P30086 (PEBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. 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'. Ref.11 Ref.13
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	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
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 Traceable author statement Ref.2. Source: ProtInc serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 187

186

Phosphatidylethanolamine-binding protein 1

PRO_0000023271

Peptide

2 – 12

11

Hippocampal cholinergic neurostimulating peptide

PRO_0000023272

Regions

Region

93 – 134

42

Interaction with RAF1

Amino acid modifications

Modified residue

42

1

Phosphothreonine Ref.14

Modified residue

52

1

Phosphoserine Ref.14 Ref.15 Ref.16 Ref.18

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

1

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187

Helix Strand Turn

Details...

Helix

5 – 7

3

Turn

8 – 12

5

Helix

14 – 16

3

Beta strand

22 – 24

3

Beta strand

26 – 28

3

Beta strand

32 – 34

3

Turn

43 – 46

4

Beta strand

51 – 54

4

Beta strand

62 – 71

10

Beta strand

76 – 78

3

Beta strand

84 – 93

10

Helix

97 – 99

3

Beta strand

100 – 104

5

Beta strand

118 – 129

12

Beta strand

140 – 142

3

Turn

144 – 146

3

Helix

151 – 157

7

Beta strand

164 – 171

8

Helix

177 – 183

7

Turn

184 – 186

3

Sequences

	Sequence		Length	Mass (Da)
	P30086 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F1E9F17E2CD11C36	FASTA	187	21,057
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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, MASS SPECTROMETRY.
[19]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00219446.

PIR

I53745.

RefSeq

NP_002558.1. NM_002567.2.

UniGene

Hs.433863.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BD9	X-ray	2.05	A/B	1-187	[»]
1BEH	X-ray	1.75	A/B	1-187	[»]
2L7W	NMR	-	A	1-187	[»]
2QYQ	X-ray	1.95	A	1-187	[»]

ProteinModelPortal

P30086.

ModBase

Search...

Protein-protein interaction databases

IntAct

P30086. 6 interactions.

MINT

MINT-5002544.

STRING

9606.ENSP00000261313.

Protein family/group databases

MEROPS

I51.002.

PTM databases

PhosphoSite

P30086.

Polymorphism databases

DMDM

1352726.

2D gel databases

DOSAC-COBS-2DPAGE

P30086.

OGP

P30086.

REPRODUCTION-2DPAGE

IPI00219446.
P30086.

SWISS-2DPAGE

P30086.

UCD-2DPAGE

P30086.

Proteomic databases

PaxDb

P30086.

PeptideAtlas

P30086.

PRIDE

P30086.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261313; ENSP00000261313; ENSG00000089220.

GeneID

5037.

KEGG

hsa:5037.

UCSC

uc001twu.1. human.

Organism-specific databases

CTD

5037.

GeneCards

GC12P118573.

HGNC

HGNC:8630. PEBP1.

HPA

CAB009906.
CAB013493.
HPA008819.

MIM

604591. gene.

neXtProt

NX_P30086.

PharmGKB

PA32968.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1881.

HOGENOM

HOG000237655.

HOVERGEN

HBG008165.

InParanoid

P30086.

OMA

NDVSSGC.

OrthoDB

EOG4FFD2T.

PhylomeDB

P30086.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_b_pathway. Aurora B signaling.

Gene expression databases

ArrayExpress

P30086.

Bgee

P30086.

CleanEx

HS_PEBP1.

Genevestigator

P30086.

GermOnline

ENSG00000089220. Homo sapiens.

Family and domain databases

Gene3D

3.90.280.10. 1 hit.

InterPro

IPR001858. Phosphotidylethanolamine-bd_CS.
IPR008914. PtdEtn-bd_prot_PEBP.
[Graphical view]

Pfam

PF01161. PBP. 1 hit.
[Graphical view]

SUPFAM

SSF49777. PEBP. 1 hit.

PROSITE

PS01220. PBP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PEBP1. human.

EvolutionaryTrace

P30086.

GenomeRNAi

5037.

NextBio

19408.

SOURCE

Search...

Entry information

Entry name

PEBP1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 143 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.