ID   DAPK1_MOUSE             Reviewed;        1442 AA.
AC   Q80YE7; Q80YE6; Q8R341; Q8VDN6; Q9CSD4; Q9JJP7;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 3.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=Death-associated protein kinase 1;
DE            Short=DAP kinase 1;
DE            EC=2.7.11.1;
GN   Name=Dapk1;
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 {ECO:0000312|EMBL:AAO91934.2};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAO91934.2};
RX   PubMed=11485996; DOI=10.1074/jbc.m101886200;
RA   Jin Y., Blue E.K., Dixon S., Hou L., Wysolmerski R.B., Gallagher P.J.;
RT   "Identification of a new form of death-associated protein kinase that
RT   promotes cell survival.";
RL   J. Biol. Chem. 276:39667-39678(2001).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Brain {ECO:0000312|EMBL:CAA65762.1};
RA   Kimchi A.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH57317.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH57317.1}, and Mammary gland
RC   {ECO:0000269|PubMed:15489334};
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 1203-1442 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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   [5]
RP   PHOSPHORYLATION AT SER-308, ACTIVITY REGULATION, AND INTERACTION WITH
RP   UNC5B.
RX   PubMed=15729359; DOI=10.1038/sj.emboj.7600584;
RA   Llambi F., Lourenco F.C., Gozuacik D., Guix C., Pays L., Del Rio G.,
RA   Kimchi A., Mehlen P.;
RT   "The dependence receptor UNC5H2 mediates apoptosis through DAP-kinase.";
RL   EMBO J. 24:1192-1201(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   FUNCTION, DEPHOSPHORYLATION AT SER-308, AND ACTIVITY REGULATION.
RX   PubMed=18806755; DOI=10.1038/cdd.2008.121;
RA   Gozuacik D., Bialik S., Raveh T., Mitou G., Shohat G., Sabanay H.,
RA   Mizushima N., Yoshimori T., Kimchi A.;
RT   "DAP-kinase is a mediator of endoplasmic reticulum stress-induced caspase
RT   activation and autophagic cell death.";
RL   Cell Death Differ. 15:1875-1886(2008).
RN   [8]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH GRIN2B,
RP   PHOSPHORYLATION AT SER-308, AND DISRUPTION PHENOTYPE.
RX   PubMed=20141836; DOI=10.1016/j.cell.2009.12.055;
RA   Tu W., Xu X., Peng L., Zhong X., Zhang W., Soundarapandian M.M., Balel C.,
RA   Wang M., Jia N., Zhang W., Lew F., Chan S.L., Chen Y., Lu Y.;
RT   "DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage
RT   in stroke.";
RL   Cell 140:222-234(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-1115 AND SER-1433,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Lung;
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   [10]
RP   FUNCTION.
RX   PubMed=23071094; DOI=10.1128/mcb.01168-12;
RA   Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
RT   "Heterotrimeric GAIT complex drives transcript-selective translation
RT   inhibition in murine macrophages.";
RL   Mol. Cell. Biol. 32:5046-5055(2012).
CC   -!- FUNCTION: Calcium/calmodulin-dependent serine/threonine kinase involved
CC       in multiple cellular signaling pathways that trigger cell survival,
CC       apoptosis, and autophagy. Regulates both type I apoptotic and type II
CC       autophagic cell deaths signal, depending on the cellular setting. The
CC       former is caspase-dependent, while the latter is caspase-independent
CC       and is characterized by the accumulation of autophagic vesicles.
CC       Phosphorylates PIN1 resulting in inhibition of its catalytic activity,
CC       nuclear localization, and cellular function. Phosphorylates TPM1,
CC       enhancing stress fiber formation in endothelial cells. Phosphorylates
CC       STX1A and significantly decreases its binding to STXBP1. Phosphorylates
CC       PRKD1 and regulates JNK signaling by binding and activating PRKD1 under
CC       oxidative stress. Phosphorylates BECN1, reducing its interaction with
CC       BCL2 and BCL2L1 and promoting the induction of autophagy.
CC       Phosphorylates TSC2, disrupting the TSC1-TSC2 complex and stimulating
CC       mTORC1 activity in a growth factor-dependent pathway. Phosphorylates
CC       RPS6, MYL9 and DAPK3 (By similarity). Acts as a signaling amplifier of
CC       NMDA receptors at extrasynaptic sites for mediating brain damage in
CC       stroke. Cerebral ischemia recruits DAPK1 into the NMDA receptor complex
CC       and it phosphorylates GRINB at Ser-1303 inducing injurious Ca(2+)
CC       influx through NMDA receptor channels, resulting in an irreversible
CC       neuronal death. Required together with DAPK3 for phosphorylation of
CC       RPL13A upon interferon-gamma activation which is causing RPL13A
CC       involvement in transcript-selective translation inhibition.
CC       {ECO:0000250, ECO:0000269|PubMed:11485996, ECO:0000269|PubMed:18806755,
CC       ECO:0000269|PubMed:20141836, ECO:0000269|PubMed:23071094}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:11485996};
CC   -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Regulated by a
CC       locking mechanism, involving autophosphorylation at Ser-308 and
CC       calmodulin binding. In the inactive state, Ser-308 is phosphorylated.
CC       Activation involves its dephosphorylation and a release-of-
CC       autoinhibition mechanism where binding of calmodulin induces a
CC       conformational change that relieves the steric block of the active site
CC       by the autoinhibitory domain. Activity is modulated by UNC5B and NTN1.
CC       UNC5B activates it by inhibiting the phosphorylation at Ser-308,
CC       whereas NTN1 inhibits UNC5B-mediated activation of DAPK1. Endoplasmic-
CC       stress activates by causing Ser-308 dephosphorylation.
CC       {ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:18806755}.
CC   -!- SUBUNIT: Interacts with KLHL20 (By similarity). Interacts (via death
CC       domain) with MAPK1 and MAPK3 (By similarity). Interacts with MAP1B (via
CC       N-terminus) (By similarity). Interacts with PRKD1 in an oxidative
CC       stress-regulated manner (By similarity). Interacts with PIN1, PDCD6,
CC       BECN1, TSC2 and STX1A (By similarity). Interacts (via kinase domain)
CC       with DAPK3 (via kinase domain) (By similarity). Interacts with GRINB
CC       (PubMed:20141836). Interacts (via death domain) with UNC5B (via death
CC       domain) (PubMed:15729359). Interacts with UNC5C (via death domain) (By
CC       similarity). {ECO:0000250|UniProtKB:P53355,
CC       ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:20141836}.
CC   -!- INTERACTION:
CC       Q80YE7; Q01097: Grin2b; NbExp=8; IntAct=EBI-2584874, EBI-400125;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000305}; Synonyms=Beta;
CC         IsoId=Q80YE7-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305}; Synonyms=Alpha;
CC         IsoId=Q80YE7-2; Sequence=VSP_050629;
CC   -!- TISSUE SPECIFICITY: High levels in bladder, uterus, vas deferens, lung,
CC       liver and kidney. {ECO:0000269|PubMed:11485996}.
CC   -!- DOMAIN: The autoinhibitory domain sterically blocks the substrate
CC       peptide-binding site by making both hydrophobic and electrostatic
CC       contacts with the kinase core.
CC   -!- PTM: Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex,
CC       leading to its degradation by the proteasome. {ECO:0000250}.
CC   -!- PTM: In response to mitogenic stimulation (PMA or EGF), phosphorylated
CC       at Ser-289; phosphorylation suppresses DAPK1 pro-apoptotic function.
CC       Autophosphorylation at Ser-308 inhibits its catalytic activity.
CC       Phosphorylation at Ser-734 by MAPK1 increases its catalytic activity
CC       and promotes cytoplasmic retention of MAPK1. Endoplasmic-stress can
CC       cause dephosphorylation at Ser-308. {ECO:0000269|PubMed:15729359,
CC       ECO:0000269|PubMed:20141836}.
CC   -!- DISRUPTION PHENOTYPE: Mice are protected against cerebral ischemic
CC       neuronal death. {ECO:0000269|PubMed:20141836}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. DAP kinase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21490.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY245540; AAO91934.2; -; mRNA.
DR   EMBL; AY245541; AAO91935.1; -; mRNA.
DR   EMBL; X97048; CAA65762.1; -; mRNA.
DR   EMBL; BC021490; AAH21490.1; ALT_INIT; mRNA.
DR   EMBL; BC026671; AAH26671.1; -; mRNA.
DR   EMBL; BC057317; AAH57317.1; -; mRNA.
DR   EMBL; BC060161; AAH60161.1; -; mRNA.
DR   EMBL; AK013153; BAB28681.1; -; mRNA.
DR   CCDS; CCDS26581.1; -. [Q80YE7-2]
DR   CCDS; CCDS88466.1; -. [Q80YE7-1]
DR   RefSeq; NP_001272846.1; NM_001285917.1. [Q80YE7-1]
DR   RefSeq; NP_083929.2; NM_029653.3. [Q80YE7-2]
DR   RefSeq; NP_598823.1; NM_134062.2. [Q80YE7-2]
DR   RefSeq; XP_006517433.1; XM_006517370.3. [Q80YE7-1]
DR   AlphaFoldDB; Q80YE7; -.
DR   SMR; Q80YE7; -.
DR   BioGRID; 213581; 14.
DR   ComplexPortal; CPX-106; DAPK1 - calmodulin complex.
DR   IntAct; Q80YE7; 6.
DR   MINT; Q80YE7; -.
DR   STRING; 10090.ENSMUSP00000076666; -.
DR   GlyGen; Q80YE7; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q80YE7; -.
DR   PhosphoSitePlus; Q80YE7; -.
DR   MaxQB; Q80YE7; -.
DR   PaxDb; 10090-ENSMUSP00000076666; -.
DR   PeptideAtlas; Q80YE7; -.
DR   ProteomicsDB; 279165; -. [Q80YE7-1]
DR   ProteomicsDB; 279166; -. [Q80YE7-2]
DR   Pumba; Q80YE7; -.
DR   Antibodypedia; 6771; 496 antibodies from 37 providers.
DR   DNASU; 69635; -.
DR   Ensembl; ENSMUST00000044083.9; ENSMUSP00000040825.8; ENSMUSG00000021559.15. [Q80YE7-2]
DR   Ensembl; ENSMUST00000077453.13; ENSMUSP00000076666.6; ENSMUSG00000021559.15. [Q80YE7-2]
DR   Ensembl; ENSMUST00000226059.2; ENSMUSP00000153607.2; ENSMUSG00000021559.15. [Q80YE7-1]
DR   GeneID; 69635; -.
DR   KEGG; mmu:69635; -.
DR   UCSC; uc007qvm.2; mouse. [Q80YE7-1]
DR   AGR; MGI:1916885; -.
DR   CTD; 1612; -.
DR   MGI; MGI:1916885; Dapk1.
DR   VEuPathDB; HostDB:ENSMUSG00000021559; -.
DR   eggNOG; KOG0032; Eukaryota.
DR   GeneTree; ENSGT00940000153424; -.
DR   HOGENOM; CLU_002849_2_0_1; -.
DR   InParanoid; Q80YE7; -.
DR   OMA; RSMHDFQ; -.
DR   OrthoDB; 4580305at2759; -.
DR   PhylomeDB; Q80YE7; -.
DR   TreeFam; TF314166; -.
DR   BioGRID-ORCS; 69635; 1 hit in 81 CRISPR screens.
DR   ChiTaRS; Dapk1; mouse.
DR   PRO; PR:Q80YE7; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q80YE7; Protein.
DR   Bgee; ENSMUSG00000021559; Expressed in saccule of membranous labyrinth and 237 other cell types or tissues.
DR   ExpressionAtlas; Q80YE7; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:1990722; C:DAPK1-calmodulin complex; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; ISO:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0004672; F:protein kinase activity; IDA:MGI.
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:0017075; F:syntaxin-1 binding; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR   GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0071447; P:cellular response to hydroperoxide; ISO:MGI.
DR   GO; GO:0071346; P:cellular response to type II interferon; IMP:UniProtKB.
DR   GO; GO:0002357; P:defense response to tumor cell; ISO:MGI.
DR   GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:1904094; P:positive regulation of autophagic cell death; ISO:MGI.
DR   GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:UniProtKB.
DR   GO; GO:0002834; P:regulation of response to tumor cell; ISO:MGI.
DR   CDD; cd08782; Death_DAPK1; 1.
DR   CDD; cd14194; STKc_DAPK1; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 1.20.5.460; Single helix bin; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR020676; DAPK1_cat.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24342:SF17; DEATH-ASSOCIATED PROTEIN KINASE 1; 1.
DR   PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 9.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 7.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51424; ROC; 1.
DR   Genevisible; Q80YE7; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Apoptosis; ATP-binding;
KW   Calmodulin-binding; GTP-binding; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Translation regulation;
KW   Ubl conjugation.
FT   CHAIN           1..1442
FT                   /note="Death-associated protein kinase 1"
FT                   /id="PRO_0000085911"
FT   DOMAIN          13..275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REPEAT          378..407
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000305"
FT   REPEAT          411..440
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000305"
FT   REPEAT          444..473
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000305"
FT   REPEAT          477..506
FT                   /note="ANK 4"
FT                   /evidence="ECO:0000305"
FT   REPEAT          510..539
FT                   /note="ANK 5"
FT                   /evidence="ECO:0000305"
FT   REPEAT          543..572
FT                   /note="ANK 6"
FT                   /evidence="ECO:0000305"
FT   REPEAT          576..605
FT                   /note="ANK 7"
FT                   /evidence="ECO:0000305"
FT   REPEAT          609..638
FT                   /note="ANK 8"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          681..955
FT                   /note="Roc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT   REPEAT          875..904
FT                   /note="ANK 9"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1164..1196
FT                   /note="ANK 10"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          1312..1396
FT                   /note="Death"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT   REGION          267..334
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          292..301
FT                   /note="Autoinhibitory domain"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         19..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         289
FT                   /note="Phosphoserine; by RPS6KA1 and RPS6KA3"
FT                   /evidence="ECO:0000250|UniProtKB:P53355"
FT   MOD_RES         308
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:15729359,
FT                   ECO:0000269|PubMed:20141836"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53355"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         734
FT                   /note="Phosphoserine; by MAPK1"
FT                   /evidence="ECO:0000250|UniProtKB:P53355"
FT   MOD_RES         1115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1431..1442
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11485996,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|Ref.2"
FT                   /id="VSP_050629"
FT   CONFLICT        354
FT                   /note="D -> N (in Ref. 2; CAA65762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        441
FT                   /note="K -> Q (in Ref. 3; AAH57317/AAH60161)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        461
FT                   /note="V -> A (in Ref. 2; CAA65762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        960
FT                   /note="S -> P (in Ref. 2; CAA65762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1000
FT                   /note="N -> T (in Ref. 2; CAA65762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1038..1042
FT                   /note="RWLCT -> PMALH (in Ref. 2; CAA65762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1105
FT                   /note="A -> V (in Ref. 1; AAO91934/AAO91935)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1442 AA;  161442 MW;  243A14D7C6598F63 CRC64;
     MTVFRQENVD DYYDTGEELG SGQFAVVKKC REKSTGLQYA AKFIKKRRTK SSRRGVSRED
     IEREVSILKE IRHPNVITLH EVYENKTDVI LILELVAGGE LFDFLAEKES LTEEEATEFL
     KQILSGVYYL HSLQIAHFDL KPENIMLLDR NVPKPRIKII DFGLAHKIDF GNEFKNIFGT
     PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYDFEEEF
     FRNTSTLAKD FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA
     ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH AINDDNVPGL
     QHLLGSLSSY DVNQPNKHGT PPLLIAAGCG NIQMLQLLIK RGSRIDVQDK GGSNAIYWAS
     RHGHVDTLKF LNENKCPLDV KDKSGETALH VAARYGHADV VQLLCSFGSN PDFQDKEEET
     PLHCAAWHGY YSVAKALCEV GCNVNIKNRE GETPLLTASA RGYHDIVECL AEHGADLNAS
     DKDGHIALHL AVRRCQMEVI KTLLGHGSFV DFQDRHGNTP LHVACKDGSA PIVVALCEAS
     CNLDISNKYG RTPLHLAANN GILDVVRYLC LMGANVEALT SDGKTAEDLA KAEQHEHVAG
     LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK STLVESLKCG LLRSFFRRRR
     PRLSSTNSTR FPPSPLAAKP TVSVSINNLY PGCENVSVRS RSMMFEPGLT KGMLEVFVAP
     SHHLHCSTDD QSTKAIDIQN AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHIIVF
     SLEEPYEIQL NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL RVVLVATHAD IMNIPRPAGG
     EFGYDKDTSL LKEIRNRFGN DLHVSNKLFV LDAGASGSKD IKVLRNHLQE IRSQIVSGCS
     PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN PLASEDDLRR IAQQLHSTGE
     INIMQSETVQ DVLLLDPRWL CTNVLGKLLS VETPRALHHY RGRYTMEDIQ RLVPDSDVEE
     LLQILDAMDI CARDLSSGTM VDIPALIKTD SLQRSWADEE DEVMVYGGVR IVPVEHLTPF
     PCGIFHKVQV NLCRWIHQQS AEGDADIRLW VSGCRIANRG AELLVLLVNH GQGIEVQVRG
     LETEKIKCCL LLDSVCSTIE TVMATTLPGL LTVKHYLSPQ QLREHHEPVM VYQPRDFFRA
     QTLKESSLTN TMGGYKESFS SITCFGCHDV YSQASLGMDI HASDLSLLTR RKLSRLLDPP
     DPMGKDWCLL AMNLGLPDMV AKHNVNNRAS RDFLPSPVHA LLQEWTSYPE STVGILISKL
     RELGRRDAAD FLLKASSVFK INLDGNGQEA YASSCNSGTS YNSISSVVSR RDSHAWTPLY
     DL
//