dbPTM

DAPK2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DAPK2_HUMAN
UniProt AC	Q9UIK4
Protein Name	Death-associated protein kinase 2
Gene Name	DAPK2
Organism	Homo sapiens (Human).
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. Regulates both type I apoptotic and type II autophagic cell death signals, 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. Acts as a mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation. [PubMed: 17347302 Regulates granulocytic motility by controlling cell spreading and polarization]
Protein Sequence	MFQASMRSPNMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFRKQYVRRRWKLSFSIVSLCNHLTRSLMKKVHLRPDEDLRNCESDTEEDIARRKALHPRRRSSTS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MFQASMRSPNMEPFK CCCCCCCCCCCCCHH	16.40	25159151
49	Phosphorylation	EKSTGLEYAAKFIKK HHCCHHHHHHHHHHH	19.53	-
120	Phosphorylation	DFLAQKESLSEEEAT HHHHHHCCCCHHHHH	44.20	22798277
128	Phosphorylation	LSEEEATSFIKQILD CCHHHHHHHHHHHHH	31.83	24719451
139	Phosphorylation	QILDGVNYLHTKKIA HHHHHCCCCCCCEEE	9.46	28102081
142	Phosphorylation	DGVNYLHTKKIAHFD HHCCCCCCCEEECCC	31.29	28102081
151	Ubiquitination	KIAHFDLKPENIMLL EEECCCCCHHHEEEE	52.72	-
190	Phosphorylation	EFKNIFGTPEFVAPE EEEECCCCCCEECCC	14.64	15611134
275	Phosphorylation	KETRKRLTIQEALRH HHHHHCCCHHHHHCC	25.34	23312004
299	Phosphorylation	QAMVRRESVVNLENF CHHHHHHHHCCHHHH	29.56	30266825
318	Phosphorylation	VRRRWKLSFSIVSLC HHHHHHHHHHHHHHH	17.14	22617229
320	Phosphorylation	RRWKLSFSIVSLCNH HHHHHHHHHHHHHHH	20.78	28348404
335	Ubiquitination	LTRSLMKKVHLRPDE HHHHHHHHHCCCCCH	22.41	-
349	Phosphorylation	EDLRNCESDTEEDIA HHHCCCCCCCHHHHH	52.62	23401153
351	Phosphorylation	LRNCESDTEEDIARR HCCCCCCCHHHHHHH	51.02	22167270
367	Phosphorylation	ALHPRRRSSTS---- HHCCCCCCCCC----	35.84	-
368	Phosphorylation	LHPRRRSSTS----- HCCCCCCCCC-----	30.75	-
369	Phosphorylation	HPRRRSSTS------ CCCCCCCCC------	39.44	21408167

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
318	S	Phosphorylation	Kinase	DAPK2	Q9UIK4	PSP
369	T	Phosphorylation	Kinase	AKT1	P31749	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
318	S	Phosphorylation	11230133
Autophosphorylation at Ser-318 inhibits its catalytic activity.
318	S	Phosphorylation	11230133
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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DAPK2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DAPK2_HUMAN	DAPK2	physical	10629061
A4_HUMAN	APP	physical	21832049
DAPK2_HUMAN	DAPK2	physical	10376525
FAM9B_HUMAN	FAM9B	physical	25416956

Drug and Disease Associations

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

Regulatory Network of DAPK2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Autophosphorylation restrains the apoptotic activity of DRP-1 kinaseby controlling dimerization and calmodulin binding."; Shani G., Henis-Korenblit S., Jona G., Gileadi O., Eisenstein M.,Ziv T., Admon A., Kimchi A.; EMBO J. 20:1099-1113(2001). Cited for: FUNCTION, HOMODIMERIZATION, MUTAGENESIS OF LYS-52; SER-299; SER-318;SER-320; SER-323 AND THR-329, AND PHOSPHORYLATION AT SER-318.	11230133 [Abstract]