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Protein

Pro-opiomelanocortin

Gene

POMC

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

Functioni

ACTH stimulates the adrenal glands to release cortisol.
MSH (melanocyte-stimulating hormone) increases the pigmentation of skin by increasing melanin production in melanocytes.
Beta-endorphin and Met-enkephalin are endogenous opiates.

GO - Molecular functioni

  1. G-protein coupled receptor binding Source: BHF-UCL
  2. hormone activity Source: UniProtKB
  3. receptor binding Source: UniProtKB
  4. type 1 melanocortin receptor binding Source: BHF-UCL
  5. type 3 melanocortin receptor binding Source: BHF-UCL
  6. type 4 melanocortin receptor binding Source: BHF-UCL

GO - Biological processi

  1. cell-cell signaling Source: UniProtKB
  2. cellular pigmentation Source: UniProtKB
  3. cellular protein metabolic process Source: Reactome
  4. generation of precursor metabolites and energy Source: UniProtKB
  5. glucose homeostasis Source: Ensembl
  6. negative regulation of tumor necrosis factor production Source: BHF-UCL
  7. neuropeptide signaling pathway Source: UniProtKB-KW
  8. peptide hormone processing Source: Reactome
  9. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  10. regulation of appetite Source: UniProtKB
  11. regulation of blood pressure Source: UniProtKB
  12. regulation of corticosterone secretion Source: Ensembl
  13. regulation of glycogen metabolic process Source: Ensembl
  14. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Endorphin, Hormone

Enzyme and pathway databases

ReactomeiREACT_11036. Glucocorticoid biosynthesis.
REACT_11059. Androgen biosynthesis.
REACT_13812. Endogenous sterols.
REACT_14819. Peptide ligand-binding receptors.
REACT_15295. Opioid Signalling.
REACT_15452. Peptide hormone biosynthesis.
REACT_15457. G-protein activation.
REACT_19231. G alpha (i) signalling events.
REACT_19327. G alpha (s) signalling events.
REACT_267874. Defective ACTH causes Obesity and Pro-opiomelanocortinin deficiency (POMCD).

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-opiomelanocortin
Short name:
POMC
Alternative name(s):
Corticotropin-lipotropin
Cleaved into the following 11 chains:
Alternative name(s):
Gamma-MSH
Alternative name(s):
Adrenocorticotropic hormone
Short name:
ACTH
Alternative name(s):
Alpha-MSH
Alternative name(s):
Beta-LPH
Alternative name(s):
Gamma-LPH
Alternative name(s):
Beta-MSH
Gene namesi
Name:POMC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9201. POMC.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProtKB
  4. peroxisomal matrix Source: UniProtKB
  5. secretory granule Source: UniProtKB
  6. secretory granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Obesity (OBESITY)1 Publication

Disease susceptibility may be associated with variations affecting the gene represented in this entry.

Disease descriptionA condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat.

See also OMIM:601665
Pro-opiomelanocortinin deficiency (POMCD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAffected individuals present early-onset obesity, adrenal insufficiency and red hair.

See also OMIM:609734

Keywords - Diseasei

Obesity

Organism-specific databases

MIMi601665. phenotype.
609734. phenotype.
Orphaneti71526. Obesity due to pro-opiomelanocortin deficiency.
PharmGKBiPA33526.

Chemistry

DrugBankiDB00836. Loperamide.

Polymorphism and mutation databases

BioMutaiPOMC.
DMDMi116880.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26263 PublicationsAdd
BLAST
Peptidei27 – 10276NPPPRO_0000024966Add
BLAST
Peptidei77 – 8711Melanotropin gamma1 PublicationPRO_0000024967Add
BLAST
Peptidei105 – 13430Potential peptidePRO_0000024968Add
BLAST
Peptidei138 – 17639CorticotropinPRO_0000024969Add
BLAST
Peptidei138 – 15013Melanotropin alphaPRO_0000024970Add
BLAST
Peptidei156 – 17621Corticotropin-like intermediary peptidePRO_0000024971Add
BLAST
Peptidei179 – 26789Lipotropin betaPRO_0000024972Add
BLAST
Peptidei179 – 23456Lipotropin gammaPRO_0000024973Add
BLAST
Peptidei217 – 23418Melanotropin betaPRO_0000024974Add
BLAST
Peptidei237 – 26731Beta-endorphinPRO_0000024975Add
BLAST
Peptidei237 – 2415Met-enkephalinPRO_0000024976

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 50By similarity
Glycosylationi71 – 711O-linked (HexNAc...)1 Publication
Modified residuei87 – 871Phenylalanine amideBy similarity
Glycosylationi91 – 911N-linked (GlcNAc...)
Modified residuei134 – 1341Glutamic acid 1-amide1 Publication
Modified residuei138 – 1381N-acetylserineBy similarity
Modified residuei150 – 1501Valine amideBy similarity
Modified residuei168 – 1681Phosphoserine1 Publication

Post-translational modificationi

Specific enzymatic cleavages at paired basic residues yield the different active peptides.1 Publication
O-glycosylated; reducing sugar is probably N-acetylgalactosamine.

Keywords - PTMi

Acetylation, Amidation, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP01189.
PRIDEiP01189.

PTM databases

PhosphoSiteiP01189.

Miscellaneous databases

PMAP-CutDBP01189.

Expressioni

Tissue specificityi

ACTH and MSH are produced by the pituitary gland.

Gene expression databases

BgeeiP01189.
CleanExiHS_POMC.
ExpressionAtlasiP01189. baseline.
GenevestigatoriP01189.

Interactioni

Protein-protein interaction databases

BioGridi111439. 14 interactions.
STRINGi9606.ENSP00000264708.

Structurei

3D structure databases

ProteinModelPortaliP01189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the POMC family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG45039.
GeneTreeiENSGT00390000016811.
HOVERGENiHBG004341.
InParanoidiP01189.
KOiK05228.
OMAiRACKPDL.
OrthoDBiEOG74TX0W.
PhylomeDBiP01189.
TreeFamiTF333215.

Family and domain databases

InterProiIPR001941. Mcortin_ACTH.
IPR013531. Mcrtin_ACTH_cent.
IPR013593. Melanocortin_N.
IPR013532. Opioid_neuropept.
[Graphical view]
PfamiPF00976. ACTH_domain. 1 hit.
PF08384. NPP. 1 hit.
PF08035. Op_neuropeptide. 1 hit.
[Graphical view]
PRINTSiPR00383. MELANOCORTIN.

Sequencei

Sequence statusi: Complete.

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

P01189-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRSCCSRSG ALLLALLLQA SMEVRGWCLE SSQCQDLTTE SNLLECIRAC
60 70 80 90 100
KPDLSAETPM FPGNGDEQPL TENPRKYVMG HFRWDRFGRR NSSSSGSSGA
110 120 130 140 150
GQKREDVSAG EDCGPLPEGG PEPRSDGAKP GPREGKRSYS MEHFRWGKPV
160 170 180 190 200
GKKRRPVKVY PNGAEDESAE AFPLEFKREL TGQRLREGDG PDGPADDGAG
210 220 230 240 250
AQADLEHSLL VAAEKKDEGP YRMEHFRWGS PPKDKRYGGF MTSEKSQTPL
260
VTLFKNAIIK NAYKKGE
Length:267
Mass (Da):29,424
Last modified:February 1, 1991 - v2
Checksum:iB927323474A67536
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481R → G (PubMed:6254047).Curated
Sequence conflicti115 – 1151P → T (PubMed:6299668).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71S → T.1 Publication
VAR_010699
Natural varianti9 – 91S → L.1 Publication
Corresponds to variant rs139750421 [ dbSNP | Ensembl ].
VAR_010700
Natural varianti62 – 621P → L.
Corresponds to variant rs28932471 [ dbSNP | Ensembl ].
VAR_029762
Natural varianti97 – 993Missing .3 Publications
VAR_010714
Natural varianti106 – 1061D → N.1 Publication
VAR_010715
Natural varianti132 – 1321P → A.
Corresponds to variant rs8192606 [ dbSNP | Ensembl ].
VAR_029314
Natural varianti214 – 2141E → G.1 Publication
Corresponds to variant rs80326661 [ dbSNP | Ensembl ].
VAR_010716
Natural varianti236 – 2361R → G May confer susceptibility to obesity; reduces the ability to activate melanocortin receptor 4. 2 Publications
Corresponds to variant rs28932472 [ dbSNP | Ensembl ].
VAR_010701
Natural varianti236 – 2361R → Q.1 Publication
VAR_012201

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38297 mRNA. Translation: AAA60140.1.
J00292, J00291 Genomic DNA. Translation: AAB59621.1.
V01510 Genomic DNA. Translation: CAA24754.1.
AC012457 Genomic DNA. Translation: AAY24354.1.
CH471053 Genomic DNA. Translation: EAX00729.1.
CH471053 Genomic DNA. Translation: EAX00730.1.
BC065832 mRNA. Translation: AAH65832.1.
M25896 mRNA. Translation: AAA35799.1.
CCDSiCCDS1717.1.
PIRiA17229. CTHUP.
RefSeqiNP_000930.1. NM_000939.2.
NP_001030333.1. NM_001035256.1.
UniGeneiHs.1897.

Genome annotation databases

EnsembliENST00000264708; ENSP00000264708; ENSG00000115138.
ENST00000380794; ENSP00000370171; ENSG00000115138.
ENST00000395826; ENSP00000379170; ENSG00000115138.
ENST00000405623; ENSP00000384092; ENSG00000115138.
GeneIDi5443.
KEGGihsa:5443.
UCSCiuc002rfy.1. human.

Polymorphism and mutation databases

BioMutaiPOMC.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Melanocyte-stimulating hormone entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38297 mRNA. Translation: AAA60140.1.
J00292, J00291 Genomic DNA. Translation: AAB59621.1.
V01510 Genomic DNA. Translation: CAA24754.1.
AC012457 Genomic DNA. Translation: AAY24354.1.
CH471053 Genomic DNA. Translation: EAX00729.1.
CH471053 Genomic DNA. Translation: EAX00730.1.
BC065832 mRNA. Translation: AAH65832.1.
M25896 mRNA. Translation: AAA35799.1.
CCDSiCCDS1717.1.
PIRiA17229. CTHUP.
RefSeqiNP_000930.1. NM_000939.2.
NP_001030333.1. NM_001035256.1.
UniGeneiHs.1897.

3D structure databases

ProteinModelPortaliP01189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111439. 14 interactions.
STRINGi9606.ENSP00000264708.

Chemistry

DrugBankiDB00836. Loperamide.

PTM databases

PhosphoSiteiP01189.

Polymorphism and mutation databases

BioMutaiPOMC.
DMDMi116880.

Proteomic databases

PaxDbiP01189.
PRIDEiP01189.

Protocols and materials databases

DNASUi5443.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264708; ENSP00000264708; ENSG00000115138.
ENST00000380794; ENSP00000370171; ENSG00000115138.
ENST00000395826; ENSP00000379170; ENSG00000115138.
ENST00000405623; ENSP00000384092; ENSG00000115138.
GeneIDi5443.
KEGGihsa:5443.
UCSCiuc002rfy.1. human.

Organism-specific databases

CTDi5443.
GeneCardsiGC02M025383.
GeneReviewsiPOMC.
HGNCiHGNC:9201. POMC.
MIMi176830. gene.
601665. phenotype.
609734. phenotype.
neXtProtiNX_P01189.
Orphaneti71526. Obesity due to pro-opiomelanocortin deficiency.
PharmGKBiPA33526.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG45039.
GeneTreeiENSGT00390000016811.
HOVERGENiHBG004341.
InParanoidiP01189.
KOiK05228.
OMAiRACKPDL.
OrthoDBiEOG74TX0W.
PhylomeDBiP01189.
TreeFamiTF333215.

Enzyme and pathway databases

ReactomeiREACT_11036. Glucocorticoid biosynthesis.
REACT_11059. Androgen biosynthesis.
REACT_13812. Endogenous sterols.
REACT_14819. Peptide ligand-binding receptors.
REACT_15295. Opioid Signalling.
REACT_15452. Peptide hormone biosynthesis.
REACT_15457. G-protein activation.
REACT_19231. G alpha (i) signalling events.
REACT_19327. G alpha (s) signalling events.
REACT_267874. Defective ACTH causes Obesity and Pro-opiomelanocortinin deficiency (POMCD).

Miscellaneous databases

ChiTaRSiPOMC. human.
GeneWikiiProopiomelanocortin.
GenomeRNAii5443.
NextBioi21063.
PMAP-CutDBP01189.
PROiP01189.
SOURCEiSearch...

Gene expression databases

BgeeiP01189.
CleanExiHS_POMC.
ExpressionAtlasiP01189. baseline.
GenevestigatoriP01189.

Family and domain databases

InterProiIPR001941. Mcortin_ACTH.
IPR013531. Mcrtin_ACTH_cent.
IPR013593. Melanocortin_N.
IPR013532. Opioid_neuropept.
[Graphical view]
PfamiPF00976. ACTH_domain. 1 hit.
PF08384. NPP. 1 hit.
PF08035. Op_neuropeptide. 1 hit.
[Graphical view]
PRINTSiPR00383. MELANOCORTIN.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and structural organization of the human corticotropin-beta-lipotropin precursor gene."
    Takahashi H., Teranishi Y., Nakanishi S., Numa S.
    FEBS Lett. 135:97-102(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The human pro-opiomelanocortin gene: organization, sequence, and interspersion with repetitive DNA."
    Whitfeld P.L., Seeburg P.H., Shine J.
    DNA 1:133-143(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete nucleotide sequence of the human corticotropin-beta-lipotropin precursor gene."
    Takahashi H., Hakamata Y., Watanabe Y., Kikuno R., Miyata T., Numa S.
    Nucleic Acids Res. 11:6847-6858(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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: Pituitary.
  7. "Synthesis, cloning and primary structure of DNA complementary to mRNA for human pituitary pro-opiomelanocortin."
    Golovin S.Y., Karginov V.A., Bondar A.A., Beklemishev A.B., Chekhranova M.K., Mertvetsov N.P., Pankov Y.A.
    Bioorg. Khim. 13:562-564(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-267.
  8. "Structural organization of human genomic DNA encoding the pro-opiomelanocortin peptide."
    Chang A.C.Y., Cochet M., Cohen S.N.
    Proc. Natl. Acad. Sci. U.S.A. 77:4890-4894(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-267.
  9. "Complete amino acid sequence of a human pituitary glycopeptide: an important maturation product of pro-opiomelanocortin."
    Seidah N.G., Chretien M.
    Proc. Natl. Acad. Sci. U.S.A. 78:4236-4240(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-102.
  10. "Primary structure of the major human pituitary pro-opiomelanocortin NH2-terminal glycopeptide. Evidence for an aldosterone-stimulating activity."
    Seidah N.G., Rochemont J., Hamelin J., Lis M., Chretien M.
    J. Biol. Chem. 256:7977-7984(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-102.
  11. "The missing fragment of the pro-sequence of human pro-opiomelanocortin: sequence and evidence for C-terminal amidation."
    Seidah N.G., Rochemont J., Hamelin J., Benjannet S., Chretien M.
    Biochem. Biophys. Res. Commun. 102:710-716(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 105-134, AMIDATION AT GLU-134.
  12. "Confirmation of the 1-20 amino acid sequence of human adrenocorticotrophin."
    Bennett H.P.J., Lowry P.J., McMartin C.
    Biochem. J. 133:11-13(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 138-176.
  13. "On the structure of human corticotropin (adrenocorticotropic hormone)."
    Lee T.H., Lerner A.B., Buettner-Janusch V.
    J. Biol. Chem. 236:2970-2974(1961) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 138-176.
  14. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-41.
  15. "Revised amino-acid sequences for porcine and human adrenocorticotrophic hormone."
    Riniker B., Sieber P., Rittel W., Zuber H.
    Nature New Biol. 235:114-115(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION (CORTICOTROPIN).
  16. "Synthesis of the human adrenal cortex hormone (alpha-h-ACTH) with a revised amino-acid sequence."
    Sieber P., Rittel W., Riniker B.
    Helv. Chim. Acta 55:1243-1266(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF CORTICOTROPIN.
  17. "Adrenocorticotropins. 44. Total synthesis of the human hormone by the solid-phase method."
    Yamashiro D., Li C.H.
    J. Am. Chem. Soc. 95:1310-1315(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF CORTICOTROPIN.
  18. "Primary structure of human beta-lipotropin."
    Li C.H., Chung D.
    Nature 260:622-624(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 179-267.
  19. "Structure of a melanocyte-stimulating hormone from the human pituitary gland."
    Harris J.I.
    Nature 184:167-169(1959)
    Cited for: PROTEIN SEQUENCE OF 217-234.
  20. "Primary structure and morphine-like activity of human beta-endorphin."
    Dragon N., Seidah N.G., Lis M., Routhier R., Chretien M.
    Can. J. Biochem. 55:666-670(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 237-267.
  21. "Gamma-endorphin and schizophrenia: amino acid composition of gamma-endorphin and nucleotide sequence of gamma-endorphin cDNA from pituitary glands of schizophrenic patients."
    Bovenberg R.A.L., Burbach J.P.H., Wiegant V.M., Veeneman G.H., van Boom J.H., Baas P.D., Jansz H.S., de Wied D.
    Brain Res. 376:29-37(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 235-256.
  22. "Alpha-amidated peptides derived from pro-opiomelanocortin in normal human pituitary."
    Fenger M., Johnsen A.H.
    Biochem. J. 250:781-788(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  23. "Reduced expression of a naturally deleted form of human proopiomelanocortin complementary deoxyribonucleic acid after transfection into Chinese hamster ovary cells."
    Morris J.C., Savva D., Lowry P.J.
    Endocrinology 136:195-201(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 75-104, VARIANT 97-SER--GLY-99 DEL.
    Tissue: Pituitary.
  24. "Severe early-onset obesity, adrenal insufficiency and red hair pigmentation caused by POMC mutations in humans."
    Krude H., Biebermann H., Luck W., Horn R., Brabant G., Grueters A.
    Nat. Genet. 19:155-157(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN POMCD.
  25. "Association between common polymorphisms of the proopiomelanocortin gene and body fat distribution: a family study."
    Baker M., Gaukrodger N., Mayosi B.M., Imrie H., Farrall M., Watkins H., Connell J.M.C., Avery P.J., Keavney B.
    Diabetes 54:2492-2496(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ABDOMINAL BODY FAT DISTRIBUTION.
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary.
  27. "Systematic mutation screening of the pro-opiomelanocortin gene: identification of several genetic variants including three different insertions, one nonsense and two missense point mutations in probands of different weight extremes."
    Hinney A., Becker I., Heibult O., Nottebom K., Schmidt A., Ziegler A., Mayer H., Siegfried W., Blum W.F., Remschmidt H., Hebebrand J.
    J. Clin. Endocrinol. Metab. 83:3737-3741(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ASN-106; GLY-214 AND 97-SER--GLY-99 DEL.
  28. "Mutational analysis of the proopiomelanocortin gene in Caucasians with early onset obesity."
    Echwald S.M., Sorensen T.I., Andersen T., Tybjaerg-Hansen A., Clausen J.O., Pedersen O.
    Int. J. Obes. Relat. Metab. Disord. 23:293-298(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLN-236.
  29. "Molecular screening of the proopiomelanocortin (POMC) gene in Italian obese children: report of three new mutations."
    del Giudice E.M., Cirillo G., Santoro N., D'Urso L., Carbone M.T., Toro R.D., Perrone L.
    Int. J. Obes. Relat. Metab. Disord. 25:61-67(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-7; LEU-9; GLY-236 AND 97-SER--GLY-99 DEL.
  30. "A missense mutation disrupting a dibasic prohormone processing site in pro-opiomelanocortin (POMC) increases susceptibility to early-onset obesity through a novel molecular mechanism."
    Challis B.G., Pritchard L.E., Creemers J.W.M., Delplanque J., Keogh J.M., Luan J., Wareham N.J., Yeo G.S.H., Bhattacharyya S., Froguel P., White A., Farooqi I.S., O'Rahilly S.
    Hum. Mol. Genet. 11:1997-2004(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLY-236, CHARACTERIZATION OF VARIANT GLY-236, POSSIBLE INVOLVEMENT IN OBESITY.

Entry informationi

Entry nameiCOLI_HUMAN
AccessioniPrimary (citable) accession number: P01189
Secondary accession number(s): P78442
, Q53T23, Q9UD39, Q9UD40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1991
Last modified: April 29, 2015
This is version 165 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. 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.