PEBP1_RAT - dbPTM
PEBP1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEBP1_RAT
UniProt AC P31044
Protein Name Phosphatidylethanolamine-binding protein 1
Gene Name Pebp1
Organism Rattus norvegicus (Rat).
Sequence Length 187
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein.
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 (By similarity).; 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..
Protein Sequence MAADISQWAGPLSLQEVDEPPQHALRVDYGGVTVDELGKVLTPTQVMNRPSSISWDGLDPGKLYTLVLTDPDAPSRKDPKFREWHHFLVVNMKGNDISSGTVLSEYVGSGPPKDTGLHRYVWLVYEQEQPLNCDEPILSNKSGDNRGKFKVESFRKKYHLGAPVAGTCFQAEWDDSVPKLHDQLAGK
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 Orthologous
Protein Cluster
2Acetylation------MAADISQWA
------CCCCHHHHC
17.531611510
6Phosphorylation--MAADISQWAGPLS
--CCCCHHHHCCCCC
21.8823984901
13PhosphorylationSQWAGPLSLQEVDEP
HHHCCCCCCCCCCCC
31.0127097102
42PhosphorylationDELGKVLTPTQVMNR
HHHCCCCCCHHHCCC
27.5527097102
44PhosphorylationLGKVLTPTQVMNRPS
HCCCCCCHHHCCCCC
28.6729779826
51PhosphorylationTQVMNRPSSISWDGL
HHHCCCCCCCCCCCC
36.7523991683
52PhosphorylationQVMNRPSSISWDGLD
HHCCCCCCCCCCCCC
24.2723991683
54PhosphorylationMNRPSSISWDGLDPG
CCCCCCCCCCCCCCC
22.5127097102
77AcetylationDPDAPSRKDPKFREW
CCCCCCCCCCCCCCC
80.7522902405
80AcetylationAPSRKDPKFREWHHF
CCCCCCCCCCCCEEE
68.1622902405
98PhosphorylationNMKGNDISSGTVLSE
ECCCCCCCCCEEHHH
26.1125575281
99PhosphorylationMKGNDISSGTVLSEY
CCCCCCCCCEEHHHC
38.5325575281
101PhosphorylationGNDISSGTVLSEYVG
CCCCCCCEEHHHCCC
21.8825575281
104PhosphorylationISSGTVLSEYVGSGP
CCCCEEHHHCCCCCC
23.6525575281
106PhosphorylationSGTVLSEYVGSGPPK
CCEEHHHCCCCCCCC
13.5125575281
113AcetylationYVGSGPPKDTGLHRY
CCCCCCCCCCCCCEE
71.6822902405
148AcetylationKSGDNRGKFKVESFR
CCCCCCCCEEEEHHH
38.4822902405
150AcetylationGDNRGKFKVESFRKK
CCCCCCEEEEHHHHH
48.8822902405
153PhosphorylationRGKFKVESFRKKYHL
CCCEEEEHHHHHCCC
33.0829779826

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
153SPhosphorylationKinasePRKCAP05696
GPS
153SPhosphorylationKinasePKCBP68403
PSP
153SPhosphorylationKinasePRKCBP68403-2
GPS
153SPhosphorylationKinasePRKCGP63318
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEBP1_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K7_MOUSEMap3k7physical
11585904
IKKB_HUMANIKBKBphysical
11585904
IKKA_HUMANCHUKphysical
11585904
M3K7_HUMANMAP3K7physical
11585904

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PEBP1_RAT

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Purification and structural analysis of hippocampal cholinergicneurostimulating peptide.";
Ojika K., Kojima S., Ueki Y., Fukushima N., Hayashi K., Yamamoto M.;
Brain Res. 572:164-171(1992).
Cited for: PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2.

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