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O43293

- DAPK3_HUMAN

UniProt

O43293 - DAPK3_HUMAN

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Protein

Death-associated protein kinase 3

Gene

DAPK3

Organism
Homo sapiens (Human)
Status
Reviewed - 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, 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 Ca2+ 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. 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.
Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Magnesium.1 Publication

Enzyme regulationi

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.3 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

Vmax=248 nmol/min/mg enzyme toward myosin (isoform 2)1 Publication

Vmax=120 nmol/min/mg enzyme toward myosin (isoform 1)1 Publication

Vmax=1.3 µmol/min/mg enzyme toward MYL12B (isoform 2)1 Publication

Vmax=271 nmol/min/mg enzyme toward MYL12B (isoform 1)1 Publication

Sites

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

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. calmodulin-dependent protein kinase activity Source: RefGenome
  3. identical protein binding Source: IntAct
  4. leucine zipper domain binding Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB
  6. protein serine/threonine kinase activity Source: UniProtKB
  7. Rho GTPase binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. apoptotic signaling pathway Source: Ensembl
  3. cellular response to interferon-gamma Source: UniProtKB
  4. chromatin modification Source: UniProtKB-KW
  5. cytokinesis Source: UniProtKB
  6. intracellular signal transduction Source: UniProtKB
  7. negative regulation of translation Source: UniProtKB
  8. neuron differentiation Source: Ensembl
  9. positive regulation of apoptotic process Source: UniProtKB
  10. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  11. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  12. protein autophosphorylation Source: UniProtKB
  13. protein phosphorylation Source: UniProtKB
  14. regulation of actin cytoskeleton reorganization Source: UniProtKB
  15. regulation of apoptotic process Source: UniProtKB
  16. regulation of autophagy Source: UniProtKB
  17. regulation of cell motility Source: UniProtKB
  18. regulation of focal adhesion assembly Source: UniProtKB
  19. regulation of mitosis Source: UniProtKB
  20. regulation of mitotic cell cycle Source: UniProtKB
  21. regulation of smooth muscle contraction Source: UniProtKB
  22. regulation of transcription, DNA-templated Source: UniProtKB
  23. 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. Role of DCC in regulating apoptosis.
SignaLinkiO43293.

Names & Taxonomyi

Protein namesi
Recommended name:
Death-associated protein kinase 3 (EC:2.7.11.1)
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: Chromosome 19

Organism-specific databases

HGNCiHGNC:2676. DAPK3.

Subcellular locationi

Nucleus. Cytoplasm. NucleusPML body. Chromosomecentromere. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
Note: The phosphorylated form is anchored in the cytoplasm and/or prevented from being shuttled to the nucleus, whereas nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation at Thr-299 promotes cytoplasmic localization. Relocates to the cytoplasm on binding PAWR where the complex appears to interact with actin filaments. Localizes to promyelocytic leukemia protein nuclear bodies (PML-NBs). Associated: with the centrosomes throughout the mitotic cell cycle, with the centromeres from prophase to anaphase and with the contractile ring during cytokinesis.

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. nucleus Source: UniProtKB
  5. PML body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, 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
Mutagenesisi225 – 2251T → A: Loss of kinase activity. 1 Publication
Mutagenesisi265 – 2651T → A: Loss of phosphorylation by ROCK1, catalytically inactive. 1 Publication
Mutagenesisi299 – 2991T → A: Loss of phosphorylation by ROCK1. 1 Publication

Organism-specific databases

PharmGKBiPA27144.

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 ROCK14 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

Ubiquitinated. Ubiquitination mediated by the UBE2D3 E3 ligase does not lead to proteasomal degradation, but influences promyelocytic leukemia protein nuclear bodies (PML-NBs) formation in the nucleus.
The phosphorylation status is critical for: its intracellular localization, ability to oligomerize and its activity. The phosphorylated form is anchored in the cytoplasm and/or prevented from being shuttled to the nucleus, whereas nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation increases the trimeric form, and its dephosphorylation shifts the equilibrium towards the monomeric form. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. Phosphorylation at Thr-299 promotes cytoplasmic localization. A species-specific loss of a key phosphorylation site in murine DAPK3 seems to direct it to the nucleus, while the presence of the Thr-299 site in human DAPK3 correlates with cytoplasmic localization. Both isoform 1 and isoform 2 can undergo autophosphorylation.6 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO43293.
PaxDbiO43293.
PRIDEiO43293.

PTM databases

PhosphoSiteiO43293.

Expressioni

Tissue specificityi

Isoform 2 is expressed in the bladder smooth muscle.1 Publication

Gene expression databases

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

Organism-specific databases

HPAiHPA028569.

Interactioni

Subunit structurei

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.10 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. 20 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 – 124
Beta strandi13 – 219
Beta strandi23 – 3210
Turni33 – 353
Beta strandi38 – 469
Helixi49 – 513
Beta strandi53 – 564
Helixi58 – 7013
Beta strandi79 – 846
Beta strandi86 – 949
Helixi101 – 1088
Helixi113 – 13220
Helixi142 – 1443
Beta strandi145 – 1484
Beta strandi150 – 1545
Beta strandi157 – 1593
Helixi181 – 1833
Helixi186 – 1894
Helixi197 – 21216
Helixi222 – 2309
Helixi238 – 2414
Helixi246 – 2538
Helixi260 – 2623
Helixi266 – 2716
Helixi273 – 2808

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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
Regioni276 – 33358Interaction with ARAdd
BLAST
Regioni278 – 31134Interaction with MYPT1Add
BLAST
Regioni395 – 45460Interaction with CDC5LBy similarityAdd
BLAST
Regioni427 – 44115Leucine-zipperAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000233016.
HOVERGENiHBG101549.
InParanoidiO43293.
KOiK08803.
OMAiLENRYEV.
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. Align

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. 1 Publication
VAR_040438
Natural varianti161 – 1611D → N in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
VAR_040439
Natural varianti216 – 2161P → S in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS12116.1. [O43293-1 ]
RefSeqi NP_001339.1. NM_001348.2. [O43293-1 ]
XP_005259565.1. XM_005259508.1. [O43293-1 ]
UniGenei Hs.631844.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YRP X-ray 3.10 A/B 1-277 [» ]
2J90 X-ray 2.00 A/B 9-289 [» ]
3BHY X-ray 1.24 A 9-289 [» ]
3BQR X-ray 1.75 A 9-289 [» ]
ProteinModelPortali O43293.
SMRi O43293. Positions 2-277.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107983. 20 interactions.
IntActi O43293. 17 interactions.
MINTi MINT-6505325.
STRINGi 9606.ENSP00000301264.

Chemistry

BindingDBi O43293.
ChEMBLi CHEMBL2468.
GuidetoPHARMACOLOGYi 2004.

PTM databases

PhosphoSitei O43293.

Proteomic databases

MaxQBi O43293.
PaxDbi O43293.
PRIDEi O43293.

Protocols and materials databases

DNASUi 1613.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301264 ; ENSP00000301264 ; ENSG00000167657 . [O43293-1 ]
ENST00000545797 ; ENSP00000442973 ; ENSG00000167657 . [O43293-1 ]
GeneIDi 1613.
KEGGi hsa:1613.
UCSCi uc002lzc.1. human. [O43293-1 ]

Organism-specific databases

CTDi 1613.
GeneCardsi GC19M003958.
HGNCi HGNC:2676. DAPK3.
HPAi HPA028569.
MIMi 603289. gene.
neXtProti NX_O43293.
PharmGKBi PA27144.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118877.
HOGENOMi HOG000233016.
HOVERGENi HBG101549.
InParanoidi O43293.
KOi K08803.
OMAi LENRYEV.
OrthoDBi EOG7QZGBH.
PhylomeDBi O43293.
TreeFami TF314166.

Enzyme and pathway databases

Reactomei REACT_22128. Role of DCC in regulating apoptosis.
SignaLinki O43293.

Miscellaneous databases

ChiTaRSi DAPK3. human.
EvolutionaryTracei O43293.
GeneWikii DAPK3.
GenomeRNAii 1613.
NextBioi 6630.
PROi O43293.
SOURCEi Search...

Gene expression databases

Bgeei O43293.
CleanExi HS_DAPK3.
ExpressionAtlasi O43293. baseline and differential.
Genevestigatori O43293.

Family and domain databases

InterProi IPR011009. 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 ]
PANTHERi PTHR22964. PTHR22964. 1 hit.
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.
    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, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH PPP1R12A AND MYOSIN, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Urinary bladder.
  6. "DAP-like kinase, a member of the death-associated protein kinase family, associates with centrosomes, centromers, and the contractile ring during mitosis."
    Preuss U., Bierbaum H., Buchenau P., Scheidtmann K.H.
    Eur. J. Cell Biol. 82:447-459(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "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, INTERACTION WITH DAXX AND PAWR.
  8. "Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase."
    Preuss U., Landsberg G., Scheidtmann K.H.
    Nucleic Acids Res. 31:878-885(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "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, INTERACTION WITH DAPK1, SUBCELLULAR LOCATION.
  10. "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.
  11. "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.
  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: FUNCTION IN PHOSPHORYLATION OF STAT3, 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.
  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. "Phosphorylation of threonine-265 in zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines."
    Sato N., Kamada N., Muromoto R., Kawai T., Sugiyama K., Watanabe T., Imoto S., Sekine Y., Ohbayashi N., Ishida M., Akira S., Matsuda T.
    Immunol. Lett. 103:127-134(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-265.
  17. 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.
  18. "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.
  19. "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.
  20. Cited for: INTERACTION WITH UBE2D1; UBE2D2 AND UBE2D3, FUNCTION, SUBCELLULAR LOCATION.
  21. "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, INTERACTION WITH AR.
  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.
  23. "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 AND TCF7L2.
  24. "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.
  25. "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.
  26. "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: October 29, 2014
This is version 137 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

Miscellaneous

The murine DAPK3 protein differs from the human ortholog, losing an important phosphorylation site and displaying distinct altered cellular localization. The murine protein localizes only to the nucleus while the human protein shows both nuclear and cytoplasmic localization. A different protein interaction capacity, with an important protein partner in the apoptosis pathway (PAWR), evolved in the murine system to maintain the basic membrane blebbing function in the apoptosis pathway.

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