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O75569 (PRKRA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PRKRA
Synonyms:PACT, RAX
ORF Names:HSD-14, HSD14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.2 Ref.12 Ref.14 Ref.15 Ref.16

Subunit structure

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). Ref.1 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19

Subcellular location

Cytoplasmperinuclear region. Cytoplasm Ref.14 Ref.15 Ref.16 Ref.19 Ref.23.

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.

Post-translational modification

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. Ref.15

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25 Ref.26

Sequence similarities

Belongs to the PRKRA family.

Contains 3 DRBM (double-stranded RNA-binding) domains.

Ontologies

Keywords
   Biological processRNA-mediated gene silencing
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Dystonia
Parkinsonism
   DomainRepeat
   LigandRNA-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

immune response

Traceable author statement Ref.1. Source: ProtInc

middle ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Traceable author statement Ref.1. Source: ProtInc

outer ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of catalytic activity

Traceable author statement Ref.1. Source: GOC

positive regulation of intrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

production of siRNA involved in RNA interference

Inferred from direct assay Ref.16. Source: UniProtKB

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

response to virus

Traceable author statement Ref.1. Source: ProtInc

skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay Ref.16. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionenzyme activator activity

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16Ref.17. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DICER1Q9UPY32EBI-713955,EBI-395506
TARBP2Q156332EBI-713955,EBI-978581

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75569-1)

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.
Isoform 2 (identifier: O75569-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MSQSRHRAEAPPLEREDSGTF → MQSTPFCGFC
Note: No experimental confirmation available.
Isoform 3 (identifier: O75569-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Interferon-inducible double-stranded RNA-dependent protein kinase activator A
PRO_0000223609

Regions

Domain34 – 10168DRBM 1
Domain126 – 19469DRBM 2
Domain240 – 30869DRBM 3
Region1 – 103103Sufficient for self-association and interaction with TARBP2
Region102 – 19594Sufficient for self-association and interaction with TARBP2
Region195 – 313119Sufficient for self-association and interaction with TARBP2

Amino acid modifications

Modified residue181Phosphoserine Ref.18 Ref.20 Ref.22
Modified residue2461Phosphoserine Ref.15
Modified residue2871Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 2525Missing in isoform 3.
VSP_017282
Alternative sequence1 – 2121MSQSR…DSGTF → MQSTPFCGFC in isoform 2.
VSP_017283
Natural variant2221P → L in DYT16. Ref.25
VAR_046213

Experimental info

Mutagenesis181S → A: No effect on apoptosis induction under conditions of stress. Ref.14 Ref.15
Mutagenesis181S → D: Does not induce apoptosis. Ref.14 Ref.15
Mutagenesis2431Q → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15
Mutagenesis2461S → A: Abrogates apoptosis induction under conditions of stress and binding to EIF2AK2. Prevents activation of EIF2AK2 in stressed cells; when associated with A-287. Ref.14 Ref.15
Mutagenesis2461S → D: Induces activation of EIF2AK2 and apoptosis in unstressed cells; when associated with D-287. Ref.14 Ref.15
Mutagenesis2601D → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15
Mutagenesis2621D → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15
Mutagenesis2651S → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15
Mutagenesis2711Q → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15
Mutagenesis2791S → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15
Mutagenesis2871S → A: Abrogates apoptosis induction under conditions of stress. Prevents activation of EIF2AK2 in stressed cells; when associated with A-246. Ref.14 Ref.15
Mutagenesis2871S → D: Induces activation of EIF2AK2 and apoptosis in unstressed cells; when associated with D-246. Ref.14 Ref.15
Mutagenesis2881G → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15
Mutagenesis2911C → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15
Mutagenesis298 – 2992AA → KK: Abrogates interaction with DICER1 but does not affect interaction with AGO2. Ref.14
Sequence conflict2821T → A in BAD96827. Ref.8

Secondary structure

............. 313
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 9B01637E6194827E

FASTA31334,404
        10         20         30         40         50         60 
MSQSRHRAEA PPLEREDSGT FSLGKMITAK PGKTPIQVLH EYGMKTKNIP VYECERSDVQ 

        70         80         90        100        110        120 
IHVPTFTFRV TVGDITCTGE GTSKKLAKHR AAEAAINILK ANASICFAVP DPLMPDPSKQ 

       130        140        150        160        170        180 
PKNQLNPIGS LQELAIHHGW RLPEYTLSQE GGPAHKREYT TICRLESFME TGKGASKKQA 

       190        200        210        220        230        240 
KRNAAEKFLA KFSNISPENH ISLTNVVGHS LGCTWHSLRN SPGEKINLLK RSLLSIPNTD 

       250        260        270        280        290        300 
YIQLLSEIAK EQGFNITYLD IDELSANGQY QCLAELSTSP ITVCHGSGIS CGNAQSDAAH 

       310 
NALQYLKIIA ERK 

« Hide

Isoform 2 [UniParc].

Checksum: 1A1002362E1095D5
Show »

FASTA30233,123
Isoform 3 [UniParc].

Checksum: E663866BAB6DF0BC
Show »

FASTA28831,635

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2279.1. [O75569-1]
CCDS46460.1. [O75569-2]
CCDS46461.1. [O75569-3]
RefSeqNP_001132989.1. NM_001139517.1. [O75569-2]
NP_001132990.1. NM_001139518.1. [O75569-3]
NP_003681.1. NM_003690.4. [O75569-1]
UniGeneHs.570274.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIXNMR-A33-103[»]
ProteinModelPortalO75569.
SMRO75569. Positions 28-104, 127-192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114143. 28 interactions.
IntActO75569. 25 interactions.
MINTMINT-5003897.
STRING9606.ENSP00000318176.

PTM databases

PhosphoSiteO75569.

Proteomic databases

MaxQBO75569.
PaxDbO75569.
PRIDEO75569.

Protocols and materials databases

DNASU8575.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325748; ENSP00000318176; ENSG00000180228. [O75569-1]
ENST00000432031; ENSP00000393883; ENSG00000180228. [O75569-2]
ENST00000487082; ENSP00000430604; ENSG00000180228. [O75569-3]
GeneID8575.
KEGGhsa:8575.
UCSCuc002umd.3. human. [O75569-1]
uc002ume.3. human. [O75569-2]

Organism-specific databases

CTD8575.
GeneCardsGC02M179260.
HGNCHGNC:9438. PRKRA.
HPACAB004648.
MIM603424. gene.
612067. phenotype.
neXtProtNX_O75569.
Orphanet210571. Dystonia 16.
PharmGKBPA33780.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245126.
HOGENOMHOG000231919.
HOVERGENHBG001700.
InParanoidO75569.
OMAPVTVCHG.
OrthoDBEOG741Z2Q.
PhylomeDBO75569.
TreeFamTF315953.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressO75569.
BgeeO75569.
CleanExHS_PRKRA.
HS_RAX.
GenevestigatorO75569.

Family and domain databases

Gene3D3.30.160.20. 3 hits.
InterProIPR014720. dsRNA-bd_dom.
[Graphical view]
PfamPF00035. dsrm. 2 hits.
[Graphical view]
SMARTSM00358. DSRM. 3 hits.
[Graphical view]
PROSITEPS50137. DS_RBD. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75569.
GeneWikiPRKRA.
GenomeRNAi8575.
NextBio32165.
PROO75569.
SOURCESearch...

Entry information

Entry namePRKRA_HUMAN
AccessionPrimary (citable) accession number: O75569
Secondary accession number(s): A8K3I6 expand/collapse secondary AC list , Q53G24, Q6X7T5, Q8NDK4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM