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Q80YE7

- DAPK1_MOUSE

UniProt

Q80YE7 - DAPK1_MOUSE

Protein

Death-associated protein kinase 1

Gene

Dapk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (28 Nov 2003)
      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 By similarity. 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.By similarity4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.1 Publication

    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.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei42 – 421ATPPROSITE-ProRule annotation
    Active sitei139 – 1391Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 279ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. calmodulin binding Source: UniProtKB
    3. calmodulin-dependent protein kinase activity Source: RefGenome
    4. protein binding Source: IntAct
    5. protein kinase activity Source: MGI

    GO - Biological processi

    1. apoptotic signaling pathway Source: ProtInc
    2. cellular response to interferon-gamma Source: UniProtKB
    3. extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
    4. intracellular signal transduction Source: UniProtKB
    5. negative regulation of apoptotic process Source: UniProtKB
    6. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
    7. negative regulation of translation Source: Ensembl
    8. protein autophosphorylation Source: Ensembl
    9. protein phosphorylation Source: UniProtKB
    10. 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

    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
    OrganismiMus musculus (Mouse)Imported
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1916885. Dapk1.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. cytoplasm Source: MGI
    3. cytosol Source: Reactome

    Pathology & Biotechi

    Disruption phenotypei

    Mice are protected against cerebral ischemic neuronal death.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14421442Death-associated protein kinase 1PRO_0000085911Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei289 – 2891Phosphoserine; by RPS6KA1 and RPS6KA3By similarity
    Modified residuei308 – 3081Phosphoserine; by autocatalysis2 Publications
    Modified residuei333 – 3331Phosphoserine1 Publication
    Modified residuei734 – 7341Phosphoserine; by MAPK1By similarity

    Post-translational modificationi

    Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex, leading to its degradation by the proteasome.By similarity
    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-308.3 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ80YE7.
    PRIDEiQ80YE7.

    PTM databases

    PhosphoSiteiQ80YE7.

    Expressioni

    Tissue specificityi

    High levels in bladder, uterus, vas deferens, lung, liver and kidney.1 Publication

    Gene expression databases

    BgeeiQ80YE7.
    CleanExiMM_DAPK1.
    GenevestigatoriQ80YE7.

    Interactioni

    Subunit structurei

    Interacts with KLHL20. Interacts (via death domain) with MAPK1 and MAPK3. Interacts with MAP1B (via N-terminus). Interacts with PRKD1 in an oxidative stress-regulated manner. Interacts with PIN1, PDCD6, BECN1, TSC2 and STX1A By similarity. Interacts (via death domain) with UNC5B (via death domain). Interacts with GRINB.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Grin2bQ010978EBI-2584874,EBI-400125

    Protein-protein interaction databases

    BioGridi213581. 3 interactions.
    IntActiQ80YE7. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ80YE7.
    SMRiQ80YE7. Positions 3-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 275263Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Repeati378 – 40730ANK 1CuratedAdd
    BLAST
    Repeati411 – 44030ANK 2CuratedAdd
    BLAST
    Repeati444 – 47330ANK 3CuratedAdd
    BLAST
    Repeati477 – 50630ANK 4CuratedAdd
    BLAST
    Repeati510 – 53930ANK 5CuratedAdd
    BLAST
    Repeati543 – 57230ANK 6CuratedAdd
    BLAST
    Repeati576 – 60530ANK 7CuratedAdd
    BLAST
    Repeati609 – 63830ANK 8CuratedAdd
    BLAST
    Repeati875 – 90430ANK 9CuratedAdd
    BLAST
    Repeati1164 – 119633ANK 10CuratedAdd
    BLAST
    Domaini1312 – 139685DeathPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni267 – 33468Calmodulin-bindingBy similarityAdd
    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.CuratedPROSITE-ProRule annotation
    Contains 1 death domain.CuratedPROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000114993.
    HOGENOMiHOG000082489.
    HOVERGENiHBG051296.
    InParanoidiQ80YE7.
    KOiK08803.
    OMAiCLAEHGA.
    OrthoDBiEOG7QZGBH.
    PhylomeDBiQ80YE7.
    TreeFamiTF314166.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    1.25.40.20. 3 hits.
    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.
    PfamiPF12796. Ank_2. 3 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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1Curated (identifier: Q80YE7-1) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    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 IRHPNVITLH EVYENKTDVI LILELVAGGE 100
    LFDFLAEKES LTEEEATEFL KQILSGVYYL HSLQIAHFDL KPENIMLLDR 150
    NVPKPRIKII DFGLAHKIDF GNEFKNIFGT PEFVAPEIVN YEPLGLEADM 200
    WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYDFEEEF FRNTSTLAKD 250
    FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA 300
    ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH 350
    AINDDNVPGL QHLLGSLSSY DVNQPNKHGT PPLLIAAGCG NIQMLQLLIK 400
    RGSRIDVQDK GGSNAIYWAS RHGHVDTLKF LNENKCPLDV KDKSGETALH 450
    VAARYGHADV VQLLCSFGSN PDFQDKEEET PLHCAAWHGY YSVAKALCEV 500
    GCNVNIKNRE GETPLLTASA RGYHDIVECL AEHGADLNAS DKDGHIALHL 550
    AVRRCQMEVI KTLLGHGSFV DFQDRHGNTP LHVACKDGSA PIVVALCEAS 600
    CNLDISNKYG RTPLHLAANN GILDVVRYLC LMGANVEALT SDGKTAEDLA 650
    KAEQHEHVAG LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK 700
    STLVESLKCG LLRSFFRRRR PRLSSTNSTR FPPSPLAAKP TVSVSINNLY 750
    PGCENVSVRS RSMMFEPGLT KGMLEVFVAP SHHLHCSTDD QSTKAIDIQN 800
    AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHIIVF SLEEPYEIQL 850
    NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL RVVLVATHAD IMNIPRPAGG 900
    EFGYDKDTSL LKEIRNRFGN DLHVSNKLFV LDAGASGSKD IKVLRNHLQE 950
    IRSQIVSGCS PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN 1000
    PLASEDDLRR IAQQLHSTGE INIMQSETVQ DVLLLDPRWL CTNVLGKLLS 1050
    VETPRALHHY RGRYTMEDIQ RLVPDSDVEE LLQILDAMDI CARDLSSGTM 1100
    VDIPALIKTD SLQRSWADEE DEVMVYGGVR IVPVEHLTPF PCGIFHKVQV 1150
    NLCRWIHQQS AEGDADIRLW VSGCRIANRG AELLVLLVNH GQGIEVQVRG 1200
    LETEKIKCCL LLDSVCSTIE TVMATTLPGL LTVKHYLSPQ QLREHHEPVM 1250
    VYQPRDFFRA QTLKESSLTN TMGGYKESFS SITCFGCHDV YSQASLGMDI 1300
    HASDLSLLTR RKLSRLLDPP DPMGKDWCLL AMNLGLPDMV AKHNVNNRAS 1350
    RDFLPSPVHA LLQEWTSYPE STVGILISKL RELGRRDAAD FLLKASSVFK 1400
    INLDGNGQEA YASSCNSGTS YNSISSVVSR RDSHAWTPLY DL 1442
    Length:1,442
    Mass (Da):161,442
    Last modified:November 28, 2003 - v3
    Checksum:i243A14D7C6598F63
    GO
    Isoform 2Curated (identifier: Q80YE7-2) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    The sequence of this isoform differs from the canonical sequence as follows:
         1431-1442: Missing.

    Show »
    Length:1,430
    Mass (Da):159,986
    Checksum:iFB5B401603C273D9
    GO

    Sequence cautioni

    The sequence AAH21490.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti354 – 3541D → N in CAA65762. 1 PublicationCurated
    Sequence conflicti441 – 4411K → Q in AAH57317. (PubMed:15489334)Curated
    Sequence conflicti441 – 4411K → Q in AAH60161. (PubMed:15489334)Curated
    Sequence conflicti461 – 4611V → A in CAA65762. 1 PublicationCurated
    Sequence conflicti960 – 9601S → P in CAA65762. 1 PublicationCurated
    Sequence conflicti1000 – 10001N → T in CAA65762. 1 PublicationCurated
    Sequence conflicti1038 – 10425RWLCT → PMALH in CAA65762. 1 PublicationCurated
    Sequence conflicti1105 – 11051A → V in AAO91934. (PubMed:11485996)Curated
    Sequence conflicti1105 – 11051A → V in AAO91935. (PubMed:11485996)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1431 – 144212Missing in isoform 2. 4 PublicationsVSP_050629Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY245540 mRNA. Translation: AAO91934.2.
    AY245541 mRNA. Translation: AAO91935.1.
    X97048 mRNA. Translation: CAA65762.1.
    BC021490 mRNA. Translation: AAH21490.1. Different initiation.
    BC026671 mRNA. Translation: AAH26671.1.
    BC057317 mRNA. Translation: AAH57317.1.
    BC060161 mRNA. Translation: AAH60161.1.
    AK013153 mRNA. Translation: BAB28681.1.
    CCDSiCCDS26581.1. [Q80YE7-2]
    RefSeqiNP_001272846.1. NM_001285917.1. [Q80YE7-1]
    NP_083929.2. NM_029653.3. [Q80YE7-2]
    NP_598823.1. NM_134062.2. [Q80YE7-2]
    XP_006517433.1. XM_006517370.1. [Q80YE7-1]
    UniGeneiMm.24103.

    Genome annotation databases

    EnsembliENSMUST00000044083; ENSMUSP00000040825; ENSMUSG00000021559. [Q80YE7-2]
    ENSMUST00000077453; ENSMUSP00000076666; ENSMUSG00000021559. [Q80YE7-2]
    GeneIDi69635.
    KEGGimmu:69635.
    UCSCiuc007qvm.1. mouse. [Q80YE7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY245540 mRNA. Translation: AAO91934.2 .
    AY245541 mRNA. Translation: AAO91935.1 .
    X97048 mRNA. Translation: CAA65762.1 .
    BC021490 mRNA. Translation: AAH21490.1 . Different initiation.
    BC026671 mRNA. Translation: AAH26671.1 .
    BC057317 mRNA. Translation: AAH57317.1 .
    BC060161 mRNA. Translation: AAH60161.1 .
    AK013153 mRNA. Translation: BAB28681.1 .
    CCDSi CCDS26581.1. [Q80YE7-2 ]
    RefSeqi NP_001272846.1. NM_001285917.1. [Q80YE7-1 ]
    NP_083929.2. NM_029653.3. [Q80YE7-2 ]
    NP_598823.1. NM_134062.2. [Q80YE7-2 ]
    XP_006517433.1. XM_006517370.1. [Q80YE7-1 ]
    UniGenei Mm.24103.

    3D structure databases

    ProteinModelPortali Q80YE7.
    SMRi Q80YE7. Positions 3-320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 213581. 3 interactions.
    IntActi Q80YE7. 3 interactions.

    PTM databases

    PhosphoSitei Q80YE7.

    Proteomic databases

    PaxDbi Q80YE7.
    PRIDEi Q80YE7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000044083 ; ENSMUSP00000040825 ; ENSMUSG00000021559 . [Q80YE7-2 ]
    ENSMUST00000077453 ; ENSMUSP00000076666 ; ENSMUSG00000021559 . [Q80YE7-2 ]
    GeneIDi 69635.
    KEGGi mmu:69635.
    UCSCi uc007qvm.1. mouse. [Q80YE7-1 ]

    Organism-specific databases

    CTDi 1612.
    MGIi MGI:1916885. Dapk1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000114993.
    HOGENOMi HOG000082489.
    HOVERGENi HBG051296.
    InParanoidi Q80YE7.
    KOi K08803.
    OMAi CLAEHGA.
    OrthoDBi EOG7QZGBH.
    PhylomeDBi Q80YE7.
    TreeFami TF314166.

    Miscellaneous databases

    NextBioi 329950.
    PROi Q80YE7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q80YE7.
    CleanExi MM_DAPK1.
    Genevestigatori Q80YE7.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    1.25.40.20. 3 hits.
    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 PF12796. Ank_2. 3 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 new form of death-associated protein kinase that promotes cell survival."
      Jin Y., Blue E.K., Dixon S., Hou L., Wysolmerski R.B., Gallagher P.J.
      J. Biol. Chem. 276:39667-39678(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
      Tissue: EmbryoImported.
    2. Kimchi A.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: BrainImported.
    3. "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] (ISOFORM 2).
      Strain: C57BL/6Imported.
      Tissue: BrainImported and Mammary gland1 Publication.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1203-1442 (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Embryo.
    5. "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.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "DAP-kinase is a mediator of endoplasmic reticulum stress-induced caspase activation and autophagic cell death."
      Gozuacik D., Bialik S., Raveh T., Mitou G., Shohat G., Sabanay H., Mizushima N., Yoshimori T., Kimchi A.
      Cell Death Differ. 15:1875-1886(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEPHOSPHORYLATION AT SER-308, ENZYME REGULATION.
    8. "DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke."
      Tu W., Xu X., Peng L., Zhong X., Zhang W., Soundarapandian M.M., Balel C., Wang M., Jia N., Zhang W., Lew F., Chan S.L., Chen Y., Lu Y.
      Cell 140:222-234(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH GRIN2B, PHOSPHORYLATION AT SER-308, DISRUPTION PHENOTYPE.
    9. "Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages."
      Arif A., Chatterjee P., Moodt R.A., Fox P.L.
      Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiDAPK1_MOUSE
    AccessioniPrimary (citable) accession number: Q80YE7
    Secondary accession number(s): Q80YE6
    , Q8R341, Q8VDN6, Q9CSD4, Q9JJP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2003
    Last sequence update: November 28, 2003
    Last modified: October 1, 2014
    This is version 120 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3