CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000823
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Death-associated protein kinase 3 
Protein Synonyms/Alias
 DAP kinase 3; DAP-like kinase; Dlk; MYPT1 kinase; ZIP-kinase 
Gene Name
 Dapk3 
Gene Synonyms/Alias
 Zipk 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
405LLGAGGLKRRLCRLEubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation, 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 (By similarity). Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, its association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. 
Sequence Annotation
 DOMAIN 13 275 Protein kinase.
 NP_BIND 19 27 ATP (By similarity).
 REGION 161 204 Activation segment (By similarity).
 REGION 276 328 Interaction with AR (By similarity).
 REGION 277 306 Interaction with MYPT1 (By similarity).
 REGION 390 448 Interaction with CDC5L (By similarity).
 REGION 422 436 Leucine-zipper (By similarity).
 ACT_SITE 139 139 Proton acceptor (By similarity).
 BINDING 42 42 ATP (Probable).
 BINDING 94 94 Inhibitor (By similarity).
 BINDING 96 96 Inhibitor (By similarity).
 MOD_RES 180 180 Phosphothreonine (By similarity).
 MOD_RES 225 225 Phosphothreonine (By similarity).
 MOD_RES 265 265 Phosphothreonine; by autocatalysis;
 MOD_RES 265 265 Phosphothreonine; by ROCK1; alternate (By
 MOD_RES 304 304 Phosphoserine; by DAPK1 (By similarity).
 MOD_RES 306 306 Phosphoserine; by autocatalysis and DAPK1
 MOD_RES 307 307 Phosphoserine; by DAPK1 (By similarity).
 MOD_RES 313 313 Phosphoserine; by DAPK1 (By similarity).
 MOD_RES 321 321 Phosphoserine; by DAPK1 (By similarity).  
Keyword
 Activator; Apoptosis; ATP-binding; Centromere; Chromatin regulator; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transcription; Transcription regulation; Transferase; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 448 AA 
Protein Sequence
MSTFRQEDVE DHYEMGEELG SGQFAIVRKC QQKGTGMEYA AKFIKKRRLP SSRRGVSREE 60
IEREVSILRE IRHPNIITLH DVFENKTDVV LILELVSGGE LFDFLAEKES LTEDEATQFL 120
KQILDGVHYL HSKRIAHFDL KPENIMLLDK HAASPRIKLI DFGIAHRIEA GSEFKNIFGT 180
PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGE TKQETLTNIS AVNYDFDEEY 240
FSSTSELAKD FIRRLLVKDP KRRMTIAQSL EHSWIKVRRR EDGARKPERR RLRAARLREY 300
SLKSHSSMPR NTSYASFERF SRVLEDVAAA EQGLRELQRG RRQCRERVCA LRAAAEQREA 360
RCRDGSAGLG RDLRRLRTEL GRTEALRTRA QEEARAALLG AGGLKRRLCR LENRYDALAA 420
QVAAEVQFVR DLVRALEQER LQAECGVR 448 
Gene Ontology
 GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0071346; P:cellular response to interferon-gamma; IMP:UniProtKB.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0006917; P:induction of apoptosis; IMP:UniProtKB.
 GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
 GO:0017148; P:negative regulation of translation; IEA:Compara.
 GO:0030182; P:neuron differentiation; IEA:Compara.
 GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; IEA:Compara.
 GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Compara.
 GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR020675; Myosin_light_ch_kinase-rel.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS