Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q80YE7

- DAPK1_MOUSE

UniProt

Q80YE7 - DAPK1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (2)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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

Mg2+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 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
Complete GO annotation...

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

ReactomeiREACT_252543. Role of DCC in regulating apoptosis.

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
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
Complete GO annotation...

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

MaxQBiQ80YE7.
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

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. DAP kinase subfamily.Curated
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.
GeneTreeiENSGT00760000118877.
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.
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

        10         20         30         40         50
MTVFRQENVD DYYDTGEELG SGQFAVVKKC REKSTGLQYA AKFIKKRRTK 
        60         70         80         90        100
SSRRGVSRED IEREVSILKE IRHPNVITLH EVYENKTDVI LILELVAGGE 
       110        120        130        140        150
LFDFLAEKES LTEEEATEFL KQILSGVYYL HSLQIAHFDL KPENIMLLDR 
       160        170        180        190        200
NVPKPRIKII DFGLAHKIDF GNEFKNIFGT PEFVAPEIVN YEPLGLEADM 
       210        220        230        240        250
WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYDFEEEF FRNTSTLAKD 
       260        270        280        290        300
FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA 
       310        320        330        340        350
ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH 
       360        370        380        390        400
AINDDNVPGL QHLLGSLSSY DVNQPNKHGT PPLLIAAGCG NIQMLQLLIK 
       410        420        430        440        450
RGSRIDVQDK GGSNAIYWAS RHGHVDTLKF LNENKCPLDV KDKSGETALH 
       460        470        480        490        500
VAARYGHADV VQLLCSFGSN PDFQDKEEET PLHCAAWHGY YSVAKALCEV 
       510        520        530        540        550
GCNVNIKNRE GETPLLTASA RGYHDIVECL AEHGADLNAS DKDGHIALHL 
       560        570        580        590        600
AVRRCQMEVI KTLLGHGSFV DFQDRHGNTP LHVACKDGSA PIVVALCEAS 
       610        620        630        640        650
CNLDISNKYG RTPLHLAANN GILDVVRYLC LMGANVEALT SDGKTAEDLA 
       660        670        680        690        700
KAEQHEHVAG LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK 
       710        720        730        740        750
STLVESLKCG LLRSFFRRRR PRLSSTNSTR FPPSPLAAKP TVSVSINNLY 
       760        770        780        790        800
PGCENVSVRS RSMMFEPGLT KGMLEVFVAP SHHLHCSTDD QSTKAIDIQN 
       810        820        830        840        850
AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHIIVF SLEEPYEIQL 
       860        870        880        890        900
NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL RVVLVATHAD IMNIPRPAGG 
       910        920        930        940        950
EFGYDKDTSL LKEIRNRFGN DLHVSNKLFV LDAGASGSKD IKVLRNHLQE 
       960        970        980        990       1000
IRSQIVSGCS PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN 
      1010       1020       1030       1040       1050
PLASEDDLRR IAQQLHSTGE INIMQSETVQ DVLLLDPRWL CTNVLGKLLS 
      1060       1070       1080       1090       1100
VETPRALHHY RGRYTMEDIQ RLVPDSDVEE LLQILDAMDI CARDLSSGTM 
      1110       1120       1130       1140       1150
VDIPALIKTD SLQRSWADEE DEVMVYGGVR IVPVEHLTPF PCGIFHKVQV 
      1160       1170       1180       1190       1200
NLCRWIHQQS AEGDADIRLW VSGCRIANRG AELLVLLVNH GQGIEVQVRG 
      1210       1220       1230       1240       1250
LETEKIKCCL LLDSVCSTIE TVMATTLPGL LTVKHYLSPQ QLREHHEPVM 
      1260       1270       1280       1290       1300
VYQPRDFFRA QTLKESSLTN TMGGYKESFS SITCFGCHDV YSQASLGMDI 
      1310       1320       1330       1340       1350
HASDLSLLTR RKLSRLLDPP DPMGKDWCLL AMNLGLPDMV AKHNVNNRAS 
      1360       1370       1380       1390       1400
RDFLPSPVHA LLQEWTSYPE STVGILISKL RELGRRDAAD FLLKASSVFK 
      1410       1420       1430       1440 
INLDGNGQEA YASSCNSGTS YNSISSVVSR RDSHAWTPLY DL
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

MaxQBi Q80YE7.
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 ENSGT00760000118877.
HOGENOMi HOG000082489.
HOVERGENi HBG051296.
InParanoidi Q80YE7.
KOi K08803.
OMAi CLAEHGA.
OrthoDBi EOG7QZGBH.
PhylomeDBi Q80YE7.
TreeFami TF314166.

Enzyme and pathway databases

Reactomei REACT_252543. Role of DCC in regulating apoptosis.

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.
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

« Hide 'large scale' publications
  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.
+Additional computationally mapped references.

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: January 7, 2015
This is version 123 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
© 2002– 2015 UniProt Consortium | License & Disclaimer