dbPAF Protein Information


Tag Content
dbPAF ID dbPAF-0001497
Uniprot Accession O43293; DAPK3_HUMAN; A0AVN4; B3KQE2; Q05JY4;
Genbank Protein ID NP_001339.1; XP_005259565.1;
Genbank Nucleotide ID NM_001348.2; XM_005259508.1;
Protein Name Death-associated protein kinase 3
Protein Synonyms/Alias
Gene Name DAPK3
Gene Synonyms/Alias ZIPK;
Organism Homo sapiens(Human)
NCBI Taxa ID 9606
Functional Description
(View all)
Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Involved in the regulation of smooth muscle contraction. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in regulation of starvation-induced autophagy. 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; the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca(2+) and promote a contractile state. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton. Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B. Overexpression leads to condensation of actin stress fibers into thick bundles. Involved in actin filament focal adhesion dynamics. The function in both reorganization of actin cytoskeleton and focal adhesion dissolution is modulated by RhoD. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Involved in regulation of cell cycle progression and cell proliferation. May be a tumor suppressor.
Phosphorylation Sites
dbPAF PTMs: 17
PositionPeptidesSourceReferences ( PMIDs )
39QKGTGKEYAAKFIKKPhosphoSitePlus22135298
50FIKKRRLSSSRRGVSdbPTM 3.0;PhosphoSitePlus18239682; 16381945; 23193290; 22135298
180EFKNIFGTPEFVAPEdbPTM 3.0;Phospho.ELM 9.0;PhosphoSitePlus;UniProt;curated15611134; 17158456; 16381945; 23193290; 22135298; 22817900
225LGETKQETLTNISAVdbPTM 3.0;Phospho.ELM 9.0;PhosphoSitePlus;UniProt;curated15611134; 16381945; 23193290; 17158456; 22135298; 22817900
265KDPKRRMTIAQSLEHdbPTM 3.0;Phospho.ELM 9.0;PhosphoSitePlus;curated15611134; 16325270; 17158456; 18239682; 16381945; 23193290;
299PERRRLKTTRLKEYTdbPTM 3.0;Phospho.ELM 9.0;PhosphoSitePlus;curated15367680; 15611134; 17158456; 20854903; 16381945; 23193290;
300ERRRLKTTRLKEYTIcurated26074081
305KTTRLKEYTIKSHSSPhosphoSitePlus;curated22135298; 26267517
306TTRLKEYTIKSHSSLdbPTM 3.0;Phospho.ELM 9.0;PhosphoSitePlus;curated15611134; 16381945; 23193290; 22135298; 22817900
309LKEYTIKSHSSLPPNdbPTM 3.0;curated15367680; 16381945; 23193290; 23898821
311EYTIKSHSSLPPNNSdbPTM 3.0;Phospho.ELM 9.0;PhosphoSitePlus;curated15367680; 15611134; 16381945; 23193290; 17158456; 22135298;
312YTIKSHSSLPPNNSYdbPTM 3.0;PhosphoSitePlus;curated15367680; 16381945; 23193290; 22135298; 25627689; 23911959;
318SSLPPNNSYADFERFdbPTM 3.015367680; 16381945; 23193290
326YADFERFSKVLEEAAdbPTM 3.015367680; 16381945; 23193290
388LRQELLKTEALKRQAPhosphoSitePlus22135298
407KGALLGTSGLKRRFSPhosphoSitePlus;curated22135298; 25627689
414SGLKRRFSRLENRYEPhosphoSitePlus22135298
Sequence
(Fasta)
MSTFRQEDVE DHYEMGEELG SGQFAIVRKC RQKGTGKEYA AKFIKKRRLS SSRRGVSREE 60
IEREVNILRE IRHPNIITLH DIFENKTDVV LILELVSGGE LFDFLAEKES LTEDEATQFL 120
KQILDGVHYL HSKRIAHFDL KPENIMLLDK NVPNPRIKLI DFGIAHKIEA GNEFKNIFGT 180
PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGE TKQETLTNIS AVNYDFDEEY 240
FSNTSELAKD FIRRLLVKDP KRRMTIAQSL EHSWIKAIRR RNVRGEDSGR KPERRRLKTT 300
RLKEYTIKSH SSLPPNNSYA DFERFSKVLE EAAAAEEGLR ELQRSRRLCH EDVEALAAIY 360
EEKEAWYREE SDSLGQDLRR LRQELLKTEA LKRQAQEEAK GALLGTSGLK RRFSRLENRY 420
EALAKQVASE MRFVQDLVRA LEQEKLQGVE CGLR 455
Keyword

KW-0002--3D-structure
KW-0010--Activator
KW-0025--Alternative splicing
KW-0053--Apoptosis
KW-0067--ATP-binding
KW-0156--Chromatin regulator
KW-0181--Complete proteome
KW-0963--Cytoplasm
KW-0418--Kinase
KW-0547--Nucleotide-binding
KW-0539--Nucleus
KW-0597--Phosphoprotein
KW-0621--Polymorphism
KW-1185--Reference proteome
KW-0723--Serine/threonine-protein kinase
KW-0804--Transcription
KW-0805--Transcription regulation
KW-0808--Transferase
KW-0810--Translation regulation
KW-0043--Tumor suppressor

Interpro

IPR020636--Ca/CaM-dep_Ca-dep_prot_Kinase
IPR011009--Kinase-like_dom
IPR000719--Prot_kinase_dom
IPR017441--Protein_kinase_ATP_BS
IPR002290--Ser/Thr_dual-sp_kinase
IPR008271--Ser/Thr_kinase_AS

PROSITE

PS00107--PROTEIN_KINASE_ATP
PS50011--PROTEIN_KINASE_DOM
PS00108--PROTEIN_KINASE_ST

Pfam

PF00069--Pkinase

Gene Ontology

GO:0005884--C:actin filament
GO:0005737--C:cytoplasm
GO:0045121--C:membrane raft
GO:0005634--C:nucleus
GO:0016605--C:PML body
GO:0005524--F:ATP binding
GO:0004683--F:calmodulin-dependent protein kinase activity
GO:0008140--F:cAMP response element binding protein binding
GO:0042802--F:identical protein binding
GO:0043522--F:leucine zipper domain binding
GO:0042803--F:protein homodimerization activity
GO:0004674--F:protein serine/threonine kinase activity
GO:0017048--F:Rho GTPase binding
GO:0006915--P:apoptotic process
GO:0097190--P:apoptotic signaling pathway
GO:0071346--P:cellular response to interferon-gamma
GO:0016568--P:chromatin modification
GO:0000910--P:cytokinesis
GO:0035556--P:intracellular signal transduction
GO:0017148--P:negative regulation of translation
GO:0030182--P:neuron differentiation
GO:0043065--P:positive regulation of apoptotic process
GO:0090263--P:positive regulation of canonical Wnt signaling pathway
GO:0030335--P:positive regulation of cell migration
GO:2001241--P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand
GO:0046777--P:protein autophosphorylation
GO:0006468--P:protein phosphorylation
GO:2000249--P:regulation of actin cytoskeleton reorganization
GO:0042981--P:regulation of apoptotic process
GO:0010506--P:regulation of autophagy
GO:2000145--P:regulation of cell motility
GO:0008360--P:regulation of cell shape
GO:0051893--P:regulation of focal adhesion assembly
GO:0007346--P:regulation of mitotic cell cycle
GO:0007088--P:regulation of mitotic nuclear division
GO:0043519--P:regulation of myosin II filament organization
GO:0006940--P:regulation of smooth muscle contraction
GO:0006355--P:regulation of transcription, DNA-templated
GO:0006351--P:transcription, DNA-templated