PEBP1_HUMAN
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 03-AUG-2022, entry version 217.
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="http://atlasgeneticsoncology.org/Genes/PEBP1ID44021ch12q24.html";
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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; 204.
DR DIP; DIP-44269N; -.
DR IntAct; P30086; 95.
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 SWISS-2DPAGE; P30086; -.
DR UCD-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; P30086; -.
DR PeptideAtlas; P30086; -.
DR PRIDE; P30086; -.
DR ProteomicsDB; 54634; -.
DR TopDownProteomics; P30086; -.
DR Antibodypedia; 2171; 701 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 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; TGCVMSD; -.
DR OrthoDB; 1557122at2759; -.
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; 18 hits in 1045 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 207 other tissues.
DR ExpressionAtlas; P30086; baseline and differential.
DR Genevisible; P30086; HS.
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; -; 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; PTHR11362; 1.
DR Pfam; PF01161; PBP; 1.
DR SUPFAM; SSF49777; SSF49777; 1.
DR PROSITE; PS01220; PBP; 1.
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
