Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Phosphatidylethanolamine-binding protein 1  

UniProtKB / Swiss-Prot ID :  PEBP1_HUMAN

Gene Name (Synonyms) : 
PEBP1, PBP, PEBP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (By similarity). 

Protein Function :  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 MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTD...
Predicted Secondary Structure CCCCCCHHCCCEEEEEECCCCCEEEEEEECCCEECCCCCEECCHHHCCCCCEEEECCCCCCCEEEEEEEC...
Protein Variant
LocationDescription
9S -> N. VAR_006048
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
42PhosphothreonineGKVLTPTQV
CCEECCHHH
27.55HPRD
Link
42PhosphothreonineGKVLTPTQV
CCEECCHHH
27.55Phosphositeplus
Link
42PhosphothreonineGKVLTPTQV
CCEECCHHH
27.55SysPTM
Link
42Phosphothreonine.GKVLTPTQV
CCEECCHHH
27.55UniProtKB
Link
47Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PTQVKNRPT
CHHHCCCCC
37.10Phosphositeplus
Link
51PhosphothreonineKNRPTSISW
CCCCCEEEE
35.14HPRD
Link
51PhosphothreonineKNRPTSISW
CCCCCEEEE
35.14Phosphositeplus
Link
52PhosphoserineNRPTSISWD
CCCCEEEEC
19.80HPRD
Link
52PhosphoserineNRPTSISWD
CCCCEEEEC
19.80PhosphoELM
Link
52PhosphoserineNRPTSISWD
CCCCEEEEC
19.80Phosphositeplus
Link
52PhosphoserineNRPTSISWD
CCCCEEEEC
19.80SysPTM
Link
52Phosphoserine.NRPTSISWD
CCCCEEEEC
19.80UniProtKB
Link
54PhosphoserinePTSISWDGL
CCEEEECCC
20.91HPRD
Link
54PhosphoserinePTSISWDGL
CCEEEECCC
20.91Phosphositeplus
Link
60PhosphoserineDGLDSGKLY
CCCCCCCEE
42.76Phosphositeplus
Link
75PhosphoserinePDAPSRKDP
CCCCCCCCC
54.40Phosphositeplus
Link
99PhosphoserineNDISSGTVL
CCCCCCCEE
38.53HPRD
Link
99PhosphoserineNDISSGTVL
CCCCCCCEE
38.53Phosphositeplus
Link
113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SGPPKGTGL
CCCCCCCCC
72.70Phosphositeplus
Link
120PhosphotyrosineGLHRYVWLV
CCEEEEEEE
5.80HPRD
Link
120PhosphotyrosineGLHRYVWLV
CCEEEEEEE
5.80Phosphositeplus
Link
125PhosphotyrosineVWLVYEQDR
EEEEEEECC
13.00HPRD
Link
125PhosphotyrosineVWLVYEQDR
EEEEEEECC
13.00Phosphositeplus
Link
132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DRPLKCDEP
CCCCCCCCC
42.18Phosphositeplus
Link
153PhosphoserineFKVASFRKK
CCHHHHHHH
28.68Phosphositeplus
Link
153Phosphoserine (PKC_alpha;PKC_delta)FKVASFRKK
CCHHHHHHH
28.68PhosphoELM
Link
153Phosphoserine (PRKCA)FKVASFRKK
CCHHHHHHH
28.68HPRD
Link
153Phosphoserine (PRKCB)FKVASFRKK
CCHHHHHHH
28.68HPRD
Link
153Phosphoserine (PRKCD)FKVASFRKK
CCHHHHHHH
28.68HPRD
Link
153Phosphoserine (PRKCG)FKVASFRKK
CCHHHHHHH
28.68HPRD
Link
153Phosphoserine (PRKCZ)FKVASFRKK
CCHHHHHHH
28.68HPRD
Link
168S-nitrosocysteineVAGTCYQAE
HHHEEEEEE
2.01dbSNO
Link
181PhosphotyrosineVPKLYEQLS
HHHHHHHHC
14.04Phosphositeplus
Link
181PhosphotyrosineVPKLYEQLS
HHHHHHHHC
14.04SysPTM
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RAF1_HUMANphysical interactionMINT-3389378MINT17097642
RAF1_HUMANphysical interactionMINT-3389495MINT17097642
RAF1_HUMANphysical interactionMINT-3389522MINT17097642
RAF1_HUMANphysical interactionMINT-3389607MINT17097642
RAF1_HUMANphysical interactionMINT-3389468MINT17097642
RAF1_HUMANdirect interactionMINT-3389581MINT17097642
RAF1_HUMANdirect interactionMINT-3389550MINT17097642
MED10_HUMANphysical interactionMINT-65335MINT16169070
STC2_HUMANphysical interactionEBI-732743
intact16169070
VHL_HUMANphysical interactionEBI-1063473
intact17353931
RAF1_HUMANin vivoHPRD:06850HPRD11853019
MP2K1_HUMANin vitro
in vivo
HPRD:06850HPRD10757792
MK01_HUMANin vitro
in vivo
HPRD:06850HPRD10757792
10490027
M3K7_HUMANin vivoHPRD:06850HPRD11585904
PEBP1_HUMANin vitroHPRD:06850HPRD9782050
STC2_HUMANyeast 2-hybridHPRD:06850HPRD16169070
RAF1_HUMANENSP00000261313STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures