NIK1_ARATH
ID NIK1_ARATH Reviewed; 638 AA.
AC Q9LFS4; Q8LA44;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein NSP-INTERACTING KINASE 1 {ECO:0000303|PubMed:15489295};
DE Short=AtNIK1 {ECO:0000303|PubMed:15489295};
DE EC=2.7.11.1 {ECO:0000269|PubMed:15489295};
DE AltName: Full=LRR receptor-like serine/threonine-protein kinase NIK1 {ECO:0000303|PubMed:15489295};
DE Flags: Precursor;
GN Name=NIK1 {ECO:0000303|PubMed:15489295};
GN OrderedLocusNames=At5g16000 {ECO:0000312|Araport:AT5G16000};
GN ORFNames=F1N13_140 {ECO:0000312|EMBL:CAC01799.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, INTERACTION WITH CABBAGE LEAF CURL VIRUS NSP, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=15489295; DOI=10.1101/gad.1245904;
RA Fontes E.P., Santos A.A., Luz D.F., Waclawovsky A.J., Chory J.;
RT "The geminivirus nuclear shuttle protein is a virulence factor that
RT suppresses transmembrane receptor kinase activity.";
RL Genes Dev. 18:2545-2556(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH RPL10A AND RPL18B.
RX PubMed=19112492; DOI=10.1371/journal.ppat.1000247;
RA Carvalho C.M., Santos A.A., Pires S.R., Rocha C.S., Saraiva D.I.,
RA Machado J.P., Mattos E.C., Fietto L.G., Fontes E.P.;
RT "Regulated nuclear trafficking of rpL10A mediated by NIK1 represents a
RT defense strategy of plant cells against virus.";
RL PLoS Pathog. 4:E1000247-E1000247(2008).
RN [8]
RP FUNCTION, AND INTERACTION WITH RPL10A AND RPL18B.
RX PubMed=18789471; DOI=10.1016/j.virol.2008.08.005;
RA Rocha C.S., Santos A.A., Machado J.P., Fontes E.P.;
RT "The ribosomal protein L10/QM-like protein is a component of the NIK-
RT mediated antiviral signaling.";
RL Virology 380:165-169(2008).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-468; THR-469 AND THR-474,
RP PHOSPHORYLATION AT THR-469 AND THR-474, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RX PubMed=19492062; DOI=10.1371/journal.pone.0005781;
RA Santos A.A., Carvalho C.M., Florentino L.H., Ramos H.J., Fontes E.P.;
RT "Conserved threonine residues within the A-loop of the receptor NIK
RT differentially regulate the kinase function required for antiviral
RT signaling.";
RL PLoS ONE 4:E5781-E5781(2009).
RN [10]
RP REVIEW.
RX PubMed=20624762; DOI=10.1093/jxb/erq219;
RA Santos A.A., Lopes K.V., Apfata J.A., Fontes E.P.;
RT "NSP-interacting kinase, NIK: a transducer of plant defence signalling.";
RL J. Exp. Bot. 61:3839-3845(2010).
RN [11]
RP FUNCTION, MUTAGENESIS OF THR-474, AND TISSUE SPECIFICITY.
RX PubMed=25707794; DOI=10.1038/nature14171;
RA Zorzatto C., Machado J.P., Lopes K.V., Nascimento K.J., Pereira W.A.,
RA Brustolini O.J., Reis P.A., Calil I.P., Deguchi M., Sachetto-Martins G.,
RA Gouveia B.C., Loriato V.A., Silva M.A., Silva F.F., Santos A.A., Chory J.,
RA Fontes E.P.;
RT "NIK1-mediated translation suppression functions as a plant antiviral
RT immunity mechanism.";
RL Nature 520:679-682(2015).
CC -!- FUNCTION: Involved in defense response to geminivirus and begomovirus
CC infection via regulation of the nuclear trafficking of RPL10A.
CC Phosphorylates RPL10A in vitro (PubMed:15489295, PubMed:18789471,
CC PubMed:19112492, PubMed:19492062, PubMed:25707794). Activation of NIK1
CC down-regulates cytosolic translation (PubMed:25707794).
CC {ECO:0000269|PubMed:15489295, ECO:0000269|PubMed:18789471,
CC ECO:0000269|PubMed:19112492, ECO:0000269|PubMed:19492062,
CC ECO:0000269|PubMed:25707794}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:15489295};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15489295};
CC -!- ACTIVITY REGULATION: Inhibited by the viral nuclear shuttle protein
CC (NSP) that binds to the region required for oligomerization.
CC {ECO:0000269|PubMed:15489295}.
CC -!- SUBUNIT: Oligomer. Interacts with geminivirus nuclear shuttle protein
CC (NSP) (PubMed:15489295). Interacts with RPL10A and RPL18B
CC (PubMed:18789471, PubMed:19112492). {ECO:0000269|PubMed:15489295,
CC ECO:0000269|PubMed:18789471, ECO:0000269|PubMed:19112492}.
CC -!- INTERACTION:
CC Q9LFS4; C0LGD7-2: At1g06840; NbExp=2; IntAct=EBI-16146189, EBI-20651159;
CC Q9LFS4; O04567: At1g27190; NbExp=2; IntAct=EBI-16146189, EBI-1238687;
CC Q9LFS4; C0LGI5: At1g69990; NbExp=2; IntAct=EBI-16146189, EBI-20651225;
CC Q9LFS4; O65924: At2g19210; NbExp=3; IntAct=EBI-16146189, EBI-20662256;
CC Q9LFS4; Q9LFG1: At3g53590; NbExp=3; IntAct=EBI-16146189, EBI-20664191;
CC Q9LFS4; Q8VYT3: At4g30520; NbExp=4; IntAct=EBI-16146189, EBI-16902452;
CC Q9LFS4; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-16146189, EBI-6298290;
CC Q9LFS4; Q94F62: BAK1; NbExp=4; IntAct=EBI-16146189, EBI-617138;
CC Q9LFS4; Q9ZWC8: BRL1; NbExp=2; IntAct=EBI-16146189, EBI-590903;
CC Q9LFS4; Q9LJF3: BRL3; NbExp=2; IntAct=EBI-16146189, EBI-20651413;
CC Q9LFS4; C0LGT6: EFR; NbExp=2; IntAct=EBI-16146189, EBI-8801168;
CC Q9LFS4; Q42371: ERECTA; NbExp=3; IntAct=EBI-16146189, EBI-16940407;
CC Q9LFS4; Q6XAT2: ERL2; NbExp=4; IntAct=EBI-16146189, EBI-16895926;
CC Q9LFS4; C0LGX3: HSL2; NbExp=2; IntAct=EBI-16146189, EBI-16904927;
CC Q9LFS4; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-16146189, EBI-20651739;
CC Q9LFS4; Q9LFS4: NIK1; NbExp=3; IntAct=EBI-16146189, EBI-16146189;
CC Q9LFS4; Q9C7S5: PSY1R; NbExp=3; IntAct=EBI-16146189, EBI-16904988;
CC Q9LFS4; Q9ZRF9: RPK1; NbExp=4; IntAct=EBI-16146189, EBI-1238953;
CC Q9LFS4; Q9SKG5: SERK4; NbExp=4; IntAct=EBI-16146189, EBI-6290483;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15489295};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15489295}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, roots, stems and
CC flowers. {ECO:0000269|PubMed:15489295, ECO:0000269|PubMed:25707794}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:19492062}.
CC -!- DISRUPTION PHENOTYPE: Enhanced susceptibility to geminivirus infection.
CC {ECO:0000269|PubMed:15489295, ECO:0000269|PubMed:19492062}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65586.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL391145; CAC01799.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92233.1; -; Genomic_DNA.
DR EMBL; AY074263; AAL66960.1; -; mRNA.
DR EMBL; BT002366; AAN86199.1; -; mRNA.
DR EMBL; FJ708777; ACN59368.1; -; mRNA.
DR EMBL; AY088040; AAM65586.1; ALT_INIT; mRNA.
DR PIR; T51383; T51383.
DR RefSeq; NP_197104.1; NM_121605.3.
DR AlphaFoldDB; Q9LFS4; -.
DR SMR; Q9LFS4; -.
DR BioGRID; 16733; 63.
DR DIP; DIP-61517N; -.
DR IntAct; Q9LFS4; 76.
DR STRING; 3702.AT5G16000.1; -.
DR iPTMnet; Q9LFS4; -.
DR PaxDb; Q9LFS4; -.
DR PRIDE; Q9LFS4; -.
DR ProteomicsDB; 251151; -.
DR EnsemblPlants; AT5G16000.1; AT5G16000.1; AT5G16000.
DR GeneID; 831457; -.
DR Gramene; AT5G16000.1; AT5G16000.1; AT5G16000.
DR KEGG; ath:AT5G16000; -.
DR Araport; AT5G16000; -.
DR TAIR; locus:2146102; AT5G16000.
DR eggNOG; ENOG502QVM7; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q9LFS4; -.
DR OMA; WITRQRI; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LFS4; -.
DR PRO; PR:Q9LFS4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFS4; baseline and differential.
DR Genevisible; Q9LFS4; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004672; F:protein kinase activity; IMP:CAFA.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IMP:CAFA.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:CAFA.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:CAFA.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:CAFA.
DR GO; GO:0006468; P:protein phosphorylation; IMP:CAFA.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Host-virus interaction; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Plant defense; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..638
FT /note="Protein NSP-INTERACTING KINASE 1"
FT /id="PRO_0000409725"
FT TOPO_DOM 32..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 104..128
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 130..152
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 153..175
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 177..200
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 312..593
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 422..502
FT /note="Interaction with geminivirus NSP protein"
FT ACT_SITE 435
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 318..326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 468
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 469
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19492062"
FT MOD_RES 474
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19492062"
FT MOD_RES 482
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 485
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 566
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 468
FT /note="T->A: Impaired autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19492062"
FT MUTAGEN 469
FT /note="T->A: Enhanced kinase activation."
FT /evidence="ECO:0000269|PubMed:19492062"
FT MUTAGEN 474
FT /note="T->A: Impaired autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19492062"
FT MUTAGEN 474
FT /note="T->D: Constitutive activation."
FT /evidence="ECO:0000269|PubMed:25707794"
FT MUTAGEN 474
FT /note="T->E: Impaired autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19492062"
FT CONFLICT 118
FT /note="K -> T (in Ref. 5; AAM65586)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="V -> I (in Ref. 5; AAM65586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 70546 MW; 2757C6CDD6F5D9B6 CRC64;
MESTIVMMMM ITRSFFCFLG FLCLLCSSVH GLLSPKGVNF EVQALMDIKA SLHDPHGVLD
NWDRDAVDPC SWTMVTCSSE NFVIGLGTPS QNLSGTLSPS ITNLTNLRIV LLQNNNIKGK
IPAEIGRLTR LETLDLSDNF FHGEIPFSVG YLQSLQYLRL NNNSLSGVFP LSLSNMTQLA
FLDLSYNNLS GPVPRFAAKT FSIVGNPLIC PTGTEPDCNG TTLIPMSMNL NQTGVPLYAG
GSRNHKMAIA VGSSVGTVSL IFIAVGLFLW WRQRHNQNTF FDVKDGNHHE EVSLGNLRRF
GFRELQIATN NFSSKNLLGK GGYGNVYKGI LGDSTVVAVK RLKDGGALGG EIQFQTEVEM
ISLAVHRNLL RLYGFCITQT EKLLVYPYMS NGSVASRMKA KPVLDWSIRK RIAIGAARGL
VYLHEQCDPK IIHRDVKAAN ILLDDYCEAV VGDFGLAKLL DHQDSHVTTA VRGTVGHIAP
EYLSTGQSSE KTDVFGFGIL LLELVTGQRA FEFGKAANQK GVMLDWVKKI HQEKKLELLV
DKELLKKKSY DEIELDEMVR VALLCTQYLP GHRPKMSEVV RMLEGDGLAE KWEASQRSDS
VSKCSNRINE LMSSSDRYSD LTDDSSLLVQ AMELSGPR
