DAPK1_MOUSE
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 03-AUG-2022, entry version 179.
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
RC Mammary gland {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};
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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 iPTMnet; Q80YE7; -.
DR PhosphoSitePlus; Q80YE7; -.
DR MaxQB; Q80YE7; -.
DR PaxDb; Q80YE7; -.
DR PeptideAtlas; Q80YE7; -.
DR PRIDE; Q80YE7; -.
DR ProteomicsDB; 279165; -. [Q80YE7-1]
DR ProteomicsDB; 279166; -. [Q80YE7-2]
DR Antibodypedia; 6771; 416 antibodies from 37 providers.
DR DNASU; 69635; -.
DR Ensembl; ENSMUST00000044083; ENSMUSP00000040825; ENSMUSG00000021559. [Q80YE7-2]
DR Ensembl; ENSMUST00000077453; ENSMUSP00000076666; ENSMUSG00000021559. [Q80YE7-2]
DR Ensembl; ENSMUST00000226059; ENSMUSP00000153607; ENSMUSG00000021559. [Q80YE7-1]
DR GeneID; 69635; -.
DR KEGG; mmu:69635; -.
DR UCSC; uc007qvm.2; mouse. [Q80YE7-1]
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 PhylomeDB; Q80YE7; -.
DR TreeFam; TF314166; -.
DR BioGRID-ORCS; 69635; 1 hit in 76 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 234 other tissues.
DR ExpressionAtlas; Q80YE7; baseline and differential.
DR Genevisible; Q80YE7; MM.
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:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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 interferon-gamma; 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:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; 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 Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR020676; DAPK1.
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; PTHR24342:SF17; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
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; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
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
