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Death-associated protein kinase 1 (DAP kinase 1) (EC 2.7.11.1)

 DAPK1_HUMAN             Reviewed;        1430 AA.
P53355; B7ZLD2; B7ZLE7; Q14CQ7; Q1W5W0; Q68CP8; Q6ZRZ3; Q9BTL8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 6.
22-NOV-2017, entry version 195.
RecName: Full=Death-associated protein kinase 1;
Short=DAP kinase 1;
EC=2.7.11.1;
Name=DAPK1; Synonyms=DAPK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION,
MUTAGENESIS OF LYS-42, AND VARIANT ASN-1346.
PubMed=7828849; DOI=10.1101/gad.9.1.15;
Deiss L.P., Feinstein E., Berissi H., Cohen O., Kimchi A.;
"Identification of a novel serine/threonine kinase and a novel 15-kD
protein as potential mediators of the gamma interferon-induced cell
death.";
Genes Dev. 9:15-30(1995).
[2]
SEQUENCE REVISION TO 164-171.
Feinstein E.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASN-1346.
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-591; MET-622;
ASN-1346 AND VAL-1405.
NIEHS SNPs program;
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-1346.
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-363.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10629061; DOI=10.1128/MCB.20.3.1044-1054.2000;
Inbal B., Shani G., Cohen O., Kissil J.L., Kimchi A.;
"Death-associated protein kinase-related protein 1, a novel
serine/threonine kinase involved in apoptosis.";
Mol. Cell. Biol. 20:1044-1054(2000).
[11]
FUNCTION, ENZYME REGULATION, MUTAGENESIS OF LYS-42; SER-308 AND
SER-313, AND PHOSPHORYLATION AT SER-308.
PubMed=11579085; DOI=10.1074/jbc.M105133200;
Shohat G., Spivak-Kroizman T., Cohen O., Bialik S., Shani G.,
Berissi H., Eisenstein M., Kimchi A.;
"The pro-apoptotic function of death-associated protein kinase is
controlled by a unique inhibitory autophosphorylation-based
mechanism.";
J. Biol. Chem. 276:47460-47467(2001).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11980920; DOI=10.1083/jcb.200109094;
Inbal B., Bialik S., Sabanay I., Shani G., Kimchi A.;
"DAP kinase and DRP-1 mediate membrane blebbing and the formation of
autophagic vesicles during programmed cell death.";
J. Cell Biol. 157:455-468(2002).
[13]
FUNCTION IN PHOSPHORYLATION OF STX1A, AND INTERACTION WITH STX1A.
PubMed=12730201; DOI=10.1074/jbc.M300492200;
Tian J.H., Das S., Sheng Z.H.;
"Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated
protein (DAP) kinase regulates its interaction with Munc18.";
J. Biol. Chem. 278:26265-26274(2003).
[14]
FUNCTION IN PHOSPHORYLATION OF DAPK3, AND INTERACTION WITH DAPK3.
PubMed=15367680; DOI=10.1128/MCB.24.19.8611-8626.2004;
Shani G., Marash L., Gozuacik D., Bialik S., Teitelbaum L., Shohat G.,
Kimchi A.;
"Death-associated protein kinase phosphorylates ZIP kinase, forming a
unique kinase hierarchy to activate its cell death functions.";
Mol. Cell. Biol. 24:8611-8626(2004).
[15]
INTERACTION WITH PDCD6.
PubMed=16132846; DOI=10.1007/s10529-005-7869-x;
Lee J.H., Rho S.B., Chun T.;
"Programmed cell death 6 (PDCD6) protein interacts with death-
associated protein kinase 1 (DAPk1): additive effect on apoptosis via
caspase-3 dependent pathway.";
Biotechnol. Lett. 27:1011-1015(2005).
[16]
PHOSPHORYLATION AT SER-289.
PubMed=16213824; DOI=10.1016/j.cub.2005.08.050;
Anjum R., Roux P.P., Ballif B.A., Gygi S.P., Blenis J.;
"The tumor suppressor DAP kinase is a target of RSK-mediated survival
signaling.";
Curr. Biol. 15:1762-1767(2005).
[17]
PHOSPHORYLATION AT SER-734, AND INTERACTION WITH MAPK1 AND MAPK3.
PubMed=15616583; DOI=10.1038/sj.emboj.7600510;
Chen C.H., Wang W.J., Kuo J.C., Tsai H.C., Lin J.R., Chang Z.F.,
Chen R.H.;
"Bidirectional signals transduced by DAPK-ERK interaction promote the
apoptotic effect of DAPK.";
EMBO J. 24:294-304(2005).
[18]
PHOSPHORYLATION AT SER-308, ENZYME REGULATION, AND INTERACTION WITH
UNC5B.
PubMed=15729359; DOI=10.1038/sj.emboj.7600584;
Llambi F., Lourenco F.C., Gozuacik D., Guix C., Pays L., Del Rio G.,
Kimchi A., Mehlen P.;
"The dependence receptor UNC5H2 mediates apoptosis through DAP-
kinase.";
EMBO J. 24:1192-1201(2005).
[19]
REVIEW ON FUNCTION.
PubMed=16756490; DOI=10.1146/annurev.biochem.75.103004.142615;
Bialik S., Kimchi A.;
"The death-associated protein kinases: structure, function, and
beyond.";
Annu. Rev. Biochem. 75:189-210(2006).
[20]
ALTERNATIVE SPLICING (ISOFORM 3), PHOSPHORYLATION AT SER-308,
DEPHOSPHORYLATION, AND ENZYME REGULATION.
PubMed=17056602; DOI=10.1074/jbc.M605097200;
Jin Y., Blue E.K., Gallagher P.J.;
"Control of death-associated protein kinase (DAPK) activity by
phosphorylation and proteasomal degradation.";
J. Biol. Chem. 281:39033-39040(2006).
[21]
FUNCTION IN PHOSPHORYLATION OF PRKD1, AND INTERACTION WITH PRKD1.
PubMed=17703233; DOI=10.1038/sj.cdd.4402212;
Eisenberg-Lerner A., Kimchi A.;
"DAP kinase regulates JNK signaling by binding and activating protein
kinase D under oxidative stress.";
Cell Death Differ. 14:1908-1915(2007).
[22]
FUNCTION IN PHOSPHORYLATION OF TPM1.
PubMed=17895359; DOI=10.1242/jcs.003251;
Houle F., Poirier A., Dumaresq J., Huot J.;
"DAP kinase mediates the phosphorylation of tropomyosin-1 downstream
of the ERK pathway, which regulates the formation of stress fibers in
response to oxidative stress.";
J. Cell Sci. 120:3666-3677(2007).
[23]
ALTERNATIVE SPLICING (ISOFORM 2), PROTEOLYTIC PROCESSING, FUNCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18422656; DOI=10.1111/j.1742-4658.2008.06404.x;
Lin Y., Stevens C., Hrstka R., Harrison B., Fourtouna A., Pathuri S.,
Vojtesek B., Hupp T.;
"An alternative transcript from the death-associated protein kinase 1
locus encoding a small protein selectively mediates membrane
blebbing.";
FEBS J. 275:2574-2584(2008).
[24]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAP1B.
PubMed=18195017; DOI=10.1074/jbc.M706040200;
Harrison B., Kraus M., Burch L., Stevens C., Craig A.,
Gordon-Weeks P., Hupp T.R.;
"DAPK-1 binding to a linear peptide motif in MAP1B stimulates
autophagy and membrane blebbing.";
J. Biol. Chem. 283:9999-10014(2008).
[25]
FUNCTION.
PubMed=18995835; DOI=10.1016/j.molcel.2008.09.019;
Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L.;
"DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating
inflammatory gene expression.";
Mol. Cell 32:371-382(2008).
[26]
FUNCTION IN PHOSPHORYLATION OF BECN1, AND INTERACTION WITH BECN1.
PubMed=19180116; DOI=10.1038/embor.2008.246;
Zalckvar E., Berissi H., Mizrachy L., Idelchuk Y., Koren I.,
Eisenstein M., Sabanay H., Pinkas-Kramarski R., Kimchi A.;
"DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1
promotes dissociation of beclin 1 from Bcl-XL and induction of
autophagy.";
EMBO Rep. 10:285-292(2009).
[27]
FUNCTION IN PHOSPHORYLATION OF TSC2 AND RPS6, AND INTERACTION WITH
TSC2.
PubMed=18974095; DOI=10.1074/jbc.M805165200;
Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O.,
Hupp T.;
"Peptide combinatorial libraries identify TSC2 as a death-associated
protein kinase (DAPK) death domain-binding protein and reveal a
stimulatory role for DAPK in mTORC1 signaling.";
J. Biol. Chem. 284:334-344(2009).
[28]
UBIQUITINATION, AND INTERACTION WITH KLHL20.
PubMed=20389280; DOI=10.1038/emboj.2010.62;
Lee Y.R., Yuan W.C., Ho H.C., Chen C.H., Shih H.M., Chen R.H.;
"The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to
control interferon responses.";
EMBO J. 29:1748-1761(2010).
[29]
REVIEW ON FUNCTION.
PubMed=19878313; DOI=10.1111/j.1742-4658.2009.07411.x;
Lin Y., Hupp T.R., Stevens C.;
"Death-associated protein kinase (DAPK) and signal transduction:
additional roles beyond cell death.";
FEBS J. 277:48-57(2010).
[30]
FUNCTION IN PHOSPHORYLATION OF PIN1, AND INTERACTION WITH PIN1.
PubMed=21497122; DOI=10.1016/j.molcel.2011.03.005;
Lee T.H., Chen C.H., Suizu F., Huang P., Schiene-Fischer C., Daum S.,
Zhang Y.J., Goate A., Chen R.H., Zhou X.Z., Lu K.P.;
"Death-associated protein kinase 1 phosphorylates Pin1 and inhibits
its prolyl isomerase activity and cellular function.";
Mol. Cell 42:147-159(2011).
[31]
FUNCTION.
PubMed=21408167; DOI=10.1371/journal.pone.0017344;
Shoval Y., Berissi H., Kimchi A., Pietrokovski S.;
"New modularity of DAP-kinases: alternative splicing of the DRP-1 gene
produces a ZIPk-like isoform.";
PLoS ONE 6:E17344-E17344(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-285 IN COMPLEX WITH ATP
ANALOG AND DIVALENT METAL CATION.
PubMed=11573098; DOI=10.1038/nsb1001-899;
Tereshko V., Teplova M., Brunzelle J., Watterson D.M., Egli M.;
"Crystal structures of the catalytic domain of human protein kinase
associated with apoptosis and tumor suppression.";
Nat. Struct. Biol. 8:899-907(2001).
[36]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-285 IN COMPLEX WITH
SYNTHETIC INHIBITOR.
PubMed=14505650; DOI=10.1016/S0960-894X(03)00733-9;
Velentza A.V., Wainwright M.S., Zasadzki M., Mirzoeva S.,
Schumacher A.M., Haiech J., Focia P.J., Egli M., Watterson D.M.;
"An aminopyridazine-based inhibitor of a pro-apoptotic protein kinase
attenuates hypoxia-ischemia induced acute brain injury.";
Bioorg. Med. Chem. Lett. 13:3465-3470(2003).
[37]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-278 IN COMPLEX WITH
INHIBITORS.
Ueda Y., Ogata H., Yamakawa A., Higuchi Y.;
"Complex structure of kinase domain of DAP kinase with
staurosporine.";
Submitted (APR-2006) to the PDB data bank.
[38]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 302-320 IN COMPLEX WITH
CALMODULIN.
Kursula P., Vahokoski J., Wilmanns M.;
"Recognition of human death-associated protein kinases by
calmodulin.";
Submitted (JUL-2006) to the PDB data bank.
[39]
VARIANTS [LARGE SCALE ANALYSIS] ILE-416; SER-461; ALA-519; TYR-540;
THR-941; TRP-977; ASN-978; CYS-993; GLU-994; GLN-1005; TYR-1007;
PRO-1008; CYS-1010; ALA-1018; ILE-1272; ASN-1346 AND VAL-1405.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Calcium/calmodulin-dependent serine/threonine kinase
involved in multiple cellular signaling pathways that trigger cell
survival, apoptosis, and autophagy. Regulates both type I
apoptotic and type II autophagic cell deaths signal, depending on
the cellular setting. The former is caspase-dependent, while the
latter is caspase-independent and is characterized by the
accumulation of autophagic vesicles. Phosphorylates PIN1 resulting
in inhibition of its catalytic activity, nuclear localization, and
cellular function. Phosphorylates TPM1, enhancing stress fiber
formation in endothelial cells. Phosphorylates STX1A and
significantly decreases its binding to STXBP1. Phosphorylates
PRKD1 and regulates JNK signaling by binding and activating PRKD1
under oxidative stress. Phosphorylates BECN1, reducing its
interaction with BCL2 and BCL2L1 and promoting the induction of
autophagy. Phosphorylates TSC2, disrupting the TSC1-TSC2 complex
and stimulating mTORC1 activity in a growth factor-dependent
pathway. Phosphorylates RPS6, MYL9 and DAPK3. Acts as a signaling
amplifier of NMDA receptors at extrasynaptic sites for mediating
brain damage in stroke. Cerebral ischemia recruits DAPK1 into the
NMDA receptor complex and it phosphorylates GRINB at Ser-1303
inducing injurious Ca(2+) influx through NMDA receptor channels,
resulting in an irreversible neuronal death. Required together
with DAPK3 for phosphorylation of RPL13A upon interferon-gamma
activation which is causing RPL13A involvement in transcript-
selective translation inhibition.
-!- FUNCTION: Isoform 2 cannot induce apoptosis but can induce
membrane blebbing.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Regulated by a
locking mechanism, involving autophosphorylation at Ser-308 and
calmodulin binding. In the inactive state, Ser-308 is
phosphorylated. Activation involves its dephosphorylation and a
release-of-autoinhibition mechanism where binding of calmodulin
induces a conformational change that relieves the steric block of
the active site by the autoinhibitory domain. Activity is
modulated by UNC5B and NTN1. UNC5B activates it by inhibiting the
phosphorylation at Ser-308, whereas NTN1 inhibits UNC5B-mediated
activation of DAPK1. Endoplasmic-stress activates by causing Ser-
308 dephosphorylation. {ECO:0000269|PubMed:11579085,
ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:17056602}.
-!- SUBUNIT: Interacts with KLHL20. Interacts (via death domain) with
MAPK1 and MAPK3. Interacts with MAP1B (via N-terminus). Interacts
(via death domain) with UNC5B (via death domain). Interacts with
PRKD1 in an oxidative stress-regulated manner. Interacts with
PIN1, PDCD6, BECN1, GRINB, TSC2 and STX1A. Interacts (via kinase
domain) with DAPK3 (via kinase domain).
{ECO:0000269|PubMed:11573098, ECO:0000269|PubMed:12730201,
ECO:0000269|PubMed:14505650, ECO:0000269|PubMed:15367680,
ECO:0000269|PubMed:15616583, ECO:0000269|PubMed:15729359,
ECO:0000269|PubMed:16132846, ECO:0000269|PubMed:17703233,
ECO:0000269|PubMed:18195017, ECO:0000269|PubMed:18974095,
ECO:0000269|PubMed:19180116, ECO:0000269|PubMed:20389280,
ECO:0000269|PubMed:21497122, ECO:0000269|Ref.37,
ECO:0000269|Ref.38}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-358616, EBI-358616;
Q14457:BECN1; NbExp=4; IntAct=EBI-358616, EBI-949378;
P62158:CALM3; NbExp=6; IntAct=EBI-358616, EBI-397435;
Q9Y2M5:KLHL20; NbExp=11; IntAct=EBI-358616, EBI-714379;
Q38SD2:LRRK1; NbExp=2; IntAct=EBI-358616, EBI-1050422;
Q5S007:LRRK2; NbExp=2; IntAct=EBI-358616, EBI-5323863;
P27361:MAPK3; NbExp=5; IntAct=EBI-358616, EBI-73995;
O75340:PDCD6; NbExp=3; IntAct=EBI-358616, EBI-352915;
P14618:PKM; NbExp=3; IntAct=EBI-358616, EBI-353408;
P14618-1:PKM; NbExp=2; IntAct=EBI-358616, EBI-4304679;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cytoplasm,
cytoskeleton. Note=Colocalizes with MAP1B in the microtubules and
cortical actin fibers.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Cytoplasm,
cytoskeleton.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Alpha;
IsoId=P53355-1; Sequence=Displayed;
Name=2; Synonyms=s-DAPK-1;
IsoId=P53355-2; Sequence=VSP_042053, VSP_042054, VSP_042055;
Name=3; Synonyms=Beta;
IsoId=P53355-3; Sequence=VSP_042056;
Name=4;
IsoId=P53355-4; Sequence=VSP_054478;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 2 is expressed in normal intestinal
tissue as well as in colorectal carcinomas.
{ECO:0000269|PubMed:18422656}.
-!- INDUCTION: Up-regulated following treatment with IFNG/IFN-gamma.
{ECO:0000269|PubMed:7828849}.
-!- DOMAIN: The autoinhibitory domain sterically blocks the substrate
peptide-binding site by making both hydrophobic and electrostatic
contacts with the kinase core.
-!- PTM: Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex,
leading to its degradation by the proteasome.
{ECO:0000269|PubMed:20389280}.
-!- PTM: Removal of the C-terminal tail of isoform 2 (corresponding to
amino acids 296-337 of isoform 2) by proteolytic cleavage
stimulates maximally its membrane-blebbing function.
{ECO:0000269|PubMed:18422656}.
-!- PTM: In response to mitogenic stimulation (PMA or EGF),
phosphorylated at Ser-289; phosphorylation suppresses DAPK1 pro-
apoptotic function. Autophosphorylation at Ser-308 inhibits its
catalytic activity. Phosphorylation at Ser-734 by MAPK1 increases
its catalytic activity and promotes cytoplasmic retention of
MAPK1. Endoplasmic-stress can cause dephosphorylation at Ser-308.
{ECO:0000269|PubMed:11579085, ECO:0000269|PubMed:15616583,
ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:16213824,
ECO:0000269|PubMed:17056602}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. DAP kinase subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAP35581.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
Sequence=CAA53712.1; Type=Frameshift; Positions=462, 464; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/dapk1/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DAPK1ID417ch9q21.html";
-----------------------------------------------------------------------
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EMBL; X76104; CAA53712.1; ALT_FRAME; mRNA.
EMBL; AK127855; BAC87163.1; -; mRNA.
EMBL; CR749834; CAH18690.1; -; mRNA.
EMBL; DQ436495; ABD96827.1; -; Genomic_DNA.
EMBL; AL160279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL161787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL591852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471089; EAW62727.1; -; Genomic_DNA.
EMBL; BC113660; AAI13661.1; -; mRNA.
EMBL; BC143733; AAI43734.1; -; mRNA.
EMBL; BC143759; AAI43760.1; -; mRNA.
EMBL; BT006935; AAP35581.1; ALT_SEQ; mRNA.
CCDS; CCDS43842.1; -. [P53355-1]
PIR; I37275; I37275.
RefSeq; NP_001275658.1; NM_001288729.1. [P53355-1]
RefSeq; NP_001275659.1; NM_001288730.1. [P53355-1]
RefSeq; NP_001275660.1; NM_001288731.1. [P53355-1]
RefSeq; NP_004929.2; NM_004938.3. [P53355-1]
UniGene; Hs.380277; -.
UniGene; Hs.693441; -.
PDB; 1IG1; X-ray; 1.80 A; A=2-285.
PDB; 1JKK; X-ray; 2.40 A; A=2-285.
PDB; 1JKL; X-ray; 1.62 A; A=2-285.
PDB; 1JKS; X-ray; 1.50 A; A=2-285.
PDB; 1JKT; X-ray; 3.50 A; A/B=2-285.
PDB; 1P4F; X-ray; 1.90 A; A=2-285.
PDB; 1WVW; X-ray; 2.40 A; A=1-278.
PDB; 1WVX; X-ray; 2.60 A; A=1-278.
PDB; 1WVY; X-ray; 2.80 A; A=1-278.
PDB; 1YR5; X-ray; 1.70 A; B=302-320.
PDB; 2W4J; X-ray; 1.30 A; A=1-277.
PDB; 2W4K; X-ray; 1.90 A; A=1-302.
PDB; 2X0G; X-ray; 2.20 A; A=1-334.
PDB; 2XUU; X-ray; 1.80 A; A=1-334.
PDB; 2XZS; X-ray; 2.00 A; A/B=2-312.
PDB; 2Y0A; X-ray; 2.60 A; A=2-304.
PDB; 2Y4P; X-ray; 2.65 A; A/B/C/D=1-285.
PDB; 2Y4V; X-ray; 1.80 A; B=302-320.
PDB; 2YAK; X-ray; 2.20 A; A=1-285.
PDB; 3DFC; X-ray; 1.90 A; B=1-285.
PDB; 3DGK; X-ray; 1.70 A; A=1-285.
PDB; 3EH9; X-ray; 1.70 A; A=2-285.
PDB; 3EHA; X-ray; 1.60 A; A=2-285.
PDB; 3F5G; X-ray; 1.85 A; A=2-285.
PDB; 3F5U; X-ray; 2.00 A; A=1-285.
PDB; 3GU4; X-ray; 1.35 A; A=1-285.
PDB; 3GU5; X-ray; 1.65 A; A=1-285.
PDB; 3GU6; X-ray; 1.49 A; A=1-285.
PDB; 3GU7; X-ray; 1.90 A; A=1-285.
PDB; 3GU8; X-ray; 1.60 A; A=1-285.
PDB; 3GUB; X-ray; 1.71 A; A=1-285.
PDB; 3ZXT; X-ray; 2.65 A; A/B/C/D=1-285.
PDB; 4B4L; X-ray; 1.75 A; A=1-334.
PDB; 4PF4; X-ray; 1.13 A; A=1-277.
PDB; 4TL0; X-ray; 2.70 A; A=1-334.
PDB; 4TXC; X-ray; 1.95 A; A=1-285.
PDB; 4UV0; X-ray; 2.49 A; A=1-321.
PDB; 4YO4; X-ray; 1.60 A; A=2-285.
PDB; 4YPD; X-ray; 1.40 A; A=2-285.
PDB; 5AUT; X-ray; 1.70 A; A=1-285.
PDB; 5AUU; X-ray; 1.70 A; A=1-285.
PDB; 5AUV; X-ray; 1.50 A; A=1-285.
PDB; 5AUW; X-ray; 1.50 A; A=1-285.
PDB; 5AUX; X-ray; 1.50 A; A=1-285.
PDB; 5AUY; X-ray; 2.00 A; A=1-285.
PDB; 5AUZ; X-ray; 1.60 A; A=1-285.
PDB; 5AV0; X-ray; 1.85 A; A=1-285.
PDB; 5AV1; X-ray; 1.50 A; A=1-285.
PDB; 5AV2; X-ray; 1.50 A; A=1-285.
PDB; 5AV3; X-ray; 1.90 A; A=1-285.
PDB; 5AV4; X-ray; 1.40 A; A=1-285.
PDBsum; 1IG1; -.
PDBsum; 1JKK; -.
PDBsum; 1JKL; -.
PDBsum; 1JKS; -.
PDBsum; 1JKT; -.
PDBsum; 1P4F; -.
PDBsum; 1WVW; -.
PDBsum; 1WVX; -.
PDBsum; 1WVY; -.
PDBsum; 1YR5; -.
PDBsum; 2W4J; -.
PDBsum; 2W4K; -.
PDBsum; 2X0G; -.
PDBsum; 2XUU; -.
PDBsum; 2XZS; -.
PDBsum; 2Y0A; -.
PDBsum; 2Y4P; -.
PDBsum; 2Y4V; -.
PDBsum; 2YAK; -.
PDBsum; 3DFC; -.
PDBsum; 3DGK; -.
PDBsum; 3EH9; -.
PDBsum; 3EHA; -.
PDBsum; 3F5G; -.
PDBsum; 3F5U; -.
PDBsum; 3GU4; -.
PDBsum; 3GU5; -.
PDBsum; 3GU6; -.
PDBsum; 3GU7; -.
PDBsum; 3GU8; -.
PDBsum; 3GUB; -.
PDBsum; 3ZXT; -.
PDBsum; 4B4L; -.
PDBsum; 4PF4; -.
PDBsum; 4TL0; -.
PDBsum; 4TXC; -.
PDBsum; 4UV0; -.
PDBsum; 4YO4; -.
PDBsum; 4YPD; -.
PDBsum; 5AUT; -.
PDBsum; 5AUU; -.
PDBsum; 5AUV; -.
PDBsum; 5AUW; -.
PDBsum; 5AUX; -.
PDBsum; 5AUY; -.
PDBsum; 5AUZ; -.
PDBsum; 5AV0; -.
PDBsum; 5AV1; -.
PDBsum; 5AV2; -.
PDBsum; 5AV3; -.
PDBsum; 5AV4; -.
ProteinModelPortal; P53355; -.
SMR; P53355; -.
BioGrid; 107982; 51.
IntAct; P53355; 33.
MINT; MINT-1136108; -.
STRING; 9606.ENSP00000350785; -.
BindingDB; P53355; -.
ChEMBL; CHEMBL2558; -.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
GuidetoPHARMACOLOGY; 2002; -.
iPTMnet; P53355; -.
PhosphoSitePlus; P53355; -.
BioMuta; DAPK1; -.
DMDM; 317373595; -.
EPD; P53355; -.
MaxQB; P53355; -.
PaxDb; P53355; -.
PeptideAtlas; P53355; -.
PRIDE; P53355; -.
DNASU; 1612; -.
Ensembl; ENST00000358077; ENSP00000350785; ENSG00000196730. [P53355-1]
Ensembl; ENST00000408954; ENSP00000386135; ENSG00000196730. [P53355-1]
Ensembl; ENST00000469640; ENSP00000418885; ENSG00000196730. [P53355-4]
Ensembl; ENST00000472284; ENSP00000417076; ENSG00000196730. [P53355-1]
Ensembl; ENST00000491893; ENSP00000419026; ENSG00000196730. [P53355-4]
Ensembl; ENST00000622514; ENSP00000484267; ENSG00000196730. [P53355-1]
GeneID; 1612; -.
KEGG; hsa:1612; -.
UCSC; uc004apc.5; human. [P53355-1]
CTD; 1612; -.
DisGeNET; 1612; -.
EuPathDB; HostDB:ENSG00000196730.12; -.
GeneCards; DAPK1; -.
HGNC; HGNC:2674; DAPK1.
HPA; CAB037302; -.
HPA; HPA040472; -.
HPA; HPA048436; -.
MIM; 600831; gene.
neXtProt; NX_P53355; -.
OpenTargets; ENSG00000196730; -.
PharmGKB; PA27142; -.
eggNOG; KOG0032; Eukaryota.
eggNOG; ENOG410XRMJ; LUCA.
GeneTree; ENSGT00760000118877; -.
HOGENOM; HOG000082489; -.
HOVERGEN; HBG051296; -.
InParanoid; P53355; -.
KO; K08803; -.
OMA; CQMEVIK; -.
OrthoDB; EOG091G0J2O; -.
PhylomeDB; P53355; -.
TreeFam; TF314166; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-418889; Ligand-independent caspase activation via DCC.
SignaLink; P53355; -.
SIGNOR; P53355; -.
ChiTaRS; DAPK1; human.
EvolutionaryTrace; P53355; -.
GeneWiki; DAPK1; -.
GenomeRNAi; 1612; -.
PRO; PR:P53355; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000196730; -.
CleanEx; HS_DAPK1; -.
ExpressionAtlas; P53355; baseline and differential.
Genevisible; P53355; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:UniProtKB.
GO; GO:0017075; F:syntaxin-1 binding; IPI:UniProtKB.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0071447; P:cellular response to hydroperoxide; IMP:ParkinsonsUK-UCL.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; TAS:UniProtKB.
GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:UniProtKB.
CDD; cd00204; ANK; 3.
Gene3D; 1.25.40.20; -; 4.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR020676; DAPK1.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR020859; ROC_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR44619; PTHR44619; 1.
Pfam; PF12796; Ank_2; 2.
Pfam; PF00531; Death; 1.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 9.
SMART; SM00005; DEATH; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 7.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS51424; ROC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; Apoptosis;
ATP-binding; Calmodulin-binding; Complete proteome; Cytoplasm;
Cytoskeleton; GTP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Translation regulation;
Ubl conjugation.
CHAIN 1 1430 Death-associated protein kinase 1.
/FTId=PRO_0000085910.
DOMAIN 13 275 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REPEAT 378 407 ANK 1.
REPEAT 411 440 ANK 2.
REPEAT 444 473 ANK 3.
REPEAT 477 506 ANK 4.
REPEAT 510 539 ANK 5.
REPEAT 543 572 ANK 6.
REPEAT 576 605 ANK 7.
REPEAT 609 638 ANK 8.
DOMAIN 681 955 Roc. {ECO:0000255|PROSITE-
ProRule:PRU00758}.
REPEAT 875 904 ANK 9.
REPEAT 1162 1196 ANK 10.
DOMAIN 1312 1396 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
NP_BIND 19 27 ATP.
NP_BIND 94 96 ATP.
REGION 267 334 Calmodulin-binding.
REGION 292 301 Autoinhibitory domain. {ECO:0000250}.
ACT_SITE 139 139 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 42 42 ATP.
BINDING 100 100 ATP.
BINDING 161 161 ATP.
MOD_RES 289 289 Phosphoserine; by RPS6KA1 and RPS6KA3.
{ECO:0000269|PubMed:16213824}.
MOD_RES 308 308 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:11579085,
ECO:0000269|PubMed:15729359,
ECO:0000269|PubMed:17056602}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 734 734 Phosphoserine; by MAPK1.
{ECO:0000269|PubMed:15616583}.
MOD_RES 1115 1115 Phosphoserine.
{ECO:0000250|UniProtKB:Q80YE7}.
VAR_SEQ 1 446 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042053.
VAR_SEQ 742 783 VSVSINNLYPGCENVSVRSRSMMFEPGLTKGMLEVFVAPTH
H -> GRNLHAGPVSPAGVGFRTLSFQGLGGKGVVFGSLGL
YWTLWP (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042054.
VAR_SEQ 784 1430 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042055.
VAR_SEQ 805 870 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054478.
VAR_SEQ 1430 1430 R -> RRNSHVWNPTV (in isoform 3).
{ECO:0000305}.
/FTId=VSP_042056.
VARIANT 416 416 V -> I (in dbSNP:rs12343465).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_033235.
VARIANT 461 461 A -> S. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040420.
VARIANT 519 519 S -> A. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040421.
VARIANT 540 540 C -> Y (in dbSNP:rs56327474).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040422.
VARIANT 591 591 P -> L (in dbSNP:rs36214022).
{ECO:0000269|Ref.5}.
/FTId=VAR_060693.
VARIANT 622 622 I -> M (in dbSNP:rs36215047).
{ECO:0000269|Ref.5}.
/FTId=VAR_060694.
VARIANT 941 941 M -> T. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040423.
VARIANT 977 977 R -> W. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040424.
VARIANT 978 978 K -> N. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040425.
VARIANT 993 993 Y -> C. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040426.
VARIANT 994 994 D -> E. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040427.
VARIANT 1005 1005 E -> Q. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040428.
VARIANT 1007 1007 D -> Y. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040429.
VARIANT 1008 1008 L -> P. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040430.
VARIANT 1010 1010 R -> C (in dbSNP:rs371784492).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040431.
VARIANT 1018 1018 T -> A. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040432.
VARIANT 1272 1272 M -> I (in dbSNP:rs56169226).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040433.
VARIANT 1346 1346 S -> N (in dbSNP:rs1056719).
{ECO:0000269|PubMed:15164053,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:7828849,
ECO:0000269|Ref.5}.
/FTId=VAR_040434.
VARIANT 1405 1405 G -> V (in dbSNP:rs36220450).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.5}.
/FTId=VAR_040435.
MUTAGEN 42 42 K->A: Loss of activity, apoptotic
function and of autophosphorylation.
{ECO:0000269|PubMed:11579085,
ECO:0000269|PubMed:7828849}.
MUTAGEN 289 289 S->A: Loss of phosphorylation and
significant increase in proapoptotic
activity.
MUTAGEN 289 289 S->E: Reduction in proapoptotic activity.
MUTAGEN 308 308 S->A: Elevated Ca(2+)-calmodulin binding
and Ca(2+)-calmodulin-independent kinase
activity. Increases apoptotic activity.
{ECO:0000269|PubMed:11579085}.
MUTAGEN 308 308 S->D: Reduced Ca(2+)-calmodulin binding
and Ca(2+)-calmodulin-independent kinase
activity. Decreases apoptotic activity.
{ECO:0000269|PubMed:11579085}.
MUTAGEN 313 313 S->A: Minimal effect on activity.
{ECO:0000269|PubMed:11579085}.
CONFLICT 490 490 Y -> H (in Ref. 3; BAC87163).
{ECO:0000305}.
CONFLICT 1217 1217 S -> G (in Ref. 4; CAH18690).
{ECO:0000305}.
HELIX 9 11 {ECO:0000244|PDB:4PF4}.
STRAND 13 21 {ECO:0000244|PDB:4PF4}.
STRAND 23 32 {ECO:0000244|PDB:4PF4}.
TURN 33 35 {ECO:0000244|PDB:4PF4}.
STRAND 38 46 {ECO:0000244|PDB:4PF4}.
STRAND 48 51 {ECO:0000244|PDB:2W4J}.
STRAND 53 56 {ECO:0000244|PDB:4PF4}.
HELIX 58 70 {ECO:0000244|PDB:4PF4}.
STRAND 79 84 {ECO:0000244|PDB:4PF4}.
STRAND 86 94 {ECO:0000244|PDB:4PF4}.
HELIX 101 107 {ECO:0000244|PDB:4PF4}.
STRAND 108 110 {ECO:0000244|PDB:3ZXT}.
HELIX 113 132 {ECO:0000244|PDB:4PF4}.
STRAND 134 136 {ECO:0000244|PDB:1JKT}.
HELIX 142 144 {ECO:0000244|PDB:4PF4}.
STRAND 145 148 {ECO:0000244|PDB:4PF4}.
STRAND 150 154 {ECO:0000244|PDB:4PF4}.
STRAND 157 159 {ECO:0000244|PDB:4PF4}.
HELIX 162 164 {ECO:0000244|PDB:4UV0}.
STRAND 169 171 {ECO:0000244|PDB:2W4J}.
HELIX 181 183 {ECO:0000244|PDB:4PF4}.
HELIX 186 189 {ECO:0000244|PDB:4PF4}.
HELIX 197 212 {ECO:0000244|PDB:4PF4}.
HELIX 222 230 {ECO:0000244|PDB:4PF4}.
HELIX 238 241 {ECO:0000244|PDB:4PF4}.
STRAND 242 244 {ECO:0000244|PDB:1P4F}.
HELIX 246 255 {ECO:0000244|PDB:4PF4}.
TURN 260 262 {ECO:0000244|PDB:4PF4}.
HELIX 266 271 {ECO:0000244|PDB:4PF4}.
TURN 273 275 {ECO:0000244|PDB:4PF4}.
HELIX 280 288 {ECO:0000244|PDB:4B4L}.
HELIX 293 302 {ECO:0000244|PDB:4B4L}.
HELIX 304 318 {ECO:0000244|PDB:1YR5}.
SEQUENCE 1430 AA; 160046 MW; E2C4246E7C78A6D2 CRC64;
MTVFRQENVD DYYDTGEELG SGQFAVVKKC REKSTGLQYA AKFIKKRRTK SSRRGVSRED
IEREVSILKE IQHPNVITLH EVYENKTDVI LILELVAGGE LFDFLAEKES LTEEEATEFL
KQILNGVYYL HSLQIAHFDL KPENIMLLDR NVPKPRIKII DFGLAHKIDF GNEFKNIFGT
PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYEFEDEY
FSNTSALAKD FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA
ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH AINDDNVPGL
QHLLGSLSNY DVNQPNKHGT PPLLIAAGCG NIQILQLLIK RGSRIDVQDK GGSNAVYWAA
RHGHVDTLKF LSENKCPLDV KDKSGEMALH VAARYGHADV AQLLCSFGSN PNIQDKEEET
PLHCAAWHGY YSVAKALCEA GCNVNIKNRE GETPLLTASA RGYHDIVECL AEHGADLNAC
DKDGHIALHL AVRRCQMEVI KTLLSQGCFV DYQDRHGNTP LHVACKDGNM PIVVALCEAN
CNLDISNKYG RTPLHLAANN GILDVVRYLC LMGASVEALT TDGKTAEDLA RSEQHEHVAG
LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK TTLVESLKCG LLRSFFRRRR
PRLSSTNSSR FPPSPLASKP TVSVSINNLY PGCENVSVRS RSMMFEPGLT KGMLEVFVAP
THHPHCSADD QSTKAIDIQN AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHVVVF
SLEEPYEIQL NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL QVVLVATHAD IMNVPRPAGG
EFGYDKDTSL LKEIRNRFGN DLHISNKLFV LDAGASGSKD MKVLRNHLQE IRSQIVSVCP
PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN PLASEEDLRR IAQQLHSTGE
INIMQSETVQ DVLLLDPRWL CTNVLGKLLS VETPRALHHY RGRYTVEDIQ RLVPDSDVEE
LLQILDAMDI CARDLSSGTM VDVPALIKTD NLHRSWADEE DEVMVYGGVR IVPVEHLTPF
PCGIFHKVQV NLCRWIHQQS TEGDADIRLW VNGCKLANRG AELLVLLVNH GQGIEVQVRG
LETEKIKCCL LLDSVCSTIE NVMATTLPGL LTVKHYLSPQ QLREHHEPVM IYQPRDFFRA
QTLKETSLTN TMGGYKESFS SIMCFGCHDV YSQASLGMDI HASDLNLLTR RKLSRLLDPP
DPLGKDWCLL AMNLGLPDLV AKYNTSNGAP KDFLPSPLHA LLREWTTYPE STVGTLMSKL
RELGRRDAAD FLLKASSVFK INLDGNGQEA YASSCNSGTS YNSISSVVSR


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