DAPK2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DAPK2_MOUSE
• UniProt AC: Q8VDF3
• Protein Name: Death-associated protein kinase 2
• Gene Name: Dapk2
• Organism: Mus musculus (Mouse).
• Sequence Length: 370
• Subcellular Localization: Cytoplasm. Cytoplasmic vesicle, autophagosome lumen.
• Protein Description: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Capable of regulating both type I apoptotic and type II autophagic cell death signals. The former involves caspase activation, chromatin and mitochondrial condensation while the latter involves caspase-independent cell death in conjunction with accumulation of mature autophagic vesicles, plasma membrane blebs, and nuclear condensation without DNA degradation. Mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation (By similarity). Regulates granulocytes motility by controlling cell spreading and polarization. [PubMed: 24163421]
• Protein Sequence: MVQASMRSPNMETFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVCREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDTQQAMVRRESVVNLENFKKQYVRRRWKLSFSIVSLCNHLTRSLMKKVHLRTSEDLRNCESDTEENIARRKALHPRRRSSTS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	MRSPNMETFKQQKVE CCCCCHHHHHHHHHH	25.93	28576409
299	Phosphorylation	QAMVRRESVVNLENF HHHHHHHHHCCHHHH	29.56	25521595
318	Phosphorylation	VRRRWKLSFSIVSLC HHHHHHHHHHHHHHH	17.14	22817900
340	Phosphorylation	MKKVHLRTSEDLRNC HHHHCCCCHHHHHCC	42.71	27087446
349	Phosphorylation	EDLRNCESDTEENIA HHHHCCCCCHHHHHH	52.62	25521595
351	Phosphorylation	LRNCESDTEENIARR HHCCCCCHHHHHHHH	55.25	22324799
367	Phosphorylation	ALHPRRRSSTS---- HHCCCCCCCCC----	35.84	-
368	Phosphorylation	LHPRRRSSTS----- HCCCCCCCCC-----	30.75	-
369	Phosphorylation	HPRRRSSTS------ CCCCCCCCC------	39.44	-
370	Phosphorylation	PRRRSSTS------- CCCCCCCC-------	39.92	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
369	T	Phosphorylation	Kinase	AKT3	Q9WUA6	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
318	S	Phosphorylation	Autophosphorylation at Ser-318 inhibits its catalytic activity.	-
318	S	Phosphorylation	Dephosphorylated at Ser-318 in response to activated Fas and TNF-alpha receptors.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DAPK2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of DAPK2_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASSSPECTROMETRY.
PubMed: 19367708

"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASSSPECTROMETRY.
PubMed: 17203969