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Reviewed, UniProtKB/Swiss-Prot P30086 (PEBP1_HUMAN)

Last modified June 16, 2009. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
Name: PEBP1
Synonyms: PBP, PEBP
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 187186Phosphatidylethanolamine-binding protein 1
PRO_0000023271
Peptide2 – 1211Hippocampal cholinergic neurostimulating peptide
PRO_0000023272

Amino acid modifications

Modified residue421Phosphothreonine Ref.11
Modified residue521Phosphoserine Ref.11 Ref.10
Modified residue541Phosphoserine By similarity

Natural variations

Natural variant91S → N
VAR_006048

Experimental info

Sequence conflict81W → K Ref.2

Secondary structure

.................................. 187
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30086-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F1E9F17E2CD11C36

FASTA18721,057
        10         20         30         40         50         60 
MPVDLSKWSG PLSLQEVDEQ PQHPLHVTYA GAAVDELGKV LTPTQVKNRP TSISWDGLDS 

        70         80         90        100        110        120 
GKLYTLVLTD PDAPSRKDPK YREWHHFLVV NMKGNDISSG TVLSDYVGSG PPKGTGLHRY 

       130        140        150        160        170        180 
VWLVYEQDRP LKCDEPILSN RSGDHRGKFK VASFRKKYEL RAPVAGTCYQ AEWDDYVPKL 


YEQLSGK 

« Hide

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.
IPIIPI00219446.
PIRI53745.
RefSeqNP_002558.1.
UniGeneHs.433863
Hs.713526

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BD9X-ray2.05A/B1-187[»]
1BEHX-ray1.75A/B1-187[»]
2QYQX-ray1.95A1-187[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP30086. 13 interactions.

Protein family/group databases

MEROPSI51.002.

PTM databases

PhosphoSiteP30086.

2-D gel databases

SWISS-2DPAGEP30086.
DOSAC-COBS-2DPAGEP30086.
OGPP30086.
REPRODUCTION-2DPAGEIPI00219446.
P30086.
Siena-2DPAGEP30086.

Proteomic databases

PeptideAtlasP30086.
PRIDEP30086.

Genome annotation databases

EnsemblENSG00000089220. Homo sapiens. [Contig view]
GeneID5037.
KEGGhsa:5037.

Organism-specific databases

GeneCardsGC12P117058.
H-InvDBHIX0011046.
HGNCHGNC:8630. PEBP1.
HPACAB009906.
CAB013493.
HPA008819.
MIM604591. gene.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP30086.
HOVERGENP30086.
OMAP30086. QEVDERP.

Enzyme and pathway databases

Pathway_Interaction_DBaurora_b_pathway. Aurora B signaling.

Gene expression databases

BgeeP30086.
CleanExHS_PEBP1.
GermOnlineENSG00000089220. Homo sapiens.

Family and domain databases

InterProIPR001858. Phosphotidylethanolamine_bd_CS.
IPR008914. PtdEtn-bd_prot_PEBP.
[Graphical view]
PfamPF01161. PBP. 1 hit.
[Graphical view]
ProDomPD004330. PBP. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS01220. PBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio19408.
SOURCESearch...

Entry information

Entry namePEBP1_HUMAN
AccessionPrimary (citable) accession number: P30086
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents