dbPTM

PEBP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PEBP1_HUMAN
UniProt AC	P30086
Protein Name	Phosphatidylethanolamine-binding protein 1
Gene Name	PEBP1
Organism	Homo sapiens (Human).
Sequence Length	187
Subcellular Localization	Cytoplasm.
Protein Description	Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation.; HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor (By similarity)..
Protein Sequence	MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSGTVLSDYVGSGPPKGTGLHRYVWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKLYEQLSGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MPVDLSKWSGPLS --CCCCHHHCCCCCC	27.84	24275569
7	Ubiquitination	-MPVDLSKWSGPLSL -CCCCHHHCCCCCCH	53.31	-
9	Phosphorylation	PVDLSKWSGPLSLQE CCCHHHCCCCCCHHC	33.98	28857561
13	Phosphorylation	SKWSGPLSLQEVDEQ HHCCCCCCHHCCCCC	31.01	25159151
28	Phosphorylation	PQHPLHVTYAGAAVD CCCCCEEEECCCHHH	9.26	-
39	Acetylation	AAVDELGKVLTPTQV CHHHHHCCCCCCHHC	46.85	23236377
42	Phosphorylation	DELGKVLTPTQVKNR HHHCCCCCCHHCCCC	27.55	25159151
44	Phosphorylation	LGKVLTPTQVKNRPT HCCCCCCHHCCCCCC	40.53	20068231
47	Ubiquitination	VLTPTQVKNRPTSIS CCCCHHCCCCCCCCE	37.10	21890473
47	Acetylation	VLTPTQVKNRPTSIS CCCCHHCCCCCCCCE	37.10	25953088
47	Malonylation	VLTPTQVKNRPTSIS CCCCHHCCCCCCCCE	37.10	26320211
51	Phosphorylation	TQVKNRPTSISWDGL HHCCCCCCCCEECCC	35.14	22167270
52	Phosphorylation	QVKNRPTSISWDGLD HCCCCCCCCEECCCC	19.80	22167270
54	Phosphorylation	KNRPTSISWDGLDSG CCCCCCCEECCCCCC	20.91	22167270
60	Phosphorylation	ISWDGLDSGKLYTLV CEECCCCCCCEEEEE	42.76	22167270
62	Acetylation	WDGLDSGKLYTLVLT ECCCCCCCEEEEEEE	42.12	24847203
64	Phosphorylation	GLDSGKLYTLVLTDP CCCCCCEEEEEEECC	11.08	28152594
64	Nitration	GLDSGKLYTLVLTDP CCCCCCEEEEEEECC	11.08	-
65	Phosphorylation	LDSGKLYTLVLTDPD CCCCCEEEEEEECCC	22.34	24719451
69	Phosphorylation	KLYTLVLTDPDAPSR CEEEEEEECCCCCCC	37.70	-
75	Phosphorylation	LTDPDAPSRKDPKYR EECCCCCCCCCCCCC	54.40	21406692
77	Acetylation	DPDAPSRKDPKYREW CCCCCCCCCCCCCCC	80.75	23954790
77	Succinylation	DPDAPSRKDPKYREW CCCCCCCCCCCCCCC	80.75	23954790
80	Acetylation	APSRKDPKYREWHHF CCCCCCCCCCCCEEE	68.05	70543
81	Phosphorylation	PSRKDPKYREWHHFL CCCCCCCCCCCEEEE	21.10	27155012
92	Sulfoxidation	HHFLVVNMKGNDISS EEEEEEECCCCCCCC	3.87	30846556
98	Phosphorylation	NMKGNDISSGTVLSD ECCCCCCCCCEECCC	26.11	28258704
99	Phosphorylation	MKGNDISSGTVLSDY CCCCCCCCCEECCCC	38.53	20166139
101	Phosphorylation	GNDISSGTVLSDYVG CCCCCCCEECCCCCC	21.88	28152594
104	Phosphorylation	ISSGTVLSDYVGSGP CCCCEECCCCCCCCC	23.66	28152594
106	Phosphorylation	SGTVLSDYVGSGPPK CCEECCCCCCCCCCC	11.88	28152594
106	Nitration	SGTVLSDYVGSGPPK CCEECCCCCCCCCCC	11.88	-
109	Phosphorylation	VLSDYVGSGPPKGTG ECCCCCCCCCCCCCC	37.77	28152594
113	Ubiquitination	YVGSGPPKGTGLHRY CCCCCCCCCCCCCEE	72.70	21890473
113	Acetylation	YVGSGPPKGTGLHRY CCCCCCCCCCCCCEE	72.70	26051181
113	Malonylation	YVGSGPPKGTGLHRY CCCCCCCCCCCCCEE	72.70	26320211
120	Phosphorylation	KGTGLHRYVWLVYEQ CCCCCCEEEEEEEEC	5.80	28152594
125	Phosphorylation	HRYVWLVYEQDRPLK CEEEEEEEECCCCCC	13.00	28152594
129	Methylation	WLVYEQDRPLKCDEP EEEEECCCCCCCCCC	37.84	115491313
132	Acetylation	YEQDRPLKCDEPILS EECCCCCCCCCCCCC	42.18	25953088
132	Ubiquitination	YEQDRPLKCDEPILS EECCCCCCCCCCCCC	42.18	21906983
139	Phosphorylation	KCDEPILSNRSGDHR CCCCCCCCCCCCCCC	30.80	28258704
150	Acetylation	GDHRGKFKVASFRKK CCCCCCEEEEEEECE	40.14	27178108
150	Malonylation	GDHRGKFKVASFRKK CCCCCCEEEEEEECE	40.14	26320211
153	Phosphorylation	RGKFKVASFRKKYEL CCCEEEEEEECEEEE	28.68	22617229
167	Phosphorylation	LRAPVAGTCYQAEWD EECCCCCEEEEECHH	9.78	28152594
168	S-nitrosylation	RAPVAGTCYQAEWDD ECCCCCEEEEECHHH	2.01	19483679
168	Glutathionylation	RAPVAGTCYQAEWDD ECCCCCEEEEECHHH	2.01	22555962
168	S-nitrosocysteine	RAPVAGTCYQAEWDD ECCCCCEEEEECHHH	2.01	-
169	Phosphorylation	APVAGTCYQAEWDDY CCCCCEEEEECHHHH	15.59	28152594
176	Phosphorylation	YQAEWDDYVPKLYEQ EEECHHHHHHHHHHH	19.04	28152594
179	Acetylation	EWDDYVPKLYEQLSG CHHHHHHHHHHHHCC	54.37	23954790
179	Ubiquitination	EWDDYVPKLYEQLSG CHHHHHHHHHHHHCC	54.37	-
181	Phosphorylation	DDYVPKLYEQLSGK- HHHHHHHHHHHCCC-	14.04	25159151
185	Phosphorylation	PKLYEQLSGK----- HHHHHHHCCC-----	44.20	28985074
187	Ubiquitination	LYEQLSGK------- HHHHHCCC-------	54.51	-

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
42	T	Phosphorylation	Kinase	CDK5	Q00535	PSP
109	S	Phosphorylation	Kinase	TBK1	Q9UHD2	PSP
153	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
153	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PEBP1_HUMAN !!

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 PEBP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STC2_HUMAN	STC2	physical	16169070
RAF1_HUMAN	RAF1	physical	10757792
MP2K1_HUMAN	MAP2K1	physical	10757792
MK01_HUMAN	MAPK1	physical	10757792
PRDX1_HUMAN	PRDX1	physical	22939629
PTGR1_HUMAN	PTGR1	physical	22939629
RAF1_HUMAN	RAF1	physical	14654844
ARBK1_HUMAN	ADRBK1	physical	14654844
ASNS_HUMAN	ASNS	physical	26344197
CK054_HUMAN	C11orf54	physical	26344197
GNPI2_HUMAN	GNPDA2	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
LEG3_HUMAN	LGALS3	physical	26344197
6PGL_HUMAN	PGLS	physical	26344197
PPIA_HUMAN	PPIA	physical	26344197
PRDX5_HUMAN	PRDX5	physical	26344197
RIFK_HUMAN	RFK	physical	26344197
MFTC_HUMAN	SLC25A32	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
RAF1_HUMAN	RAF1	physical	21831839
LOX15_HUMAN	ALOX15	physical	21831839

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 PEBP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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 THR-42 AND SER-52, 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-52, AND MASSSPECTROMETRY.	17081983 [Abstract]
"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 THR-42, AND MASSSPECTROMETRY.	19413330 [Abstract]