PRKRA_HUMAN - dbPTM
PRKRA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRKRA_HUMAN
UniProt AC O75569
Protein Name Interferon-inducible double-stranded RNA-dependent protein kinase activator A
Gene Name PRKRA
Organism Homo sapiens (Human).
Sequence Length 313
Subcellular Localization Cytoplasm, perinuclear region. Cytoplasm.
Protein Description 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)..
Protein Sequence MSQSRHRAEAPPLEREDSGTFSLGKMITAKPGKTPIQVLHEYGMKTKNIPVYECERSDVQIHVPTFTFRVTVGDITCTGEGTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYTTICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNVVGHSLGCTWHSLRNSPGEKINLLKRSLLSIPNTDYIQLLSEIAKEQGFNITYLDIDELSANGQYQCLAELSTSPITVCHGSGISCGNAQSDAAHNALQYLKIIAERK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSQSRHRAE
------CCCCCCCCC		36.5419413330
2Phosphorylation------MSQSRHRAE
------CCCCCCCCC		36.5426074081
4Phosphorylation----MSQSRHRAEAP
----CCCCCCCCCCC		23.8125159151
11 (in isoform 2)Phosphorylation-26.0525693802
18PhosphorylationPPLEREDSGTFSLGK
CCCCCCCCCCEEECC		34.6729255136
20PhosphorylationLEREDSGTFSLGKMI
CCCCCCCCEEECCEE		17.6329255136
22PhosphorylationREDSGTFSLGKMITA
CCCCCCEEECCEEEC		35.7329255136
25AcetylationSGTFSLGKMITAKPG
CCCEEECCEEECCCC		32.2125953088
28PhosphorylationFSLGKMITAKPGKTP
EEECCEEECCCCCCC		25.7326074081
30UbiquitinationLGKMITAKPGKTPIQ
ECCEEECCCCCCCHH		45.73-
34PhosphorylationITAKPGKTPIQVLHE
EECCCCCCCHHHHHH		31.3820068231
42PhosphorylationPIQVLHEYGMKTKNI
CHHHHHHCCCCCCCC		16.2727642862
45AcetylationVLHEYGMKTKNIPVY
HHHHCCCCCCCCCEE		52.5725953088
45UbiquitinationVLHEYGMKTKNIPVY
HHHHCCCCCCCCCEE		52.57-
47UbiquitinationHEYGMKTKNIPVYEC
HHCCCCCCCCCEEEE		47.57-
52PhosphorylationKTKNIPVYECERSDV
CCCCCCEEEEECCCC		14.9828796482
67PhosphorylationQIHVPTFTFRVTVGD
EEECCEEEEEEEECC		17.01-
71PhosphorylationPTFTFRVTVGDITCT
CEEEEEEEECCEEEE		17.9520068231
76PhosphorylationRVTVGDITCTGEGTS
EEEECCEEEECCCCC		14.5721406692
78PhosphorylationTVGDITCTGEGTSKK
EECCEEEECCCCCHH		29.6220068231
82PhosphorylationITCTGEGTSKKLAKH
EEEECCCCCHHHHHH		32.8220068231
83PhosphorylationTCTGEGTSKKLAKHR
EEECCCCCHHHHHHH		38.3521406692
84AcetylationCTGEGTSKKLAKHRA
EECCCCCHHHHHHHH		52.2025953088
84UbiquitinationCTGEGTSKKLAKHRA
EECCCCCHHHHHHHH		52.20-
85UbiquitinationTGEGTSKKLAKHRAA
ECCCCCHHHHHHHHH		54.14-
104PhosphorylationNILKANASICFAVPD
HHHHHCCEEEEEECC		21.5030622161
130PhosphorylationNQLNPIGSLQELAIH
CCCCCCCCHHHHHHH		27.8328464451
145PhosphorylationHGWRLPEYTLSQEGG
CCCCCCCCCCCCCCC		15.8428796482
146PhosphorylationGWRLPEYTLSQEGGP
CCCCCCCCCCCCCCC		20.4728796482
148PhosphorylationRLPEYTLSQEGGPAH
CCCCCCCCCCCCCCC		20.5628857561
156UbiquitinationQEGGPAHKREYTTIC
CCCCCCCCCEEEEEE		49.37-
159PhosphorylationGPAHKREYTTICRLE
CCCCCCEEEEEEEHH		17.1428796482
160PhosphorylationPAHKREYTTICRLES
CCCCCEEEEEEEHHH		12.6326552605
161PhosphorylationAHKREYTTICRLESF
CCCCEEEEEEEHHHH		19.7121130716
167PhosphorylationTTICRLESFMETGKG
EEEEEHHHHHHHCCC		34.1930266825
171PhosphorylationRLESFMETGKGASKK
EHHHHHHHCCCCCHH		32.1923312004
173UbiquitinationESFMETGKGASKKQA
HHHHHHCCCCCHHHH		59.74-
176PhosphorylationMETGKGASKKQAKRN
HHHCCCCCHHHHHHH		49.4021130716
177UbiquitinationETGKGASKKQAKRNA
HHCCCCCHHHHHHHH		48.66-
187AcetylationAKRNAAEKFLAKFSN
HHHHHHHHHHHHHCC		40.7425953088
187UbiquitinationAKRNAAEKFLAKFSN
HHHHHHHHHHHHHCC		40.74-
196PhosphorylationLAKFSNISPENHISL
HHHHCCCCCCCCEEH		30.3427251275
202PhosphorylationISPENHISLTNVVGH
CCCCCCEEHHHHHHH		22.9127251275
210PhosphorylationLTNVVGHSLGCTWHS
HHHHHHHHCCCCHHH		22.1127251275
214PhosphorylationVGHSLGCTWHSLRNS
HHHHCCCCHHHHCCC		25.1427251275
217PhosphorylationSLGCTWHSLRNSPGE
HCCCCHHHHCCCCHH		22.1528857561
221PhosphorylationTWHSLRNSPGEKINL
CHHHHCCCCHHHHHH		28.0429214152
225UbiquitinationLRNSPGEKINLLKRS
HCCCCHHHHHHHHHH		42.69-
232PhosphorylationKINLLKRSLLSIPNT
HHHHHHHHHHCCCCC		31.8828857561
235PhosphorylationLLKRSLLSIPNTDYI
HHHHHHHCCCCCHHH		41.0925693802
241PhosphorylationLSIPNTDYIQLLSEI
HCCCCCHHHHHHHHH		6.63-
246PhosphorylationTDYIQLLSEIAKEQG
CHHHHHHHHHHHHCC		35.2321526770
270PhosphorylationELSANGQYQCLAELS
HHCCCCCEEEEEECC		11.5522817900
287PhosphorylationPITVCHGSGISCGNA
CEEEEECCCCCCCCC		14.8621526770
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PRKRA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
246SPhosphorylation

16982605
246SPhosphorylation

16982605
246SPhosphorylation

16982605
287SPhosphorylation

16982605
287SPhosphorylation

16982605
287SPhosphorylation

16982605
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PRKRA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HNRPQ_HUMANSYNCRIPphysical
17353931
IF2B1_HUMANIGF2BP1physical
17353931
KPRA_HUMANPRPSAP1physical
17353931
RL36_HUMANRPL36physical
17353931
CSN6_HUMANCOPS6physical
16169070
GDF9_HUMANGDF9physical
16169070
PRKRA_HUMANPRKRAphysical
16169070
SETB1_HUMANSETDB1physical
16169070
E2AK2_HUMANEIF2AK2physical
9687506
E2AK2_HUMANEIF2AK2genetic
9687506
ZFP28_HUMANZFP28physical
21900206
SHC1_HUMANSHC1physical
21900206
ZN746_HUMANZNF746physical
21900206
CEBPZ_HUMANCEBPZphysical
21900206
TRBP2_HUMANTARBP2physical
21900206
NKRF_HUMANNKRFphysical
21900206
CE126_HUMANKIAA1377physical
21900206
PRKRA_HUMANPRKRAphysical
21900206
SNX5_HUMANSNX5physical
21900206
PRKRA_HUMANPRKRAphysical
22214662
UBC9_HUMANUBE2Iphysical
22214662
STAU2_HUMANSTAU2physical
24778252
CC124_HUMANCCDC124physical
24778252
DDX50_HUMANDDX50physical
24778252
DICER_HUMANDICER1physical
24778252
H10_HUMANH1F0physical
24778252
MMTA2_HUMANC1orf35physical
24778252
NOC3L_HUMANNOC3Lphysical
24778252
NOP16_HUMANNOP16physical
24778252
TCOF_HUMANTCOF1physical
24778252
NOG1_HUMANGTPBP4physical
24778252
EBP2_HUMANEBNA1BP2physical
24778252
E2AK2_HUMANEIF2AK2physical
24778252
IFRD2_HUMANIFRD2physical
24778252
RBM34_HUMANRBM34physical
24778252
TRBP2_HUMANTARBP2physical
24778252
ZN346_HUMANZNF346physical
24778252
PRKRA_HUMANPRKRAphysical
25416956
LYAR_HUMANLYARphysical
25416956
ZMAT3_HUMANZMAT3physical
25416956
FBW1A_HUMANBTRCphysical
28049764
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612067Dystonia 16 (DYT16)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRKRA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.
"Phosphorylation of specific serine residues in the PKR activationdomain 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).
Cited for: FUNCTION, INTERACTION WITH EIF2AK2, SUBCELLULAR LOCATION,PHOSPHORYLATION AT SER-246 AND SER-287, AND 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.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.

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