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Protein

Pro-neuropeptide Y

Gene

NPY

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

Functioni

NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone.

GO - Molecular functioni

  • calcium channel regulator activity Source: ProtInc
  • G-protein coupled receptor activity Source: ProtInc
  • G-protein coupled receptor binding Source: GO_Central
  • neuropeptide hormone activity Source: ProtInc
  • receptor binding Source: ProtInc

GO - Biological processi

  • adult feeding behavior Source: HGNC
  • antibacterial humoral response Source: UniProtKB
  • antifungal humoral response Source: UniProtKB
  • behavior Source: ProtInc
  • blood circulation Source: ProtInc
  • calcium ion transport Source: ProtInc
  • cell proliferation Source: ProtInc
  • central nervous system neuron development Source: DFLAT
  • cerebral cortex development Source: DFLAT
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • digestion Source: GO_Central
  • feeding behavior Source: ProtInc
  • G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc
  • innate immune response Source: UniProtKB
  • movement of cell or subcellular component Source: ProtInc
  • neuron projection development Source: DFLAT
  • neuropeptide signaling pathway Source: GO_Central
  • positive regulation of appetite Source: HGNC
  • regulation of appetite Source: GO_Central
  • regulation of blood pressure Source: Ensembl
  • response to yeast Source: UniProtKB
  • synaptic transmission Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Neuropeptide

Enzyme and pathway databases

ReactomeiR-HSA-375276. Peptide ligand-binding receptors.
R-HSA-418594. G alpha (i) signalling events.
SIGNORiP01303.

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-neuropeptide Y
Cleaved into the following 2 chains:
Alternative name(s):
Neuropeptide tyrosine
Short name:
NPY
Gene namesi
Name:NPY
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:7955. NPY.

Subcellular locationi

GO - Cellular componenti

  • cell Source: ProtInc
  • extracellular region Source: Reactome
  • extracellular space Source: HGNC
  • Golgi apparatus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA255.

Polymorphism and mutation databases

BioMutaiNPY.
DMDMi128117.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Peptidei29 – 6436Neuropeptide YPRO_0000025321Add
BLAST
Peptidei68 – 9730C-flanking peptide of NPYPRO_0000025322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Tyrosine amide1 Publication
Modified residuei83 – 831PhosphothreonineCombined sources

Post-translational modificationi

The neuropeptide Y form is cleaved at Pro-30 by the prolyl endopeptidase FAP (seprase) activity (in vitro).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei30 – 312Cleavage; by FAP1 Publication

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Phosphoprotein

Proteomic databases

PaxDbiP01303.
PeptideAtlasiP01303.
PRIDEiP01303.

PTM databases

iPTMnetiP01303.
PhosphoSiteiP01303.

Miscellaneous databases

PMAP-CutDBP01303.

Expressioni

Tissue specificityi

One of the most abundant peptides in the nervous system. Also found in some chromaffin cells of the adrenal medulla.

Gene expression databases

BgeeiP01303.
CleanExiHS_NPY.
ExpressionAtlasiP01303. baseline and differential.
GenevisibleiP01303. HS.

Organism-specific databases

HPAiCAB016733.
CAB034368.
HPA044572.
HPA056798.

Interactioni

GO - Molecular functioni

  • G-protein coupled receptor binding Source: GO_Central
  • neuropeptide hormone activity Source: ProtInc
  • receptor binding Source: ProtInc

Protein-protein interaction databases

BioGridi110914. 7 interactions.
IntActiP01303. 10 interactions.
MINTiMINT-7900013.
STRINGi9606.ENSP00000242152.

Chemistry

BindingDBiP01303.

Structurei

Secondary structure

1
97
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 333Combined sources
Helixi41 – 444Combined sources
Helixi53 – 6311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QFANMR-A52-64[»]
1RONNMR-A29-64[»]
ProteinModelPortaliP01303.
SMRiP01303. Positions 29-64.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01303.

Family & Domainsi

Sequence similaritiesi

Belongs to the NPY family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J0KC. Eukaryota.
ENOG41128I2. LUCA.
GeneTreeiENSGT00390000010775.
HOGENOMiHOG000252942.
HOVERGENiHBG006485.
InParanoidiP01303.
KOiK05232.
OMAiFEDPSMW.
OrthoDBiEOG7WDN4S.
PhylomeDBiP01303.
TreeFamiTF332778.

Family and domain databases

InterProiIPR001955. Pancreatic_hormone-like.
IPR020392. Pancreatic_hormone-like_CS.
[Graphical view]
PANTHERiPTHR10533. PTHR10533. 1 hit.
PfamiPF00159. Hormone_3. 1 hit.
[Graphical view]
PRINTSiPR00278. PANCHORMONE.
ProDomiPD001267. Pancreatic_hormone-like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00309. PAH. 1 hit.
[Graphical view]
PROSITEiPS00265. PANCREATIC_HORMONE_1. 1 hit.
PS50276. PANCREATIC_HORMONE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01303-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGNKRLGLS GLTLALSLLV CLGALAEAYP SKPDNPGEDA PAEDMARYYS
60 70 80 90
ALRHYINLIT RQRYGKRSSP ETLISDLLMR ESTENVPRTR LEDPAMW
Length:97
Mass (Da):10,851
Last modified:July 21, 1986 - v1
Checksum:i832CF124321718F2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531R → G in AAA59945 (PubMed:2427515).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71L → P.
Corresponds to variant rs16139 [ dbSNP | Ensembl ].
VAR_014598
Natural varianti22 – 221L → M.
Corresponds to variant rs5571 [ dbSNP | Ensembl ].
VAR_014599

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01911 mRNA. Translation: AAA59944.1.
M14298, M14296, M14297 Genomic DNA. Translation: AAA59945.1.
M15789 mRNA. Translation: AAA59946.1.
AC004485 Genomic DNA. Translation: AAQ96843.1.
BC029497 mRNA. Translation: AAH29497.1.
CCDSiCCDS5387.1.
PIRiA25198. NYHUY.
RefSeqiNP_000896.1. NM_000905.3.
UniGeneiHs.1832.

Genome annotation databases

EnsembliENST00000242152; ENSP00000242152; ENSG00000122585.
ENST00000405982; ENSP00000385282; ENSG00000122585.
ENST00000407573; ENSP00000384364; ENSG00000122585.
GeneIDi4852.
KEGGihsa:4852.
UCSCiuc003sww.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Neuropeptide Y entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01911 mRNA. Translation: AAA59944.1.
M14298, M14296, M14297 Genomic DNA. Translation: AAA59945.1.
M15789 mRNA. Translation: AAA59946.1.
AC004485 Genomic DNA. Translation: AAQ96843.1.
BC029497 mRNA. Translation: AAH29497.1.
CCDSiCCDS5387.1.
PIRiA25198. NYHUY.
RefSeqiNP_000896.1. NM_000905.3.
UniGeneiHs.1832.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QFANMR-A52-64[»]
1RONNMR-A29-64[»]
ProteinModelPortaliP01303.
SMRiP01303. Positions 29-64.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110914. 7 interactions.
IntActiP01303. 10 interactions.
MINTiMINT-7900013.
STRINGi9606.ENSP00000242152.

Chemistry

BindingDBiP01303.

PTM databases

iPTMnetiP01303.
PhosphoSiteiP01303.

Polymorphism and mutation databases

BioMutaiNPY.
DMDMi128117.

Proteomic databases

PaxDbiP01303.
PeptideAtlasiP01303.
PRIDEiP01303.

Protocols and materials databases

DNASUi4852.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242152; ENSP00000242152; ENSG00000122585.
ENST00000405982; ENSP00000385282; ENSG00000122585.
ENST00000407573; ENSP00000384364; ENSG00000122585.
GeneIDi4852.
KEGGihsa:4852.
UCSCiuc003sww.3. human.

Organism-specific databases

CTDi4852.
GeneCardsiNPY.
HGNCiHGNC:7955. NPY.
HPAiCAB016733.
CAB034368.
HPA044572.
HPA056798.
MIMi162640. gene.
neXtProtiNX_P01303.
PharmGKBiPA255.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J0KC. Eukaryota.
ENOG41128I2. LUCA.
GeneTreeiENSGT00390000010775.
HOGENOMiHOG000252942.
HOVERGENiHBG006485.
InParanoidiP01303.
KOiK05232.
OMAiFEDPSMW.
OrthoDBiEOG7WDN4S.
PhylomeDBiP01303.
TreeFamiTF332778.

Enzyme and pathway databases

ReactomeiR-HSA-375276. Peptide ligand-binding receptors.
R-HSA-418594. G alpha (i) signalling events.
SIGNORiP01303.

Miscellaneous databases

ChiTaRSiNPY. human.
EvolutionaryTraceiP01303.
GeneWikiiNeuropeptide_Y.
GenomeRNAii4852.
PMAP-CutDBP01303.
PROiP01303.
SOURCEiSearch...

Gene expression databases

BgeeiP01303.
CleanExiHS_NPY.
ExpressionAtlasiP01303. baseline and differential.
GenevisibleiP01303. HS.

Family and domain databases

InterProiIPR001955. Pancreatic_hormone-like.
IPR020392. Pancreatic_hormone-like_CS.
[Graphical view]
PANTHERiPTHR10533. PTHR10533. 1 hit.
PfamiPF00159. Hormone_3. 1 hit.
[Graphical view]
PRINTSiPR00278. PANCHORMONE.
ProDomiPD001267. Pancreatic_hormone-like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00309. PAH. 1 hit.
[Graphical view]
PROSITEiPS00265. PANCREATIC_HORMONE_1. 1 hit.
PS50276. PANCREATIC_HORMONE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, characterization, and DNA sequence of a human cDNA encoding neuropeptide tyrosine."
    Minth C.D., Bloom S.R., Polak J.M., Dixon J.E.
    Proc. Natl. Acad. Sci. U.S.A. 81:4577-4581(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT TYR-64.
  2. "Characterization, sequence, and expression of the cloned human neuropeptide Y gene."
    Minth C.D., Andrews P.C., Dixon J.E.
    J. Biol. Chem. 261:11974-11979(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Genes encoding pancreatic polypeptide and neuropeptide Y are on human chromosomes 17 and 7."
    Takeuchi T., Gumucio D.L., Yamada T., Meisler M.H., Minth C.D., Dixon J.E., Eddy R.E., Shows T.B.
    J. Clin. Invest. 77:1038-1041(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "Presence of the predicted C-flanking peptide of neuropeptide Y (CPON) in tissue extracts."
    Allen J.M., Polak J.M., Bloom S.R.
    Neuropeptides 6:95-100(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF CPON.
  7. "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.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Solution conformation of human neuropeptide Y by 1H nuclear magnetic resonance and restrained molecular dynamics."
    Darbon H., Bernassau J.-M., Deleuze C., Chenu J., Roussel A., Cambillau C.
    Eur. J. Biochem. 209:765-771(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 29-64.
  10. Cited for: STRUCTURE BY NMR OF 29-64.
  11. "Helical structure and self-association in a 13 residue neuropeptide Y Y2 receptor agonist: relationship to biological activity."
    Barnham K.J., Catalfamo F., Pallaghy P.K., Howlett G.J., Norton R.S.
    Biochim. Biophys. Acta 1435:127-137(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 52-64.

Entry informationi

Entry nameiNPY_HUMAN
AccessioniPrimary (citable) accession number: P01303
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 169 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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

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 one 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.