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Protein Page:
PACT (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PACT a double strand RNA binding protein (dsRBP). Interacts with TRBP and Dicer to stimulate the cleavage of double-stranded or short hairpin RNA to siRNA. Appears to have a pro-apoptotic function that may be suppressed in the presence of growth factor. Activates the interferon-induced protein kinase PKR. Three alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: RNA processing; Activator protein; RNA binding protein
Chromosomal Location of Human Ortholog: 2q31.2
Cellular Component: nucleoplasm; membrane; perinuclear region of cytoplasm; cytoplasm; cytosol
Molecular Function: protein binding; protein homodimerization activity; enzyme activator activity
Biological Process: positive regulation of catalytic activity; negative regulation of cell proliferation; skeletal morphogenesis; response to virus; outer ear morphogenesis; immune response; gene expression; middle ear morphogenesis; protein amino acid phosphorylation; RNA interference, production of siRNA
Disease: Dystonia 16
Reference #:  O75569 (UniProtKB)
Alt. Names/Synonyms: DYT16; HSD14; Interferon-inducible double stranded RNA-dependent protein kinase activator A; PACT; PKR-associated protein X; PKR-associating protein X; PRKRA; Protein activator of the interferon-induced protein kinase; protein kinase, interferon-inducible double stranded RNA dependent activator; Protein kinase, interferon-inducible double stranded RNA-dependent activator; RAX
Gene Symbols: PRKRA
Molecular weight: 34,404 Da
Basal Isoelectric point: 8.68  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PACT

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: S246‑p, S287‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
3 160 S18-p PPLEREDsGtFsLGK
0 18 T20-p LEREDsGtFsLGKMI
0 5 S22-p REDsGtFsLGKMITA
0 1 K25 sGtFsLGKMITAKPG
0 1 T71-p PTFTFRVtVGDITCT
0 5 S130-p NQLNPIGsLQELAIH
0 1 Y159-p GPAHKREytTICRLE
0 2 T160-p PAHKREytTICRLEs
0 92 S167-p tTICRLEsFMETGKG
0 1 S217-p SLGCTWHsLRNSPGE
0 1 S235-p LLKRSLLsIPNTDYI
3 1 S246-p TDYIQLLsEIAKEQG
0 1 Y270-p ELSANGQyQCLAELS
3 0 S287-p PITVCHGsGISCGNA
  mouse

 
S18-p PPLQREDsGtFsLGK
T20-p LQREDsGtFsLGKMI
S22-p REDsGtFsLGKMITA
K25 sGtFsLGKMITAKPG
T71 PTFTFRVTVGDITCT
S130-p NQLNPIGsLQELAIH
Y159 GPAHKREYTTICRLE
T160 PAHKREYTTICRLEs
S167-p TTICRLEsFMETGKG
S217 SLGCTWHSLRNSPGE
S235 LLKRSLLSLPNTDYI
S246 TDYIQLLSEIASEQG
Y270 ELSANGQYQCLAELS
S287 PITVCHGSGISCGNA
  rat

 
S18-p PPLQREDsGTFSLGk
T20 LQREDsGTFSLGkMI
S22 REDsGTFSLGkMITA
K25-ac sGTFSLGkMITAKPG
T71 PTFTFRVTVGDITCT
S130 NQLNPIGSLQELAIH
Y159 GPAHKREYTTICRLE
T160 PAHKREYTTICRLEs
S167-p TTICRLEsFMETGKG
S217 SLGCTWHSLRNSPGE
S235 LLKRSLLSLPNTDYI
S246 TDYIQLLSEIAKEQG
Y270 ELSANGQYQCLAELS
S287 PITVCHGSGISCGNA
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