Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P01189 (COLI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pro-opiomelanocortin

Short name=POMC
Alternative name(s):
Corticotropin-lipotropin

Cleaved into the following 11 chains:

  1. NPP
  2. Melanotropin gamma
    Alternative name(s):
    Gamma-MSH
  3. Potential peptide
  4. Corticotropin
    Alternative name(s):
    Adrenocorticotropic hormone
    Short name=ACTH
  5. Melanotropin alpha
    Alternative name(s):
    Alpha-MSH
  6. Corticotropin-like intermediary peptide
    Short name=CLIP
  7. Lipotropin beta
    Alternative name(s):
    Beta-LPH
  8. Lipotropin gamma
    Alternative name(s):
    Gamma-LPH
  9. Melanotropin beta
    Alternative name(s):
    Beta-MSH
  10. Beta-endorphin
  11. Met-enkephalin
Gene names
Name:POMC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Secreted.

Tissue specificity

ACTH and MSH are produced by the pituitary gland.

Post-translational modification

Specific enzymatic cleavages at paired basic residues yield the different active peptides.

O-glycosylated; reducing sugar is probably N-acetylgalactosamine.

Involvement in disease

Obesity (OBESITY) [MIM:601665]: A 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.
Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry. Ref.30

Pro-opiomelanocortinin deficiency (POMCD) [MIM:609734]: Affected individuals present early-onset obesity, adrenal insufficiency and red hair.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24

Sequence similarities

Belongs to the POMC family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseObesity
   DomainSignal
   Molecular functionEndorphin
Hormone
   PTMAcetylation
Amidation
Cleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell-cell signaling

Inferred from mutant phenotype Ref.24. Source: UniProtKB

cellular pigmentation

Inferred from mutant phenotype Ref.24. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

generation of precursor metabolites and energy

Inferred from mutant phenotype Ref.24. Source: UniProtKB

negative regulation of tumor necrosis factor production

Inferred from direct assay PubMed 10233018. Source: BHF-UCL

neuropeptide signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

peptide hormone processing

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18292087. Source: BHF-UCL

regulation of appetite

Inferred from mutant phenotype Ref.24. Source: UniProtKB

regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from mutant phenotype Ref.24. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay Ref.24. Source: UniProtKB

peroxisomal matrix

Inferred from direct assay PubMed 20810565PubMed 20810565. Source: UniProtKB

secretory granule

Inferred from sequence or structural similarity. Source: UniProtKB

secretory granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionG-protein coupled receptor binding

Inferred from direct assay PubMed 19452503. Source: BHF-UCL

hormone activity

Inferred from mutant phenotype Ref.24. Source: UniProtKB

receptor binding

Inferred from mutant phenotype Ref.24. Source: UniProtKB

type 1 melanocortin receptor binding

Inferred from direct assay PubMed 18292087. Source: BHF-UCL

type 3 melanocortin receptor binding

Inferred from physical interaction PubMed 19743876. Source: BHF-UCL

type 4 melanocortin receptor binding

Inferred from physical interaction PubMed 19743876. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.9 Ref.10 Ref.14
Peptide27 – 10276NPP Ref.9 Ref.10
PRO_0000024966
Peptide77 – 8711Melanotropin gamma Ref.22
PRO_0000024967
Peptide105 – 13430Potential peptide
PRO_0000024968
Peptide138 – 17639Corticotropin Ref.12 Ref.13
PRO_0000024969
Peptide138 – 15013Melanotropin alpha
PRO_0000024970
Peptide156 – 17621Corticotropin-like intermediary peptide
PRO_0000024971
Peptide179 – 26789Lipotropin beta Ref.18
PRO_0000024972
Peptide179 – 23456Lipotropin gamma
PRO_0000024973
Peptide217 – 23418Melanotropin beta Ref.19
PRO_0000024974
Peptide237 – 26731Beta-endorphin Ref.20
PRO_0000024975
Peptide237 – 2415Met-enkephalin
PRO_0000024976

Amino acid modifications

Modified residue871Phenylalanine amide By similarity
Modified residue1341Glutamic acid 1-amide Ref.11
Modified residue1381N-acetylserine By similarity
Modified residue1501Valine amide By similarity
Modified residue1681Phosphoserine Ref.26
Glycosylation711O-linked (HexNAc...) Ref.10
Glycosylation911N-linked (GlcNAc...)
Disulfide bond28 ↔ 50 By similarity

Natural variations

Natural variant71S → T. Ref.29
VAR_010699
Natural variant91S → L. Ref.29
Corresponds to variant rs139750421 [ dbSNP | Ensembl ].
VAR_010700
Natural variant621P → L.
Corresponds to variant rs28932471 [ dbSNP | Ensembl ].
VAR_029762
Natural variant97 – 993Missing.
VAR_010714
Natural variant1061D → N. Ref.27
VAR_010715
Natural variant1321P → A.
Corresponds to variant rs8192606 [ dbSNP | Ensembl ].
VAR_029314
Natural variant2141E → G. Ref.27
Corresponds to variant rs80326661 [ dbSNP | Ensembl ].
VAR_010716
Natural variant2361R → G May confer susceptibility to obesity; reduces the ability to activate melanocortin receptor 4. Ref.29 Ref.30
Corresponds to variant rs28932472 [ dbSNP | Ensembl ].
VAR_010701
Natural variant2361R → Q. Ref.28
VAR_012201

Experimental info

Sequence conflict481R → G Ref.8
Sequence conflict1151P → T Ref.2

Sequences

Sequence LengthMass (Da)Tools
P01189 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: B927323474A67536

FASTA26729,424
        10         20         30         40         50         60 
MPRSCCSRSG ALLLALLLQA SMEVRGWCLE SSQCQDLTTE SNLLECIRAC KPDLSAETPM 

        70         80         90        100        110        120 
FPGNGDEQPL TENPRKYVMG HFRWDRFGRR NSSSSGSSGA GQKREDVSAG EDCGPLPEGG 

       130        140        150        160        170        180 
PEPRSDGAKP GPREGKRSYS MEHFRWGKPV GKKRRPVKVY PNGAEDESAE AFPLEFKREL 

       190        200        210        220        230        240 
TGQRLREGDG PDGPADDGAG AQADLEHSLL VAAEKKDEGP YRMEHFRWGS PPKDKRYGGF 

       250        260 
MTSEKSQTPL VTLFKNAIIK NAYKKGE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , 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 (SEP-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: 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]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Melanocyte-stimulating hormone entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1717.1.
PIRCTHUP. A17229.
RefSeqNP_000930.1. NM_000939.2.
NP_001030333.1. NM_001035256.1.
UniGeneHs.1897.

3D structure databases

ProteinModelPortalP01189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111439. 7 interactions.
STRING9606.ENSP00000264708.

Chemistry

DrugBankDB00741. Hydrocortisone.
DB00836. Loperamide.
DB01108. Trilostane.

PTM databases

PhosphoSiteP01189.

Polymorphism databases

DMDM116880.

Proteomic databases

PaxDbP01189.
PRIDEP01189.

Protocols and materials databases

DNASU5443.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264708; ENSP00000264708; ENSG00000115138.
ENST00000380794; ENSP00000370171; ENSG00000115138.
ENST00000395826; ENSP00000379170; ENSG00000115138.
ENST00000405623; ENSP00000384092; ENSG00000115138.
GeneID5443.
KEGGhsa:5443.
UCSCuc002rfy.1. human.

Organism-specific databases

CTD5443.
GeneCardsGC02M025383.
GeneReviewsPOMC.
HGNCHGNC:9201. POMC.
HPACAB002765.
MIM176830. gene.
601665. phenotype.
609734. phenotype.
neXtProtNX_P01189.
Orphanet71526. Obesity due to pro-opiomelanocortin deficiency.
PharmGKBPA33526.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45039.
HOVERGENHBG004341.
InParanoidP01189.
KOK05228.
OMARACKPDL.
OrthoDBEOG74TX0W.
PhylomeDBP01189.
TreeFamTF333215.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP01189.
BgeeP01189.
CleanExHS_POMC.
GenevestigatorP01189.

Family and domain databases

InterProIPR001941. Mcortin_ACTH.
IPR013531. Mcrtin_ACTH_cent.
IPR013593. Melanocortin_N.
IPR013532. Opioid_neuropept.
[Graphical view]
PfamPF00976. ACTH_domain. 1 hit.
PF08384. NPP. 1 hit.
PF08035. Op_neuropeptide. 1 hit.
[Graphical view]
PRINTSPR00383. MELANOCORTIN.
ProtoNetSearch...

Other

ChiTaRSPOMC. human.
GeneWikiProopiomelanocortin.
GenomeRNAi5443.
NextBio21063.
PMAP-CutDBP01189.
PROP01189.
SOURCESearch...

Entry information

Entry nameCOLI_HUMAN
AccessionPrimary (citable) accession number: P01189
Secondary accession number(s): P78442 expand/collapse secondary AC list , Q53T23, Q9UD39, Q9UD40
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM