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O75569

- PRKRA_HUMAN

UniProt

O75569 - PRKRA_HUMAN

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Protein

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

Gene
PRKRA, PACT, RAX, HSD-14, HSD14
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.6 Publications

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
Complete GO annotation...

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

Cytoplasmperinuclear region. Cytoplasm 5 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.1 Publication

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).7 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.

Miscellaneous databases

EvolutionaryTraceiO75569.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 10168DRBM 1Add
BLAST
Domaini126 – 19469DRBM 2Add
BLAST
Domaini240 – 30869DRBM 3Add
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.

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

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. VSP_017282Add
BLAST
Alternative sequencei1 – 2121MSQSR…DSGTF → MQSTPFCGFC in isoform 2. VSP_017283Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 129 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

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