[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Liver; DOI=10.1038/349423a0; PubMed=1846945 [NCBI, ExPASy, EBI, Israel, Japan] Potter E., Behan D.P., Fischer W.H., Linton E.A., Lowry P.J., Vale W.W.; "Cloning and characterization of the cDNAs for human and rat corticotropin releasing factor-binding proteins."; Nature 349:423-426(1991).
[2]	SEQUENCE REVISION TO 47-48 AND 248, AND DISULFIDE BONDS. PubMed=8307998 [NCBI, ExPASy, EBI, Israel, Japan] Fischer W.H., Behan D.P., Park M., Potter E., Lowry P.J., Vale W.W.; "Assignment of disulfide bonds in corticotropin-releasing factor-binding protein."; J. Biol. Chem. 269:4313-4316(1994).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Hippocampus; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27. DOI=10.1006/geno.1993.1141; PubMed=8198617 [NCBI, ExPASy, EBI, Israel, Japan] Behan D.P., Potter E., Lewis K.A., Jenkins N.A., Copeland N.G., Lowry P.J., Vale W.W.; "Cloning and structure of the human corticotrophin releasing factor-binding protein gene (CRHBP)."; Genomics 16:63-68(1993).

Comments

FUNCTION: Binds CRF and inactivates it. May prevent inappropriate pituitary-adrenal stimulation in pregnancy.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X58022; CAA41086.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S60697; AAD13916.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018038; AAH18038.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00306844; -.

S13640; S13640.

NP_001873.2; -.

3D structure databases

ModBase

P24387.

Organism-specific databases

GC05P076284; -.

HIX0004962; -.

HGNC:2356; CRHBP.

122559; gene. [NCBI / EBI]

PharmGKB

PA26873; -.

Gene expression databases

P24387; -.

P24387; -.

HS_CRHBP; -.

ENSG00000145708; Homo sapiens.

Ontologies

GO:0005625;	Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (traceable author statement from ProtInc).
GO:0007565;	Biological process: female pregnancy (traceable author statement from ProtInc).
GO:0007611;	Biological process: learning or memory (traceable author statement from ProtInc).
GO:0007165;	Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR008435; CRF_bd.
Graphical view of domain structure.

PANTHER

PTHR10278; CRF_bd; 1.

Pfam

PF05428; CRF-BP; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF009279; CRF_bd; 1.

Proteomic databases

PeptideAtlas

P24387; -.

PRIDE

P24387; -.

Genome annotation databases

Ensembl

ENSG00000145708; Homo sapiens. [Contig view]

GeneID

1393; -.

KEGG

hsa:1393; -.

Phylogenomic databases

HOGENOM

P24387; -.

HOVERGEN

P24387; -.

OMA

P24387; QTPNGRF.

Other

5699; -.

CRHBP; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Disulfide bond; Glycoprotein; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`
`CHAIN`	`25 322`	`298`	`Corticotropin-releasing factor-binding protein.`	`PRO_0000020994`
`CARBOHYD`	`204 204`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`60 81`
`DISULFID`	`104 141`
`DISULFID`	`183 205`
`DISULFID`	`237 264`
`DISULFID`	`277 318`

Sequence information

Length: 322 AA [This is the length of the unprocessed precursor]

Molecular weight: 36144 Da [This is the MW of the unprocessed precursor]

CRC64: 771A894BE06039BD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSPNFKLQCH FILIFLTALR GESRYLELRE AADYDPFLLF SANLKRELAG EQPYRRALRC 

        70         80         90        100        110        120 
LDMLSLQGQF TFTADRPQLH CAAFFISEPE EFITIHYDQV SIDCQGGDFL KVFDGWILKG 

       130        140        150        160        170        180 
EKFPSSQDHP LPSAERYIDF CESGLSRRSI RSSQNVAMIF FRVHEPGNGF TLTIKTDPNL 

       190        200        210        220        230        240 
FPCNVISQTP NGKFTLVVPH QHRNCSFSII YPVVIKISDL TLGHVNGLQL KKSSAGCEGI 

       250        260        270        280        290        300 
GDFVELLGGT GLDPSKMTPL ADLCYPFHGP AQMKVGCDNT VVRMVSSGKH VNRVTFEYRQ 

       310        320 
LEPYELENPN GNSIGEFCLS GL

P24387 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools