STK39_HUMAN
ID STK39_HUMAN Reviewed; 545 AA.
AC Q9UEW8; O14774; Q53S90; Q53SL7; Q53SS1; Q9UER4; X5D9C8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=STE20/SPS1-related proline-alanine-rich protein kinase;
DE Short=Ste-20-related kinase;
DE EC=2.7.11.1;
DE AltName: Full=DCHT;
DE AltName: Full=Serine/threonine-protein kinase 39;
GN Name=STK39; Synonyms=SPAK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10980603; DOI=10.1038/sj.onc.1203784;
RA Johnston A.M., Naselli G., Gonez L.J., Martin R.M., Harrison L.C.,
RA de Aizpurua H.J.;
RT "SPAK, a STE20/SPS1-related kinase that activates the p38 pathway.";
RL Oncogene 19:4290-4297(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=24722188; DOI=10.1038/ncomms4650;
RA Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M.,
RA Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I.,
RA Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A.,
RA Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D.,
RA Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.;
RT "Protein interaction network of alternatively spliced isoforms from brain
RT links genetic risk factors for autism.";
RL Nat. Commun. 5:3650-3650(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Melnick M.B., Petitt M., Perrimon N., Comb M.J.;
RT "New human member of the Ste20 family.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 279-545 (ISOFORM 1).
RC TISSUE=Testis;
RA Baytel D., Don J.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION AT SER-309.
RX PubMed=14988727; DOI=10.1038/sj.emboj.7600125;
RA Li Y., Hu J., Vita R., Sun B., Tabata H., Altman A.;
RT "SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-
RT induced AP-1 activation pathway.";
RL EMBO J. 23:1112-1122(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-371 AND SER-385, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-349, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP INTERACTION WITH SORL1.
RX PubMed=20385770; DOI=10.1128/mcb.01560-09;
RA Reiche J., Theilig F., Rafiqi F.H., Carlo A.S., Militz D., Mutig K.,
RA Todiras M., Christensen E.I., Ellison D.H., Bader M., Nykjaer A.,
RA Bachmann S., Alessi D., Willnow T.E.;
RT "SORLA/SORL1 functionally interacts with SPAK to control renal activation
RT of Na(+)-K(+)-Cl(-) cotransporter 2.";
RL Mol. Cell. Biol. 30:3027-3037(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-354 AND SER-385, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May act as a mediator of stress-activated signals. Mediates
CC the inhibition of SLC4A4, SLC26A6 as well as CFTR activities by the WNK
CC scaffolds, probably through phosphorylation. Phosphorylates RELT.
CC {ECO:0000250|UniProtKB:Q9Z1W9}.
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 -!- 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;
CC -!- SUBUNIT: The phosphorylated form forms a complex with WNK2 (By
CC similarity). Interacts with RELT (By similarity). Interacts with SORL1
CC (via cytosolic C-terminus) (PubMed:20385770).
CC {ECO:0000250|UniProtKB:Q9Z1W9, ECO:0000269|PubMed:20385770}.
CC -!- INTERACTION:
CC Q9UEW8; Q9Y376: CAB39; NbExp=4; IntAct=EBI-2680974, EBI-306905;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC Note=Nucleus when caspase-cleaved. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UEW8-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=Q9UEW8-2; Sequence=VSP_055889;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain and pancreas
CC followed by heart, lung, kidney, skeletal muscle, liver, placenta and
CC testis.
CC -!- DOMAIN: PAPA box (proline-alanine repeats) may target the kinase to a
CC specific subcellular location by facilitating interaction with
CC intracellular proteins such as actin or actin-like proteins.
CC -!- PTM: Phosphorylated at Ser-309 by PRKCQ (PubMed:14988727).
CC Autophosphorylation at Thr-231 positively regulates its activity (By
CC similarity). {ECO:0000250|UniProtKB:Q9Z1W9,
CC ECO:0000269|PubMed:14988727}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AF099989; AAC72238.1; -; mRNA.
DR EMBL; KJ534948; AHW56588.1; -; mRNA.
DR EMBL; AF030403; AAD01901.1; -; mRNA.
DR EMBL; AC016723; AAY15003.1; -; Genomic_DNA.
DR EMBL; AC017069; AAY14897.1; -; Genomic_DNA.
DR EMBL; AC067940; AAY24032.1; -; Genomic_DNA.
DR EMBL; AF017635; AAB70552.1; -; mRNA.
DR CCDS; CCDS42770.1; -. [Q9UEW8-1]
DR RefSeq; NP_037365.2; NM_013233.2. [Q9UEW8-1]
DR PDB; 7O86; X-ray; 1.73 A; A/B=441-545.
DR PDBsum; 7O86; -.
DR AlphaFoldDB; Q9UEW8; -.
DR SMR; Q9UEW8; -.
DR BioGRID; 118159; 91.
DR CORUM; Q9UEW8; -.
DR ELM; Q9UEW8; -.
DR IntAct; Q9UEW8; 27.
DR MINT; Q9UEW8; -.
DR STRING; 9606.ENSP00000348278; -.
DR BindingDB; Q9UEW8; -.
DR ChEMBL; CHEMBL1163108; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9UEW8; -.
DR GlyGen; Q9UEW8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UEW8; -.
DR PhosphoSitePlus; Q9UEW8; -.
DR BioMuta; STK39; -.
DR DMDM; 317373508; -.
DR EPD; Q9UEW8; -.
DR jPOST; Q9UEW8; -.
DR MassIVE; Q9UEW8; -.
DR MaxQB; Q9UEW8; -.
DR PaxDb; Q9UEW8; -.
DR PeptideAtlas; Q9UEW8; -.
DR PRIDE; Q9UEW8; -.
DR ProteomicsDB; 84159; -. [Q9UEW8-1]
DR Antibodypedia; 33792; 803 antibodies from 41 providers.
DR DNASU; 27347; -.
DR Ensembl; ENST00000355999.5; ENSP00000348278.4; ENSG00000198648.11. [Q9UEW8-1]
DR GeneID; 27347; -.
DR KEGG; hsa:27347; -.
DR MANE-Select; ENST00000355999.5; ENSP00000348278.4; NM_013233.3; NP_037365.2.
DR UCSC; uc002uea.4; human. [Q9UEW8-1]
DR CTD; 27347; -.
DR DisGeNET; 27347; -.
DR GeneCards; STK39; -.
DR HGNC; HGNC:17717; STK39.
DR HPA; ENSG00000198648; Low tissue specificity.
DR MIM; 607648; gene.
DR neXtProt; NX_Q9UEW8; -.
DR OpenTargets; ENSG00000198648; -.
DR PharmGKB; PA38243; -.
DR VEuPathDB; HostDB:ENSG00000198648; -.
DR eggNOG; KOG0582; Eukaryota.
DR GeneTree; ENSGT00940000154621; -.
DR HOGENOM; CLU_000288_111_1_1; -.
DR InParanoid; Q9UEW8; -.
DR OMA; KEENPEX; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; Q9UEW8; -.
DR TreeFam; TF105339; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; Q9UEW8; -.
DR SignaLink; Q9UEW8; -.
DR SIGNOR; Q9UEW8; -.
DR BioGRID-ORCS; 27347; 14 hits in 1101 CRISPR screens.
DR ChiTaRS; STK39; human.
DR GeneWiki; STK39; -.
DR GenomeRNAi; 27347; -.
DR Pharos; Q9UEW8; Tchem.
DR PRO; PR:Q9UEW8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UEW8; protein.
DR Bgee; ENSG00000198648; Expressed in endothelial cell and 204 other tissues.
DR Genevisible; Q9UEW8; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; IEA:Ensembl.
DR GO; GO:0071476; P:cellular hypotonic response; IC:ParkinsonsUK-UCL.
DR GO; GO:1990869; P:cellular response to chemokine; IMP:BHF-UCL.
DR GO; GO:0035865; P:cellular response to potassium ion; IEA:Ensembl.
DR GO; GO:0038146; P:chemokine (C-X-C motif) ligand 12 signaling pathway; IMP:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR GO; GO:0036438; P:maintenance of lens transparency; ISS:ParkinsonsUK-UCL.
DR GO; GO:1905408; P:negative regulation of creatine transmembrane transporter activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090188; P:negative regulation of pancreatic juice secretion; IEA:Ensembl.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IDA:ParkinsonsUK-UCL.
DR GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032414; P:positive regulation of ion transmembrane transporter activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IMP:UniProtKB.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IEA:Ensembl.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; IMP:BHF-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:1904044; P:response to aldosterone; IEA:Ensembl.
DR GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IDA:ParkinsonsUK-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IEA:Ensembl.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF12202; OSR1_C; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..545
FT /note="STE20/SPS1-related proline-alanine-rich protein
FT kinase"
FT /id="PRO_0000086722"
FT DOMAIN 63..337
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 310..536
FT /note="Interaction with RELT"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1W9"
FT REGION 361..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 360..366
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 387..391
FT /note="Caspase cleavage related site"
FT COMPBIAS 391..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 231
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1W9"
FT MOD_RES 309
FT /note="Phosphoserine; by PKC/PRKCQ"
FT /evidence="ECO:0000269|PubMed:14988727"
FT MOD_RES 349
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17487921,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1W9"
FT VAR_SEQ 28..46
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:24722188"
FT /id="VSP_055889"
FT CONFLICT 41
FT /note="A -> AAP (in Ref. 1; AAC72238 and 3; AAD01901)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="L -> F (in Ref. 3; AAD01901)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="A -> V (in Ref. 2; AHW56588)"
FT /evidence="ECO:0000305"
FT STRAND 452..459
FT /evidence="ECO:0007829|PDB:7O86"
FT STRAND 465..472
FT /evidence="ECO:0007829|PDB:7O86"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:7O86"
FT HELIX 479..488
FT /evidence="ECO:0007829|PDB:7O86"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:7O86"
FT HELIX 497..508
FT /evidence="ECO:0007829|PDB:7O86"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:7O86"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:7O86"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:7O86"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:7O86"
FT TURN 533..536
FT /evidence="ECO:0007829|PDB:7O86"
FT STRAND 537..544
FT /evidence="ECO:0007829|PDB:7O86"
SQ SEQUENCE 545 AA; 59474 MW; 35E68F400A38A861 CRC64;
MAEPSGSPVH VQLPQQAAPV TAAAAAAPAA ATAAPAPAAP AAPAPAPAPA AQAVGWPICR
DAYELQEVIG SGATAVVQAA LCKPRQERVA IKRINLEKCQ TSMDELLKEI QAMSQCSHPN
VVTYYTSFVV KDELWLVMKL LSGGSMLDII KYIVNRGEHK NGVLEEAIIA TILKEVLEGL
DYLHRNGQIH RDLKAGNILL GEDGSVQIAD FGVSAFLATG GDVTRNKVRK TFVGTPCWMA
PEVMEQVRGY DFKADMWSFG ITAIELATGA APYHKYPPMK VLMLTLQNDP PTLETGVEDK
EMMKKYGKSF RKLLSLCLQK DPSKRPTAAE LLKCKFFQKA KNREYLIEKL LTRTPDIAQR
AKKVRRVPGS SGHLHKTEDG DWEWSDDEMD EKSEEGKAAF SQEKSRRVKE ENPEIAVSAS
TIPEQIQSLS VHDSQGPPNA NEDYREASSC AVNLVLRLRN SRKELNDIRF EFTPGRDTAD
GVSQELFSAG LVDGHDVVIV AANLQKIVDD PKALKTLTFK LASGCDGSEI PDEVKLIGFA
QLSVS
