Reviewed,
UniProtKB/Swiss-Prot P30086 (PEBP1_HUMAN)
Last modified
June 16, 2009.
Version 101.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Phosphatidylethanolamine-binding protein 1 Short name=PEBP-1 Alternative name(s): Prostatic-binding protein HCNPpp Neuropolypeptide h3 Raf kinase inhibitor protein Short name=RKIP Cleaved into the following chain: 1- Recommended name: Hippocampal cholinergic neurostimulating peptide Short name=HCNP | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 187 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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. 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. |
| Subunit structure | Interacts with Raf-1 and seems to inhibit it. Ref.9 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the phosphatidylethanolamine-binding protein family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Lipid-binding Nucleotide-binding |
| Molecular function | Protease inhibitor Serine protease inhibitor |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylethanolamine binding Ref.2Traceable author statement. Source: ProtInc protein bindingInferred from physical interaction. Source: IntAct serine-type endopeptidase inhibitor activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| CDK2 | P24941 | 1 | EBI-716384,EBI-375096 | |
| PACSIN3 | Q9UKS6 | 1 | EBI-716384,EBI-77926 | |
| PIK3R1 | P27986 | 1 | EBI-716384,EBI-79464 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.5 | |||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 187 | 186 | Phosphatidylethanolamine-binding protein 1 | PRO_0000023271 | ||||||||||||||||||||||||||||||||||||||
| Peptide | 2 – 12 | 11 | Hippocampal cholinergic neurostimulating peptide | PRO_0000023272 | ||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 42 | 1 | Phosphothreonine Ref.11 | |||||||||||||||||||||||||||||||||||||||
| Modified residue | 52 | 1 | Phosphoserine Ref.11 Ref.10 | |||||||||||||||||||||||||||||||||||||||
| Modified residue | 54 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 9 | 1 | S → N | VAR_006048 | ||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 8 | 1 | W → K Ref.2 | |||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 6 – 9 | 4 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 14 – 16 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 22 – 24 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 26 – 29 | 4 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 32 – 34 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 44 – 46 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 51 – 54 | 4 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 62 – 70 | 9 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 76 – 78 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 84 – 93 | 10 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 97 – 99 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 100 – 104 | 5 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 118 – 126 | 9 | ||||||||||||||||||||||||||||||||||||||||
| Turn | 144 – 146 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 151 – 157 | 7 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 164 – 171 | 8 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 177 – 183 | 7 | ||||||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "A human cDNA sequence homologue of bovine phosphatidylethanolamine-binding protein." Hori N., Keon-Sang C., Murakawa K., Matoba R., Fukushima A., Okubo K., Matsubara K. Gene 140:293-294(1994) [PubMed: 8144042] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein." Tohdoh N., Tojo S., Agui H., Ojika K. Brain Res. Mol. Brain Res. 30:381-384(1995) [PubMed: 7637590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta. |
| [3] | Hall L. Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Hypothalamus and Lung. |
| [5] | "Human liver protein map: a reference database established by microsequencing and gel comparison." Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J. Electrophoresis 13:992-1001(1992) [PubMed: 1286669] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11. Tissue: Liver. |
| [6] | Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 8-39; 48-77; 81-113; 120-141 AND 162-187, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex. |
| [7] | "Amino acid sequence of the Homo sapiens brain 21-23-kDa protein (neuropolypeptide h3), comparison with its counterparts from Rattus norvegicus and Bos taurus species, and expression of its mRNA in different tissues." Seddiqi N., Bollengier F., Alliel P.M., Perin J.-P., Bonnet F., Bucquoy S., Jolles P., Schoentgen F. J. Mol. Evol. 39:655-660(1994) [PubMed: 7807553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-187. Tissue: Brain. |
| [8] | "Hippocampal cholinergic neurostimulating peptides (HCNP)." Ojika K., Mitake S., Tohdoh N., Appel S.H., Otsuka Y., Katada E., Matsukawa N. Prog. Neurobiol. 60:37-83(2000) [PubMed: 10622376] [Abstract] Cited for: CHARACTERIZATION OF HCNP. |
| [9] | "Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP." Yeung K., Seitz T., Li S., Janosch P., McFerran B., Kaiser C., Fee F., Katsanakis K.D., Rose D.W., Mischak H., Sedivy J.M., Kolch W. Nature 401:173-177(1999) [PubMed: 10490027] [Abstract] Cited for: INTERACTION WITH RAF-1. |
| [10] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, MASS SPECTROMETRY. Tissue: Epithelium. |
| [11] | "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) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 AND SER-52, MASS SPECTROMETRY. |
| [12] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [13] | "Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction." Banfield M.J., Barker J.J., Perry A.C., Brady R.L. Structure 6:1245-1254(1998) [PubMed: 9782050] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| D16111 mRNA. Translation: BAA03684.1. X75252 mRNA. Translation: CAA53031.1. X85033 mRNA. Translation: CAA59404.1. BC008714 mRNA. Translation: AAH08714.1. BC017396 mRNA. Translation: AAH17396.1. BC031102 mRNA. Translation: AAH31102.1. S76773 mRNA. Translation: AAD14234.1. | |||||||||||||||||||||||||
| IPI | IPI00219446. | ||||||||||||||||||||||||
| PIR | I53745. | ||||||||||||||||||||||||
| RefSeq | NP_002558.1. | ||||||||||||||||||||||||
| UniGene | Hs.433863 Hs.713526 | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| |||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| IntAct | P30086. 13 interactions. | ||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||
| MEROPS | I51.002. | ||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||
| PhosphoSite | P30086. | ||||||||||||||||||||||||
2-D gel databases | |||||||||||||||||||||||||
| SWISS-2DPAGE | P30086. | ||||||||||||||||||||||||
| DOSAC-COBS-2DPAGE | P30086. | ||||||||||||||||||||||||
| OGP | P30086. | ||||||||||||||||||||||||
| REPRODUCTION-2DPAGE | IPI00219446. P30086. | ||||||||||||||||||||||||
| Siena-2DPAGE | P30086. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PeptideAtlas | P30086. | ||||||||||||||||||||||||
| PRIDE | P30086. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENSG00000089220. Homo sapiens. [Contig view] | ||||||||||||||||||||||||
| GeneID | 5037. | ||||||||||||||||||||||||
| KEGG | hsa:5037. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| GeneCards | GC12P117058. | ||||||||||||||||||||||||
| H-InvDB | HIX0011046. | ||||||||||||||||||||||||
| HGNC | HGNC:8630. PEBP1. | ||||||||||||||||||||||||
| HPA | CAB009906. CAB013493. HPA008819. | ||||||||||||||||||||||||
| MIM | 604591. gene. | ||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOGENOM | P30086. | ||||||||||||||||||||||||
| HOVERGEN | P30086. | ||||||||||||||||||||||||
| OMA | P30086. QEVDERP. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| Pathway_Interaction_DB | aurora_b_pathway. Aurora B signaling. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| Bgee | P30086. | ||||||||||||||||||||||||
| CleanEx | HS_PEBP1. | ||||||||||||||||||||||||
| GermOnline | ENSG00000089220. Homo sapiens. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR001858. Phosphotidylethanolamine_bd_CS. IPR008914. PtdEtn-bd_prot_PEBP. [Graphical view] | ||||||||||||||||||||||||
| Pfam | PF01161. PBP. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProDom | PD004330. PBP. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||||||||
| PROSITE | PS01220. PBP. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||
| NextBio | 19408. | ||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | PEBP1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P30086 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 12 Human chromosome 12: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


