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Interferon-inducible double-stranded RNA-dependent protein kinase activator A (PKR-associated protein X) (PKR-associating protein X) (Protein activator of the interferon-induced protein kinase) (Protein kinase, interferon-inducible double-stranded RNA-dependent activator)

 PRKRA_HUMAN             Reviewed;         313 AA.
O75569; A8K3I6; Q53G24; Q6X7T5; Q8NDK4;
21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 164.
RecName: Full=Interferon-inducible double-stranded RNA-dependent protein kinase activator A;
AltName: Full=PKR-associated protein X;
AltName: Full=PKR-associating protein X;
AltName: Full=Protein activator of the interferon-induced protein kinase;
AltName: Full=Protein kinase, interferon-inducible double-stranded RNA-dependent activator;
Name=PRKRA; Synonyms=PACT, RAX; ORFNames=HSD-14, HSD14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
EIF2AK2.
TISSUE=Placenta;
PubMed=9687506; DOI=10.1093/emboj/17.15.4379;
Patel R.C., Sen G.C.;
"PACT, a protein activator of the interferon-induced protein kinase,
PKR.";
EMBO J. 17:4379-4390(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=10336432; DOI=10.1074/jbc.274.22.15427;
Ito T., Yang M., May W.S.;
"RAX, a cellular activator for double-stranded RNA-dependent protein
kinase during stress signaling.";
J. Biol. Chem. 274:15427-15432(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
Hu T.H., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.;
"A new spermatogenesis-related gene.";
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Heart;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[10]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[12]
FUNCTION, AND INTERACTION WITH EIF2AK2.
PubMed=11238927; DOI=10.1128/MCB.21.6.1908-1920.2001;
Peters G.A., Hartmann R., Qin J., Sen G.C.;
"Modular structure of PACT: distinct domains for binding and
activating PKR.";
Mol. Cell. Biol. 21:1908-1920(2001).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
FUNCTION, INTERACTION WITH DICER1; AGO2 AND TARBP2, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF 298-ALA-ALA-299.
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).
[15]
FUNCTION, INTERACTION WITH EIF2AK2, SUBCELLULAR LOCATION,
PHOSPHORYLATION AT SER-246 AND SER-287, AND MUTAGENESIS OF SER-18;
GLN-243; SER-246; ASP-260; ASP-262; SER-265; GLN-271; SER-279;
SER-287; GLY-288 AND CYS-291.
PubMed=16982605; DOI=10.1074/jbc.M607714200;
Peters G.A., Li S., Sen G.C.;
"Phosphorylation of specific serine residues in the PKR activation
domain of PACT is essential for its ability to mediate apoptosis.";
J. Biol. Chem. 281:35129-35136(2006).
[16]
FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DICER1 AND TARBP2, 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 DUS2L.
PubMed=18096616; DOI=10.1093/nar/gkm1129;
Mittelstadt M., Frump A., Khuu T., Fowlkes V., Handy I., Patel C.V.,
Patel R.C.;
"Interaction of human tRNA-dihydrouridine synthase-2 with interferon-
induced protein kinase PKR.";
Nucleic Acids Res. 36:998-1008(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND 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).
[19]
SELF-ASSOCIATION, INTERACTION WITH EIF2AK2 AND TARBP2, 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
SUBCELLULAR LOCATION.
PubMed=22214662; DOI=10.4161/cc.11.2.18999;
Bennett R.L., Pan Y., Christian J., Hui T., May W.S. Jr.;
"The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and
activation, leading to G(1) arrest.";
Cell Cycle 11:407-417(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-167, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
STRUCTURE BY NMR OF 32-104.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the DSRM domain of protein activator of the
interferon-induced protein kinase.";
Submitted (SEP-2006) to the PDB data bank.
[27]
VARIANT DYT16 LEU-222.
PubMed=18243799; DOI=10.1016/S1474-4422(08)70022-X;
Camargos S., Scholz S., Simon-Sanchez J., Paisan-Ruiz C., Lewis P.,
Hernandez D., Ding J., Gibbs J.R., Cookson M.R., Bras J.,
Guerreiro R., Oliveira C.R., Lees A., Hardy J., Cardoso F.,
Singleton A.B.;
"DYT16, a novel young-onset dystonia-parkinsonism disorder:
identification of a segregating mutation in the stress-response
protein PRKRA.";
Lancet Neurol. 7:207-215(2008).
[28]
INVOLVEMENT IN DYT16.
PubMed=18420150; DOI=10.1016/S1474-4422(08)70075-9;
Seibler P., Djarmati A., Langpap B., Hagenah J., Schmidt A.,
Brueggemann N., Siebner H., Jabusch H.-C., Altenmueller E.,
Muenchau A., Lohmann K., Klein C.;
"A heterozygous frameshift mutation in PRKRA (DYT16) associated with
generalised dystonia in a German patient.";
Lancet Neurol. 7:380-381(2008).
-!- FUNCTION: Activates EIF2AK2/PKR in the absence of double-stranded
RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and
inhibition of translation and induction of apoptosis. Required for
siRNA production by DICER1 and for subsequent siRNA-mediated post-
transcriptional gene silencing. Does not seem to be required for
processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53
association and sumoylation and phosphorylation of p53/TP53 at
'Lys-386' at 'Ser-392' respectively and enhances its activity in a
EIF2AK2/PKR-dependent manner (By similarity). {ECO:0000250,
ECO:0000269|PubMed:10336432, ECO:0000269|PubMed:11238927,
ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:16982605,
ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:9687506}.
-!- SUBUNIT: Homodimer. Interacts with EIF2AK2/PKR through its DRBM
domains. Interacts with DICER1, AGO2 and TARBP2. Also able to
interact with dsRNA. Interacts with UBC9 (By similarity). Forms a
complex with UBC9 and p53/TP53 (By similarity). Interacts with
DUS2L (via DRBM domain). {ECO:0000250,
ECO:0000269|PubMed:11238927, ECO:0000269|PubMed:16424907,
ECO:0000269|PubMed:16982605, ECO:0000269|PubMed:17452327,
ECO:0000269|PubMed:18096616, ECO:0000269|PubMed:18421256,
ECO:0000269|PubMed:9687506}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-713955, EBI-713955;
P78563-4:ADARB1; NbExp=4; IntAct=EBI-713955, EBI-12002366;
Q9UKV8:AGO2; NbExp=5; IntAct=EBI-713955, EBI-528269;
O95786:DDX58; NbExp=2; IntAct=EBI-713955, EBI-995350;
Q9UPY3:DICER1; NbExp=7; IntAct=EBI-713955, EBI-395506;
P19525:EIF2AK2; NbExp=4; IntAct=EBI-713955, EBI-640775;
Q9NX58:LYAR; NbExp=4; IntAct=EBI-713955, EBI-713507;
O15226:NKRF; NbExp=3; IntAct=EBI-713955, EBI-766011;
P03496:NS (xeno); NbExp=3; IntAct=EBI-713955, EBI-2547442;
Q67020:PA (xeno); NbExp=3; IntAct=EBI-713955, EBI-11514477;
Q15633:TARBP2; NbExp=12; IntAct=EBI-713955, EBI-978581;
Q05127:VP35 (xeno); NbExp=2; IntAct=EBI-713955, EBI-6148294;
Q9HA38:ZMAT3; NbExp=3; IntAct=EBI-713955, EBI-2548480;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O75569-1; Sequence=Displayed;
Name=2;
IsoId=O75569-2; Sequence=VSP_017283;
Note=No experimental confirmation available.;
Name=3;
IsoId=O75569-3; Sequence=VSP_017282;
Note=No experimental confirmation available.;
-!- DOMAIN: Self-association may occur via interactions between DRBM
domains as follows: DRBM 1/DRBM 1, DRBM 1/DRBM 2, DRBM 2/DRBM 2 or
DRBM 3/DRBM3.
-!- PTM: Phosphorylated at Ser-246 in unstressed cells and at Ser-287
in stressed cells. Phosphorylation at Ser-246 appears to be a
prerequisite for subsequent phosphorylation at Ser-287.
Phosphorylation at Ser-246 and Ser-287 are necessary for
activation of EIF2AK2/PKR under conditions of stress.
{ECO:0000269|PubMed:16982605}.
-!- DISEASE: Dystonia 16 (DYT16) [MIM:612067]: An early-onset
dystonia-parkinsonism disorder. Dystonia is defined by the
presence of sustained involuntary muscle contraction, often
leading to abnormal postures. DYT16 patients have progressive,
generalized dystonia with axial muscle involvement, oro-mandibular
(sardonic smile) and laryngeal dystonia and, in some cases,
parkinsonian features. {ECO:0000269|PubMed:18243799,
ECO:0000269|PubMed:18420150}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the PRKRA family. {ECO:0000305}.
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EMBL; AF072860; AAC25672.1; -; mRNA.
EMBL; AF083033; AAD33099.1; -; mRNA.
EMBL; AY251164; AAP20061.1; -; mRNA.
EMBL; AL136615; CAB66550.1; -; mRNA.
EMBL; AL833867; CAD38725.1; -; Transcribed_RNA.
EMBL; BT007243; AAP35907.1; -; mRNA.
EMBL; AK290601; BAF83290.1; -; mRNA.
EMBL; CR533525; CAG38556.1; -; mRNA.
EMBL; AK223107; BAD96827.1; -; mRNA.
EMBL; AC009948; AAX88882.1; -; Genomic_DNA.
EMBL; CH471058; EAX11036.1; -; Genomic_DNA.
EMBL; BC009470; AAH09470.1; -; mRNA.
CCDS; CCDS2279.1; -. [O75569-1]
CCDS; CCDS46460.1; -. [O75569-2]
CCDS; CCDS46461.1; -. [O75569-3]
RefSeq; NP_001132989.1; NM_001139517.1. [O75569-2]
RefSeq; NP_001132990.1; NM_001139518.1. [O75569-3]
RefSeq; NP_003681.1; NM_003690.4. [O75569-1]
UniGene; Hs.570274; -.
PDB; 2DIX; NMR; -; A=33-103.
PDBsum; 2DIX; -.
ProteinModelPortal; O75569; -.
SMR; O75569; -.
BioGrid; 114143; 65.
DIP; DIP-41809N; -.
IntAct; O75569; 46.
MINT; MINT-5003897; -.
STRING; 9606.ENSP00000318176; -.
iPTMnet; O75569; -.
PhosphoSitePlus; O75569; -.
BioMuta; PRKRA; -.
EPD; O75569; -.
MaxQB; O75569; -.
PaxDb; O75569; -.
PeptideAtlas; O75569; -.
PRIDE; O75569; -.
DNASU; 8575; -.
Ensembl; ENST00000325748; ENSP00000318176; ENSG00000180228. [O75569-1]
Ensembl; ENST00000432031; ENSP00000393883; ENSG00000180228. [O75569-2]
Ensembl; ENST00000487082; ENSP00000430604; ENSG00000180228. [O75569-3]
GeneID; 8575; -.
KEGG; hsa:8575; -.
UCSC; uc002umd.4; human. [O75569-1]
CTD; 8575; -.
DisGeNET; 8575; -.
EuPathDB; HostDB:ENSG00000180228.12; -.
GeneCards; PRKRA; -.
HGNC; HGNC:9438; PRKRA.
HPA; CAB004648; -.
HPA; HPA034996; -.
HPA; HPA034997; -.
MalaCards; PRKRA; -.
MIM; 603424; gene.
MIM; 612067; phenotype.
neXtProt; NX_O75569; -.
OpenTargets; ENSG00000180228; -.
Orphanet; 210571; Dystonia 16.
PharmGKB; PA33780; -.
eggNOG; KOG3732; Eukaryota.
eggNOG; ENOG410XSCK; LUCA.
GeneTree; ENSGT00900000141030; -.
HOGENOM; HOG000231919; -.
HOVERGEN; HBG001700; -.
InParanoid; O75569; -.
OMA; VTVCHGT; -.
OrthoDB; EOG091G0I2L; -.
PhylomeDB; O75569; -.
TreeFam; TF315953; -.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
EvolutionaryTrace; O75569; -.
GeneWiki; PRKRA; -.
GenomeRNAi; 8575; -.
PRO; PR:O75569; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000180228; -.
CleanEx; HS_PRKRA; -.
CleanEx; HS_RAX; -.
ExpressionAtlas; O75569; baseline and differential.
Genevisible; O75569; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070578; C:RISC-loading complex; IDA:BHF-UCL.
GO; GO:0003725; F:double-stranded RNA binding; IDA:BHF-UCL.
GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
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:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl.
GO; GO:0010586; P:miRNA metabolic process; TAS:Reactome.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:0042473; P:outer ear morphogenesis; IEA:Ensembl.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0031054; P:pre-miRNA processing; IDA:BHF-UCL.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0030422; P:production of siRNA involved in RNA interference; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL.
GO; GO:0009615; P:response to virus; TAS:ProtInc.
GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR033363; PRKRA.
InterPro; IPR032478; Staufen_C.
PANTHER; PTHR10910:SF8; PTHR10910:SF8; 1.
Pfam; PF00035; dsrm; 2.
Pfam; PF16482; Staufen_C; 1.
SMART; SM00358; DSRM; 3.
PROSITE; PS50137; DS_RBD; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Disease mutation; Dystonia; Parkinsonism; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing.
CHAIN 1 313 Interferon-inducible double-stranded RNA-
dependent protein kinase activator A.
/FTId=PRO_0000223609.
DOMAIN 34 101 DRBM 1. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 126 194 DRBM 2. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 240 308 DRBM 3. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
REGION 1 103 Sufficient for self-association and
interaction with TARBP2.
REGION 102 195 Sufficient for self-association and
interaction with TARBP2.
REGION 195 313 Sufficient for self-association and
interaction with TARBP2.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000269|PubMed:16982605}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000269|PubMed:16982605}.
VAR_SEQ 1 25 Missing (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_017282.
VAR_SEQ 1 21 MSQSRHRAEAPPLEREDSGTF -> MQSTPFCGFC (in
isoform 2).
{ECO:0000303|PubMed:11230166}.
/FTId=VSP_017283.
VARIANT 222 222 P -> L (in DYT16; dbSNP:rs121434410).
{ECO:0000269|PubMed:18243799}.
/FTId=VAR_046213.
MUTAGEN 18 18 S->A: No effect on apoptosis induction
under conditions of stress.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 18 18 S->D: Does not induce apoptosis.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 243 243 Q->A: Abrogates apoptosis induction under
conditions of stress.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 246 246 S->A: Abrogates apoptosis induction under
conditions of stress and binding to
EIF2AK2. Prevents activation of EIF2AK2
in stressed cells; when associated with
A-287. {ECO:0000269|PubMed:16982605}.
MUTAGEN 246 246 S->D: Induces activation of EIF2AK2 and
apoptosis in unstressed cells; when
associated with D-287.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 260 260 D->A: Abrogates apoptosis induction under
conditions of stress.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 262 262 D->A: Abrogates apoptosis induction under
conditions of stress.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 265 265 S->A: Abrogates apoptosis induction under
conditions of stress.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 271 271 Q->A: Abrogates apoptosis induction under
conditions of stress.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 279 279 S->A: Abrogates apoptosis induction under
conditions of stress.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 287 287 S->A: Abrogates apoptosis induction under
conditions of stress. Prevents activation
of EIF2AK2 in stressed cells; when
associated with A-246.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 287 287 S->D: Induces activation of EIF2AK2 and
apoptosis in unstressed cells; when
associated with D-246.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 288 288 G->A: Abrogates apoptosis induction under
conditions of stress.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 291 291 C->A: Abrogates apoptosis induction under
conditions of stress.
{ECO:0000269|PubMed:16982605}.
MUTAGEN 298 299 AA->KK: Abrogates interaction with DICER1
but does not affect interaction with
AGO2. {ECO:0000269|PubMed:16424907}.
CONFLICT 282 282 T -> A (in Ref. 8; BAD96827).
{ECO:0000305}.
HELIX 35 45 {ECO:0000244|PDB:2DIX}.
STRAND 51 58 {ECO:0000244|PDB:2DIX}.
STRAND 60 63 {ECO:0000244|PDB:2DIX}.
STRAND 65 72 {ECO:0000244|PDB:2DIX}.
STRAND 75 79 {ECO:0000244|PDB:2DIX}.
HELIX 86 101 {ECO:0000244|PDB:2DIX}.
SEQUENCE 313 AA; 34404 MW; 9B01637E6194827E CRC64;
MSQSRHRAEA PPLEREDSGT FSLGKMITAK PGKTPIQVLH EYGMKTKNIP VYECERSDVQ
IHVPTFTFRV TVGDITCTGE GTSKKLAKHR AAEAAINILK ANASICFAVP DPLMPDPSKQ
PKNQLNPIGS LQELAIHHGW RLPEYTLSQE GGPAHKREYT TICRLESFME TGKGASKKQA
KRNAAEKFLA KFSNISPENH ISLTNVVGHS LGCTWHSLRN SPGEKINLLK RSLLSIPNTD
YIQLLSEIAK EQGFNITYLD IDELSANGQY QCLAELSTSP ITVCHGSGIS CGNAQSDAAH
NALQYLKIIA ERK


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