ID PEBP1_HUMAN Reviewed; 187 AA. AC P30086; B2R4S1; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 226. DE RecName: Full=Phosphatidylethanolamine-binding protein 1; DE Short=PEBP-1; DE AltName: Full=HCNPpp; DE AltName: Full=Neuropolypeptide h3; DE AltName: Full=Prostatic-binding protein; DE AltName: Full=Raf kinase inhibitor protein; DE Short=RKIP; DE Contains: DE RecName: Full=Hippocampal cholinergic neurostimulating peptide; DE Short=HCNP; GN Name=PEBP1; Synonyms=PBP, PEBP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8144042; DOI=10.1016/0378-1119(94)90562-2; RA Hori N., Keon-Sang C., Murakawa K., Matoba R., Fukushima A., Okubo K., RA Matsubara K.; RT "A human cDNA sequence homologue of bovine phosphatidylethanolamine-binding RT protein."; RL Gene 140:293-294(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX PubMed=7637590; DOI=10.1016/0169-328x(95)00029-r; RA Tohdoh N., Tojo S., Agui H., Ojika K.; RT "Sequence homology of rat and human HCNP precursor proteins, bovine RT phosphatidylethanolamine-binding protein and rat 23-kDa protein associated RT with the opioid-binding protein."; RL Brain Res. Mol. Brain Res. 30:381-384(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Hall L.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Hypothalamus, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 2-11. RC TISSUE=Liver; RX PubMed=1286669; DOI=10.1002/elps.11501301201; RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., RA Appel R.D., Hughes G.J.; RT "Human liver protein map: a reference database established by RT microsequencing and gel comparison."; RL Electrophoresis 13:992-1001(1992). RN [8] RP PROTEIN SEQUENCE OF 8-39; 48-77; 81-113; 120-141 AND 162-187, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-187. RC TISSUE=Brain; RX PubMed=7807553; DOI=10.1007/bf00160411; RA Seddiqi N., Bollengier F., Alliel P.M., Perin J.-P., Bonnet F., Bucquoy S., RA Jolles P., Schoentgen F.; RT "Amino acid sequence of the Homo sapiens brain 21-23-kDa protein RT (neuropolypeptide h3), comparison with its counterparts from Rattus RT norvegicus and Bos taurus species, and expression of its mRNA in different RT tissues."; RL J. Mol. Evol. 39:655-660(1994). RN [10] RP CHARACTERIZATION OF HCNP. RX PubMed=10622376; DOI=10.1016/s0301-0082(99)00021-0; RA Ojika K., Mitake S., Tohdoh N., Appel S.H., Otsuka Y., Katada E., RA Matsukawa N.; RT "Hippocampal cholinergic neurostimulating peptides (HCNP)."; RL Prog. Neurobiol. 60:37-83(2000). RN [11] RP INTERACTION WITH RAF-1. RX PubMed=10490027; DOI=10.1038/43686; RA Yeung K., Seitz T., Li S., Janosch P., McFerran B., Kaiser C., Fee F., RA Katsanakis K.D., Rose D.W., Mischak H., Sedivy J.M., Kolch W.; RT "Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP."; RL Nature 401:173-177(1999). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP FUNCTION, AND INTERACTION WITH RAF1. RX PubMed=18294816; DOI=10.1016/j.cellsig.2008.01.012; RA Rath O., Park S., Tang H.H., Banfield M.J., Brady R.L., Lee Y.C., RA Dignam J.D., Sedivy J.M., Kolch W., Yeung K.C.; RT "The RKIP (Raf-1 Kinase Inhibitor Protein) conserved pocket binds to the RT phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated RT phosphorylation of MEK."; RL Cell. Signal. 20:935-941(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 AND SER-52, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP INTERACTION WITH ALOX15. RX PubMed=21831839; DOI=10.1073/pnas.1018075108; RA Zhao J., O'Donnell V.B., Balzar S., St Croix C.M., Trudeau J.B., RA Wenzel S.E.; RT "15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein RT to regulate MAPK signaling in human airway epithelial cells."; RL Proc. Natl. Acad. Sci. U.S.A. 108:14246-14251(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42; SER-52 AND SER-54, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-52; SER-54; SER-98 AND RP SER-153, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). RX PubMed=9782050; DOI=10.1016/s0969-2126(98)00125-7; RA Banfield M.J., Barker J.J., Perry A.C., Brady R.L.; RT "Function from structure? The crystal structure of human RT phosphatidylethanolamine-binding protein suggests a role in membrane signal RT transduction."; RL Structure 6:1245-1254(1998). CC -!- FUNCTION: Binds ATP, opioids and phosphatidylethanolamine. Has lower CC affinity for phosphatidylinositol and phosphatidylcholine. Serine CC protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin CC but not trypsin, tissue type plasminogen activator and elastase (By CC similarity). Inhibits the kinase activity of RAF1 by inhibiting its CC activation and by dissociating the RAF1/MEK complex and acting as a CC competitive inhibitor of MEK phosphorylation. {ECO:0000250, CC ECO:0000269|PubMed:18294816}. CC -!- FUNCTION: HCNP may be involved in the function of the presynaptic CC cholinergic neurons of the central nervous system. HCNP increases the CC production of choline acetyltransferase but not acetylcholinesterase. CC Seems to be mediated by a specific receptor (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Has a tendency to form dimers by disulfide cross-linking (By CC similarity). Interacts with RAF1 and this interaction is enhanced if CC RAF1 is phosphorylated on residues 'Ser-338', 'Ser-339', 'Tyr-340' and CC 'Tyr-341'. Interacts with ALOX15; in response to IL13/interleukin-13, CC prevents the interaction of PEBP1 with RAF1 to activate the ERK CC signaling cascade. {ECO:0000250, ECO:0000269|PubMed:10490027, CC ECO:0000269|PubMed:18294816, ECO:0000269|PubMed:21831839}. CC -!- INTERACTION: CC P30086; P16050: ALOX15; NbExp=3; IntAct=EBI-716384, EBI-14035397; CC P30086; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-716384, EBI-79165; CC P30086; P04049: RAF1; NbExp=10; IntAct=EBI-716384, EBI-365996; CC P30086; Q15208: STK38; NbExp=3; IntAct=EBI-716384, EBI-458376; CC P30086; Q9NS68: TNFRSF19; NbExp=4; IntAct=EBI-716384, EBI-530381; CC P30086; Q9JLL3: Tnfrsf19; Xeno; NbExp=4; IntAct=EBI-716384, EBI-20800437; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein CC family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44021/PEBP1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D16111; BAA03684.1; -; mRNA. DR EMBL; X75252; CAA53031.1; -; mRNA. DR EMBL; X85033; CAA59404.1; -; mRNA. DR EMBL; AK311927; BAG34868.1; -; mRNA. DR EMBL; CH471054; EAW98122.1; -; Genomic_DNA. DR EMBL; BC008714; AAH08714.1; -; mRNA. DR EMBL; BC017396; AAH17396.1; -; mRNA. DR EMBL; BC031102; AAH31102.1; -; mRNA. DR EMBL; S76773; AAD14234.1; -; mRNA. DR CCDS; CCDS9187.1; -. DR PIR; I53745; I53745. DR RefSeq; NP_002558.1; NM_002567.3. DR PDB; 1BD9; X-ray; 2.05 A; A/B=1-187. DR PDB; 1BEH; X-ray; 1.75 A; A/B=1-187. DR PDB; 2L7W; NMR; -; A=1-187. DR PDB; 2QYQ; X-ray; 1.95 A; A=1-187. DR PDBsum; 1BD9; -. DR PDBsum; 1BEH; -. DR PDBsum; 2L7W; -. DR PDBsum; 2QYQ; -. DR AlphaFoldDB; P30086; -. DR BMRB; P30086; -. DR SMR; P30086; -. DR BioGRID; 111076; 243. DR DIP; DIP-44269N; -. DR IntAct; P30086; 104. DR MINT; P30086; -. DR STRING; 9606.ENSP00000261313; -. DR ChEMBL; CHEMBL4105856; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB09568; Omega-3-carboxylic acids. DR MEROPS; I51.002; -. DR GlyGen; P30086; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P30086; -. DR MetOSite; P30086; -. DR PhosphoSitePlus; P30086; -. DR SwissPalm; P30086; -. DR BioMuta; PEBP1; -. DR DOSAC-COBS-2DPAGE; P30086; -. DR OGP; P30086; -. DR REPRODUCTION-2DPAGE; IPI00219446; -. DR REPRODUCTION-2DPAGE; P30086; -. DR CPTAC; CPTAC-1568; -. DR CPTAC; CPTAC-423; -. DR CPTAC; CPTAC-424; -. DR EPD; P30086; -. DR jPOST; P30086; -. DR MassIVE; P30086; -. DR MaxQB; P30086; -. DR PaxDb; 9606-ENSP00000261313; -. DR PeptideAtlas; P30086; -. DR PRIDE; P30086; -. DR ProteomicsDB; 54634; -. DR Pumba; P30086; -. DR TopDownProteomics; P30086; -. DR Antibodypedia; 2171; 742 antibodies from 44 providers. DR CPTC; P30086; 2 antibodies. DR DNASU; 5037; -. DR Ensembl; ENST00000261313.3; ENSP00000261313.2; ENSG00000089220.5. DR GeneID; 5037; -. DR KEGG; hsa:5037; -. DR MANE-Select; ENST00000261313.3; ENSP00000261313.2; NM_002567.4; NP_002558.1. DR UCSC; uc001twu.2; human. DR AGR; HGNC:8630; -. DR CTD; 5037; -. DR DisGeNET; 5037; -. DR GeneCards; PEBP1; -. DR HGNC; HGNC:8630; PEBP1. DR HPA; ENSG00000089220; Tissue enhanced (liver). DR MIM; 604591; gene. DR neXtProt; NX_P30086; -. DR OpenTargets; ENSG00000089220; -. DR PharmGKB; PA32968; -. DR VEuPathDB; HostDB:ENSG00000089220; -. DR eggNOG; KOG3346; Eukaryota. DR GeneTree; ENSGT00940000163122; -. DR HOGENOM; CLU_043994_5_0_1; -. DR InParanoid; P30086; -. DR OMA; LIYEQKC; -. DR OrthoDB; 3412953at2759; -. DR PhylomeDB; P30086; -. DR TreeFam; TF315074; -. DR PathwayCommons; P30086; -. DR Reactome; R-HSA-5674135; MAP2K and MAPK activation. DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway. DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants. DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants. DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions. DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF. DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants. DR SignaLink; P30086; -. DR SIGNOR; P30086; -. DR BioGRID-ORCS; 5037; 19 hits in 1123 CRISPR screens. DR ChiTaRS; PEBP1; human. DR EvolutionaryTrace; P30086; -. DR GeneWiki; Phosphatidylethanolamine_binding_protein_1; -. DR GenomeRNAi; 5037; -. DR Pharos; P30086; Tchem. DR PRO; PR:P30086; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P30086; Protein. DR Bgee; ENSG00000089220; Expressed in renal medulla and 209 other cell types or tissues. DR ExpressionAtlas; P30086; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0008429; F:phosphatidylethanolamine binding; TAS:ProtInc. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central. DR CDD; cd00866; PEBP_euk; 1. DR Gene3D; 3.90.280.10; PEBP-like; 1. DR InterPro; IPR008914; PEBP. DR InterPro; IPR036610; PEBP-like_sf. DR InterPro; IPR035810; PEBP_euk. DR InterPro; IPR001858; Phosphatidylethanolamine-bd_CS. DR PANTHER; PTHR11362:SF150; PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN; 1. DR PANTHER; PTHR11362; PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN; 1. DR Pfam; PF01161; PBP; 1. DR SUPFAM; SSF49777; PEBP-like; 1. DR PROSITE; PS01220; PBP; 1. DR SWISS-2DPAGE; P30086; -. DR UCD-2DPAGE; P30086; -. DR Genevisible; P30086; HS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; KW Disulfide bond; Lipid-binding; Nucleotide-binding; Phosphoprotein; KW Protease inhibitor; Reference proteome; Serine protease inhibitor. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1286669" FT CHAIN 2..187 FT /note="Phosphatidylethanolamine-binding protein 1" FT /id="PRO_0000023271" FT PEPTIDE 2..12 FT /note="Hippocampal cholinergic neurostimulating peptide" FT /id="PRO_0000023272" FT REGION 93..134 FT /note="Interaction with RAF1" FT /evidence="ECO:0000269|PubMed:18294816" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31044" FT MOD_RES 42 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 52 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 54 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 98 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 153 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VARIANT 9 FT /note="S -> N" FT /id="VAR_006048" FT CONFLICT 8 FT /note="W -> K (in Ref. 2)" FT /evidence="ECO:0000305" FT HELIX 5..7 FT /evidence="ECO:0007829|PDB:1BEH" FT TURN 8..12 FT /evidence="ECO:0007829|PDB:2QYQ" FT HELIX 14..16 FT /evidence="ECO:0007829|PDB:1BEH" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:1BEH" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:1BEH" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:2QYQ" FT TURN 43..46 FT /evidence="ECO:0007829|PDB:1BEH" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:1BEH" FT STRAND 62..71 FT /evidence="ECO:0007829|PDB:1BEH" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:1BEH" FT STRAND 84..93 FT /evidence="ECO:0007829|PDB:1BEH" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:1BEH" FT STRAND 100..104 FT /evidence="ECO:0007829|PDB:1BEH" FT STRAND 118..129 FT /evidence="ECO:0007829|PDB:1BEH" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:1BEH" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:1BD9" FT HELIX 151..157 FT /evidence="ECO:0007829|PDB:1BEH" FT STRAND 164..171 FT /evidence="ECO:0007829|PDB:1BEH" FT HELIX 177..183 FT /evidence="ECO:0007829|PDB:1BEH" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:2L7W" SQ SEQUENCE 187 AA; 21057 MW; F1E9F17E2CD11C36 CRC64; MPVDLSKWSG PLSLQEVDEQ PQHPLHVTYA GAAVDELGKV LTPTQVKNRP TSISWDGLDS GKLYTLVLTD PDAPSRKDPK YREWHHFLVV NMKGNDISSG TVLSDYVGSG PPKGTGLHRY VWLVYEQDRP LKCDEPILSN RSGDHRGKFK VASFRKKYEL RAPVAGTCYQ AEWDDYVPKL YEQLSGK //