PEA15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PEA15_HUMAN
• UniProt AC: Q15121
• Protein Name: Astrocytic phosphoprotein PEA-15
• Gene Name: PEA15
• Organism: Homo sapiens (Human).
• Sequence Length: 130
• Subcellular Localization: Cytoplasm. Associated with microtubules.
• Protein Description: Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm (By similarity). Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface..
• Protein Sequence: MAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLESHNKLDKDNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEDELDTKLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA

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
4	Phosphorylation	----MAEYGTLLQDL ----CCCHHHHHHHH	13.08	18491316
6	Phosphorylation	--MAEYGTLLQDLTN --CCCHHHHHHHHHC	24.32	17287340
12	Phosphorylation	GTLLQDLTNNITLED HHHHHHHHCCCCHHH	34.21	25867546
24	Ubiquitination	LEDLEQLKSACKEDI HHHHHHHHHHHHHCC	35.38	-
25	Phosphorylation	EDLEQLKSACKEDIP HHHHHHHHHHHHCCC	47.71	17287340
27	S-nitrosylation	LEQLKSACKEDIPSE HHHHHHHHHHCCCCC	6.82	2212679
28	Ubiquitination	EQLKSACKEDIPSEK HHHHHHHHHCCCCCC	59.13	-
35	Acetylation	KEDIPSEKSEEITTG HHCCCCCCCCCCCCC	68.46	23236377
43	Phosphorylation	SEEITTGSAWFSFLE CCCCCCCHHHHHHHH	21.89	26657352
54	Ubiquitination	SFLESHNKLDKDNLS HHHHHCCCCCCCCCH	53.27	-
56	Acetylation	LESHNKLDKDNLSYI HHHCCCCCCCCCHHH	58.85	-
61	Phosphorylation	KLDKDNLSYIEHIFE CCCCCCCHHHHHHHH	30.25	22617229
62	Phosphorylation	LDKDNLSYIEHIFEI CCCCCCHHHHHHHHH	17.31	23403867
78	Sulfoxidation	RRPDLLTMVVDYRTR CCCCHHHHHHCCCCE	2.52	30846556
90	Phosphorylation	RTRVLKISEEDELDT CCEEEECCCHHHHCH	33.09	25849741
97	Phosphorylation	SEEDELDTKLTRIPS CCHHHHCHHHCCCCC	40.35	26261332
98	Ubiquitination	EEDELDTKLTRIPSA CHHHHCHHHCCCCCH	47.75	21906983
98	2-Hydroxyisobutyrylation	EEDELDTKLTRIPSA CHHHHCHHHCCCCCH	47.75	-
100	Phosphorylation	DELDTKLTRIPSAKK HHHCHHHCCCCCHHH	28.27	23403867
104	Phosphorylation	TKLTRIPSAKKYKDI HHHCCCCCHHHHHHH	50.80	26846344
108	Phosphorylation	RIPSAKKYKDIIRQP CCCCHHHHHHHCCCC	17.12	23927012
109	Methylation	IPSAKKYKDIIRQPS CCCHHHHHHHCCCCC	51.86	116252721
116	Phosphorylation	KDIIRQPSEEEIIKL HHHCCCCCHHHHHHH	49.67	29255136
119	Ubiquitination	IRQPSEEEIIKLAPP CCCCCHHHHHHHCCC	46.06	-

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
104	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
104	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
116	S	Phosphorylation	Kinase	AKT1	P31749	PSP
116	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
116	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
116	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
116	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PEA15_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 PEA15_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KS6A3_HUMAN	RPS6KA3	physical	12796492
PLD1_HUMAN	PLD1	physical	10926929
CASP8_HUMAN	CASP8	physical	10493725
FADD_HUMAN	FADD	physical	10493725
MK03_HUMAN	MAPK3	physical	11702783
MK01_HUMAN	MAPK1	physical	11702783

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

Phosphorylation

"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-116, 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-116, AND MASSSPECTROMETRY.
PubMed: 18669648

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND MASSSPECTROMETRY.
PubMed: 18187866

"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 THR-6; SER-25; SER-104;TYR-108 AND SER-116, AND MASS SPECTROMETRY.
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-104 AND SER-116, ANDMASS SPECTROMETRY.
PubMed: 17081983