DAP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DAP1_HUMAN
• UniProt AC: P51397
• Protein Name: Death-associated protein 1
• Gene Name: DAP
• Organism: Homo sapiens (Human).
• Sequence Length: 102
• Protein Description: Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death..
• Protein Sequence: MSSPPEGKLETKAGHPPAVKAGGMRIVQKHPHTGDTKEEKDKDDQEWESPSPPKPTVFISGVIARGDKDFPPAAAQVAHQKPHASMDKHPSPRTQHIQQPRK

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
2	Phosphorylation	------MSSPPEGKL ------CCCCCCCCC	52.10	23401153
2	Acetylation	------MSSPPEGKL ------CCCCCCCCC	52.10	20068231
3	Phosphorylation	-----MSSPPEGKLE -----CCCCCCCCCC	43.08	23401153
8	Acetylation	MSSPPEGKLETKAGH CCCCCCCCCCCCCCC	41.30	25953088
8	Ubiquitination	MSSPPEGKLETKAGH CCCCCCCCCCCCCCC	41.30	-
11	Phosphorylation	PPEGKLETKAGHPPA CCCCCCCCCCCCCCC	36.31	29396449
12	Ubiquitination	PEGKLETKAGHPPAV CCCCCCCCCCCCCCE	42.89	-
20	Acetylation	AGHPPAVKAGGMRIV CCCCCCEEECCEEEE	43.34	26822725
29	Acetylation	GGMRIVQKHPHTGDT CCEEEEECCCCCCCC	48.48	26822725
29	Ubiquitination	GGMRIVQKHPHTGDT CCEEEEECCCCCCCC	48.48	21906983
33	Phosphorylation	IVQKHPHTGDTKEEK EEECCCCCCCCCCCC	41.00	26074081
36	Phosphorylation	KHPHTGDTKEEKDKD CCCCCCCCCCCCCCC	41.52	26091039
49	Phosphorylation	KDDQEWESPSPPKPT CCCCCCCCCCCCCCE	31.58	22167270
51	Phosphorylation	DQEWESPSPPKPTVF CCCCCCCCCCCCEEE	64.21	22167270
56	Phosphorylation	SPSPPKPTVFISGVI CCCCCCCEEEEEEEE	33.89	30175587
60	Phosphorylation	PKPTVFISGVIARGD CCCEEEEEEEEECCC	18.62	22115753
68	Acetylation	GVIARGDKDFPPAAA EEEECCCCCCCHHHH	65.18	23954790
81	Acetylation	AAQVAHQKPHASMDK HHHHHHCCCCCCCCC	28.98	23954790
85	Phosphorylation	AHQKPHASMDKHPSP HHCCCCCCCCCCCCC	25.20	23927012
91	Phosphorylation	ASMDKHPSPRTQHIQ CCCCCCCCCCHHHCC	27.08	23927012
93	Methylation	MDKHPSPRTQHIQQP CCCCCCCCHHHCCCC	51.89	-
94	Phosphorylation	DKHPSPRTQHIQQPR CCCCCCCHHHCCCCC	28.08	29514088

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
3	S	Phosphorylation	Kinase	MTOR	P42345	Uniprot
51	S	Phosphorylation	Kinase	MTOR	P42345	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DAP1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of DAP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SETB1_HUMAN	SETDB1	physical	16169070

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.

Related Literatures of Post-Translational Modification

Acetylation

"Beyond linker histones and high mobility group proteins: globalprofiling of perchloric acid soluble proteins.";
Zougman A., Wisniewski J.R.;
J. Proteome Res. 5:925-934(2006).
Cited for: PROTEIN SEQUENCE OF 2-8 AND 41-65, ACETYLATION AT SER-2,PHOSPHORYLATION AT SER-3; SER-49 AND SER-51, AND MASS SPECTROMETRY.
PubMed: 16602700

Phosphorylation

"DAP1, a novel substrate of mTOR, negatively regulates autophagy.";
Koren I., Reem E., Kimchi A.;
Curr. Biol. 20:1093-1098(2010).
Cited for: FUNCTION IN AUTOPHAGY, AND PHOSPHORYLATION AT SER-3 AND SER-51 BYMTOR.
PubMed: 20537536

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-49; SER-51 AND SER-91,AND MASS SPECTROMETRY.
PubMed: 18669648

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND MASSSPECTROMETRY.
PubMed: 17287340

"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-51, AND MASSSPECTROMETRY.
PubMed: 17081983

"Beyond linker histones and high mobility group proteins: globalprofiling of perchloric acid soluble proteins.";
Zougman A., Wisniewski J.R.;
J. Proteome Res. 5:925-934(2006).
Cited for: PROTEIN SEQUENCE OF 2-8 AND 41-65, ACETYLATION AT SER-2,PHOSPHORYLATION AT SER-3; SER-49 AND SER-51, AND MASS SPECTROMETRY.
PubMed: 16602700