EKS-HOS-00422
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00422
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
CAMK/DAPK481.92.1E-14413275263
StatusReviewed
Ensembl ProteinENSP00000301264
UniProt AccessionO43293; A0AVN4; B3KQE2; Q05JY4;
Protein NameDeath-associated protein kinase 3
Protein Synonyms/Alias DAP kinase 3; DAP-like kinase; Dlk; MYPT1 kinase; Zipper-interacting protein kinase; ZIP-kinase;
Gene NameDAPK3
Gene Synonyms/Alias DAPK3; ZIPK;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000167657ENSP00000470168ENST00000594894
ENSG00000167657ENSP00000442973ENST00000545797
ENSG00000167657ENSP00000301264ENST00000301264
ENSG00000167657ENSP00000472988ENST00000601824
ENSG00000167657ENSP00000471154ENST00000596311
ENSG00000167657ENSP00000470115ENST00000593844
OrganismHomo sapiens
Functional DescriptionSerine/threonine kinase which is involved in theregulation 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. Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B.
Protein Length454
Protein 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 454
Nucleotide Sequence
(FASTA)
ATGTCCACGT TCAGGCAGGA GGACGTGGAG GACCATTATG AGATGGGGGA GGAGCTGGGC 60
AGCGGCCAGT TTGCGATCGT GCGGAAGTGC CGGCAGAAGG GCACGGGCAA GGAGTACGCA 120
GCCAAGTTCA TCAAGAAGCG CCGCCTGTCA TCCAGCCGGC GTGGGGTGAG CCGGGAGGAG 180
ATCGAGCGGG AGGTGAACAT CCTGCGGGAG ATCCGGCACC CCAACATCAT CACCCTGCAC 240
GACATCTTCG AGAACAAGAC GGACGTGGTC CTCATCCTGG AGCTGGTCTC TGGCGGGGAG 300
CTCTTTGACT TCCTGGCGGA GAAGGAGTCG CTGACGGAGG ACGAGGCCAC CCAGTTCCTC 360
AAGCAGATCC TGGACGGCGT TCACTACCTG CACTCTAAGC GCATCGCACA CTTTGACCTG 420
AAGCCGGAAA ACATCATGCT GCTGGACAAG AACGTGCCCA ACCCACGAAT CAAGCTCATC 480
GACTTCGGCA TCGCGCACAA GATCGAGGCG GGGAACGAGT TCAAGAACAT CTTCGGCACC 540
CCGGAGTTTG TGGCCCCAGA GATTGTGAAC TATGAGCCGC TGGGCCTGGA GGCGGACATG 600
TGGAGCATCG GTGTCATCAC CTATATCCTC CTGAGCGGTG CATCCCCGTT CCTGGGCGAG 660
ACCAAGCAGG AGACGCTCAC CAACATCTCA GCCGTGAACT ACGACTTCGA CGAGGAGTAC 720
TTCAGCAACA CCAGCGAGCT GGCCAAGGAC TTCATTCGCC GGCTGCTCGT CAAAGATCCC 780
AAGCGGAGAA TGACCATTGC CCAGAGCCTG GAACATTCCT GGATTAAGGC GATCCGGCGG 840
CGGAACGTGC GTGGTGAGGA CAGCGGCCGC AAGCCCGAGC GGCGGCGCCT GAAGACCACG 900
CGTCTGAAGG AGTACACCAT CAAGTCGCAC TCCAGCTTGC CGCCCAACAA CAGCTACGCC 960
GACTTCGAGC GCTTCTCCAA GGTGCTGGAG GAGGCGGCGG CCGCCGAGGA GGGCCTGCGC 1020
GAGCTGCAGC GCAGCCGGCG GCTCTGCCAC GAGGACGTGG AGGCGCTGGC CGCCATCTAC 1080
GAGGAGAAGG AGGCCTGGTA CCGCGAGGAG AGCGACAGCC TGGGCCAGGA CCTGCGGAGG 1140
CTACGGCAGG AGCTGCTCAA GACCGAGGCG CTCAAGCGGC AGGCGCAGGA GGAGGCCAAG 1200
GGCGCGCTGC TGGGGACCAG CGGCCTCAAG CGCCGCTTCA GCCGCCTGGA GAACCGCTAC 1260
GAGGCGCTGG CCAAGCAAGT AGCCTCCGAG ATGCGCTTCG TGCAGGACCT CGTGCGCGCC 1320
CTGGAGCAGG AGAAGCTGCA GGGCGTGGAG TGCGGGCTGC GCTAG 1365
Domain Profile
S: 1     letgkelgsGkfavvrkcrekstGkeyaakflkkrrlkssrrgvsreeierevavlkeir  60
         +e+g+elgsG+fa+vrkcr+k tGkeyaakf+kkrrl+ssrrgvsreeierev++l+eir
Q: 13    YEMGEELGSGQFAIVRKCRQKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIR  72
         5789********************************************************
S: 61    sepnvinlhevyenksdvililelvaGGelfdllaekeslseeeatellkqilegvkylh  120
          +pn+i+lh+++enk+dv+lilelv+GGelfd+laekesl+e+eat++lkqil+gv+ylh
Q: 73    -HPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLH  131
         .***********************************************************
S: 121   skkivhldlkPenillldkkvpkgdiklidfGlsrkieegaelkeilGtPefvaPeivny  180
         sk+i+h+dlkPeni+lldk+vp+++iklidfG+++kie+g+e+k+i+GtPefvaPeivny
Q: 132   SKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIFGTPEFVAPEIVNY  191
         ************************************************************
S: 181   eplsletdmwsiGvityillsgasPflGdtkqetllnisavnldfseelfssvselakdf  240
         epl+le+dmwsiGvityillsgasPflG+tkqetl+nisavn+df+ee+fs++selakdf
Q: 192   EPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAKDF  251
         ************************************************************
S: 241   irrllvkdpekrltieeclehswl  264
         irrllvkdp++r+ti+++lehsw+
Q: 252   IRRLLVKDPKRRMTIAQSLEHSWI  275
         ***********************8
Domain Sequence
(FASTA)
YEMGEELGSG QFAIVRKCRQ KGTGKEYAAK FIKKRRLSSS RRGVSREEIE REVNILREIR 60
HPNIITLHDI FENKTDVVLI LELVSGGELF DFLAEKESLT EDEATQFLKQ ILDGVHYLHS 120
KRIAHFDLKP ENIMLLDKNV PNPRIKLIDF GIAHKIEAGN EFKNIFGTPE FVAPEIVNYE 180
PLGLEADMWS IGVITYILLS GASPFLGETK QETLTNISAV NYDFDEEYFS NTSELAKDFI 240
RRLLVKDPKR RMTIAQSLEH SWI 263
Keyword3D-structure; Activator; Alternative splicing; Apoptosis; ATP-binding; Centromere; Chromatin regulator; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transcription; Transcription regulation; Transferase; Ubl conjugation.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Bos taurus"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Ciona intestinalis"; ?>Danio rerio"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Ochotona princeps"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Procavia capensis"; ?>Pteropus vampyrus"; ?>Rattus norvegicus"; ?>Sorex araneus"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Tupaia belangeri"; ?>Tursiops truncatus"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00387
EKS-BOT-00412
EKS-CAJ-00417
EKS-CAF-00415
EKS-CAP-00440
EKS-CII-00239
EKS-DAR-00801
EKS-EQC-00405
EKS-FEC-00399
EKS-GAM-00241
EKS-GAA-00504
EKS-GOG-00407
EKS-ICT-00395
EKS-LAC-00429
EKS-LOA-00425
EKS-MAM-00411
EKS-MEG-00343
EKS-MOD-00401
EKS-MUM-00450
EKS-MUP-00409
EKS-MYL-00407
EKS-OCP-00088
EKS-ORN-00526
EKS-ORA-00360
EKS-ORL-00480
EKS-OTG-00418
EKS-PAT-00390
EKS-PES-00368
EKS-POA-00406
EKS-PRC-00016
EKS-PTV-00118
EKS-RAN-00431
EKS-SOA-00016
EKS-TAG-00482
EKS-TAR-00521
EKS-TEN-00522
EKS-TUB-00015
EKS-TUT-00127
EKS-XIM-00516
Gene Ontology
GO:0000775; C:chromosome, centromeric region
GO:0005815; C:microtubule organizing center
GO:0005634; C:nucleus
GO:0016605; C:PML body
GO:0005524; F:ATP binding
GO:0042803; F:protein homodimerization activity
GO:0004674; F:protein serine/threonine kinase activity
GO:0006915; P:apoptotic process
GO:0016568; P:chromatin modification
GO:0000910; P:cytokinesis
GO:0006917; P:induction of apoptosis
GO:0007243; P:intracellular protein kinase cascade
GO:0030182; P:neuron differentiation
GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway
GO:0046777; P:protein autophosphorylation
GO:2000249; P:regulation of actin cytoskeleton reorganization
GO:0010506; P:regulation of autophagy
GO:2000145; P:regulation of cell motility
GO:0007088; P:regulation of mitosis
GO:0006940; P:regulation of smooth muscle contraction
GO:0006355; P:regulation of transcription, DNA-dependent
GO:0006351; P:transcription, DNA-dependent
KEGG
hsa:1613;
InterPros
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; 1.
SMARTs
SM00220; S_TKc; 1.
Prosites
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Prints
Created Date20-Feb-2013