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UniProtKB/Swiss-Prot entry P19525


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name E2AK2_HUMAN
Primary accession number P19525
Secondary accession numbers Q52M43 Q9UIR4
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on May 1, 1991 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 118)
Name and origin of the protein
Protein name Interferon-induced, double-stranded RNA-activated protein kinase
Synonyms EC 2.7.11.1
Interferon-inducible RNA-dependent protein kinase
Eukaryotic translation initiation factor 2-alpha kinase 2
eIF-2A protein kinase 2
Protein kinase RNA-activated
PKR
p68 kinase
P1/eIF-2A protein kinase
Gene name
Name: EIF2AK2
Synonyms: PKR, PRKR
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 101-118 AND 309-325.
DOI=10.1016/0092-8674(90)90374-N; PubMed=1695551 [NCBI, ExPASy, EBI, Israel, Japan]
Meurs E., Chong K., Galabru J., Thomas N.S.B., Kerr I.M., Williams B.R.G., Hovanessian A.G.;
"Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon.";
Cell 62:379-390(1990).
[2]
SEQUENCE REVISION.
Meurs E.;
Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0042-6822(92)90732-5; PubMed=1373553 [NCBI, ExPASy, EBI, Israel, Japan]
Thomis D.C., Doohan J.P., Samuel C.E.;
"Mechanism of interferon action: cDNA structure, expression, and regulation of the interferon-induced, RNA-dependent P1/eIF-2 alpha protein kinase from human cells.";
Virology 188:33-46(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1016/0378-1119(96)00314-9; PubMed=8921913 [NCBI, ExPASy, EBI, Israel, Japan]
Kuhen K.L., Shen X., Samuel C.E.;
"Mechanism of interferon action sequence of the human interferon-inducible RNA-dependent protein kinase (PKR) deduced from genomic clones.";
Gene 178:191-193(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
DOI=10.1006/geno.1996.0446; PubMed=8812437 [NCBI, ExPASy, EBI, Israel, Japan]
Kuhen K.L., Shen X., Carlisle E.R., Richardson A.L., Weier H.-U.G., Tanaka H., Samuel C.E.;
"Structural organization of the human gene (PKR) encoding an interferon-inducible RNA-dependent protein kinase (PKR) and differences from its mouse homolog.";
Genomics 36:197-201(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1089/jir.1998.18.609; PubMed=9726442 [NCBI, ExPASy, EBI, Israel, Japan]
Xu Z., Williams B.R.;
"Genomic features of human PKR: alternative splicing and a polymorphic CGG repeat in the 5'-untranslated region.";
J. Interferon Cytokine Res. 18:609-616(1998).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
INTERACTION WITH DNAJC3.
DOI=10.1074/jbc.271.3.1702; PubMed=8576172 [NCBI, ExPASy, EBI, Israel, Japan]
Polyak S.J., Tang N., Wambach M., Barber G.N., Katze M.G.;
"The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity.";
J. Biol. Chem. 271:1702-1707(1996).
[11]
INTERACTION WITH HIV-1 TAT.
DOI=10.1074/jbc.272.13.8388; PubMed=9079663 [NCBI, ExPASy, EBI, Israel, Japan]
Brand S.R., Kobayashi R., Mathews M.B.;
"The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR.";
J. Biol. Chem. 272:8388-8395(1997).
[12]
INTERACTION WITH HCV NS5A.
DOI=10.1006/viro.1997.8493; PubMed=9143277 [NCBI, ExPASy, EBI, Israel, Japan]
Gale M.J. Jr., Korth M.J., Tang N.M., Tan S.-L., Hopkins D.A., Dever T.E., Polyak S.J., Gretch D.R., Katze M.G.;
"Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein.";
Virology 230:217-227(1997).
[13]
INTERACTION WITH INFLUENZA A NS1 PROTEIN.
DOI=10.1089/jir.1998.18.757; PubMed=9781815 [NCBI, ExPASy, EBI, Israel, Japan]
Tan S.L., Katze M.G.;
"Biochemical and genetic evidence for complex formation between the influenza A virus NS1 protein and the interferon-induced PKR protein kinase.";
J. Interferon Cytokine Res. 18:757-766(1998).
[14]
INTERACTION WITH HCV E2 ENVELOPE PROTEIN.
DOI=10.1126/science.285.5424.107; PubMed=10390359 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor D.R., Shi S.T., Romano P.R., Barber G.N., Lai M.M.C.;
"Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein.";
Science 285:107-110(1999).
[15]
PHOSPHORYLATION AT SER-83; THR-88; THR-89; THR-90; SER-242; THR-255 AND THR-258, MUTAGENESIS OF SER-83; THR-88; THR-89; THR-90; SER-242; THR-255; THR-258 AND LYS-296, AND INHIBITION BY HCV E2 ENVELOPE PROTEIN.
DOI=10.1128/JVI.75.3.1265-1273.2001; PubMed=11152499 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor D.R., Tian B., Romano P.R., Hinnebusch A.G., Lai M.M.C., Mathews M.B.;
"Hepatitis C virus envelope protein E2 does not inhibit PKR by simple competition with autophosphorylation sites in the RNA-binding domain.";
J. Virol. 75:1265-1273(2001).
[16]
MUTAGENESIS, AND PHOSPHORYLATION AT THR-446 AND THR-451.
DOI=10.1074/jbc.M102108200; PubMed=11337501 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang F., Romano P.R., Nagamura-Inoue T., Tian B., Dever T.E., Mathews M.B., Ozato K., Hinnebusch A.G.;
"Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop.";
J. Biol. Chem. 276:24946-24958(2001).
[17]
INHIBITION BY VACCINIA VIRUS PROTEIN E3.
DOI=10.1016/j.virol.2004.03.012; PubMed=15207627 [NCBI, ExPASy, EBI, Israel, Japan]
Langland J.O., Jacobs B.L.;
"Inhibition of PKR by vaccinia virus: role of the N- and C-terminal domains of E3L.";
Virology 324:419-429(2004).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-456, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[20]
STRUCTURE BY NMR OF 1-175.
DOI=10.1093/emboj/17.18.5458; PubMed=9736623 [NCBI, ExPASy, EBI, Israel, Japan]
Nanduri S., Carpick B.W., Yang Y., Williams B.R.G., Qin J.;
"Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation.";
EMBO J. 17:5458-5465(1998).
[21]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 258-550 IN COMPLEX WITH EIF2ALPHA, AND PHOSPHORYLATION AT THR-446.
DOI=10.1016/j.cell.2005.06.044; PubMed=16179258 [NCBI, ExPASy, EBI, Israel, Japan]
Dar A.C., Dever T.E., Sicheri F.;
"Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR.";
Cell 122:887-900(2005).
[22]
VARIANTS [LARGE SCALE ANALYSIS] GLU-428; VAL-439 AND VAL-506.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M35663; AAA36409.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M85294; AAA18253.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50648; AAC50768.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50634; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50635; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50636; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50637; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50638; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50639; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50640; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50641; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50642; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50643; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50644; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50645; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50646; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50647; AAC50768.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167472; AAF13156.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167460; AAF13156.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167462; AAF13156.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167463; AAF13156.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167464; AAF13156.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167465; AAF13156.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167466; AAF13156.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167468; AAF13156.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167470; AAF13156.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY228338; AAO38055.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007899; AAY24317.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093676; AAH93676.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101475; AAI01476.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00019463; -.
PIR JC5225; JC5225.
RefSeq NP_001129123.1; -.
NP_002750.1; -.
UniGene Hs.131431
3D structure databases
PDB
1QU6; NMR; -; A=1-170.[ExPASy / RCSB / EBI]
2A19; X-ray; 2.50 A; B/C=258-550.[ExPASy / RCSB / EBI]
2A1A; X-ray; 2.80 A; B=258-550.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1QU6; -.
2A19; -.
2A1A; -.
SMR P19525; 257-541.
ModBase P19525.
Protein-protein interaction databases
DIP DIP:2657N; -.
IntAct P19525; 3.
PTM databases
PhosphoSite P19525; -.
Enzyme and pathway databases
BRENDA 2.7.11.1; 247.
Reactome REACT_6167; Influenza Infection.
Organism-specific databases
GeneCards GC02M037246; -.
H-InvDB HIX0029806; -.
HGNC HGNC:9437; EIF2AK2.
GenAtlas EIF2AK2.
HPA CAB003845; -.
MIM 176871; gene. [NCBI / EBI]
PharmGKB PA33779; -.
Gene expression databases
ArrayExpress P19525; -.
Bgee P19525; -.
CleanEx HS_EIF2AK2; -.
GermOnline ENSG00000055332; Homo sapiens.
Ontologies
GO
GO:0005622; Cellular component: intracellular (inferred from electronic annotation from InterPro).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003725; Molecular function: double-stranded RNA binding (traceable author statement from ProtInc).
GO:0004694; Molecular function: eukaryotic translation initiation factor 2alpha kinase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008601; Molecular function: protein phosphatase type 2A regulator activity (traceable author statement from ProtInc).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0008285; Biological process: negative regulation of cell proliferation (traceable author statement from ProtInc).
GO:0009615; Biological process: response to virus (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001159; Ds-RNA_bd.
IPR014720; dsRNA-bd-like.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.
Gene3D G3DSA:3.30.160.20; dsRNA-bd-like; 2.
Pfam PF00035; dsrm; 2.
PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00358; DSRM; 2.
SMART graphical view of domain structure.
PROSITE PS50137; DS_RBD; 2.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P19525; -.
Genome annotation databases
Ensembl ENSG00000055332; Homo sapiens. [Contig view]
GeneID 5610; -.
KEGG hsa:5610; -.
NMPDR fig|9606.3.peg.17745; -.
Phylogenomic databases
HOGENOM P19525; -.
HOVERGEN P19525; -.
OMA P19525; GPEGFHY.
Other
NextBio 21806; -.
PMAP-CutDB P19525; -.
SOURCE EIF2AK2; Homo sapiens.
ProtoNet P19525.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antiviral defense; ATP-binding; Direct protein sequencing; Host-virus interaction; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Repeat; RNA-binding; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   551  551     Interferon-induced, double-stranded RNA-activated protein kinase. PRO_0000085945
DOMAIN   9    77  69     DRBM 1. 
DOMAIN   100   167  68     DRBM 2. 
DOMAIN   267   538  272     Protein kinase. 
REPEAT   331   343  13     1. 
REPEAT   345   357  13     2. 
NP_BIND   273   281  9     ATP (By similarity). 
REGION   331   357  27     2 X 13 AA approximate repeats. 
ACT_SITE   414   414        Proton acceptor (By similarity). 
BINDING   296   296        ATP. 
MOD_RES   83    83        Phosphoserine; by autocatalysis (Probable). 
MOD_RES   88    88        Phosphothreonine; by autocatalysis (Probable). 
MOD_RES   89    89        Phosphothreonine; by autocatalysis (Probable). 
MOD_RES   90    90        Phosphothreonine; by autocatalysis (Probable). 
MOD_RES   242   242        Phosphoserine; by autocatalysis (Probable). 
MOD_RES   255   255        Phosphothreonine; by autocatalysis (Probable). 
MOD_RES   258   258        Phosphothreonine; by autocatalysis (Probable). 
MOD_RES   446   446        Phosphothreonine; by autocatalysis. 
MOD_RES   451   451        Phosphothreonine; by autocatalysis. 
MOD_RES   456   456        Phosphoserine. 
VARIANT   428   428  1     V -> E. VAR_040474 
VARIANT   439   439  1     L -> V (in a lung adenocarcinoma sample; somatic mutation). VAR_040475 
VARIANT   506   506  1     I -> V. VAR_040476 
MUTAGEN   59    60        SK->AA: In FL-PKR-2AI; moderate loss of activity but no effect on dsRNA binding. 
MUTAGEN   60    60        K->A: Impairs dsRNA binding but not dimerization or activity. 
MUTAGEN   67    67        A->E: Significant loss of activity; loss of dsRNA binding and dimerization. 
MUTAGEN   83    83        S->A: No effect on enzymatic activity; when associated with A-88; A-89 and A-90. 
MUTAGEN   88    88        T->A: No effect on enzymatic activity; when associated with A-83; A-89 and A-90. 
MUTAGEN   89    89        T->A: No effect on enzymatic activity; when associated with A-83; A-88 and A-90. 
MUTAGEN   90    90        T->A: No effect on enzymatic activity; when associated with A-83; A-88 and A-89. 
MUTAGEN   149   150        TK->AA: In FL-PKR-2AII; no effect on activity. 
MUTAGEN   242   242        S->A: Moderate loss of activity; when associated with A-255 and A-258. 
MUTAGEN   244   296        Missing: Loss of activity. 
MUTAGEN   255   255        T->A: Moderate loss of activity; when associated with A-242 and A-255. 
MUTAGEN   258   258        T->A: Moderate loss of activity. 
MUTAGEN   296   296        K->R: Loss of activity. 
MUTAGEN   446   446        T->A: Significant loss of activity and impairs autophosphorylation of T-451. 
MUTAGEN   451   451        T->A: Loss of activity. 
CONFLICT   512   512        K -> E (in Ref. 6; AAF13156). 
STRAND   5     7  3      
HELIX   10    21  12      
STRAND   26    32  7      
TURN   35    37  3      
STRAND   41    50  10      
STRAND   54    56  3      
HELIX   61    76  16      
HELIX   102   111  10      
STRAND   115   123  9      
STRAND   125   138  14      
STRAND   144   149  6      
HELIX   150   167  18      
HELIX   261   266  6      
STRAND   267   274  8      
STRAND   276   278  3      
STRAND   281   286  6      
TURN   287   289  3      
STRAND   292   299  8      
HELIX   303   305  3      
HELIX   306   314  9      
STRAND   323   332  10      
STRAND   358   366  9      
HELIX   374   380  7      
HELIX   381   383  3      
HELIX   388   407  20      
HELIX   417   419  3      
STRAND   420   424  5      
STRAND   427   430  4      
STRAND   437   440  4      
HELIX   457   461  5      
HELIX   468   482  15      
HELIX   488   499  12      
HELIX   509   518  10      
HELIX   523   525  3      
HELIX   529   539  11      
Sequence information
Length: 551 AA [This is the length of the unprocessed precursor] Molecular weight: 62094 Da [This is the MW of the unprocessed precursor] CRC64: 815AD83ACAB45DA3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGDLSAGFF MEELNTYRQK QGVVLKYQEL PNSGPPHDRR FTFQVIIDGR EFPEGEGRSK 

        70         80         90        100        110        120 
KEAKNAAAKL AVEILNKEKK AVSPLLLTTT NSSEGLSMGN YIGLINRIAQ KKRLTVNYEQ 

       130        140        150        160        170        180 
CASGVHGPEG FHYKCKMGQK EYSIGTGSTK QEAKQLAAKL AYLQILSEET SVKSDYLSSG 

       190        200        210        220        230        240 
SFATTCESQS NSLVTSTLAS ESSSEGDFSA DTSEINSNSD SLNSSSLLMN GLRNNQRKAK 

       250        260        270        280        290        300 
RSLAPRFDLP DMKETKYTVD KRFGMDFKEI ELIGSGGFGQ VFKAKHRIDG KTYVIKRVKY 

       310        320        330        340        350        360 
NNEKAEREVK ALAKLDHVNI VHYNGCWDGF DYDPETSDDS LESSDYDPEN SKNSSRSKTK 

       370        380        390        400        410        420 
CLFIQMEFCD KGTLEQWIEK RRGEKLDKVL ALELFEQITK GVDYIHSKKL IHRDLKPSNI 

       430        440        450        460        470        480 
FLVDTKQVKI GDFGLVTSLK NDGKRTRSKG TLRYMSPEQI SSQDYGKEVD LYALGLILAE 

       490        500        510        520        530        540 
LLHVCDTAFE TSKFFTDLRD GIISDIFDKK EKTLLQKLLS KKPEDRPNTS EILRTLTVWK 

       550 
KSPEKNERHT C 

P19525 in FASTA format

View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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