| IED ID | IndEnz0002000379 |
| Enzyme Type ID | protease000379 |
| Protein Name |
Phosphatidylethanolamine-binding protein 1 PEBP-1 HCNPpp Neuropolypeptide h3 Prostatic-binding protein Raf kinase inhibitor protein RKIP Cleaved into: Hippocampal cholinergic neurostimulating peptide HCNP |
| Gene Name | PEBP1 PBP PEBP |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSGTVLSDYVGSGPPKGTGLHRYVWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKLYEQLSGK |
| Enzyme Length | 187 |
| Uniprot Accession Number | P30086 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | 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. {ECO:0000250, ECO:0000269|PubMed:18294816}.; FUNCTION: 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). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (11); Chain (1); Helix (5); Initiator methionine (1); Modified residue (7); Natural variant (1); Peptide (1); Region (1); Sequence conflict (1); Turn (4) |
| Keywords | 3D-structure;ATP-binding;Cytoplasm;Direct protein sequencing;Disulfide bond;Lipid-binding;Nucleotide-binding;Phosphoprotein;Protease inhibitor;Reference proteome;Serine protease inhibitor |
| Interact With | P16050; Q9NRD5; P04049; Q15208; Q9NS68; Q9JLL3 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | MOD_RES 6; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 13; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P31044"; MOD_RES 42; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 52; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 54; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 98; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 153; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (3) |
| Cross Reference PDB | 1BD9; 1BEH; 2L7W; 2QYQ; |
| Mapped Pubmed ID | 10209122; 10409742; 10725339; 10757792; 10891492; 12473660; 12551925; 12832465; 14636584; 14654844; 14766752; 14970219; 15035987; 15327891; 15543157; 15630448; 15782137; 16135787; 16169070; 16243812; 16364920; 16513087; 16865242; 16916643; 17018026; 17030190; 17097642; 17145707; 17179102; 17353931; 17474147; 17496912; 17563371; 17911631; 17952120; 18172264; 18329792; 18375747; 18483365; 18567796; 18974108; 19034380; 19091303; 19096942; 19101508; 19103740; 19158341; 19165527; 19219045; 19228192; 19279408; 19291429; 19342899; 19357705; 19367706; 19405953; 19551145; 19564817; 19705153; 19779262; 19933846; 19955695; 19957553; 20028985; 20043910; 20130576; 20141835; 20179705; 20463977; 20526349; 20533335; 20562859; 20564197; 20682295; 20734161; 20739083; 20853079; 20855151; 20869966; 21080875; 21180766; 21303975; 21332389; 21424530; 21426659; 21556737; 21565611; 21617351; 21664646; 21672326; 21685394; 21689459; 21732351; 21779496; 21873975; 21875465; 21988832; 22031589; 22102006; 22177953; 22246605; 22248055; 22279539; 22292035; 22295570; 22373584; 22460832; 22463874; 22492043; 22505648; 22510884; 22558375; 22562283; 22569528; 22605662; 22662230; 22692503; 22745804; 22809510; 22833545; 22855160; 22875620; 22899242; 22935977; 22983529; 23066033; 23066640; 23075684; 23095933; 23254962; 23259789; 23352452; 23359513; 23376254; 23460950; 23583981; 23601922; 23632477; 23636063; 23674108; 23814485; 23872143; 23959677; 23975428; 23991415; 24048798; 24123286; 24135138; 24202393; 24286018; 24330423; 24335512; 24345920; 24392454; 24395801; 24420151; 24655025; 24763848; 24863296; 24957944; 25015191; 25017365; 25104559; 25128483; 25171481; 25172097; 25204415; 25231108; 25277181; 25337233; 25435214; 25547433; 25597351; 25597352; 25597353; 25597354; 25597355; 25597357; 25597358; 25764514; 25819500; 25907612; 25915430; 26116914; 26177829; 26238523; 26238785; 26308852; 26375811; 26479924; 26558823; 26617724; 26638075; 26716415; 26801887; 26823735; 26859895; 27197200; 27444299; 27470585; 27540684; 27565262; 27647315; 27651238; 27902472; 28031115; 28245474; 28418894; 28529999; 29053969; 29295844; 29315556; 29534584; 29858683; 29930472; 29990987; 30244177; 30282734; 30337686; 30608040; 31655041; 31960115; 32194149; 32513718; 32632129; 32924251; 33151569; 33336737; 33802672; 7565670; 9858547; |
| Motif | |
| Gene Encoded By | |
| Mass | 21,057 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |