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P30086 (PEBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylethanolamine-binding protein 1

Short name=PEBP-1
Alternative name(s):
HCNPpp
Neuropolypeptide h3
Prostatic-binding protein
Raf kinase inhibitor protein
Short name=RKIP

Cleaved into the following chain:

  1. Hippocampal cholinergic neurostimulating peptide
    Short name=HCNP
Gene names
Name:PEBP1
Synonyms:PBP, PEBP
OrganismHomo sapiens (Human) [Reference proteome]
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. 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. Ref.13

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. Ref.13

Subunit structure

Has a tendency to form dimers by disulfide cross-linking By similarity. Interacts with RAF1 and this interaction is enhanced if RAF1 is phosphorylated on residues 'Ser-338', 'Ser-339', 'Tyr-340' and 'Tyr-341'. Interacts with ALOX15; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade. Ref.11 Ref.13 Ref.18

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the phosphatidylethanolamine-binding protein family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAF1P040497EBI-716384,EBI-365996

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 187186Phosphatidylethanolamine-binding protein 1
PRO_0000023271
Peptide2 – 1211Hippocampal cholinergic neurostimulating peptide
PRO_0000023272

Regions

Region93 – 13442Interaction with RAF1

Amino acid modifications

Modified residue421Phosphothreonine Ref.14
Modified residue521Phosphoserine Ref.14 Ref.15 Ref.16 Ref.19

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 [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] [Europe PMC] [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] [Europe PMC] [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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Hypothalamus and Lung.
[7]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Tissue: Liver.
[8]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-187.
Tissue: Brain.
[10]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF HCNP.
[11]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAF-1.
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"The RKIP (Raf-1 Kinase Inhibitor Protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK."
Rath O., Park S., Tang H.H., Banfield M.J., Brady R.L., Lee Y.C., Dignam J.D., Sedivy J.M., Kolch W., Yeung K.C.
Cell. Signal. 20:935-941(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAF1.
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 AND SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells."
Zhao J., O'Donnell V.B., Balzar S., St Croix C.M., Trudeau J.B., Wenzel S.E.
Proc. Natl. Acad. Sci. U.S.A. 108:14246-14251(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALOX15.
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D16111 mRNA. Translation: BAA03684.1.
X75252 mRNA. Translation: CAA53031.1.
X85033 mRNA. Translation: CAA59404.1.
AK311927 mRNA. Translation: BAG34868.1.
CH471054 Genomic DNA. Translation: EAW98122.1.
BC008714 mRNA. Translation: AAH08714.1.
BC017396 mRNA. Translation: AAH17396.1.
BC031102 mRNA. Translation: AAH31102.1.
S76773 mRNA. Translation: AAD14234.1.
PIRI53745.
RefSeqNP_002558.1. NM_002567.2.
UniGeneHs.433863.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BD9X-ray2.05A/B1-187[»]
1BEHX-ray1.75A/B1-187[»]
2L7WNMR-A1-187[»]
2QYQX-ray1.95A1-187[»]
ProteinModelPortalP30086.
SMRP30086. Positions 3-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111076. 17 interactions.
DIPDIP-44269N.
IntActP30086. 8 interactions.
MINTMINT-5002544.
STRING9606.ENSP00000261313.

Protein family/group databases

MEROPSI51.002.

PTM databases

PhosphoSiteP30086.

2D gel databases

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

Proteomic databases

PaxDbP30086.
PeptideAtlasP30086.
PRIDEP30086.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261313; ENSP00000261313; ENSG00000089220.
GeneID5037.
KEGGhsa:5037.
UCSCuc001twu.1. human.

Organism-specific databases

CTD5037.
GeneCardsGC12P118573.
HGNCHGNC:8630. PEBP1.
HPACAB009906.
CAB013493.
HPA008819.
MIM604591. gene.
neXtProtNX_P30086.
PharmGKBPA32968.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1881.
HOGENOMHOG000237655.
HOVERGENHBG008165.
InParanoidP30086.
OMANDVSSGC.
OrthoDBEOG7P02K3.
PhylomeDBP30086.
TreeFamTF315074.

Enzyme and pathway databases

SignaLinkP30086.

Gene expression databases

ArrayExpressP30086.
BgeeP30086.
CleanExHS_PEBP1.
GenevestigatorP30086.

Family and domain databases

Gene3D3.90.280.10. 1 hit.
InterProIPR001858. Phosphotidylethanolamine-bd_CS.
IPR008914. PtdEtn-bd_prot_PEBP.
[Graphical view]
PfamPF01161. PBP. 1 hit.
[Graphical view]
SUPFAMSSF49777. SSF49777. 1 hit.
PROSITEPS01220. PBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPEBP1. human.
EvolutionaryTraceP30086.
GeneWikiPhosphatidylethanolamine_binding_protein_1.
GenomeRNAi5037.
NextBio19408.
PROP30086.
SOURCESearch...

Entry information

Entry namePEBP1_HUMAN
AccessionPrimary (citable) accession number: P30086
Secondary accession number(s): B2R4S1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM