O75569 (PRKRA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PRKRA
Synonyms:	PACT, RAX
ORF Names:	HSD-14, HSD14

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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, EIF2C2/AGO2 and TARBP2. Also able to interact with dsRNA. Ref.1 Ref.12 Ref.14 Ref.15 Ref.16 Ref.18
Subcellular location	Cytoplasm › perinuclear region Ref.14 Ref.15 Ref.16 Ref.18.
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.23 Ref.24
Sequence similarities	Belongs to the PRKRA family. Contains 3 DRBM (double-stranded RNA-binding) domains.

Ontologies

Keywords
Biological process	RNA-mediated gene silencing
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Dystonia Parkinsonism
Domain	Repeat
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	immune response Traceable author statement Ref.1. Source: ProtInc induction of apoptosis Inferred from electronic annotation. Source: Compara middle ear morphogenesis Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Traceable author statement Ref.1. Source: ProtInc outer ear morphogenesis Inferred from electronic annotation. Source: Compara production of siRNA involved in RNA interference Inferred from direct assay Ref.16. Source: UniProtKB protein phosphorylation Inferred from electronic annotation. Source: Compara response to stress Inferred from electronic annotation. Source: Compara response to virus Traceable author statement Ref.1. Source: ProtInc skeletal system morphogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay Ref.16. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	double-stranded RNA binding Inferred from electronic annotation. Source: InterPro enzyme activator activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IGF2BP1	Q9NZI8	1	EBI-713955,EBI-1053892
PRPSAP1	Q14558	1	EBI-713955,EBI-724449
RPL36	Q9Y3U8	1	EBI-713955,EBI-1057689
SYNCRIP	O60506	1	EBI-713955,EBI-1024357

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 313

313

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

PRO_0000223609

Regions

Domain

34 – 101

68

DRBM 1

Domain

126 – 194

69

DRBM 2

Domain

240 – 308

69

DRBM 3

Region

1 – 103

103

Sufficient for self-association and interaction with TARBP2

Region

102 – 195

94

Sufficient for self-association and interaction with TARBP2

Region

195 – 313

119

Sufficient for self-association and interaction with TARBP2

Amino acid modifications

Modified residue

18

1

Phosphoserine Ref.17 Ref.19 Ref.21

Modified residue

246

1

Phosphoserine Ref.15

Modified residue

287

1

Phosphoserine Ref.15

Natural variations

Alternative sequence

1 – 25

25

Missing in isoform 3.

VSP_017282

Alternative sequence

1 – 21

21

MSQSR…DSGTF → MQSTPFCGFC in isoform 2.

VSP_017283

Natural variant

222

1

P → L in DYT16. Ref.23

VAR_046213

Experimental info

Mutagenesis

18

1

S → A: No effect on apoptosis induction under conditions of stress. Ref.14 Ref.15

Mutagenesis

18

1

S → D: Does not induce apoptosis. Ref.14 Ref.15

Mutagenesis

243

1

Q → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15

Mutagenesis

246

1

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. Ref.14 Ref.15

Mutagenesis

246

1

S → D: Induces activation of EIF2AK2 and apoptosis in unstressed cells; when associated with D-287. Ref.14 Ref.15

Mutagenesis

260

1

D → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15

Mutagenesis

262

1

D → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15

Mutagenesis

265

1

S → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15

Mutagenesis

271

1

Q → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15

Mutagenesis

279

1

S → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15

Mutagenesis

287

1

S → A: Abrogates apoptosis induction under conditions of stress. Prevents activation of EIF2AK2 in stressed cells; when associated with A-246. Ref.14 Ref.15

Mutagenesis

287

1

S → D: Induces activation of EIF2AK2 and apoptosis in unstressed cells; when associated with D-246. Ref.14 Ref.15

Mutagenesis

288

1

G → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15

Mutagenesis

291

1

C → A: Abrogates apoptosis induction under conditions of stress. Ref.14 Ref.15

Mutagenesis

298 – 299

2

AA → KK: Abrogates interaction with DICER1 but does not affect interaction with EIF2C2/AGO2. Ref.14

Sequence conflict

282

1

T → A in BAD96827. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

313

Helix Strand Turn

Details...

Helix

35 – 45

11

Beta strand

51 – 58

8

Beta strand

60 – 63

4

Beta strand

65 – 72

8

Beta strand

75 – 79

5

Helix

86 – 101

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 9B01637E6194827E	FASTA	313	34,404
	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
	Isoform 2 [UniParc]. Checksum: 1A1002362E1095D5	FASTA	302	33,123
	10 20 30 40 50 60 MQSTPFCGFC SLGKMITAKP GKTPIQVLHE YGMKTKNIPV YECERSDVQI HVPTFTFRVT 70 80 90 100 110 120 VGDITCTGEG TSKKLAKHRA AEAAINILKA NASICFAVPD PLMPDPSKQP KNQLNPIGSL 130 140 150 160 170 180 QELAIHHGWR LPEYTLSQEG GPAHKREYTT ICRLESFMET GKGASKKQAK RNAAEKFLAK 190 200 210 220 230 240 FSNISPENHI SLTNVVGHSL GCTWHSLRNS PGEKINLLKR SLLSIPNTDY IQLLSEIAKE 250 260 270 280 290 300 QGFNITYLDI DELSANGQYQ CLAELSTSPI TVCHGSGISC GNAQSDAAHN ALQYLKIIAE RK
	Isoform 3 [UniParc]. Checksum: E663866BAB6DF0BC	FASTA	288	31,635
	10 20 30 40 50 60 MITAKPGKTP IQVLHEYGMK TKNIPVYECE RSDVQIHVPT FTFRVTVGDI TCTGEGTSKK 70 80 90 100 110 120 LAKHRAAEAA INILKANASI CFAVPDPLMP DPSKQPKNQL NPIGSLQELA IHHGWRLPEY 130 140 150 160 170 180 TLSQEGGPAH KREYTTICRL ESFMETGKGA SKKQAKRNAA EKFLAKFSNI SPENHISLTN 190 200 210 220 230 240 VVGHSLGCTW HSLRNSPGEK INLLKRSLLS IPNTDYIQLL SEIAKEQGFN ITYLDIDELS 250 260 270 280 ANGQYQCLAE LSTSPITVCH GSGISCGNAQ SDAAHNALQY LKIIAERK

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	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 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; EIF2C2 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]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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.
[19]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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].
[21]	"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, MASS SPECTROMETRY.
[22]	"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.
[23]	"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.
[24]	"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.

IPI

IPI00021167.
IPI00718940.
IPI00719567.

RefSeq

NP_001132989.1. NM_001139517.1.
NP_001132990.1. NM_001139518.1.
NP_003681.1. NM_003690.4.

UniGene

Hs.570274.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DIX	NMR	-	A	33-103	[»]

ProteinModelPortal

O75569.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75569. 12 interactions.

MINT

MINT-5003897.

STRING

9606.ENSP00000318176.

PTM databases

PhosphoSite

O75569.

Proteomic databases

PaxDb

O75569.

PRIDE

O75569.

Protocols and materials databases

DNASU

8575.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000325748; ENSP00000318176; ENSG00000180228.
ENST00000432031; ENSP00000393883; ENSG00000180228.
ENST00000487082; ENSP00000430604; ENSG00000180228.

GeneID

8575.

KEGG

hsa:8575.

UCSC

uc002umd.3. human.
uc002ume.3. human.

Organism-specific databases

CTD

8575.

GeneCards

GC02M179260.

HGNC

HGNC:9438. PRKRA.

HPA

CAB004648.

MIM

603424. gene.
612067. phenotype.

neXtProt

NX_O75569.

Orphanet

210571. Dystonia 16.

PharmGKB

PA33780.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG245126.

HOGENOM

HOG000231919.

HOVERGEN

HBG001700.

InParanoid

O75569.

OMA

PVTVCHG.

OrthoDB

EOG41RPVB.

PhylomeDB

O75569.

Enzyme and pathway databases

Pathway_Interaction_DB

ceramidepathway. Ceramide signaling pathway.

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O75569.

Bgee

O75569.

CleanEx

HS_PRKRA.
HS_RAX.

Genevestigator

O75569.

GermOnline

ENSG00000180228. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.20. 3 hits.

InterPro

IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like_dom.
[Graphical view]

Pfam

PF00035. dsrm. 2 hits.
[Graphical view]

SMART

SM00358. DSRM. 3 hits.
[Graphical view]

PROSITE

PS50137. DS_RBD. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O75569.

GenomeRNAi

8575.

NextBio

32165.

SOURCE

Search...

Entry information

Entry name

PRKRA_HUMAN

Accession

Primary (citable) accession number: O75569
Secondary accession number(s): A8K3I6 , Q53G24, Q6X7T5, Q8NDK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.