Death-associated protein kinase 3 (Protein name
), DAPK3_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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Gene name:
DAPK3(ZIPK);
Protein name:
Death-associated protein kinase 3(DAP kinase 3);
Alternative:
ZIP-kinase;DAP-like kinase(Dlk);Zipper-interacting protein kinase(ZIP-kinase);
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Homodimer or forms heterodimers with ATF4. 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. Interacts with AATF, CDC5L, UBE2D1, UBE2D2 AND UBE2D3.
Function:
Serine/threonine kinase which acts as a positive regulator of apoptosis. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis. Regulates myosin light chain phosphatase through phosphorylation of MYPT1 thereby regulating the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. 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.
Subcellular Location:
Nucleus
Cytoplasm
Nucleus
PML body
Relocates to the cytoplasm on binding PAWR where the complex appears to interact with actin filaments (By similarity). Localizes to promyelocytic leukemia protein nuclear bodies (PML-NBs). Associates to centromeres from prophase to anaphase.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];FUNCTION;CATALYTIC ACTIVITY;COFACTOR
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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
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Cited for: FUNCTION IN PHOSPHORYLATION OF MUSCLE MYL12B;CATALYTIC ACTIVITY
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Cited for: FUNCTION IN PHOSPHORYLATION OF NON-MUSCLE MYL12B;CATALYTIC ACTIVITY
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Cited for: FUNCTION IN APOPTOSIS;INTERACTION WITH DAXX AND PAWR
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Cited for: FUNCTION IN PHOSPHORYLATION OF MYL12B;CATALYTIC ACTIVITY
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Cited for: FUNCTION;PHOSPHORYLATION AT THR-299; SER-309; SER-311; SER-312; SER-318 AND SER-326;PHOSPHORYLATION BY DAPK1;SUBCELLULAR LOCATION
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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
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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
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Cited for: SUBCELLULAR LOCATION;ABSENCE OF INTERACTION WITH PARW
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Cited for: FUNCTION IN PHOSPHPRYLATION OF RPL13A;CATALYTIC ACTIVITY
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Cited for: FUNCTION IN ANDROGEN RECEPTOR-MEDIATED TRANSCRIPTION
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Cited for: FUNCTION AS TUMOR SUPPRESSOR;CHARACTERIZATION OF VARIANTS MET-112; ASN-161 AND SER-216;MUTAGENESIS OF THR-180;SELF-ASSOCIATION
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Cited for: PHOSPHORYLATION AT THR-299;SUBCELLULAR LOCATION;MUTAGENESIS OF 294-ARG-ARG-295
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Cited for: FUNCTION IN REGULATION OF AUTOPHAGY;INTERACTION WITH ULK1
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Cited for: FUNCTION IN REORGANIZATION OF ACTIN CYTOSKELETON;INTERACTION WITH RHOD
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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
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Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-112; ASN-161 AND SER-216