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Q9UIK4

- DAPK2_HUMAN

UniProt

Q9UIK4 - DAPK2_HUMAN

Protein

Death-associated protein kinase 2

Gene

DAPK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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. Acts as a mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation.
    Isoform 2 is not regulated by calmodulin. It can phosphorylate MYL9. It can induce membrane blebbing and autophagic cell death.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.3 Publications

    Enzyme regulationi

    Activated by Ca2+/calmodulin. Regulated by a double locking mechanism, involving autophosphorylation at Ser-318, calmodulin binding, and dimerization. In the inactive state, Ser-318 is phosphorylated, and the kinase is dimeric. Activation involves: dephosphorylation at Ser-318, release-of-autoinhibition mechanism where calmodulin binding induces a conformational change that relieves the steric block of the active site by the autoinhibitory domain, and generation of the monomeric active form of the kinase.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521ATP2 PublicationsPROSITE-ProRule annotation
    Active sitei149 – 1491Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi29 – 379ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. anoikis Source: UniProtKB
    2. apoptotic process Source: UniProtKB
    3. intracellular signal transduction Source: UniProtKB
    4. protein autophosphorylation Source: UniProtKB
    5. protein phosphorylation Source: UniProtKB
    6. regulation of apoptotic process Source: UniProtKB
    7. regulation of autophagy Source: UniProtKB
    8. regulation of intrinsic apoptotic signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_22128. Role of DCC in regulating apoptosis.
    SignaLinkiQ9UIK4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Death-associated protein kinase 2 (EC:2.7.11.1)
    Short name:
    DAP kinase 2
    Alternative name(s):
    DAP-kinase-related protein 1
    Short name:
    DRP-1
    Gene namesi
    Name:DAPK2
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:2675. DAPK2.

    Subcellular locationi

    GO - Cellular componenti

    1. autophagic vacuole lumen Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic vesicle Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521K → A: Loss of activity, apoptotic function and of autophosphorylation. 3 Publications
    Mutagenesisi299 – 33032Missing: Loss of ca(2+)-calmodulin binding, increase in activity, loss of autophosphorylation. 1 PublicationAdd
    BLAST
    Mutagenesisi299 – 2991S → A: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity. 1 Publication
    Mutagenesisi318 – 3181S → A: Loss of Ca(2+)-calmodulin independent phosphorylation, increase in apoptotic activity. 1 Publication
    Mutagenesisi318 – 3181S → D: Abolishes apoptotic activity. 1 Publication
    Mutagenesisi320 – 3201S → A: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity. 1 Publication
    Mutagenesisi323 – 3231S → A: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity. 1 Publication
    Mutagenesisi329 – 3291T → A: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA27143.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 370370Death-associated protein kinase 2PRO_0000085912Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei299 – 2991PhosphoserineBy similarity
    Modified residuei318 – 3181Phosphoserine; by autocatalysis1 Publication
    Modified residuei349 – 3491Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylation at Ser-318 inhibits its catalytic activity. Dephosphorylated at Ser-318 in response to activated Fas and TNF-alpha receptors.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UIK4.
    PaxDbiQ9UIK4.
    PRIDEiQ9UIK4.

    PTM databases

    PhosphoSiteiQ9UIK4.

    Expressioni

    Tissue specificityi

    Isoform 2 is expressed in embryonic stem cells (at protein level). Isoform 1 is ubiquitously expressed in all tissue types examined with high levels in heart, lung and skeletal muscle. It is expressed abundantly in cells differentiated toward granulocytes and low in undifferentiated, normal and leukemic hematopoietic cells and monocytes/macrophages.3 Publications

    Inductioni

    Up-regulated during granulocytic maturation.1 Publication

    Gene expression databases

    ArrayExpressiQ9UIK4.
    BgeeiQ9UIK4.
    CleanExiHS_DAPK2.
    GenevestigatoriQ9UIK4.

    Interactioni

    Subunit structurei

    Homodimer in its autoinhibited state. Active as monomer By similarity. Isoform 2 but not isoform 1 can interact with ATF4.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-77154,EBI-77154

    Protein-protein interaction databases

    BioGridi117137. 2 interactions.
    STRINGi9606.ENSP00000261891.

    Structurei

    Secondary structure

    1
    370
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 224
    Beta strandi23 – 319
    Beta strandi33 – 4210
    Turni43 – 453
    Beta strandi48 – 569
    Beta strandi58 – 614
    Beta strandi63 – 664
    Helixi68 – 8013
    Beta strandi89 – 946
    Beta strandi96 – 1038
    Helixi111 – 1166
    Helixi123 – 14220
    Beta strandi144 – 1463
    Helixi152 – 1543
    Beta strandi155 – 1584
    Beta strandi162 – 1643
    Beta strandi167 – 1693
    Helixi191 – 1933
    Helixi196 – 1994
    Helixi207 – 22216
    Helixi232 – 2409
    Helixi248 – 2514
    Helixi256 – 2638
    Turni270 – 2723
    Helixi276 – 2816
    Turni283 – 2853
    Helixi290 – 2989
    Helixi303 – 31210
    Helixi314 – 32815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WMKX-ray3.60A/B/C/D/E/F/G/H11-330[»]
    1WRZX-ray2.00B312-330[»]
    1Z9XX-ray3.93A/B/C11-330[»]
    1ZUZX-ray1.91B312-330[»]
    1ZWSX-ray2.90A/B/C/D/E/F/G/H11-297[»]
    2A27X-ray3.00A/B/C/D/E/F/G/H11-330[»]
    2A2AX-ray1.47A/B/C/D11-330[»]
    2CKEX-ray2.80A/B/C/D11-330[»]
    ProteinModelPortaliQ9UIK4.
    SMRiQ9UIK4. Positions 12-315.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UIK4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 285263Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni277 – 34468Calmodulin-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.By similarity

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233016.
    HOVERGENiHBG100551.
    InParanoidiQ9UIK4.
    KOiK08803.
    OMAiCNHLSRS.
    PhylomeDBiQ9UIK4.
    TreeFamiTF314166.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR020675. Myosin_light_ch_kinase-rel.
    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.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UIK4-1) [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

    MFQASMRSPN MEPFKQQKVE DFYDIGEELG SGQFAIVKKC REKSTGLEYA    50
    AKFIKKRQSR ASRRGVSREE IEREVSILRQ VLHHNVITLH DVYENRTDVV 100
    LILELVSGGE LFDFLAQKES LSEEEATSFI KQILDGVNYL HTKKIAHFDL 150
    KPENIMLLDK NIPIPHIKLI DFGLAHEIED GVEFKNIFGT PEFVAPEIVN 200
    YEPLGLEADM WSIGVITYIL LSGASPFLGD TKQETLANIT AVSYDFDEEF 250
    FSQTSELAKD FIRKLLVKET RKRLTIQEAL RHPWITPVDN QQAMVRRESV 300
    VNLENFRKQY VRRRWKLSFS IVSLCNHLTR SLMKKVHLRP DEDLRNCESD 350
    TEEDIARRKA LHPRRRSSTS 370
    Length:370
    Mass (Da):42,898
    Last modified:May 1, 2000 - v1
    Checksum:i035E914BBCD881A2
    GO
    Isoform 2 (identifier: Q9UIK4-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         287-370: PVDNQQAMVR...LHPRRRSSTS → SKGEGRAPEQ...TEEFLAGWKL

    Note: Contains a leucine zipper at positions 434-451.

    Show »
    Length:488
    Mass (Da):55,931
    Checksum:i34F716A709C569B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti241 – 2411A → S in AAC35001. (PubMed:10629061)Curated
    Sequence conflicti253 – 2531Q → H in AAC35001. (PubMed:10629061)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti60 – 601R → W.1 Publication
    Corresponds to variant rs56047843 [ dbSNP | Ensembl ].
    VAR_040436
    Natural varianti271 – 2711R → W.1 Publication
    Corresponds to variant rs34270163 [ dbSNP | Ensembl ].
    VAR_040437

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei287 – 37084PVDNQ…RSSTS → SKGEGRAPEQRKTEPTQLKT KHLREYTLKCHSSMPPNNSY VNFERFACVVEDVARVDLGC RALVEAHDTIQDDVEALVSI FNEKEAWYREENESARHDLS QLRYEFRKVESLKKLLREDI QATGCSLGSMARKLDHLQAQ FEILRQELSADLQWIQELVG SFQLESGSSEGLGSTFYQDT SESLSELLSRSCTEEFLAGW KL in isoform 2. 1 PublicationVSP_042057Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018001 mRNA. Translation: BAA88063.1.
    AF052941 mRNA. Translation: AAC35001.1.
    GU056176 mRNA. Translation: ADD83109.1.
    AC015914 Genomic DNA. No translation available.
    AC021541 Genomic DNA. No translation available.
    BC114506 mRNA. Translation: AAI14507.1.
    CCDSiCCDS10188.1. [Q9UIK4-1]
    RefSeqiNP_055141.2. NM_014326.3. [Q9UIK4-1]
    XP_005254323.1. XM_005254266.2. [Q9UIK4-2]
    UniGeneiHs.237886.

    Genome annotation databases

    EnsembliENST00000261891; ENSP00000261891; ENSG00000035664. [Q9UIK4-1]
    ENST00000457488; ENSP00000408277; ENSG00000035664. [Q9UIK4-1]
    ENST00000558069; ENSP00000453235; ENSG00000035664. [Q9UIK4-2]
    GeneIDi23604.
    KEGGihsa:23604.
    UCSCiuc002amr.3. human. [Q9UIK4-1]

    Polymorphism databases

    DMDMi38605084.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018001 mRNA. Translation: BAA88063.1 .
    AF052941 mRNA. Translation: AAC35001.1 .
    GU056176 mRNA. Translation: ADD83109.1 .
    AC015914 Genomic DNA. No translation available.
    AC021541 Genomic DNA. No translation available.
    BC114506 mRNA. Translation: AAI14507.1 .
    CCDSi CCDS10188.1. [Q9UIK4-1 ]
    RefSeqi NP_055141.2. NM_014326.3. [Q9UIK4-1 ]
    XP_005254323.1. XM_005254266.2. [Q9UIK4-2 ]
    UniGenei Hs.237886.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WMK X-ray 3.60 A/B/C/D/E/F/G/H 11-330 [» ]
    1WRZ X-ray 2.00 B 312-330 [» ]
    1Z9X X-ray 3.93 A/B/C 11-330 [» ]
    1ZUZ X-ray 1.91 B 312-330 [» ]
    1ZWS X-ray 2.90 A/B/C/D/E/F/G/H 11-297 [» ]
    2A27 X-ray 3.00 A/B/C/D/E/F/G/H 11-330 [» ]
    2A2A X-ray 1.47 A/B/C/D 11-330 [» ]
    2CKE X-ray 2.80 A/B/C/D 11-330 [» ]
    ProteinModelPortali Q9UIK4.
    SMRi Q9UIK4. Positions 12-315.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117137. 2 interactions.
    STRINGi 9606.ENSP00000261891.

    Chemistry

    BindingDBi Q9UIK4.
    ChEMBLi CHEMBL3123.
    GuidetoPHARMACOLOGYi 2003.

    PTM databases

    PhosphoSitei Q9UIK4.

    Polymorphism databases

    DMDMi 38605084.

    Proteomic databases

    MaxQBi Q9UIK4.
    PaxDbi Q9UIK4.
    PRIDEi Q9UIK4.

    Protocols and materials databases

    DNASUi 23604.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261891 ; ENSP00000261891 ; ENSG00000035664 . [Q9UIK4-1 ]
    ENST00000457488 ; ENSP00000408277 ; ENSG00000035664 . [Q9UIK4-1 ]
    ENST00000558069 ; ENSP00000453235 ; ENSG00000035664 . [Q9UIK4-2 ]
    GeneIDi 23604.
    KEGGi hsa:23604.
    UCSCi uc002amr.3. human. [Q9UIK4-1 ]

    Organism-specific databases

    CTDi 23604.
    GeneCardsi GC15M064199.
    HGNCi HGNC:2675. DAPK2.
    neXtProti NX_Q9UIK4.
    PharmGKBi PA27143.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233016.
    HOVERGENi HBG100551.
    InParanoidi Q9UIK4.
    KOi K08803.
    OMAi CNHLSRS.
    PhylomeDBi Q9UIK4.
    TreeFami TF314166.

    Enzyme and pathway databases

    Reactomei REACT_22128. Role of DCC in regulating apoptosis.
    SignaLinki Q9UIK4.

    Miscellaneous databases

    ChiTaRSi DAPK2. human.
    EvolutionaryTracei Q9UIK4.
    GeneWikii DAPK2.
    GenomeRNAii 23604.
    NextBioi 35500973.
    PROi Q9UIK4.

    Gene expression databases

    ArrayExpressi Q9UIK4.
    Bgeei Q9UIK4.
    CleanExi HS_DAPK2.
    Genevestigatori Q9UIK4.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR020675. Myosin_light_ch_kinase-rel.
    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.
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Death-associated protein kinase 2 is a new calcium/calmodulin-dependent protein kinase that signals apoptosis through its catalytic activity."
      Kawai T., Nomura F., Hoshino K., Copeland N.G., Gilbert D.J., Jenkins N.A., Akira S.
      Oncogene 18:3471-3480(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-52.
      Tissue: Skeletal muscle1 Publication.
    2. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, HOMODIMERIZATION, MUTAGENESIS OF LYS-52.
      Tissue: KidneyImported.
    3. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), TISSUE SPECIFICITY, INTERACTION WITH ATF4 (ISOFORM 2).
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
    6. "Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding."
      Shani G., Henis-Korenblit S., Jona G., Gileadi O., Eisenstein M., Ziv T., Admon A., Kimchi A.
      EMBO J. 20:1099-1113(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMODIMERIZATION, MUTAGENESIS OF LYS-52; SER-299; SER-318; SER-320; SER-323 AND THR-329, PHOSPHORYLATION AT SER-318.
    7. "The DAP-kinase family of proteins: study of a novel group of calcium-regulated death-promoting kinases."
      Shohat G., Shani G., Eisenstein M., Kimchi A.
      Biochim. Biophys. Acta 1600:45-50(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    8. "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.
    9. "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.
    10. "The death-associated protein kinase 2 is up-regulated during normal myeloid differentiation and enhances neutrophil maturation in myeloid leukemic cells."
      Rizzi M., Tschan M.P., Britschgi C., Britschgi A., Huegli B., Grob T.J., Leupin N., Mueller B.U., Simon H.U., Ziemiecki A., Torbett B.E., Fey M.F., Tobler A.
      J. Leukoc. Biol. 81:1599-1608(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Down-regulation of death-associated protein kinase-2 is required for beta-catenin-induced anoikis resistance of malignant epithelial cells."
      Li H., Ray G., Yoo B.H., Erdogan M., Rosen K.V.
      J. Biol. Chem. 284:2012-2022(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "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] TRP-60 AND TRP-271.

    Entry informationi

    Entry nameiDAPK2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UIK4
    Secondary accession number(s): E9JGM7, O75892, Q24JS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 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 15
      Human chromosome 15: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3