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Protein

Death-associated protein kinase 3

Gene

DAPK3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 Ca2+ 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.16 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.6 Publications

Cofactori

Mg2+1 Publication

Enzyme regulationi

A sequential activation is proposed: autophosphorylation at consensus sites is leading to dimerization of the catalytic domain stabilized by phosphorylation at Ser-50 and activation segment exchange (producing an active confirmation of both kinase modules in trans) followed by phosphorylation at Thr-180 in the activation segment and at other regulatory sites (Probable). Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. Oligomerization is required for full enzymatic activity. Inhibited by pyridone 6 (K00225), a potent, ATP-competitive inhibitor.1 Publication3 Publications

Kineticsi

  1. KM=12 µM for myosin (isoform 2)1 Publication
  2. KM=6.2 µM for myosin (isoform 1)1 Publication
  3. KM=73 µM for MYL12B (isoform 2)1 Publication
  4. KM=10.4 µM for MYL12B (isoform 1)1 Publication
  1. Vmax=248 nmol/min/mg enzyme toward myosin (isoform 2)1 Publication
  2. Vmax=120 nmol/min/mg enzyme toward myosin (isoform 1)1 Publication
  3. Vmax=1.3 µmol/min/mg enzyme toward MYL12B (isoform 2)1 Publication
  4. Vmax=271 nmol/min/mg enzyme toward MYL12B (isoform 1)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421ATPCurated
Binding sitei94 – 941Inhibitor1 Publication
Binding sitei96 – 961Inhibitor1 Publication
Active sitei139 – 1391Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 279ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • calmodulin-dependent protein kinase activity Source: GO_Central
  • cAMP response element binding protein binding Source: ParkinsonsUK-UCL
  • identical protein binding Source: IntAct
  • leucine zipper domain binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • Rho GTPase binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • apoptotic signaling pathway Source: Ensembl
  • cellular response to interferon-gamma Source: UniProtKB
  • chromatin modification Source: UniProtKB-KW
  • cytokinesis Source: UniProtKB
  • intracellular signal transduction Source: UniProtKB
  • negative regulation of translation Source: UniProtKB
  • neuron differentiation Source: Ensembl
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of cell migration Source: Ensembl
  • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of actin cytoskeleton reorganization Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
  • regulation of autophagy Source: UniProtKB
  • regulation of cell motility Source: UniProtKB
  • regulation of cell shape Source: Ensembl
  • regulation of focal adhesion assembly Source: UniProtKB
  • regulation of mitotic cell cycle Source: UniProtKB
  • regulation of mitotic nuclear division Source: UniProtKB
  • regulation of myosin II filament organization Source: Ensembl
  • regulation of smooth muscle contraction Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_22128. Ligand-independent caspase activation via DCC.
SignaLinkiO43293.

Names & Taxonomyi

Protein namesi
Recommended name:
Death-associated protein kinase 3 (EC:2.7.11.16 Publications)
Short name:
DAP kinase 3
Alternative name(s):
DAP-like kinase
Short name:
Dlk
MYPT1 kinase
Zipper-interacting protein kinase
Short name:
ZIP-kinase
Gene namesi
Name:DAPK3
Synonyms:ZIPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:2676. DAPK3.

Subcellular locationi

Isoform 1 :
  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
Isoform 2 :
  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421K → A: Loss of kinase activity at low concentrations of ATP. 1 Publication
Mutagenesisi161 – 1611D → A: Loss of kinase activity. 1 Publication
Mutagenesisi180 – 1801T → A: Greatly reduced kinase activity. 1 Publication
Mutagenesisi225 – 2251T → A: Loss of kinase activity. 1 Publication
Mutagenesisi265 – 2651T → A: Loss of phosphorylation by ROCK1, catalytically inactive. 1 Publication
Mutagenesisi294 – 2952RR → AA: Cytoplasmic loalization. 1 Publication
Mutagenesisi299 – 3002TT → AA: Predominantly nuclear localization. 1 Publication
Mutagenesisi299 – 2991T → A: Loss of phosphorylation by ROCK1. 1 Publication
Mutagenesisi299 – 2991T → D: Predominantly cytoplasmic localization; phosphomimetic. 1 Publication
Mutagenesisi427 – 4271V → A: Predominantly nuclear localization; when associated with A-434 and A-441. 1 Publication
Mutagenesisi434 – 4341V → A: Predominantly nuclear localization; when associated with A-427 and A-441. 1 Publication
Mutagenesisi441 – 4411L → A: Predominantly nuclear localization; when associated with A-427 and A-434. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA27144.

Polymorphism and mutation databases

BioMutaiDAPK3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Death-associated protein kinase 3PRO_0000085914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501Phosphoserine; by autocatalysis1 Publication
Modified residuei180 – 1801Phosphothreonine2 Publications
Modified residuei225 – 2251Phosphothreonine1 Publication
Modified residuei265 – 2651Phosphothreonine; by autocatalysis and ROCK13 Publications
Modified residuei299 – 2991Phosphothreonine; by autocatalysis, DAPK1 and ROCK14 Publications
Modified residuei306 – 3061Phosphothreonine; by autocatalysis1 Publication
Modified residuei309 – 3091Phosphoserine; by DAPK11 Publication
Modified residuei311 – 3111Phosphoserine; by autocatalysis and DAPK12 Publications
Modified residuei312 – 3121Phosphoserine; by DAPK11 Publication
Modified residuei318 – 3181Phosphoserine; by DAPK11 Publication
Modified residuei326 – 3261Phosphoserine; by DAPK11 Publication

Post-translational modificationi

The phosphorylation status is critical for kinase activity, oligomerization and intracellular localization. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. The phosphorylated form is localized in the cytoplasm promoted by phosphorylation at Thr-299; nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation increases the trimeric form, and its dephosphorylation favors a kinase-inactive monomeric form. Both isoform 1 and isoform 2 can undergo autophosphorylation.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43293.
PaxDbiO43293.
PRIDEiO43293.

PTM databases

PhosphoSiteiO43293.

Expressioni

Tissue specificityi

Widely expressed. Isoform 1 and isoform 2 are expressed in the bladder smooth muscle.2 Publications

Gene expression databases

BgeeiO43293.
CleanExiHS_DAPK3.
ExpressionAtlasiO43293. baseline and differential.
GenevestigatoriO43293.

Organism-specific databases

HPAiHPA028569.

Interactioni

Subunit structurei

HUMAN FINAL Homooligomer in its kinase-active form (homotrimers and homodimers are reported); monomeric in its kinase-inactive form. Homodimerization is required for activation segment autophosphorylation (Probable). Isoform 1 and isoform 2 interact with myosin and PPP1R12A; interaction of isoform 1 with PPP1R12A is inhibited by RhoA dominant negative form. Interacts with NLK, DAXX, STAT3, RHOD (GTP-bound form) and TCP10L. Interacts with PAWR; the interaction is reported conflictingly: according to PubMed:17953487 does not interact with PAWR. Interacts with ULK1; may be a substrate of ULK1.1 Publication10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-77293,EBI-77293
PPP1R12AO149745EBI-77293,EBI-351726
Ppp1r12aQ107282EBI-9691390,EBI-918263From a different organism.
TCP10LQ8TDR45EBI-77293,EBI-3923210

Protein-protein interaction databases

BioGridi107983. 25 interactions.
IntActiO43293. 17 interactions.
MINTiMINT-6505325.
STRINGi9606.ENSP00000301264.

Structurei

Secondary structure

1
454
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 124Combined sources
Beta strandi13 – 219Combined sources
Beta strandi23 – 3210Combined sources
Turni33 – 353Combined sources
Beta strandi38 – 469Combined sources
Helixi49 – 513Combined sources
Beta strandi53 – 564Combined sources
Helixi58 – 7013Combined sources
Beta strandi79 – 846Combined sources
Beta strandi86 – 949Combined sources
Helixi101 – 1088Combined sources
Helixi113 – 13220Combined sources
Helixi142 – 1443Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi150 – 1545Combined sources
Beta strandi157 – 1593Combined sources
Helixi181 – 1833Combined sources
Helixi186 – 1894Combined sources
Helixi197 – 21216Combined sources
Helixi222 – 2309Combined sources
Helixi238 – 2414Combined sources
Helixi246 – 2538Combined sources
Helixi260 – 2623Combined sources
Helixi266 – 2716Combined sources
Helixi273 – 2808Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YRPX-ray3.10A/B1-277[»]
2J90X-ray2.00A/B9-289[»]
3BHYX-ray1.24A9-289[»]
3BQRX-ray1.75A9-289[»]
ProteinModelPortaliO43293.
SMRiO43293. Positions 2-277.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43293.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 275263Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni161 – 20444Activation segmentBy similarityAdd
BLAST
Regioni427 – 44115Leucine-zipper1 PublicationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000233016.
HOVERGENiHBG101549.
InParanoidiO43293.
KOiK08803.
OMAiSLEHPWI.
OrthoDBiEOG7QZGBH.
PhylomeDBiO43293.
TreeFamiTF314166.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR020675. Myosin_light_ch_kinase-rel.
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.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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. AlignAdd to basket

Isoform 1 (identifier: O43293-1) [UniParc]FASTAAdd to basket

Also known as: ZIPK-L

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
MSTFRQEDVE DHYEMGEELG SGQFAIVRKC RQKGTGKEYA AKFIKKRRLS
60 70 80 90 100
SSRRGVSREE IEREVNILRE IRHPNIITLH DIFENKTDVV LILELVSGGE
110 120 130 140 150
LFDFLAEKES LTEDEATQFL KQILDGVHYL HSKRIAHFDL KPENIMLLDK
160 170 180 190 200
NVPNPRIKLI DFGIAHKIEA GNEFKNIFGT PEFVAPEIVN YEPLGLEADM
210 220 230 240 250
WSIGVITYIL LSGASPFLGE TKQETLTNIS AVNYDFDEEY FSNTSELAKD
260 270 280 290 300
FIRRLLVKDP KRRMTIAQSL EHSWIKAIRR RNVRGEDSGR KPERRRLKTT
310 320 330 340 350
RLKEYTIKSH SSLPPNNSYA DFERFSKVLE EAAAAEEGLR ELQRSRRLCH
360 370 380 390 400
EDVEALAAIY EEKEAWYREE SDSLGQDLRR LRQELLKTEA LKRQAQEEAK
410 420 430 440 450
GALLGTSGLK RRFSRLENRY EALAKQVASE MRFVQDLVRA LEQEKLQGVE

CGLR
Length:454
Mass (Da):52,536
Last modified:June 1, 1998 - v1
Checksum:i56773008A6A61CF0
GO
Isoform 2 (identifier: O43293-2) [UniParc]FASTAAdd to basket

Also known as: ZIPK-S

The sequence of this isoform differs from the canonical sequence as follows:
     313-322: LPPNNSYADF → ASPIVAPVDA
     323-454: Missing.

Note: The internal splice site between exon 8 and the 3' UTR, which yields this truncated isoform, is non-canonical.

Show »
Length:322
Mass (Da):37,048
Checksum:i616983FE83F8DDA6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121T → M in a colorectal adenocarcinoma sample; somatic mutation; greatly reduces kinase acivity, increases cell proliferation and cell survival. 2 Publications
VAR_040438
Natural varianti161 – 1611D → N in an ovarian mucinous carcinoma sample; somatic mutation; greatly reduces kinase acivity, increases cell proliferation and cell survival. 2 Publications
VAR_040439
Natural varianti216 – 2161P → S in a lung neuroendocrine carcinoma sample; somatic mutation; greatly reduces kinase acivity, increases cell proliferation, cell adhesion and cell survival. 2 Publications
VAR_040440

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei313 – 32210LPPNNSYADF → ASPIVAPVDA in isoform 2. 1 PublicationVSP_042059
Alternative sequencei323 – 454132Missing in isoform 2. 1 PublicationVSP_042060Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007144 mRNA. Translation: BAA24955.1.
AB022341 mRNA. Translation: BAA81746.1.
AK074799 mRNA. Translation: BAG52004.1.
BC126430 mRNA. Translation: AAI26431.1.
BC126432 mRNA. Translation: AAI26433.1.
AB265224 mRNA. Translation: BAF34614.1.
CCDSiCCDS12116.1. [O43293-1]
RefSeqiNP_001339.1. NM_001348.2. [O43293-1]
XP_005259565.1. XM_005259508.1. [O43293-1]
UniGeneiHs.631844.

Genome annotation databases

EnsembliENST00000301264; ENSP00000301264; ENSG00000167657. [O43293-1]
ENST00000545797; ENSP00000442973; ENSG00000167657. [O43293-1]
GeneIDi1613.
KEGGihsa:1613.
UCSCiuc002lzc.1. human. [O43293-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007144 mRNA. Translation: BAA24955.1.
AB022341 mRNA. Translation: BAA81746.1.
AK074799 mRNA. Translation: BAG52004.1.
BC126430 mRNA. Translation: AAI26431.1.
BC126432 mRNA. Translation: AAI26433.1.
AB265224 mRNA. Translation: BAF34614.1.
CCDSiCCDS12116.1. [O43293-1]
RefSeqiNP_001339.1. NM_001348.2. [O43293-1]
XP_005259565.1. XM_005259508.1. [O43293-1]
UniGeneiHs.631844.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YRPX-ray3.10A/B1-277[»]
2J90X-ray2.00A/B9-289[»]
3BHYX-ray1.24A9-289[»]
3BQRX-ray1.75A9-289[»]
ProteinModelPortaliO43293.
SMRiO43293. Positions 2-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107983. 25 interactions.
IntActiO43293. 17 interactions.
MINTiMINT-6505325.
STRINGi9606.ENSP00000301264.

Chemistry

BindingDBiO43293.
ChEMBLiCHEMBL2468.
GuidetoPHARMACOLOGYi2004.

PTM databases

PhosphoSiteiO43293.

Polymorphism and mutation databases

BioMutaiDAPK3.

Proteomic databases

MaxQBiO43293.
PaxDbiO43293.
PRIDEiO43293.

Protocols and materials databases

DNASUi1613.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301264; ENSP00000301264; ENSG00000167657. [O43293-1]
ENST00000545797; ENSP00000442973; ENSG00000167657. [O43293-1]
GeneIDi1613.
KEGGihsa:1613.
UCSCiuc002lzc.1. human. [O43293-1]

Organism-specific databases

CTDi1613.
GeneCardsiGC19M003958.
HGNCiHGNC:2676. DAPK3.
HPAiHPA028569.
MIMi603289. gene.
neXtProtiNX_O43293.
PharmGKBiPA27144.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000233016.
HOVERGENiHBG101549.
InParanoidiO43293.
KOiK08803.
OMAiSLEHPWI.
OrthoDBiEOG7QZGBH.
PhylomeDBiO43293.
TreeFamiTF314166.

Enzyme and pathway databases

ReactomeiREACT_22128. Ligand-independent caspase activation via DCC.
SignaLinkiO43293.

Miscellaneous databases

ChiTaRSiDAPK3. human.
EvolutionaryTraceiO43293.
GeneWikiiDAPK3.
GenomeRNAii1613.
NextBioi6630.
PROiO43293.
SOURCEiSearch...

Gene expression databases

BgeeiO43293.
CleanExiHS_DAPK3.
ExpressionAtlasiO43293. baseline and differential.
GenevestigatoriO43293.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR020675. Myosin_light_ch_kinase-rel.
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.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ZIP kinase, a novel serine/threonine kinase which mediates apoptosis."
    Kawai T., Matsumoto M., Takeda K., Sanjo H., Akira S.
    Mol. Cell. Biol. 18:1642-1651(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells."
    Murata-Hori M., Suizu F., Iwasaki T., Kikuchi A., Hosoya H.
    FEBS Lett. 451:81-84(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
    Tissue: Cervix carcinoma.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 165-454 (ISOFORM 2), ALTERNATIVE SPLICING, FUNCTION IN PHOSPHORYLATION OF MYOSIN; PPP1R12A AND MYL12B, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH PPP1R12A AND MYOSIN, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Urinary bladder.
  6. "Zipper-interacting protein kinase induces Ca(2+)-free smooth muscle contraction via myosin light chain phosphorylation."
    Niiro N., Ikebe M.
    J. Biol. Chem. 276:29567-29574(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MUSCLE MYL12B, CATALYTIC ACTIVITY.
  7. "HeLa ZIP kinase induces diphosphorylation of myosin II regulatory light chain and reorganization of actin filaments in nonmuscle cells."
    Murata-Hori M., Fukuta Y., Ueda K., Iwasaki T., Hosoya H.
    Oncogene 20:8175-8183(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF NON-MUSCLE MYL12B, CATALYTIC ACTIVITY.
  8. "ZIP kinase triggers apoptosis from nuclear PML oncogenic domains."
    Kawai T., Akira S., Reed J.C.
    Mol. Cell. Biol. 23:6174-6186(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH DAXX AND PAWR.
  9. "Identification and characterization of zipper-interacting protein kinase as the unique vascular smooth muscle myosin phosphatase-associated kinase."
    Endo A., Surks H.K., Mochizuki S., Mochizuki N., Mendelsohn M.E.
    J. Biol. Chem. 279:42055-42061(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R12A, TISSUE SPECIFICITY.
  10. "ZIP kinase is responsible for the phosphorylation of myosin II and necessary for cell motility in mammalian fibroblasts."
    Komatsu S., Ikebe M.
    J. Cell Biol. 165:243-254(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MYL12B, CATALYTIC ACTIVITY.
  11. "Death-associated protein kinase phosphorylates ZIP kinase, forming a unique kinase hierarchy to activate its cell death functions."
    Shani G., Marash L., Gozuacik D., Bialik S., Teitelbaum L., Shohat G., Kimchi A.
    Mol. Cell. Biol. 24:8611-8626(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-299; SER-309; SER-311; SER-312; SER-318 AND SER-326, PHOSPHORYLATION BY DAPK1, SUBCELLULAR LOCATION.
  12. "Physical and functional interactions between STAT3 and ZIP kinase."
    Sato N., Kawai T., Sugiyama K., Muromoto R., Imoto S., Sekine Y., Ishida M., Akira S., Matsuda T.
    Int. Immunol. 17:1543-1552(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STAT3.
  13. "TCP10L is expressed specifically in spermatogenic cells and binds to death associated protein kinase-3."
    Yu H., Jiang D., Guo Z., Saiyin H., Guo J., Wang X., Yu L.
    Int. J. Androl. 28:163-170(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TCP10L, SUBCELLULAR LOCATION.
  14. "Regulation of zipper-interacting protein kinase activity in vitro and in vivo by multisite phosphorylation."
    Graves P.R., Winkfield K.M., Haystead T.A.
    J. Biol. Chem. 280:9363-9374(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-180; THR-225; THR-265; THR-299; THR-306 AND SER-311, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-299; 299-THR-THR-300; VAL-427; VAL-434 AND LEU-441.
  15. "The death-associated protein kinases: structure, function, and beyond."
    Bialik S., Kimchi A.
    Annu. Rev. Biochem. 75:189-210(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  16. Cited for: FUNCTION, ENZYME REGULATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-180; THR-265 AND THR-299, MUTAGENESIS OF LYS-42; ASP-161; THR-225; THR-265 AND THR-299.
  17. "ZIPK: a unique case of murine-specific divergence of a conserved vertebrate gene."
    Shoval Y., Pietrokovski S., Kimchi A.
    PLoS Genet. 3:1884-1893(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ABSENCE OF INTERACTION WITH PARW.
  18. "Dlk/ZIP kinase, a novel Ser/Thr-specific protein kinase with multiple functions."
    Scheidtmann K.H.
    Signal Transduct. 7:248-259(2007)
    Cited for: REVIEW ON FUNCTION.
  19. "DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating inflammatory gene expression."
    Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L.
    Mol. Cell 32:371-382(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHPRYLATION OF RPL13A, CATALYTIC ACTIVITY.
  20. "ZIP kinase plays a crucial role in androgen receptor-mediated transcription."
    Leister P., Felten A., Chasan A.I., Scheidtmann K.H.
    Oncogene 27:3292-3300(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANDROGEN RECEPTOR-MEDIATED TRANSCRIPTION.
  21. "Cancer-associated loss-of-function mutations implicate DAPK3 as a tumor-suppressing kinase."
    Brognard J., Zhang Y.W., Puto L.A., Hunter T.
    Cancer Res. 71:3152-3161(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS TUMOR SUPPRESSOR, CHARACTERIZATION OF VARIANTS MET-112; ASN-161 AND SER-216, MUTAGENESIS OF THR-180, SELF-ASSOCIATION.
  22. "Phosphorylation-dependent control of ZIPK nuclear import is species specific."
    Weitzel D.H., Chambers J., Haystead T.A.
    Cell. Signal. 23:297-303(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-299, SUBCELLULAR LOCATION, MUTAGENESIS OF 294-ARG-ARG-295.
  23. "Atg1-mediated myosin II activation regulates autophagosome formation during starvation-induced autophagy."
    Tang H.W., Wang Y.B., Wang S.L., Wu M.H., Lin S.Y., Chen G.C.
    EMBO J. 30:636-651(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF AUTOPHAGY, INTERACTION WITH ULK1.
  24. "Zipper-interacting protein kinase (ZIPK) modulates canonical Wnt/beta-catenin signaling through interaction with Nemo-like kinase and T-cell factor 4 (NLK/TCF4)."
    Togi S., Ikeda O., Kamitani S., Nakasuji M., Sekine Y., Muromoto R., Nanbo A., Oritani K., Kawai T., Akira S., Matsuda T.
    J. Biol. Chem. 286:19170-19177(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NLK.
  25. "New modularity of DAP-kinases: alternative splicing of the DRP-1 gene produces a ZIPk-like isoform."
    Shoval Y., Berissi H., Kimchi A., Pietrokovski S.
    PLoS ONE 6:E17344-E17344(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATF4.
  26. "Interaction of RhoD and ZIP kinase modulates actin filament assembly and focal adhesion dynamics."
    Nehru V., Almeida F.N., Aspenstrom P.
    Biochem. Biophys. Res. Commun. 433:163-169(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REORGANIZATION OF ACTIN CYTOSKELETON, INTERACTION WITH RHOD.
  27. "Crystal structure of human ZIP kinase."
    Kursula P., Vahokoski J., Wilmanns M.
    Submitted (JUN-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-277.
  28. "Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites."
    Pike A.C., Rellos P., Niesen F.H., Turnbull A., Oliver A.W., Parker S.A., Turk B.E., Pearl L.H., Knapp S.
    EMBO J. 27:704-714(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 9-289 IN COMPLEX WITH PYRIDONE 6, ENZYME REGULATION, SUBUNIT, PHOSPHORYLATION AT SER-50 AND THR-265.
  29. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-112; ASN-161 AND SER-216.

Entry informationi

Entry nameiDAPK3_HUMAN
AccessioniPrimary (citable) accession number: O43293
Secondary accession number(s): A0AVN4, B3KQE2, Q05JY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: June 1, 1998
Last modified: May 27, 2015
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.