WNK2_MOUSE
ID WNK2_MOUSE Reviewed; 2149 AA.
AC Q3UH66; Q3V387; Q6PAN9; Q6ZPI6; Q7TNS1; Q811F2;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Serine/threonine-protein kinase WNK2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9H4A3};
DE AltName: Full=Protein kinase lysine-deficient 2 {ECO:0000312|MGI:MGI:1922857};
DE AltName: Full=Protein kinase with no lysine 2 {ECO:0000303|PubMed:21733846};
GN Name=Wnk2 {ECO:0000312|MGI:MGI:1922857};
GN Synonyms=Kiaa1760 {ECO:0000312|EMBL:BAC98249.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1506-2149 (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-2149 (ISOFORM 6), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 801-2149 (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1513-2149 (ISOFORM 4).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 761-2149 (ISOFORM 7).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1725 AND SER-1726, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1566; SER-1770 AND
RP SER-1797, AND INTERACTION WITH STK39.
RX PubMed=21733846; DOI=10.1074/jbc.m111.222893;
RA Rinehart J., Vazquez N., Kahle K.T., Hodson C.A., Ring A.M., Gulcicek E.E.,
RA Louvi A., Bobadilla N.A., Gamba G., Lifton R.P.;
RT "WNK2 is a novel regulator of essential neuronal cation-chloride
RT cotransporters.";
RL J. Biol. Chem. 286:30171-30180(2011).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-19 AND ARG-30, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Serine/threonine kinase which plays an important role in the
CC regulation of electrolyte homeostasis, cell signaling, survival, and
CC proliferation. Acts as an activator and inhibitor of sodium-coupled
CC chloride cotransporters and potassium-coupled chloride cotransporters
CC respectively. Activates SLC12A2, SCNN1A, SCNN1B, SCNN1D and SGK1 and
CC inhibits SLC12A5. Negatively regulates the EGF-induced activation of
CC the ERK/MAPK-pathway and the downstream cell cycle progression. Affects
CC MAPK3/MAPK1 activity by modulating the activity of MAP2K1 and this
CC modulation depends on phosphorylation of MAP2K1 by PAK1. WNK2 acts by
CC interfering with the activity of PAK1 by controlling the balance of the
CC activity of upstream regulators of PAK1 activity, RHOA and RAC1, which
CC display reciprocal activity. {ECO:0000269|PubMed:21733846}.
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:0000250|UniProtKB:Q9H4A3};
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:0000250|UniProtKB:Q9H4A3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9H4A3};
CC -!- ACTIVITY REGULATION: Activation requires autophosphorylation of Ser-
CC 356. Phosphorylation of Ser-352 also promotes increased activity (By
CC similarity). {ECO:0000250|UniProtKB:Q9JIH7}.
CC -!- SUBUNIT: Forms a complex with the phosphorylated form of STK39 in the
CC brain. {ECO:0000269|PubMed:21733846}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y3S1}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9Y3S1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q3UH66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UH66-2; Sequence=VSP_023369;
CC Name=3;
CC IsoId=Q3UH66-3; Sequence=VSP_023370, VSP_023372;
CC Name=4;
CC IsoId=Q3UH66-4; Sequence=VSP_023370, VSP_023371;
CC Name=5;
CC IsoId=Q3UH66-5; Sequence=VSP_023370, VSP_023372, VSP_023373;
CC Name=6;
CC IsoId=Q3UH66-6; Sequence=VSP_023366, VSP_023367, VSP_023370,
CC VSP_023371;
CC Name=7;
CC IsoId=Q3UH66-7; Sequence=VSP_023367, VSP_023368, VSP_023370,
CC VSP_023372, VSP_023374;
CC -!- TISSUE SPECIFICITY: Brain and heart. {ECO:0000269|PubMed:21733846}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9Y3S1}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WNK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Was named WNK/'with no lysine(K)' because key residues for
CC catalysis, including the lysine involved in ATP binding, are either not
CC conserved or differ compared to the residues described in other kinase
CC family proteins. {ECO:0000250|UniProtKB:Q9H4A3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46464.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH55795.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE20646.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CAAA01187366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK044381; BAE20646.1; ALT_INIT; mRNA.
DR EMBL; AK147550; BAE27991.1; -; mRNA.
DR EMBL; BC046464; AAH46464.1; ALT_INIT; mRNA.
DR EMBL; BC055795; AAH55795.1; ALT_INIT; mRNA.
DR EMBL; BC060187; AAH60187.1; -; mRNA.
DR EMBL; AK129439; BAC98249.1; -; mRNA.
DR CCDS; CCDS70454.1; -. [Q3UH66-5]
DR CCDS; CCDS70455.1; -. [Q3UH66-3]
DR RefSeq; NP_001277240.1; NM_001290311.1.
DR RefSeq; NP_001277242.1; NM_001290313.1.
DR RefSeq; NP_083637.2; NM_029361.4.
DR AlphaFoldDB; Q3UH66; -.
DR SMR; Q3UH66; -.
DR BioGRID; 217612; 11.
DR IntAct; Q3UH66; 3.
DR MINT; Q3UH66; -.
DR STRING; 10090.ENSMUSP00000089212; -.
DR iPTMnet; Q3UH66; -.
DR PhosphoSitePlus; Q3UH66; -.
DR SwissPalm; Q3UH66; -.
DR EPD; Q3UH66; -.
DR jPOST; Q3UH66; -.
DR MaxQB; Q3UH66; -.
DR PaxDb; Q3UH66; -.
DR PeptideAtlas; Q3UH66; -.
DR PRIDE; Q3UH66; -.
DR ProteomicsDB; 299689; -. [Q3UH66-1]
DR ProteomicsDB; 299690; -. [Q3UH66-2]
DR ProteomicsDB; 299691; -. [Q3UH66-3]
DR ProteomicsDB; 299692; -. [Q3UH66-4]
DR ProteomicsDB; 299693; -. [Q3UH66-5]
DR ProteomicsDB; 299694; -. [Q3UH66-6]
DR ProteomicsDB; 299695; -. [Q3UH66-7]
DR DNASU; 75607; -.
DR GeneID; 75607; -.
DR KEGG; mmu:75607; -.
DR CTD; 65268; -.
DR MGI; MGI:1922857; Wnk2.
DR eggNOG; KOG0584; Eukaryota.
DR InParanoid; Q3UH66; -.
DR OrthoDB; 27514at2759; -.
DR PhylomeDB; Q3UH66; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 75607; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Wnk2; mouse.
DR PRO; PR:Q3UH66; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UH66; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019869; F:chloride channel inhibitor activity; IBA:GO_Central.
DR GO; GO:0019870; F:potassium channel inhibitor activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0050801; P:ion homeostasis; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0010766; P:negative regulation of sodium ion transport; IBA:GO_Central.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Kinase;
KW Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2149
FT /note="Serine/threonine-protein kinase WNK2"
FT /id="PRO_0000278774"
FT DOMAIN 195..453
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1916..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2018..2044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2122..2149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..728
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1127
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1459
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1490
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2019..2033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 275..278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 19
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 30
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3S1"
FT MOD_RES 352
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT MOD_RES 356
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3S1"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3S1"
FT MOD_RES 1210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3S1"
FT MOD_RES 1507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3S1"
FT MOD_RES 1566
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21733846"
FT MOD_RES 1594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3S1"
FT MOD_RES 1725
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1770
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21733846"
FT MOD_RES 1797
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21733846"
FT MOD_RES 1962
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3S1"
FT VAR_SEQ 731..742
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023366"
FT VAR_SEQ 971..1068
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023367"
FT VAR_SEQ 1592..1593
FT /note="AE -> E (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_023368"
FT VAR_SEQ 1921..2004
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023369"
FT VAR_SEQ 1935
FT /note="R -> AHASTPP (in isoform 3, isoform 4, isoform 5,
FT isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_023370"
FT VAR_SEQ 1971..2024
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023371"
FT VAR_SEQ 2019..2025
FT /note="SLYDSPG -> R (in isoform 3, isoform 5 and isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_023372"
FT VAR_SEQ 2142..2149
FT /note="DPESEKPD -> GTVHSSLSGPPCTLPLCQYGGLLPDPVSWGPWVASGNPEG
FT SWGSQSPTQVPVFPVFLRPPVISTPGPRLHIT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023373"
FT VAR_SEQ 2142..2149
FT /note="DPESEKPD -> EACALPTPPCKFLSRPSSGQPTEGRSISGGFHDTCPGGER
FT GDENSLTPSG (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_023374"
FT CONFLICT 761..794
FT /note="PYLAPTSQVVAPAQLKPLQMPQPPLQPLAQVPPQ -> RRYLWPIFCSPQGW
FT GTRPWTRPVHACLQGLLARE (in Ref. 4; BAC98249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2149 AA; 227527 MW; A4BBF1D391FE9BEC CRC64;
MDGDGGRRDA PGALMEAGRG TGSAGMAEPR ARAARLGPQR FLRRSVVESD QEEPPGLEAA
ETPSAQPPQP LQRRVLLLCK TRRLIAERAR GRPAAPAPAA PAAPPGSPSV PSDPGPERAG
TQEPSPDPTT ASAAATQVPD GGPRQEEAPA PTQEDAGTTE AKPEPGRARK DEPEEEEDDE
DDLKAVATSL DGRFLKFDIE LGRGSFKTVY KGLDTETWVE VAWCELQDRK LTKLERQRFK
EEAEMLKGLQ HPNIVRFYDF WESSAKGKRC IVLVTELMTS GTLKTYLKRF KVMKPKVLRS
WCRQILKGLL FLHTRTPPII HRDLKCDNIF ITGPTGSVKI GDLGLATLKR ASFAKSVIGT
PEFMAPEMYE EHYDESVDVY AFGMCMLEMA TSEYPYSECQ NAAQIYRKVT CGIKPASFEK
VHDPEIKEII GECICKNKEE RYEIKDLLSH AFFAEDTGVR VELAEEDHGR KSTIALRLWV
EDPKKLKGKP KDNGAIEFTF DLEKETPDEV AQEMIDSGFF HESDVKIVAK SIRDRVALIQ
WRRERIWPAL QSQEPKDSGS PDKARGLPAP LQVQVTYHAQ SGQPGQPEPE EPEADQHLLP
PTLPASVTSL ASDSTFDSGQ GSTVYSDSQS SQQSMVLSSL VDTAPTPASC VCSPPVSEGP
GLTHSLPTLG AFQQPATVPG LSVGPVPPPA RPPLLQQHFP ESSMSFTPVL PPPSTPVPTG
PSQPAPPVQQ PLPMAQPPTL PQVLAPQPMG TVQPVPSHLP PYLAPTSQVV APAQLKPLQM
PQPPLQPLAQ VPPQMPQMPV VPPITPLTGL DGLPQTLTDL PAANVAPVPP PQYFSPAVIL
PSLTTPLPTS PALPMQAVKL PHPPGTPLAV PCQTIVPNAP AAIPLLAVAP QGVAALSIHP
AVAQIPAQPV YPAAFPQMVP GDIPPSPHHT VQSLRATPPQ LASPVPPQPV QPSVIHLPEQ
AAPTAASGTQ VLLGHPPSYT ADVAAPVSAV SLPPAVLSPP LPDTLLPTVP DLLPKVPSSL
APTVVAASQS APAQTSSLLL PTNPPLPTGP AVAGPCPAVQ LMVEVAQEEQ VSQDKPPGPP
QSSESFGGSD VTSGRDLSDS CEGTFGGGRL EGRTARKHHR RSTRARSRQE RASRPRLTIL
NVCNTGDKMV ECQLETHNHK MVTFKFDLDG DAPDEIATYM VEHDFILPAE RETFIEQMKD
VMDKAEDMLS EDTDADHGSD TGTSPPHLGT CGLATGEENR QSQANAPVYQ QNVLHTGKRW
FIICPVAEHP ATDTSESSPP LPLSSLQPEA SQDPAPYPDQ LSLTDKPSFP AAQQLLSQAG
SSNPPGGASA PLAPSSPPVT TVIPAAPATS TVPESAAGTA MQAGGPGTHQ GPASVHETLQ
PLAETRSAQC TAQPLSTGQG PCTPALEASR CSTGLGEPIS TREVSTQGEP LPASVPEPSP
PTGATQSVPG QPPPPLPITV GAISLAAPQL PSPPLGPTAP PPPPSALESD GEGPPPRVGF
VDNTIKSLDE KLRTLLYQEH VPTSSASAGT PMEASDRDFT LEPLRGDLPS ALSDKTPSLT
QQTQPSLEKS ETAPAGWALA QREQGASSPM TAESSSSNTL GCDSDAGQVA SDSSTAPSVP
QDASGSSVPT HMDPKDQNSS VPREALAAPM QSGPGSFTVG SPAQLRGARD SGSPHKRPGQ
QDNSSPAKTV GRFSVVSTQD EWTLASPHSL RYSAPPDVYL DEIPSSPEVK LAVRRVQTAS
SIEVGVEEPA SSDSGDERPR RRSQVQKQSS LPGTGGVASD FVKKATAFLH RSSRAGSLGP
ETPSRAGVKV PTISITSFHS QSSYISSDND SEFEDADIKK ELRSLREKHL KEISELQSQQ
KQEIEALYRR LGKPLPPNVG FFHTAPPMGR RRKTSKSKLK AGKLLNPLVQ QLKVVASSTG
HLSDSSRGPP TKDPRGTKAV QTQQPCSVRA SLSTDICSGL ASDGGGARGQ GWTVYHPTSE
RGAYKSSSKP RARFLSGPVS VSIWSALKRL CLGKEHSSSL YDSPGSSTSS LAPGPEPGPQ
PTLHVQAQVN NSNNKKGTFT DDLHKLVDEW TTKTVGAAQV KPTLNQLKQT QKLHDMEASG
DARATSVPRA AVGASCLAPA PGPLSTTATP GATPALPVPI PDPESEKPD
