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Protein Page:
DAPK3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DAPK3 Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, actin cytoskeleton reorganization, cell motility, smooth muscle contraction, and mitosis, particularly cytokinesis. 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. Regulates myosin phosphorylation in both smooth muscle and non- muscle cells. In smooth muscle, regulates myosin either directly by phosphorylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A, and the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca(2+) and promote a contractile state. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates STAT3 and enhances its transcriptional activity. Positively regulates the canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Can disrupt the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis. Involved in the formation of promyelocytic leukemia protein nuclear body (PML-NB), one of many subnuclear domains in the eukaryotic cell nucleus, and which is involved in oncogenesis and viral infection. Monomer and homotrimer. Can also exist as homodimer or form heterodimers with ATF4. Homodimerization is required for activation segment autophosphorylation Both interactions require an intact leucine zipper domain and oligomerization is required for full enzymatic activity. Also binds to DAXX and PAWR, possibly in a ternary complex which plays a role in caspase activation. According to PubMed:17953487, does not interact with PARW. Interacts with AATF, CDC5L, UBE2D1, UBE2D2 AND UBE2D3. Interacts with AR and this interaction is enhanced by AATF. Interacts (via leucine zipper) with TCP10L (via leucine zipper). Interacts (via kinase domain) with DAPK1 (via kinase domain).Interacts with STAT3, NLK and TCF7L2. Isoform 1 and isoform 2 can interact with myosin and PPP1R12A. Isoform 2 is expressed in the bladder smooth muscle. Inhibited by pyridone 6 (K00225), a potent, ATP-competitive inhibitor. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. Oligomerization is required for full enzymatic activity. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. DAP kinase subfamily. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, Ser/Thr (non-receptor); EC 2.7.11.1; Kinase, protein; Protein kinase, CAMK; CAMK group; DAPK family
Cellular Component: PML body; cytoplasm; microtubule organizing center; nucleus; chromosome, pericentric region
Molecular Function: identical protein binding; protein serine/threonine kinase activity; leucine zipper domain binding; protein homodimerization activity; calmodulin-dependent protein kinase activity; ATP binding
Biological Process: regulation of smooth muscle contraction; neuron differentiation; regulation of apoptosis; transcription, DNA-dependent; regulation of transcription, DNA-dependent; apoptosis; negative regulation of translation; protein amino acid autophosphorylation; regulation of mitosis; cytokinesis; regulation of autophagy; chromatin modification; protein amino acid phosphorylation
Reference #:  O43293 (UniProtKB)
Alt. Names/Synonyms: DAP kinase 3; DAP-like kinase; DAPK3; Death-associated protein kinase 3; Dlk; FLJ36473; ZIP; ZIP kinase isoform; ZIP-kinase; ZIPK
Gene Symbols: DAPK3
Molecular weight: 52,536 Da
Basal Isoelectric point: 6.44  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DAPK3

Protein Structure Not Found.

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Sites Implicated In
cytoskeletal reorganization: T265‑p
enzymatic activity, induced: T180‑p, T225‑p, T265‑p
intracellular localization: T299‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K37-m1 CRQKGTGkEYAAKFI
0 7 S50-p FIKKRRLsSSRRGVS
0 2 S51 IKKRRLsSSRRGVSR
0 2 S52 KKRRLsSSRRGVSRE
0 1 K167-ub IDFGIAHkIEAGNEF
1 0 T180-p EFKNIFGtPEFVAPE
2 0 T225-p LGETKQEtLTNISAV
3 1 T265-p KDPKRRMtIAQSLEH
0 1 K276 SLEHSWIKAIRRRNV
3 0 T299-p PERRRLKtTRLKEyt
0 6 Y305-p KtTRLKEytIKSHss
1 1 T306-p tTRLKEytIKSHssL
2 1 S311-p EytIKSHssLPPNNS
0 2 S312-p ytIKSHssLPPNNSy
0 1 N317 HssLPPNNSyADFER
0 4 S318 ssLPPNNSyADFERF
0 2 Y319-p sLPPNNSyADFERFS
0 2 D321 PPNNSyADFERFSkV
0 1 K327-ub ADFERFSkVLEEAAA
0 1 T388-p LRQELLKtEALKRQA
0 6 K410 LLGTSGLKRRFsRLE
0 1 S414-p SGLKRRFsRLENRYE
0 1 K425-ub NRYEALAkQVASEMR
  mouse

 
M37 CQQKGTGMEYAAKFI
P50 FIKKRRLPssRRGVS
S51-p IKKRRLPssRRGVSR
S52-p KKRRLPssRRGVSRE
R167 IDFGIAHRIEAGSEF
T180 EFKNIFGTPEFVAPE
T225 LGETKQETLTNISAV
T265-p KDPKRRMtIAQSLEH
K276-ac SLEHSWIkVRRREDG
A294 PERRRLRAARLREYs
Y300 RAARLREYsLKSHSS
S301-p AARLREYsLKSHSSM
S306 EYsLKSHSSMPRNts
S307 YsLKSHSSMPRNtsy
T312-p HSSMPRNtsyAsFER
S313-p SSMPRNtsyAsFERF
Y314-p SMPRNtsyAsFERFS
S316-p PRNtsyAsFERFSRV
R322 AsFERFSRVLEDVAA
T383 LRTELGRTEALRTRA
K405-ub LLGAGGLkRRLCRLE
C409 GGLkRRLCRLENRYD
A420 NRYDALAAQVAAEVQ
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