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P53355

- DAPK1_HUMAN

UniProt

P53355 - DAPK1_HUMAN

Protein

Death-associated protein kinase 1

Gene

DAPK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 6 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    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 Ca2+ 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.
    Isoform 2 cannot induce apoptosis but can induce membrane blebbing.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by Ca2+/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.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei42 – 421ATP
    Binding sitei100 – 1001ATP
    Active sitei139 – 1391Proton acceptorPROSITE-ProRule annotation
    Binding sitei161 – 1611ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 279ATP
    Nucleotide bindingi94 – 963ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. calmodulin binding Source: UniProtKB
    3. calmodulin-dependent protein kinase activity Source: UniProtKB
    4. identical protein binding Source: IntAct
    5. protein binding Source: UniProtKB
    6. protein kinase activity Source: MGI
    7. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. apoptotic signaling pathway Source: UniProtKB
    3. cellular response to interferon-gamma Source: UniProtKB
    4. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    5. intracellular signal transduction Source: UniProtKB
    6. negative regulation of apoptotic process Source: Ensembl
    7. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    8. negative regulation of translation Source: UniProtKB
    9. positive regulation of apoptotic process Source: Reactome
    10. protein autophosphorylation Source: UniProtKB
    11. protein phosphorylation Source: UniProtKB
    12. regulation of apoptotic process Source: UniProtKB
    13. regulation of autophagy Source: UniProtKB
    14. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Translation regulation

    Keywords - Ligandi

    ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_22128. Role of DCC in regulating apoptosis.
    SignaLinkiP53355.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Death-associated protein kinase 1 (EC:2.7.11.1)
    Short name:
    DAP kinase 1
    Gene namesi
    Name:DAPK1
    Synonyms:DAPK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:2674. DAPK1.

    Subcellular locationi

    Isoform 1 : Cytoplasm. Cytoplasmcytoskeleton
    Note: Colocalizes with MAP1B in the microtubules and cortical actin fibers.

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi42 – 421K → A: Loss of activity, apoptotic function and of autophosphorylation. 2 Publications
    Mutagenesisi289 – 2891S → A: Loss of phosphorylation and significant increase in proapoptotic activity.
    Mutagenesisi289 – 2891S → E: Reduction in proapoptotic activity.
    Mutagenesisi308 – 3081S → A: Elevated Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Increases apoptotic activity. 1 Publication
    Mutagenesisi308 – 3081S → D: Reduced Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Decreases apoptotic activity. 1 Publication
    Mutagenesisi313 – 3131S → A: Minimal effect on activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA27142.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14301430Death-associated protein kinase 1PRO_0000085910Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei289 – 2891Phosphoserine; by RPS6KA1 and RPS6KA31 Publication
    Modified residuei308 – 3081Phosphoserine; by autocatalysis3 Publications
    Modified residuei333 – 3331Phosphoserine1 Publication
    Modified residuei734 – 7341Phosphoserine; by MAPK11 Publication

    Post-translational modificationi

    Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex, leading to its degradation by the proteasome.1 Publication
    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.1 Publication
    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-308.6 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP53355.
    PaxDbiP53355.
    PRIDEiP53355.

    PTM databases

    PhosphoSiteiP53355.

    Expressioni

    Tissue specificityi

    Isoform 2 is expressed in normal intestinal tissue as well as in colorectal carcinomas.1 Publication

    Inductioni

    Up-regulated following treatment with IFNG/IFN-gamma.1 Publication

    Gene expression databases

    ArrayExpressiP53355.
    BgeeiP53355.
    CleanExiHS_DAPK1.
    GenevestigatoriP53355.

    Organism-specific databases

    HPAiCAB037302.

    Interactioni

    Subunit structurei

    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).15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself6EBI-358616,EBI-358616
    BECN1Q144574EBI-358616,EBI-949378
    KLHL20Q9Y2M511EBI-358616,EBI-714379
    LRRK1Q38SD22EBI-358616,EBI-1050422
    LRRK2Q5S0072EBI-358616,EBI-5323863
    MAPK3P273615EBI-358616,EBI-73995
    PDCD6O753403EBI-358616,EBI-352915
    PKMP146183EBI-358616,EBI-353408
    PKMP14618-12EBI-358616,EBI-4304679

    Protein-protein interaction databases

    BioGridi107982. 24 interactions.
    IntActiP53355. 18 interactions.
    MINTiMINT-1136108.
    STRINGi9606.ENSP00000350785.

    Structurei

    Secondary structure

    1
    1430
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 113
    Beta strandi13 – 219
    Beta strandi23 – 3210
    Turni33 – 353
    Beta strandi38 – 469
    Beta strandi48 – 514
    Beta strandi53 – 564
    Helixi58 – 7013
    Beta strandi79 – 846
    Beta strandi86 – 949
    Helixi101 – 1077
    Beta strandi108 – 1103
    Helixi113 – 13220
    Beta strandi134 – 1363
    Helixi142 – 1443
    Beta strandi145 – 1484
    Beta strandi150 – 1545
    Beta strandi157 – 1593
    Helixi162 – 1643
    Beta strandi169 – 1713
    Helixi181 – 1833
    Helixi186 – 1894
    Helixi197 – 21216
    Helixi222 – 2309
    Helixi238 – 2414
    Beta strandi242 – 2443
    Helixi246 – 25510
    Turni260 – 2623
    Helixi266 – 2716
    Turni273 – 2753
    Helixi280 – 2889
    Helixi293 – 30210
    Helixi304 – 31815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IG1X-ray1.80A2-285[»]
    1JKKX-ray2.40A2-285[»]
    1JKLX-ray1.62A2-285[»]
    1JKSX-ray1.50A2-285[»]
    1JKTX-ray3.50A/B2-285[»]
    1P4FX-ray1.90A2-285[»]
    1WVWX-ray2.40A1-278[»]
    1WVXX-ray2.60A1-278[»]
    1WVYX-ray2.80A1-278[»]
    1YR5X-ray1.70B302-320[»]
    2W4JX-ray1.30A1-277[»]
    2W4KX-ray1.90A1-302[»]
    2X0GX-ray2.20A1-334[»]
    2XUUX-ray1.80A1-334[»]
    2XZSX-ray2.00A/B2-312[»]
    2Y0AX-ray2.60A2-304[»]
    2Y4PX-ray2.65A/B/C/D1-285[»]
    2Y4VX-ray1.80B302-320[»]
    2YAKX-ray2.20A1-285[»]
    3DFCX-ray1.90B1-295[»]
    3DGKX-ray1.70A1-295[»]
    3EH9X-ray1.70A2-285[»]
    3EHAX-ray1.60A2-285[»]
    3F5GX-ray1.85A2-285[»]
    3F5UX-ray2.00A1-285[»]
    3GU4X-ray1.35A1-285[»]
    3GU5X-ray1.65A1-285[»]
    3GU6X-ray1.49A1-285[»]
    3GU7X-ray1.90A1-285[»]
    3GU8X-ray1.60A1-285[»]
    3GUBX-ray1.71A1-285[»]
    3ZXTX-ray2.65A/B/C/D1-285[»]
    4B4LX-ray1.75A1-334[»]
    4PF4X-ray1.13A1-277[»]
    ProteinModelPortaliP53355.
    SMRiP53355. Positions 3-320, 345-749.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53355.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 275263Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Repeati378 – 40730ANK 1Add
    BLAST
    Repeati411 – 44030ANK 2Add
    BLAST
    Repeati444 – 47330ANK 3Add
    BLAST
    Repeati477 – 50630ANK 4Add
    BLAST
    Repeati510 – 53930ANK 5Add
    BLAST
    Repeati543 – 57230ANK 6Add
    BLAST
    Repeati576 – 60530ANK 7Add
    BLAST
    Repeati609 – 63830ANK 8Add
    BLAST
    Repeati875 – 90430ANK 9Add
    BLAST
    Repeati1162 – 119635ANK 10Add
    BLAST
    Domaini1312 – 139685DeathPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni267 – 33468Calmodulin-bindingAdd
    BLAST
    Regioni292 – 30110Autoinhibitory domainBy similarity

    Domaini

    The autoinhibitory domain sterically blocks the substrate peptide-binding site by making both hydrophobic and electrostatic contacts with the kinase core.

    Sequence similaritiesi

    Contains 10 ANK repeats.PROSITE-ProRule annotation
    Contains 1 death domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOVERGENiHBG051296.
    KOiK08803.
    OrthoDBiEOG7QZGBH.
    PhylomeDBiP53355.
    TreeFamiTF314166.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR020676. DAPK1.
    IPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR011009. Kinase-like_dom.
    IPR020675. Myosin_light_ch_kinase-rel.
    IPR027417. P-loop_NTPase.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR22964. PTHR22964. 1 hit.
    PTHR22964:SF54. PTHR22964:SF54. 1 hit.
    PfamiPF00023. Ank. 6 hits.
    PF00531. Death. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 9 hits.
    SM00005. DEATH. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    SSF48403. SSF48403. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 7 hits.
    PS50017. DEATH_DOMAIN. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P53355-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTVFRQENVD DYYDTGEELG SGQFAVVKKC REKSTGLQYA AKFIKKRRTK     50
    SSRRGVSRED IEREVSILKE IQHPNVITLH EVYENKTDVI LILELVAGGE 100
    LFDFLAEKES LTEEEATEFL KQILNGVYYL HSLQIAHFDL KPENIMLLDR 150
    NVPKPRIKII DFGLAHKIDF GNEFKNIFGT PEFVAPEIVN YEPLGLEADM 200
    WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYEFEDEY FSNTSALAKD 250
    FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA 300
    ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH 350
    AINDDNVPGL QHLLGSLSNY DVNQPNKHGT PPLLIAAGCG NIQILQLLIK 400
    RGSRIDVQDK GGSNAVYWAA RHGHVDTLKF LSENKCPLDV KDKSGEMALH 450
    VAARYGHADV AQLLCSFGSN PNIQDKEEET PLHCAAWHGY YSVAKALCEA 500
    GCNVNIKNRE GETPLLTASA RGYHDIVECL AEHGADLNAC DKDGHIALHL 550
    AVRRCQMEVI KTLLSQGCFV DYQDRHGNTP LHVACKDGNM PIVVALCEAN 600
    CNLDISNKYG RTPLHLAANN GILDVVRYLC LMGASVEALT TDGKTAEDLA 650
    RSEQHEHVAG LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK 700
    TTLVESLKCG LLRSFFRRRR PRLSSTNSSR FPPSPLASKP TVSVSINNLY 750
    PGCENVSVRS RSMMFEPGLT KGMLEVFVAP THHPHCSADD QSTKAIDIQN 800
    AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHVVVF SLEEPYEIQL 850
    NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL QVVLVATHAD IMNVPRPAGG 900
    EFGYDKDTSL LKEIRNRFGN DLHISNKLFV LDAGASGSKD MKVLRNHLQE 950
    IRSQIVSVCP PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN 1000
    PLASEEDLRR IAQQLHSTGE INIMQSETVQ DVLLLDPRWL CTNVLGKLLS 1050
    VETPRALHHY RGRYTVEDIQ RLVPDSDVEE LLQILDAMDI CARDLSSGTM 1100
    VDVPALIKTD NLHRSWADEE DEVMVYGGVR IVPVEHLTPF PCGIFHKVQV 1150
    NLCRWIHQQS TEGDADIRLW VNGCKLANRG AELLVLLVNH GQGIEVQVRG 1200
    LETEKIKCCL LLDSVCSTIE NVMATTLPGL LTVKHYLSPQ QLREHHEPVM 1250
    IYQPRDFFRA QTLKETSLTN TMGGYKESFS SIMCFGCHDV YSQASLGMDI 1300
    HASDLNLLTR RKLSRLLDPP DPLGKDWCLL AMNLGLPDLV AKYNTSNGAP 1350
    KDFLPSPLHA LLREWTTYPE STVGTLMSKL RELGRRDAAD FLLKASSVFK 1400
    INLDGNGQEA YASSCNSGTS YNSISSVVSR 1430
    Length:1,430
    Mass (Da):160,046
    Last modified:January 11, 2011 - v6
    Checksum:iE2C4246E7C78A6D2
    GO
    Isoform 2 (identifier: P53355-2) [UniParc]FASTAAdd to Basket

    Also known as: s-DAPK-1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-446: Missing.
         742-783: VSVSINNLYP...LEVFVAPTHH → GRNLHAGPVS...SLGLYWTLWP
         784-1430: Missing.

    Show »
    Length:337
    Mass (Da):36,765
    Checksum:i3BA58BA79D87E0C6
    GO
    Isoform 3 (identifier: P53355-3) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1430-1430: R → RRNSHVWNPTV

    Show »
    Length:1,440
    Mass (Da):161,237
    Checksum:iD43BB6B6A3F0ABF9
    GO
    Isoform 4 (identifier: P53355-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         805-870: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,364
    Mass (Da):152,467
    Checksum:i60E285E6A32348CB
    GO

    Sequence cautioni

    The sequence AAP35581.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.
    The sequence CAA53712.1 differs from that shown. Reason: Frameshift at positions 462 and 464.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti490 – 4901Y → H in BAC87163. (PubMed:14702039)Curated
    Sequence conflicti1217 – 12171S → G in CAH18690. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti416 – 4161V → I.1 Publication
    Corresponds to variant rs12343465 [ dbSNP | Ensembl ].
    VAR_033235
    Natural varianti461 – 4611A → S.1 Publication
    VAR_040420
    Natural varianti519 – 5191S → A.1 Publication
    VAR_040421
    Natural varianti540 – 5401C → Y.1 Publication
    Corresponds to variant rs56327474 [ dbSNP | Ensembl ].
    VAR_040422
    Natural varianti591 – 5911P → L.1 Publication
    VAR_060693
    Natural varianti622 – 6221I → M.1 Publication
    Corresponds to variant rs36215047 [ dbSNP | Ensembl ].
    VAR_060694
    Natural varianti941 – 9411M → T.1 Publication
    VAR_040423
    Natural varianti977 – 9771R → W.1 Publication
    VAR_040424
    Natural varianti978 – 9781K → N.1 Publication
    VAR_040425
    Natural varianti993 – 9931Y → C.1 Publication
    VAR_040426
    Natural varianti994 – 9941D → E.1 Publication
    VAR_040427
    Natural varianti1005 – 10051E → Q.1 Publication
    VAR_040428
    Natural varianti1007 – 10071D → Y.1 Publication
    VAR_040429
    Natural varianti1008 – 10081L → P.1 Publication
    VAR_040430
    Natural varianti1010 – 10101R → C.1 Publication
    VAR_040431
    Natural varianti1018 – 10181T → A.1 Publication
    VAR_040432
    Natural varianti1272 – 12721M → I.1 Publication
    Corresponds to variant rs56169226 [ dbSNP | Ensembl ].
    VAR_040433
    Natural varianti1346 – 13461S → N.5 Publications
    Corresponds to variant rs1056719 [ dbSNP | Ensembl ].
    VAR_040434
    Natural varianti1405 – 14051G → V.2 Publications
    Corresponds to variant rs36220450 [ dbSNP | Ensembl ].
    VAR_040435

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 446446Missing in isoform 2. 1 PublicationVSP_042053Add
    BLAST
    Alternative sequencei742 – 78342VSVSI…APTHH → GRNLHAGPVSPAGVGFRTLS FQGLGGKGVVFGSLGLYWTL WP in isoform 2. 1 PublicationVSP_042054Add
    BLAST
    Alternative sequencei784 – 1430647Missing in isoform 2. 1 PublicationVSP_042055Add
    BLAST
    Alternative sequencei805 – 87066Missing in isoform 4. 1 PublicationVSP_054478Add
    BLAST
    Alternative sequencei1430 – 14301R → RRNSHVWNPTV in isoform 3. CuratedVSP_042056

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76104 mRNA. Translation: CAA53712.1. Frameshift.
    AK127855 mRNA. Translation: BAC87163.1.
    CR749834 mRNA. Translation: CAH18690.1.
    DQ436495 Genomic DNA. Translation: ABD96827.1.
    AL160279 Genomic DNA. No translation available.
    AL161787 Genomic DNA. No translation available.
    AL591852 Genomic DNA. No translation available.
    CH471089 Genomic DNA. Translation: EAW62727.1.
    BC113660 mRNA. Translation: AAI13661.1.
    BC143733 mRNA. Translation: AAI43734.1.
    BC143759 mRNA. Translation: AAI43760.1.
    BT006935 mRNA. Translation: AAP35581.1. Sequence problems.
    CCDSiCCDS43842.1. [P53355-1]
    PIRiI37275.
    RefSeqiNP_001275658.1. NM_001288729.1. [P53355-1]
    NP_001275659.1. NM_001288730.1. [P53355-1]
    NP_001275660.1. NM_001288731.1. [P53355-1]
    NP_004929.2. NM_004938.3. [P53355-1]
    UniGeneiHs.380277.
    Hs.693441.

    Genome annotation databases

    EnsembliENST00000358077; ENSP00000350785; ENSG00000196730. [P53355-1]
    ENST00000408954; ENSP00000386135; ENSG00000196730. [P53355-1]
    ENST00000472284; ENSP00000417076; ENSG00000196730. [P53355-1]
    ENST00000491893; ENSP00000419026; ENSG00000196730. [P53355-4]
    GeneIDi1612.
    KEGGihsa:1612.
    UCSCiuc004apc.3. human. [P53355-1]
    uc004apf.1. human. [P53355-2]

    Polymorphism databases

    DMDMi317373595.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76104 mRNA. Translation: CAA53712.1 . Frameshift.
    AK127855 mRNA. Translation: BAC87163.1 .
    CR749834 mRNA. Translation: CAH18690.1 .
    DQ436495 Genomic DNA. Translation: ABD96827.1 .
    AL160279 Genomic DNA. No translation available.
    AL161787 Genomic DNA. No translation available.
    AL591852 Genomic DNA. No translation available.
    CH471089 Genomic DNA. Translation: EAW62727.1 .
    BC113660 mRNA. Translation: AAI13661.1 .
    BC143733 mRNA. Translation: AAI43734.1 .
    BC143759 mRNA. Translation: AAI43760.1 .
    BT006935 mRNA. Translation: AAP35581.1 . Sequence problems.
    CCDSi CCDS43842.1. [P53355-1 ]
    PIRi I37275.
    RefSeqi NP_001275658.1. NM_001288729.1. [P53355-1 ]
    NP_001275659.1. NM_001288730.1. [P53355-1 ]
    NP_001275660.1. NM_001288731.1. [P53355-1 ]
    NP_004929.2. NM_004938.3. [P53355-1 ]
    UniGenei Hs.380277.
    Hs.693441.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IG1 X-ray 1.80 A 2-285 [» ]
    1JKK X-ray 2.40 A 2-285 [» ]
    1JKL X-ray 1.62 A 2-285 [» ]
    1JKS X-ray 1.50 A 2-285 [» ]
    1JKT X-ray 3.50 A/B 2-285 [» ]
    1P4F X-ray 1.90 A 2-285 [» ]
    1WVW X-ray 2.40 A 1-278 [» ]
    1WVX X-ray 2.60 A 1-278 [» ]
    1WVY X-ray 2.80 A 1-278 [» ]
    1YR5 X-ray 1.70 B 302-320 [» ]
    2W4J X-ray 1.30 A 1-277 [» ]
    2W4K X-ray 1.90 A 1-302 [» ]
    2X0G X-ray 2.20 A 1-334 [» ]
    2XUU X-ray 1.80 A 1-334 [» ]
    2XZS X-ray 2.00 A/B 2-312 [» ]
    2Y0A X-ray 2.60 A 2-304 [» ]
    2Y4P X-ray 2.65 A/B/C/D 1-285 [» ]
    2Y4V X-ray 1.80 B 302-320 [» ]
    2YAK X-ray 2.20 A 1-285 [» ]
    3DFC X-ray 1.90 B 1-295 [» ]
    3DGK X-ray 1.70 A 1-295 [» ]
    3EH9 X-ray 1.70 A 2-285 [» ]
    3EHA X-ray 1.60 A 2-285 [» ]
    3F5G X-ray 1.85 A 2-285 [» ]
    3F5U X-ray 2.00 A 1-285 [» ]
    3GU4 X-ray 1.35 A 1-285 [» ]
    3GU5 X-ray 1.65 A 1-285 [» ]
    3GU6 X-ray 1.49 A 1-285 [» ]
    3GU7 X-ray 1.90 A 1-285 [» ]
    3GU8 X-ray 1.60 A 1-285 [» ]
    3GUB X-ray 1.71 A 1-285 [» ]
    3ZXT X-ray 2.65 A/B/C/D 1-285 [» ]
    4B4L X-ray 1.75 A 1-334 [» ]
    4PF4 X-ray 1.13 A 1-277 [» ]
    ProteinModelPortali P53355.
    SMRi P53355. Positions 3-320, 345-749.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107982. 24 interactions.
    IntActi P53355. 18 interactions.
    MINTi MINT-1136108.
    STRINGi 9606.ENSP00000350785.

    Chemistry

    BindingDBi P53355.
    ChEMBLi CHEMBL2558.
    GuidetoPHARMACOLOGYi 2002.

    PTM databases

    PhosphoSitei P53355.

    Polymorphism databases

    DMDMi 317373595.

    Proteomic databases

    MaxQBi P53355.
    PaxDbi P53355.
    PRIDEi P53355.

    Protocols and materials databases

    DNASUi 1612.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358077 ; ENSP00000350785 ; ENSG00000196730 . [P53355-1 ]
    ENST00000408954 ; ENSP00000386135 ; ENSG00000196730 . [P53355-1 ]
    ENST00000472284 ; ENSP00000417076 ; ENSG00000196730 . [P53355-1 ]
    ENST00000491893 ; ENSP00000419026 ; ENSG00000196730 . [P53355-4 ]
    GeneIDi 1612.
    KEGGi hsa:1612.
    UCSCi uc004apc.3. human. [P53355-1 ]
    uc004apf.1. human. [P53355-2 ]

    Organism-specific databases

    CTDi 1612.
    GeneCardsi GC09P090112.
    HGNCi HGNC:2674. DAPK1.
    HPAi CAB037302.
    MIMi 600831. gene.
    neXtProti NX_P53355.
    PharmGKBi PA27142.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOVERGENi HBG051296.
    KOi K08803.
    OrthoDBi EOG7QZGBH.
    PhylomeDBi P53355.
    TreeFami TF314166.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_22128. Role of DCC in regulating apoptosis.
    SignaLinki P53355.

    Miscellaneous databases

    ChiTaRSi DAPK1. human.
    EvolutionaryTracei P53355.
    GeneWikii DAPK1.
    GenomeRNAii 1612.
    NextBioi 35481278.
    PROi P53355.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53355.
    Bgeei P53355.
    CleanExi HS_DAPK1.
    Genevestigatori P53355.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR020676. DAPK1.
    IPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR011009. Kinase-like_dom.
    IPR020675. Myosin_light_ch_kinase-rel.
    IPR027417. P-loop_NTPase.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR22964. PTHR22964. 1 hit.
    PTHR22964:SF54. PTHR22964:SF54. 1 hit.
    Pfami PF00023. Ank. 6 hits.
    PF00531. Death. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 9 hits.
    SM00005. DEATH. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    SSF48403. SSF48403. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 7 hits.
    PS50017. DEATH_DOMAIN. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the gamma interferon-induced cell death."
      Deiss L.P., Feinstein E., Berissi H., Cohen O., Kimchi A.
      Genes Dev. 9:15-30(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, MUTAGENESIS OF LYS-42, VARIANT ASN-1346.
    2. Feinstein E.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 164-171.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-1346.
      Tissue: Amygdala.
    5. NIEHS SNPs program
      Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-591; MET-622; ASN-1346 AND VAL-1405.
    6. "DNA sequence and analysis of human chromosome 9."
      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.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-1346.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
      Tissue: Cerebellum.
    9. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      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.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-363.
    10. "Death-associated protein kinase-related protein 1, a novel serine/threonine kinase involved in apoptosis."
      Inbal B., Shani G., Cohen O., Kissil J.L., Kimchi A.
      Mol. Cell. Biol. 20:1044-1054(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "The pro-apoptotic function of death-associated protein kinase is controlled by a unique inhibitory autophosphorylation-based mechanism."
      Shohat G., Spivak-Kroizman T., Cohen O., Bialik S., Shani G., Berissi H., Eisenstein M., Kimchi A.
      J. Biol. Chem. 276:47460-47467(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF LYS-42; SER-308 AND SER-313, PHOSPHORYLATION AT SER-308.
    12. "DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death."
      Inbal B., Bialik S., Sabanay I., Shani G., Kimchi A.
      J. Cell Biol. 157:455-468(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated protein (DAP) kinase regulates its interaction with Munc18."
      Tian J.H., Das S., Sheng Z.H.
      J. Biol. Chem. 278:26265-26274(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF STX1A, INTERACTION WITH STX1A.
    14. "Death-associated protein kinase phosphorylates ZIP kinase, forming a unique kinase hierarchy to activate its cell death functions."
      Shani G., Marash L., Gozuacik D., Bialik S., Teitelbaum L., Shohat G., Kimchi A.
      Mol. Cell. Biol. 24:8611-8626(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF DAPK3, INTERACTION WITH DAPK3.
    15. "Programmed cell death 6 (PDCD6) protein interacts with death-associated protein kinase 1 (DAPk1): additive effect on apoptosis via caspase-3 dependent pathway."
      Lee J.H., Rho S.B., Chun T.
      Biotechnol. Lett. 27:1011-1015(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDCD6.
    16. "The tumor suppressor DAP kinase is a target of RSK-mediated survival signaling."
      Anjum R., Roux P.P., Ballif B.A., Gygi S.P., Blenis J.
      Curr. Biol. 15:1762-1767(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-289.
    17. "Bidirectional signals transduced by DAPK-ERK interaction promote the apoptotic effect of DAPK."
      Chen C.H., Wang W.J., Kuo J.C., Tsai H.C., Lin J.R., Chang Z.F., Chen R.H.
      EMBO J. 24:294-304(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-734, INTERACTION WITH MAPK1 AND MAPK3.
    18. "The dependence receptor UNC5H2 mediates apoptosis through DAP-kinase."
      Llambi F., Lourenco F.C., Gozuacik D., Guix C., Pays L., Del Rio G., Kimchi A., Mehlen P.
      EMBO J. 24:1192-1201(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-308, ENZYME REGULATION, INTERACTION WITH UNC5B.
    19. "The death-associated protein kinases: structure, function, and beyond."
      Bialik S., Kimchi A.
      Annu. Rev. Biochem. 75:189-210(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    20. "Control of death-associated protein kinase (DAPK) activity by phosphorylation and proteasomal degradation."
      Jin Y., Blue E.K., Gallagher P.J.
      J. Biol. Chem. 281:39033-39040(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 3), PHOSPHORYLATION AT SER-308, DEPHOSPHORYLATION, ENZYME REGULATION.
    21. "DAP kinase regulates JNK signaling by binding and activating protein kinase D under oxidative stress."
      Eisenberg-Lerner A., Kimchi A.
      Cell Death Differ. 14:1908-1915(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PRKD1, INTERACTION WITH PRKD1.
    22. "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."
      Houle F., Poirier A., Dumaresq J., Huot J.
      J. Cell Sci. 120:3666-3677(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TPM1.
    23. "An alternative transcript from the death-associated protein kinase 1 locus encoding a small protein selectively mediates membrane blebbing."
      Lin Y., Stevens C., Hrstka R., Harrison B., Fourtouna A., Pathuri S., Vojtesek B., Hupp T.
      FEBS J. 275:2574-2584(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2), PROTEOLYTIC PROCESSING, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    24. "DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing."
      Harrison B., Kraus M., Burch L., Stevens C., Craig A., Gordon-Weeks P., Hupp T.R.
      J. Biol. Chem. 283:9999-10014(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAP1B.
    25. "DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating inflammatory gene expression."
      Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L.
      Mol. Cell 32:371-382(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    26. "DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy."
      Zalckvar E., Berissi H., Mizrachy L., Idelchuk Y., Koren I., Eisenstein M., Sabanay H., Pinkas-Kramarski R., Kimchi A.
      EMBO Rep. 10:285-292(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BECN1, INTERACTION WITH BECN1.
    27. "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."
      Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O., Hupp T.
      J. Biol. Chem. 284:334-344(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TSC2 AND RPS6, INTERACTION WITH TSC2.
    28. "The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to control interferon responses."
      Lee Y.R., Yuan W.C., Ho H.C., Chen C.H., Shih H.M., Chen R.H.
      EMBO J. 29:1748-1761(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH KLHL20.
    29. "Death-associated protein kinase (DAPK) and signal transduction: additional roles beyond cell death."
      Lin Y., Hupp T.R., Stevens C.
      FEBS J. 277:48-57(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    30. "Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function."
      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.
      Mol. Cell 42:147-159(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PIN1, INTERACTION WITH PIN1.
    31. "New modularity of DAP-kinases: alternative splicing of the DRP-1 gene produces a ZIPk-like isoform."
      Shoval Y., Berissi H., Kimchi A., Pietrokovski S.
      PLoS ONE 6:E17344-E17344(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    32. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression."
      Tereshko V., Teplova M., Brunzelle J., Watterson D.M., Egli M.
      Nat. Struct. Biol. 8:899-907(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-285 IN COMPLEX WITH ATP ANALOG AND DIVALENT METAL CATION.
    34. "An aminopyridazine-based inhibitor of a pro-apoptotic protein kinase attenuates hypoxia-ischemia induced acute brain injury."
      Velentza A.V., Wainwright M.S., Zasadzki M., Mirzoeva S., Schumacher A.M., Haiech J., Focia P.J., Egli M., Watterson D.M.
      Bioorg. Med. Chem. Lett. 13:3465-3470(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-285 IN COMPLEX WITH SYNTHETIC INHIBITOR.
    35. "Complex structure of kinase domain of DAP kinase with staurosporine."
      Ueda Y., Ogata H., Yamakawa A., Higuchi Y.
      Submitted (APR-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-278 IN COMPLEX WITH INHIBITORS.
    36. "Recognition of human death-associated protein kinases by calmodulin."
      Kursula P., Vahokoski J., Wilmanns M.
      Submitted (JUL-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 302-320 IN COMPLEX WITH CALMODULIN.
    37. "Patterns of somatic mutation in human cancer genomes."
      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.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: 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.

    Entry informationi

    Entry nameiDAPK1_HUMAN
    AccessioniPrimary (citable) accession number: P53355
    Secondary accession number(s): B7ZLD2
    , B7ZLE7, Q14CQ7, Q1W5W0, Q68CP8, Q6ZRZ3, Q9BTL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 163 of the entry and version 6 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3