EBI-978581;
P55265-1:ADAR; NbExp=2; IntAct=EBI-978581, EBI-6913056;
P55265-5:ADAR; NbExp=3; IntAct=EBI-978581, EBI-6913210;
P78563-4:ADARB1; NbExp=4; IntAct=EBI-978581, EBI-12002366;
Q9UKV8:AGO2; NbExp=5; IntAct=EBI-978581, EBI-528269;
Q9UPY3:DICER1; NbExp=21; IntAct=EBI-978581, EBI-395506;
P19525:EIF2AK2; NbExp=2; IntAct=EBI-978581, EBI-640775;
O75569:PRKRA; NbExp=12; IntAct=EBI-978581, EBI-713955;
Q96SI9:STRBP; NbExp=3; IntAct=EBI-978581, EBI-740355;
Q8N8B7:TCEANC; NbExp=3; IntAct=EBI-978581, EBI-954696;
Q9UL40:ZNF346; NbExp=5; IntAct=EBI-978581, EBI-2462313;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=1; Synonyms=TRBP2;
IsoId=Q15633-1; Sequence=Displayed;
Name=2; Synonyms=TRBP1;
IsoId=Q15633-2; Sequence=VSP_035584;
-!- SIMILARITY: Belongs to the TARBP2 family. {ECO:0000255|HAMAP-
Rule:MF_03034}.
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EMBL; M60801; AAA36765.1; -; mRNA.
EMBL; U08998; AAB50581.2; -; mRNA.
EMBL; BT007140; AAP35804.1; -; mRNA.
EMBL; CH471054; EAW96720.1; -; Genomic_DNA.
EMBL; BC005860; AAH05860.1; -; mRNA.
EMBL; AF281068; AAL55730.1; -; Genomic_DNA.
EMBL; AF281068; AAL55731.1; -; Genomic_DNA.
CCDS; CCDS41791.1; -. [Q15633-2]
CCDS; CCDS8861.1; -. [Q15633-1]
PIR; G01420; G01420.
RefSeq; NP_004169.3; NM_004178.4. [Q15633-2]
RefSeq; NP_599150.1; NM_134323.1. [Q15633-1]
RefSeq; NP_599151.2; NM_134324.2. [Q15633-2]
RefSeq; XP_005269171.1; XM_005269114.1. [Q15633-2]
RefSeq; XP_005269172.1; XM_005269115.2. [Q15633-2]
UniGene; Hs.326; -.
UniGene; Hs.604255; -.
PDB; 2CPN; NMR; -; A=150-225.
PDB; 3ADL; X-ray; 2.20 A; A=161-231.
PDB; 3LLH; X-ray; 2.14 A; A/B=22-105.
PDB; 4WYQ; X-ray; 3.20 A; B/E=289-363.
PDBsum; 2CPN; -.
PDBsum; 3ADL; -.
PDBsum; 3LLH; -.
PDBsum; 4WYQ; -.
ProteinModelPortal; Q15633; -.
SMR; Q15633; -.
BioGrid; 112758; 78.
DIP; DIP-29665N; -.
IntAct; Q15633; 30.
MINT; MINT-92451; -.
STRING; 9606.ENSP00000266987; -.
iPTMnet; Q15633; -.
PhosphoSitePlus; Q15633; -.
BioMuta; TARBP2; -.
DMDM; 209572714; -.
EPD; Q15633; -.
MaxQB; Q15633; -.
PaxDb; Q15633; -.
PeptideAtlas; Q15633; -.
PRIDE; Q15633; -.
DNASU; 6895; -.
Ensembl; ENST00000266987; ENSP00000266987; ENSG00000139546. [Q15633-1]
Ensembl; ENST00000394357; ENSP00000377885; ENSG00000139546. [Q15633-2]
Ensembl; ENST00000456234; ENSP00000416077; ENSG00000139546. [Q15633-2]
GeneID; 6895; -.
KEGG; hsa:6895; -.
UCSC; uc001sdo.4; human. [Q15633-1]
CTD; 6895; -.
DisGeNET; 6895; -.
GeneCards; TARBP2; -.
HGNC; HGNC:11569; TARBP2.
HPA; CAB069406; -.
HPA; HPA051181; -.
HPA; HPA061454; -.
MIM; 605053; gene.
neXtProt; NX_Q15633; -.
OpenTargets; ENSG00000139546; -.
PharmGKB; PA36334; -.
eggNOG; KOG3732; Eukaryota.
eggNOG; ENOG410XSCK; LUCA.
GeneTree; ENSGT00890000139380; -.
HOGENOM; HOG000231919; -.
HOVERGEN; HBG001700; -.
InParanoid; Q15633; -.
KO; K18420; -.
OMA; PMEVQPP; -.
OrthoDB; EOG091G0I2L; -.
PhylomeDB; Q15633; -.
TreeFam; TF315953; -.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
SIGNOR; Q15633; -.
EvolutionaryTrace; Q15633; -.
GeneWiki; TARBP2; -.
GenomeRNAi; 6895; -.
PRO; PR:Q15633; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139546; -.
CleanEx; HS_TARBP2; -.
ExpressionAtlas; Q15633; baseline and differential.
Genevisible; Q15633; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016442; C:RISC complex; IEA:InterPro.
GO; GO:0070578; C:RISC-loading complex; IDA:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070883; F:pre-miRNA binding; IDA:BHF-UCL.
GO; GO:0036002; F:pre-mRNA binding; TAS:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:BHF-UCL.
GO; GO:0035197; F:siRNA binding; IDA:UniProtKB.
GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0010586; P:miRNA metabolic process; TAS:Reactome.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0050689; P:negative regulation of defense response to virus by host; IDA:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; TAS:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:0045070; P:positive regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0031054; P:pre-miRNA processing; IDA:UniProtKB.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IDA:UniProtKB.
GO; GO:0030422; P:production of siRNA involved in RNA interference; IDA:UniProtKB.
GO; GO:0046782; P:regulation of viral transcription; IDA:UniProtKB.
GO; GO:0007338; P:single fertilization; IEA:Ensembl.
GO; GO:0035087; P:siRNA loading onto RISC involved in RNA interference; IDA:UniProtKB.
GO; GO:0007286; P:spermatid development; IEA:Ensembl.
GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; IMP:UniProtKB.
HAMAP; MF_03034; TRBP2; 1.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR028605; TRBP2.
PANTHER; PTHR10910:SF124; PTHR10910:SF124; 1.
Pfam; PF00035; dsrm; 2.
SMART; SM00358; DSRM; 3.
PROSITE; PS50137; DS_RBD; 3.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Complete proteome;
Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; RNA-binding; RNA-mediated gene silencing;
Translation regulation.
CHAIN 1 366 RISC-loading complex subunit TARBP2.
/FTId=PRO_0000065622.
DOMAIN 30 97 DRBM 1. {ECO:0000255|HAMAP-
Rule:MF_03034}.
DOMAIN 159 227 DRBM 2. {ECO:0000255|HAMAP-
Rule:MF_03034}.
DOMAIN 293 361 DRBM 3. {ECO:0000255|HAMAP-
Rule:MF_03034}.
REGION 22 105 Sufficient for interaction with PRKRA.
REGION 152 234 Sufficient for interaction with PRKRA.
REGION 228 366 Sufficient for interaction with DICER1.
REGION 287 366 Sufficient for interaction with PRKRA.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 21 Missing (in isoform 2).
{ECO:0000303|PubMed:2011739}.
/FTId=VSP_035584.
VARIANT 251 251 S -> F (in dbSNP:rs1126500).
{ECO:0000269|PubMed:2011739,
ECO:0000269|PubMed:7774957}.
/FTId=VAR_046992.
CONFLICT 144 144 P -> A (in Ref. 1; AAA36765).
{ECO:0000305}.
HELIX 31 41 {ECO:0000244|PDB:3LLH}.
STRAND 47 53 {ECO:0000244|PDB:3LLH}.
STRAND 62 68 {ECO:0000244|PDB:3LLH}.
STRAND 71 79 {ECO:0000244|PDB:3LLH}.
HELIX 80 95 {ECO:0000244|PDB:3LLH}.
HELIX 161 170 {ECO:0000244|PDB:3ADL}.
STRAND 177 185 {ECO:0000244|PDB:3ADL}.
STRAND 187 189 {ECO:0000244|PDB:2CPN}.
STRAND 191 198 {ECO:0000244|PDB:3ADL}.
STRAND 201 209 {ECO:0000244|PDB:3ADL}.
HELIX 210 226 {ECO:0000244|PDB:3ADL}.
STRAND 291 293 {ECO:0000244|PDB:4WYQ}.
HELIX 294 305 {ECO:0000244|PDB:4WYQ}.
STRAND 309 316 {ECO:0000244|PDB:4WYQ}.
STRAND 323 329 {ECO:0000244|PDB:4WYQ}.
STRAND 331 333 {ECO:0000244|PDB:4WYQ}.
STRAND 335 343 {ECO:0000244|PDB:4WYQ}.
HELIX 344 362 {ECO:0000244|PDB:4WYQ}.
SEQUENCE 366 AA; 39039 MW; 768BA11751DA4912 CRC64;
MSEEEQGSGT TTGCGLPSIE QMLAANPGKT PISLLQEYGT RIGKTPVYDL LKAEGQAHQP
NFTFRVTVGD TSCTGQGPSK KAAKHKAAEV ALKHLKGGSM LEPALEDSSS FSPLDSSLPE
DIPVFTAAAA ATPVPSVVLT RSPPMELQPP VSPQQSECNP VGALQELVVQ KGWRLPEYTV
TQESGPAHRK EFTMTCRVER FIEIGSGTSK KLAKRNAAAK MLLRVHTVPL DARDGNEVEP
DDDHFSIGVG SRLDGLRNRG PGCTWDSLRN SVGEKILSLR SCSLGSLGAL GPACCRVLSE
LSEEQAFHVS YLDIEELSLS GLCQCLVELS TQPATVCHGS ATTREAARGE AARRALQYLK
IMAGSK


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