DAPK3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DAPK3_MOUSE
• UniProt AC: O54784
• Protein Name: Death-associated protein kinase 3
• Gene Name: Dapk3
• Organism: Mus musculus (Mouse).
• Sequence Length: 448
• Subcellular Localization: Nucleus . Nucleus, PML body . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Chromosome, centromere . Cytoplasm . Predominantly localized to the nucleus. Relocates to the cytoplasm on binding PAWR where the complex appears to in
• Protein Description: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in formation of promyelocytic leukemia protein nuclear body (PML-NB). Involved in apoptosis involving PAWR which mediates cytoplasmic relocation; in vitro phosphorylates PAWR (By similarity). Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton such as in regulation of cell polarity and cell migration. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2; disrupts the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates STAT3 and enhances its transcriptional activity. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis (By similarity). 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..
• Protein Sequence: MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERFSRVLEDVAAAEQGLRELQRGRRQCRERVCALRAAAEQREARCRDGSAGLGRDLRRLRTELGRTEALRTRAQEEARAALLGAGGLKRRLCRLENRYDALAAQVAAEVQFVRDLVRALEQERLQAECGVR

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
51	Phosphorylation	IKKRRLPSSRRGVSR HHHCCCCCCCCCCCH	40.86	20531401
52	Phosphorylation	KKRRLPSSRRGVSRE HHCCCCCCCCCCCHH	24.85	20531401
180	Phosphorylation	EFKNIFGTPEFVAPE CHHHHHCCCCCCCCC	14.64	-
225	Phosphorylation	LGETKQETLTNISAV CCCCCCHHHHHCEEE	36.07	-
265	Phosphorylation	KDPKRRMTIAQSLEH CCHHHCCCHHHHHHH	16.02	16325270
273	Phosphorylation	IAQSLEHSWIKVRRR HHHHHHHCCEEEEEC	22.56	21454597
276	Acetylation	SLEHSWIKVRRREDG HHHHCCEEEEECCCC	24.35	6566181
300	Phosphorylation	RAARLREYSLKSHSS HHHHHHHHHCCCCCC	16.93	25367039
301	Phosphorylation	AARLREYSLKSHSSM HHHHHHHHCCCCCCC	25.27	25263469
304	Phosphorylation	LREYSLKSHSSMPRN HHHHHCCCCCCCCCC	33.62	23140645
306	Phosphorylation	EYSLKSHSSMPRNTS HHHCCCCCCCCCCCC	35.11	24899341
307	Phosphorylation	YSLKSHSSMPRNTSY HHCCCCCCCCCCCCH	27.64	23684622
312	Phosphorylation	HSSMPRNTSYASFER CCCCCCCCCHHHHHH	25.13	26824392
313	Phosphorylation	SSMPRNTSYASFERF CCCCCCCCHHHHHHH	23.42	26824392
314	Phosphorylation	SMPRNTSYASFERFS CCCCCCCHHHHHHHH	12.29	29472430
316	Phosphorylation	PRNTSYASFERFSRV CCCCCHHHHHHHHHH	21.29	23684622
321	Phosphorylation	YASFERFSRVLEDVA HHHHHHHHHHHHHHH	27.92	-
378	Phosphorylation	RDLRRLRTELGRTEA HHHHHHHHHHHCHHH	39.90	29514104
405	Ubiquitination	LLGAGGLKRRLCRLE HHCCCHHHHHHHHHH	38.45	22790023

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
265	T	Phosphorylation	Kinase	DAPK3	O54784	PSP
265	T	Phosphorylation	Kinase	ROCK1	P70335	Uniprot
304	S	Phosphorylation	Kinase	DAPK1	Q80YE7	Uniprot
306	S	Phosphorylation	Kinase	DAPK1	Q80YE7	Uniprot
307	S	Phosphorylation	Kinase	DAPK1	Q80YE7	Uniprot
313	S	Phosphorylation	Kinase	DAPK1	Q80YE7	Uniprot
321	S	Phosphorylation	Kinase	DAPK1	Q80YE7	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
180	T	Phosphorylation	Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity.	-
225	T	Phosphorylation	Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity.	-
265	T	Phosphorylation	Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity.	16325270

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of DAPK3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DAPK3_MOUSE	Dapk3	physical	9488481
UB2D3_MOUSE	Ube2d3	physical	18515077
UB2D1_MOUSE	Ube2d1	physical	18515077
UB2D2_MOUSE	Ube2d2a	physical	18515077

Drug and Disease Associations

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