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Protein

Natriuretic peptides B

Gene

NPPB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cardiac hormone which may function as a paracrine antifibrotic factor in the heart. Also plays a key role in cardiovascular homeostasis through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei104 – 1052Cleavage; by FAP1 Publication

GO - Molecular functioni

  • diuretic hormone activity Source: UniProtKB
  • hormone activity Source: UniProtKB
  • receptor binding Source: UniProtKB

GO - Biological processi

  • body fluid secretion Source: UniProtKB
  • cell surface receptor signaling pathway Source: UniProtKB
  • cGMP biosynthetic process Source: UniProtKB
  • negative regulation of angiogenesis Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • positive regulation of renal sodium excretion Source: UniProtKB
  • positive regulation of urine volume Source: UniProtKB
  • receptor guanylyl cyclase signaling pathway Source: UniProtKB
  • regulation of blood pressure Source: UniProtKB
  • regulation of blood vessel size Source: UniProtKB-KW
  • regulation of vascular permeability Source: UniProtKB
  • regulation of vasodilation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hormone, Vasoactive

Names & Taxonomyi

Protein namesi
Recommended name:
Natriuretic peptides B
Alternative name(s):
Gamma-brain natriuretic peptide
Cleaved into the following 16 chains:
Gene namesi
Name:NPPB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7940. NPPB.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

Available under the name Nesiritide (Scios). Used for the treatment of heart failure.

Organism-specific databases

PharmGKBiPA31734.

Chemistry

DrugBankiDB01136. Carvedilol.

Polymorphism and mutation databases

BioMutaiNPPB.
DMDMi113836.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 134108Natriuretic peptides BPRO_0000001531Add
BLAST
Peptidei103 – 13432Brain natriuretic peptide 32PRO_0000001532Add
BLAST
Peptidei103 – 13230BNP(1-30)PRO_0000364993Add
BLAST
Peptidei103 – 13129BNP(1-29)PRO_0000364994Add
BLAST
Peptidei103 – 13028BNP(1-28)PRO_0000364995Add
BLAST
Peptidei104 – 13330BNP(2-31)PRO_0000364996Add
BLAST
Peptidei105 – 13430BNP(3-32)PRO_0000364997Add
BLAST
Peptidei105 – 13228BNP(3-30)PRO_0000364998Add
BLAST
Peptidei105 – 13127BNP(3-29)PRO_0000364999Add
BLAST
Peptidei106 – 13429BNP(4-32)PRO_0000365000Add
BLAST
Peptidei106 – 13328BNP(4-31)PRO_0000365001Add
BLAST
Peptidei106 – 13227BNP(4-30)PRO_0000365002Add
BLAST
Peptidei106 – 13126BNP(4-29)PRO_0000365003Add
BLAST
Peptidei106 – 12924BNP(4-27)PRO_0000365004Add
BLAST
Peptidei107 – 13428BNP(5-32)PRO_0000365005Add
BLAST
Peptidei107 – 13327BNP(5-31)PRO_0000365006Add
BLAST
Peptidei107 – 13125BNP(5-29)PRO_0000365007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621O-linked (HexNAc...); Partial1 Publication
Glycosylationi63 – 631O-linked (HexNAc...)1 Publication
Glycosylationi70 – 701O-linked (HexNAc...)1 Publication
Glycosylationi74 – 741O-linked (HexNAc...)1 Publication
Glycosylationi79 – 791O-linked (HexNAc...)1 Publication
Glycosylationi84 – 841O-linked (HexNAc...); Partial1 Publication
Glycosylationi97 – 971O-linked (HexNAc...)1 Publication
Disulfide bondi112 ↔ 1281 Publication

Post-translational modificationi

The brain natriuretic peptide 32 form is cleaved at Pro-104 by the prolyl endopeptidase FAP (seprase) activity (in vitro).1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP16860.
PRIDEiP16860.

PTM databases

PhosphoSiteiP16860.

Miscellaneous databases

PMAP-CutDBP16860.

Expressioni

Tissue specificityi

Brain and also in atria, but at much lower levels than ANP.

Gene expression databases

BgeeiP16860.
CleanExiHS_NPPB.
GenevestigatoriP16860.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KRT40Q6A1623EBI-747044,EBI-10171697
KRTAP10-9P604113EBI-747044,EBI-10172052
NOTCH2NLQ7Z3S93EBI-747044,EBI-945833
PSMA3P257883EBI-747044,EBI-348380

Protein-protein interaction databases

BioGridi110939. 11 interactions.
IntActiP16860. 7 interactions.
MINTiMINT-1434895.
STRINGi9606.ENSP00000365651.

Structurei

Secondary structure

1
134
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi121 – 1233Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YK1X-ray2.90E111-131[»]
3N56X-ray3.10C/D103-134[»]
DisProtiDP00551.
ProteinModelPortaliP16860.
SMRiP16860. Positions 103-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16860.

Family & Domainsi

Sequence similaritiesi

Belongs to the natriuretic peptide family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG67899.
GeneTreeiENSGT00510000049822.
HOGENOMiHOG000033937.
HOVERGENiHBG004227.
InParanoidiP16860.
KOiK12335.
OMAiSGCFGRK.
OrthoDBiEOG7P2XV4.
PhylomeDBiP16860.
TreeFamiTF106304.

Family and domain databases

InterProiIPR000663. Natr_peptide.
IPR030480. Natr_peptide_CS.
IPR002408. Natriuretic_peptide_brain.
[Graphical view]
PfamiPF00212. ANP. 1 hit.
[Graphical view]
PRINTSiPR00712. BNATPEPTIDE.
SMARTiSM00183. NAT_PEP. 1 hit.
[Graphical view]
PROSITEiPS00263. NATRIURETIC_PEPTIDE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16860-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPQTAPSRA LLLLLFLHLA FLGGRSHPLG SPGSASDLET SGLQEQRNHL
60 70 80 90 100
QGKLSELQVE QTSLEPLQES PRPTGVWKSR EVATEGIRGH RKMVLYTLRA
110 120 130
PRSPKMVQGS GCFGRKMDRI SSSSGLGCKV LRRH
Length:134
Mass (Da):14,726
Last modified:August 1, 1990 - v1
Checksum:iDC884D9408462146
GO

Sequence cautioni

The sequence BAA90441.1 differs from that shown. Reason: Frameshift at position 44. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251R → L.
Corresponds to variant rs5227 [ dbSNP | Ensembl ].
VAR_014580
Natural varianti47 – 471R → H.
Corresponds to variant rs5229 [ dbSNP | Ensembl ].
VAR_014581
Natural varianti93 – 931M → L.
Corresponds to variant rs5230 [ dbSNP | Ensembl ].
VAR_014582

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31776 Genomic DNA. Translation: AAA35603.1.
M25296 mRNA. Translation: AAA36355.1.
AB037521 Genomic DNA. Translation: BAA90441.1. Frameshift.
CR541976 mRNA. Translation: CAG46774.1.
CR542003 mRNA. Translation: CAG46800.1.
EU326309 Genomic DNA. Translation: ACA05917.1.
AL021155 Genomic DNA. Translation: CAA15956.1.
CH471130 Genomic DNA. Translation: EAW71718.1.
BC025785 mRNA. Translation: AAH25785.1.
CCDSiCCDS140.1.
PIRiA36736. AWHUB.
RefSeqiNP_002512.1. NM_002521.2.
UniGeneiHs.219140.

Genome annotation databases

EnsembliENST00000376468; ENSP00000365651; ENSG00000120937.
GeneIDi4879.
KEGGihsa:4879.
UCSCiuc001atj.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Brain natriuretic peptide entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31776 Genomic DNA. Translation: AAA35603.1.
M25296 mRNA. Translation: AAA36355.1.
AB037521 Genomic DNA. Translation: BAA90441.1. Frameshift.
CR541976 mRNA. Translation: CAG46774.1.
CR542003 mRNA. Translation: CAG46800.1.
EU326309 Genomic DNA. Translation: ACA05917.1.
AL021155 Genomic DNA. Translation: CAA15956.1.
CH471130 Genomic DNA. Translation: EAW71718.1.
BC025785 mRNA. Translation: AAH25785.1.
CCDSiCCDS140.1.
PIRiA36736. AWHUB.
RefSeqiNP_002512.1. NM_002521.2.
UniGeneiHs.219140.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YK1X-ray2.90E111-131[»]
3N56X-ray3.10C/D103-134[»]
DisProtiDP00551.
ProteinModelPortaliP16860.
SMRiP16860. Positions 103-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110939. 11 interactions.
IntActiP16860. 7 interactions.
MINTiMINT-1434895.
STRINGi9606.ENSP00000365651.

Chemistry

DrugBankiDB01136. Carvedilol.

PTM databases

PhosphoSiteiP16860.

Polymorphism and mutation databases

BioMutaiNPPB.
DMDMi113836.

Proteomic databases

PaxDbiP16860.
PRIDEiP16860.

Protocols and materials databases

DNASUi4879.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376468; ENSP00000365651; ENSG00000120937.
GeneIDi4879.
KEGGihsa:4879.
UCSCiuc001atj.3. human.

Organism-specific databases

CTDi4879.
GeneCardsiGC01M011918.
HGNCiHGNC:7940. NPPB.
MIMi600295. gene.
neXtProtiNX_P16860.
PharmGKBiPA31734.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG67899.
GeneTreeiENSGT00510000049822.
HOGENOMiHOG000033937.
HOVERGENiHBG004227.
InParanoidiP16860.
KOiK12335.
OMAiSGCFGRK.
OrthoDBiEOG7P2XV4.
PhylomeDBiP16860.
TreeFamiTF106304.

Miscellaneous databases

EvolutionaryTraceiP16860.
GeneWikiiBrain_natriuretic_peptide.
GenomeRNAii4879.
NextBioi18780.
PMAP-CutDBP16860.
PROiP16860.
SOURCEiSearch...

Gene expression databases

BgeeiP16860.
CleanExiHS_NPPB.
GenevestigatoriP16860.

Family and domain databases

InterProiIPR000663. Natr_peptide.
IPR030480. Natr_peptide_CS.
IPR002408. Natriuretic_peptide_brain.
[Graphical view]
PfamiPF00212. ANP. 1 hit.
[Graphical view]
PRINTSiPR00712. BNATPEPTIDE.
SMARTiSM00183. NAT_PEP. 1 hit.
[Graphical view]
PROSITEiPS00263. NATRIURETIC_PEPTIDE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning and sequence analysis of cDNA encoding a precursor for human brain natriuretic peptide."
    Sudoh T., Maekawa K., Kojima M., Minamino N., Kangawa K., Matsuo H.
    Biochem. Biophys. Res. Commun. 159:1427-1434(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Silver Project."
    Kitano T., Kobayakawa H., Saitou N.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Pancreas and Spleen.
  9. "Isolation and identification of human brain natriuretic peptides in cardiac atrium."
    Hino J., Tateyaa H., Minamino N., Kangawa K., Matsuo H.
    Biochem. Biophys. Res. Commun. 167:693-700(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-58 AND 103-134.
  10. "Isolation and sequence determination of human brain natriuretic peptide in human atrium."
    Kambayashi Y., Nakao K., Mukoyama M., Saito Y., Ogawa Y., Shiono S., Inouye K., Yoshida N., Imura H.
    FEBS Lett. 259:341-345(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 103-134.
  11. "Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP)."
    Koller K.J., Lowe D.G., Bennett G.L., Minamino N., Kangawa K., Matsuo H., Goeddel D.V.
    Science 252:120-123(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The precursor to B-type natriuretic peptide is an O-linked glycoprotein."
    Schellenberger U., O'Rear J., Guzzetta A., Jue R.A., Protter A.A., Pollitt N.S.
    Arch. Biochem. Biophys. 451:160-166(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-62; SER-63; SER-70; THR-74; SER-79; THR-84 AND THR-97.
  13. "Detection of endogenous B-type natriuretic peptide at very low concentrations in patients with heart failure."
    Niederkofler E.E., Kiernan U.A., O'Rear J., Menon S., Saghir S., Protter A.A., Nelson R.W., Schellenberger U.
    Circ. Heart Fail. 1:258-264(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are novel substrates of fibroblast activation protein-alpha."
    Keane F.M., Nadvi N.A., Yao T.W., Gorrell M.D.
    FEBS J. 278:1316-1332(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY FAP, CLEAVAGE SITE.
  15. "Structural determinants of natriuretic peptide receptor specificity and degeneracy."
    He X.-L., Dukkipati A., Garcia K.C.
    J. Mol. Biol. 361:698-714(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 111-131 IN COMPLEX WITH NPR3, DISULFIDE BOND.

Entry informationi

Entry nameiANFB_HUMAN
AccessioniPrimary (citable) accession number: P16860
Secondary accession number(s): B0ZBE9, Q6FGY0, Q9P2Q7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 29, 2015
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.