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O75569

- PRKRA_HUMAN

UniProt

O75569 - PRKRA_HUMAN

Protein

Interferon-inducible double-stranded RNA-dependent protein kinase activator A

Gene

PRKRA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Molecular functioni

    1. enzyme activator activity Source: ProtInc
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to oxidative stress Source: Ensembl
    2. gene expression Source: Reactome
    3. immune response Source: ProtInc
    4. middle ear morphogenesis Source: Ensembl
    5. negative regulation of cell proliferation Source: ProtInc
    6. outer ear morphogenesis Source: Ensembl
    7. positive regulation of catalytic activity Source: GOC
    8. positive regulation of intrinsic apoptotic signaling pathway Source: Ensembl
    9. production of siRNA involved in RNA interference Source: UniProtKB
    10. protein phosphorylation Source: Ensembl
    11. response to virus Source: ProtInc
    12. skeletal system morphogenesis Source: Ensembl

    Keywords - Biological processi

    RNA-mediated gene silencing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118560. Small interfering RNA (siRNA) biogenesis.
    REACT_12417. MicroRNA (miRNA) biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon-inducible double-stranded RNA-dependent protein kinase activator A
    Alternative name(s):
    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
    Gene namesi
    Name:PRKRA
    Synonyms:PACT, RAX
    ORF Names:HSD-14, HSD14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9438. PRKRA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB
    4. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti222 – 2221P → L in DYT16. 1 Publication
    VAR_046213

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi18 – 181S → A: No effect on apoptosis induction under conditions of stress. 2 Publications
    Mutagenesisi18 – 181S → D: Does not induce apoptosis. 2 Publications
    Mutagenesisi243 – 2431Q → A: Abrogates apoptosis induction under conditions of stress. 2 Publications
    Mutagenesisi246 – 2461S → A: Abrogates apoptosis induction under conditions of stress and binding to EIF2AK2. Prevents activation of EIF2AK2 in stressed cells; when associated with A-287. 2 Publications
    Mutagenesisi246 – 2461S → D: Induces activation of EIF2AK2 and apoptosis in unstressed cells; when associated with D-287. 2 Publications
    Mutagenesisi260 – 2601D → A: Abrogates apoptosis induction under conditions of stress. 2 Publications
    Mutagenesisi262 – 2621D → A: Abrogates apoptosis induction under conditions of stress. 2 Publications
    Mutagenesisi265 – 2651S → A: Abrogates apoptosis induction under conditions of stress. 2 Publications
    Mutagenesisi271 – 2711Q → A: Abrogates apoptosis induction under conditions of stress. 2 Publications
    Mutagenesisi279 – 2791S → A: Abrogates apoptosis induction under conditions of stress. 2 Publications
    Mutagenesisi287 – 2871S → A: Abrogates apoptosis induction under conditions of stress. Prevents activation of EIF2AK2 in stressed cells; when associated with A-246. 2 Publications
    Mutagenesisi287 – 2871S → D: Induces activation of EIF2AK2 and apoptosis in unstressed cells; when associated with D-246. 2 Publications
    Mutagenesisi288 – 2881G → A: Abrogates apoptosis induction under conditions of stress. 2 Publications
    Mutagenesisi291 – 2911C → A: Abrogates apoptosis induction under conditions of stress. 2 Publications
    Mutagenesisi298 – 2992AA → KK: Abrogates interaction with DICER1 but does not affect interaction with AGO2. 1 Publication

    Keywords - Diseasei

    Disease mutation, Dystonia, Parkinsonism

    Organism-specific databases

    MIMi612067. phenotype.
    Orphaneti210571. Dystonia 16.
    PharmGKBiPA33780.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313Interferon-inducible double-stranded RNA-dependent protein kinase activator APRO_0000223609Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181Phosphoserine3 Publications
    Modified residuei246 – 2461Phosphoserine1 Publication
    Modified residuei287 – 2871Phosphoserine1 Publication

    Post-translational modificationi

    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.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75569.
    PaxDbiO75569.
    PRIDEiO75569.

    PTM databases

    PhosphoSiteiO75569.

    Expressioni

    Gene expression databases

    ArrayExpressiO75569.
    BgeeiO75569.
    CleanExiHS_PRKRA.
    HS_RAX.
    GenevestigatoriO75569.

    Organism-specific databases

    HPAiCAB004648.

    Interactioni

    Subunit structurei

    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).By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DICER1Q9UPY32EBI-713955,EBI-395506
    TARBP2Q156332EBI-713955,EBI-978581

    Protein-protein interaction databases

    BioGridi114143. 42 interactions.
    IntActiO75569. 25 interactions.
    MINTiMINT-5003897.
    STRINGi9606.ENSP00000318176.

    Structurei

    Secondary structure

    1
    313
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi35 – 4511
    Beta strandi51 – 588
    Beta strandi60 – 634
    Beta strandi65 – 728
    Beta strandi75 – 795
    Helixi86 – 10116

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DIXNMR-A33-103[»]
    ProteinModelPortaliO75569.
    SMRiO75569. Positions 28-104, 127-192.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75569.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 10168DRBM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini126 – 19469DRBM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini240 – 30869DRBM 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 103103Sufficient for self-association and interaction with TARBP2Add
    BLAST
    Regioni102 – 19594Sufficient for self-association and interaction with TARBP2Add
    BLAST
    Regioni195 – 313119Sufficient for self-association and interaction with TARBP2Add
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Belongs to the PRKRA family.Curated
    Contains 3 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG245126.
    HOGENOMiHOG000231919.
    HOVERGENiHBG001700.
    InParanoidiO75569.
    OMAiPVTVCHG.
    OrthoDBiEOG741Z2Q.
    PhylomeDBiO75569.
    TreeFamiTF315953.

    Family and domain databases

    Gene3Di3.30.160.20. 3 hits.
    InterProiIPR014720. dsRNA-bd_dom.
    [Graphical view]
    PfamiPF00035. dsrm. 2 hits.
    [Graphical view]
    SMARTiSM00358. DSRM. 3 hits.
    [Graphical view]
    PROSITEiPS50137. DS_RBD. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75569-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSQSRHRAEA PPLEREDSGT FSLGKMITAK PGKTPIQVLH EYGMKTKNIP    50
    VYECERSDVQ IHVPTFTFRV TVGDITCTGE GTSKKLAKHR AAEAAINILK 100
    ANASICFAVP DPLMPDPSKQ PKNQLNPIGS LQELAIHHGW RLPEYTLSQE 150
    GGPAHKREYT TICRLESFME TGKGASKKQA KRNAAEKFLA KFSNISPENH 200
    ISLTNVVGHS LGCTWHSLRN SPGEKINLLK RSLLSIPNTD YIQLLSEIAK 250
    EQGFNITYLD IDELSANGQY QCLAELSTSP ITVCHGSGIS CGNAQSDAAH 300
    NALQYLKIIA ERK 313
    Length:313
    Mass (Da):34,404
    Last modified:November 1, 1998 - v1
    Checksum:i9B01637E6194827E
    GO
    Isoform 2 (identifier: O75569-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MSQSRHRAEAPPLEREDSGTF → MQSTPFCGFC

    Note: No experimental confirmation available.

    Show »
    Length:302
    Mass (Da):33,123
    Checksum:i1A1002362E1095D5
    GO
    Isoform 3 (identifier: O75569-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:288
    Mass (Da):31,635
    Checksum:iE663866BAB6DF0BC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti282 – 2821T → A in BAD96827. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti222 – 2221P → L in DYT16. 1 Publication
    VAR_046213

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2525Missing in isoform 3. 1 PublicationVSP_017282Add
    BLAST
    Alternative sequencei1 – 2121MSQSR…DSGTF → MQSTPFCGFC in isoform 2. 1 PublicationVSP_017283Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072860 mRNA. Translation: AAC25672.1.
    AF083033 mRNA. Translation: AAD33099.1.
    AY251164 mRNA. Translation: AAP20061.1.
    AL136615 mRNA. Translation: CAB66550.1.
    AL833867 Transcribed RNA. Translation: CAD38725.1.
    BT007243 mRNA. Translation: AAP35907.1.
    AK290601 mRNA. Translation: BAF83290.1.
    CR533525 mRNA. Translation: CAG38556.1.
    AK223107 mRNA. Translation: BAD96827.1.
    AC009948 Genomic DNA. Translation: AAX88882.1.
    CH471058 Genomic DNA. Translation: EAX11036.1.
    BC009470 mRNA. Translation: AAH09470.1.
    CCDSiCCDS2279.1. [O75569-1]
    CCDS46460.1. [O75569-2]
    CCDS46461.1. [O75569-3]
    RefSeqiNP_001132989.1. NM_001139517.1. [O75569-2]
    NP_001132990.1. NM_001139518.1. [O75569-3]
    NP_003681.1. NM_003690.4. [O75569-1]
    UniGeneiHs.570274.

    Genome annotation databases

    EnsembliENST00000325748; ENSP00000318176; ENSG00000180228. [O75569-1]
    ENST00000432031; ENSP00000393883; ENSG00000180228. [O75569-2]
    ENST00000487082; ENSP00000430604; ENSG00000180228. [O75569-3]
    GeneIDi8575.
    KEGGihsa:8575.
    UCSCiuc002umd.3. human. [O75569-1]
    uc002ume.3. human. [O75569-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072860 mRNA. Translation: AAC25672.1 .
    AF083033 mRNA. Translation: AAD33099.1 .
    AY251164 mRNA. Translation: AAP20061.1 .
    AL136615 mRNA. Translation: CAB66550.1 .
    AL833867 Transcribed RNA. Translation: CAD38725.1 .
    BT007243 mRNA. Translation: AAP35907.1 .
    AK290601 mRNA. Translation: BAF83290.1 .
    CR533525 mRNA. Translation: CAG38556.1 .
    AK223107 mRNA. Translation: BAD96827.1 .
    AC009948 Genomic DNA. Translation: AAX88882.1 .
    CH471058 Genomic DNA. Translation: EAX11036.1 .
    BC009470 mRNA. Translation: AAH09470.1 .
    CCDSi CCDS2279.1. [O75569-1 ]
    CCDS46460.1. [O75569-2 ]
    CCDS46461.1. [O75569-3 ]
    RefSeqi NP_001132989.1. NM_001139517.1. [O75569-2 ]
    NP_001132990.1. NM_001139518.1. [O75569-3 ]
    NP_003681.1. NM_003690.4. [O75569-1 ]
    UniGenei Hs.570274.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DIX NMR - A 33-103 [» ]
    ProteinModelPortali O75569.
    SMRi O75569. Positions 28-104, 127-192.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114143. 42 interactions.
    IntActi O75569. 25 interactions.
    MINTi MINT-5003897.
    STRINGi 9606.ENSP00000318176.

    PTM databases

    PhosphoSitei O75569.

    Proteomic databases

    MaxQBi O75569.
    PaxDbi O75569.
    PRIDEi O75569.

    Protocols and materials databases

    DNASUi 8575.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325748 ; ENSP00000318176 ; ENSG00000180228 . [O75569-1 ]
    ENST00000432031 ; ENSP00000393883 ; ENSG00000180228 . [O75569-2 ]
    ENST00000487082 ; ENSP00000430604 ; ENSG00000180228 . [O75569-3 ]
    GeneIDi 8575.
    KEGGi hsa:8575.
    UCSCi uc002umd.3. human. [O75569-1 ]
    uc002ume.3. human. [O75569-2 ]

    Organism-specific databases

    CTDi 8575.
    GeneCardsi GC02M179260.
    HGNCi HGNC:9438. PRKRA.
    HPAi CAB004648.
    MIMi 603424. gene.
    612067. phenotype.
    neXtProti NX_O75569.
    Orphaneti 210571. Dystonia 16.
    PharmGKBi PA33780.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG245126.
    HOGENOMi HOG000231919.
    HOVERGENi HBG001700.
    InParanoidi O75569.
    OMAi PVTVCHG.
    OrthoDBi EOG741Z2Q.
    PhylomeDBi O75569.
    TreeFami TF315953.

    Enzyme and pathway databases

    Reactomei REACT_118560. Small interfering RNA (siRNA) biogenesis.
    REACT_12417. MicroRNA (miRNA) biogenesis.

    Miscellaneous databases

    EvolutionaryTracei O75569.
    GeneWikii PRKRA.
    GenomeRNAii 8575.
    NextBioi 32165.
    PROi O75569.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75569.
    Bgeei O75569.
    CleanExi HS_PRKRA.
    HS_RAX.
    Genevestigatori O75569.

    Family and domain databases

    Gene3Di 3.30.160.20. 3 hits.
    InterProi IPR014720. dsRNA-bd_dom.
    [Graphical view ]
    Pfami PF00035. dsrm. 2 hits.
    [Graphical view ]
    SMARTi SM00358. DSRM. 3 hits.
    [Graphical view ]
    PROSITEi PS50137. DS_RBD. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PACT, a protein activator of the interferon-induced protein kinase, PKR."
      Patel R.C., Sen G.C.
      EMBO J. 17:4379-4390(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EIF2AK2.
      Tissue: Placenta.
    2. "RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling."
      Ito T., Yang M., May W.S.
      J. Biol. Chem. 274:15427-15432(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    3. "A new spermatogenesis-related gene."
      Hu T.H., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      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.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Heart.
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. 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
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      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.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    12. "Modular structure of PACT: distinct domains for binding and activating PKR."
      Peters G.A., Hartmann R., Qin J., Sen G.C.
      Mol. Cell. Biol. 21:1908-1920(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "The role of PACT in the RNA silencing pathway."
      Lee Y., Hur I., Park S.-Y., Kim Y.-K., Suh M.R., Kim V.N.
      EMBO J. 25:522-532(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DICER1; AGO2 AND TARBP2, SUBCELLULAR LOCATION, MUTAGENESIS OF 298-ALA-ALA-299.
    15. "Phosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosis."
      Peters G.A., Li S., Sen G.C.
      J. Biol. Chem. 281:35129-35136(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EIF2AK2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-246 AND SER-287, 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.
    16. "Human TRBP and PACT directly interact with each other and associate with dicer to facilitate the production of small interfering RNA."
      Kok K.H., Ng M.-H., Ching Y.-P., Jin D.-Y.
      J. Biol. Chem. 282:17649-17657(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DICER1 AND TARBP2, SUBCELLULAR LOCATION.
    17. "Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKR."
      Mittelstadt M., Frump A., Khuu T., Fowlkes V., Handy I., Patel C.V., Patel R.C.
      Nucleic Acids Res. 36:998-1008(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DUS2L.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Interactions between the double-stranded RNA-binding proteins TRBP and PACT define the Medipal domain that mediates protein-protein interactions."
      Laraki G., Clerzius G., Daher A., Melendez-Pena C., Daniels S., Gatignol A.
      RNA Biol. 5:92-103(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION, INTERACTION WITH EIF2AK2 AND TARBP2, SUBCELLULAR LOCATION.
    20. "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-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G(1) arrest."
      Bennett R.L., Pan Y., Christian J., Hui T., May W.S. Jr.
      Cell Cycle 11:407-417(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    24. "Solution structure of the DSRM domain of protein activator of the interferon-induced protein kinase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (SEP-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 32-104.
    25. "DYT16, a novel young-onset dystonia-parkinsonism disorder: identification of a segregating mutation in the stress-response protein PRKRA."
      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.
      Lancet Neurol. 7:207-215(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DYT16 LEU-222.
    26. "A heterozygous frameshift mutation in PRKRA (DYT16) associated with generalised dystonia in a German patient."
      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.
      Lancet Neurol. 7:380-381(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN DYT16.

    Entry informationi

    Entry nameiPRKRA_HUMAN
    AccessioniPrimary (citable) accession number: O75569
    Secondary accession number(s): A8K3I6
    , Q53G24, Q6X7T5, Q8NDK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2006
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3