A database of hormones and their receptors |
|
|
|
|
|
|
HMRbase accession number | 10024 |
Swiss-prot Accession number | P63296 (Sequence in FASTA format) |
Description | Secretin. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Stimulates formation of NaHCO(3)-rich pancreatic juice and secretion of NaHCO(3)-rich bile and inhibits HCl production by the stomach |
Protein Length | 27 Amino acids |
Molecular weight | 3056 |
References | 1 PubMed abstract 7250377 |
Domain Name | Hormone_2 |
Hormone Name | Secretin |
Mature Hormone Sequence | HSDGTFTSELSRLRDSARLQRLLQGLV |
Position of mature hormone in Pre-Hormone protein | 27 Residues from position (1-27) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10238 |
Swiss-prot Accession number | P62326 (Sequence in FASTA format) |
Description | Thymosin beta-4 (T beta 4) [Contains: Hematopoietic system regulatorypeptide (Seraspenide)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Cytoplasm |
Developmental Stage | N/A |
Similarity | Belongs to the thymosin beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Seraspenide inhibits the entry of hematopoeitic pluripotent stem cells into the S-phase |
Protein Length | 44 Amino acids |
Molecular weight | 5053 |
References | 1 Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.; "Analysis of sequences obtained from constructed full-length bovinecDNA libraries."; Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
2 Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. 3 PubMed abstract 6940133 4 PubMed abstract 2915977 5 PubMed abstract 2253778 6 PubMed abstract 1551869 7 PubMed abstract 2261438 8 PubMed abstract 8269922 |
Domain Name | Thymosin |
Hormone Name | Hematopoietic system regulatory peptide |
Mature Hormone Sequence | SDKP |
Position of mature hormone in Pre-Hormone protein | 4 Residues from position (2-5) |
Receptor | N/A |
Gene ID | 781334 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10276 |
Swiss-prot Accession number | Q863C3 (Sequence in FASTA format) |
Description | Gastrin-releasing peptide precursor (GRP) [Contains: Neuromedin-C(GRP-10) (GRP-(18-27))] (Fragment). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the bombesin/neuromedin-B/ranatensin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | N/A |
Protein Length | 126 Amino acids |
Molecular weight | 13840 |
References | 1 Budipitojo T., Sasaki T., Cruzana M.B.C., Kitamura N., Yamada J.; "Molecular cloning of cDNA encoding an endometrial gastrin-releasingpeptide (GRP) of cow."; Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2755876 |
Domain Name | Bombesin |
Hormone Name | Neuromedin-C |
Mature Hormone Sequence | GNHWAVGHLM |
Position of mature hormone in Pre-Hormone protein | 10 Residues from position (41-50) |
Receptor | N/A |
Gene ID | 615323 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10303 |
Swiss-prot Accession number | P81264 (Sequence in FASTA format) |
Description | Prolactin-releasing peptide precursor (PrRP) (Prolactin-releasinghormone) [Contains: Prolactin-releasing peptide PrRP31; Prolactin-releasing peptide PrRP20]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | N/A |
Tissue Specificity | Medulla oblongata and hypothalamus |
Post translational modification | N/A |
Function | Stimulates prolactin (PRL) release and regulates the expression of prolactin through its receptor GPR10. May stimulate lactotrophs directly to secrete PRL |
Protein Length | 98 Amino acids |
Molecular weight | 10544 |
References | 1 PubMed abstract 9607765 |
Domain Name | N/A |
Hormone Name | Prolactin-releasing peptide PrRP31 |
Mature Hormone Sequence | SRAHQHSMEIRTPDINPAWYAGRGIRPVGRF |
Position of mature hormone in Pre-Hormone protein | 31 Residues from position (23-53) |
Receptor | Q4EW11
Detail in HMRbase |
Gene ID | 286856 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 10304 |
Swiss-prot Accession number | P81264 (Sequence in FASTA format) |
Description | Prolactin-releasing peptide precursor (PrRP) (Prolactin-releasinghormone) [Contains: Prolactin-releasing peptide PrRP31; Prolactin-releasing peptide PrRP20]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | N/A |
Tissue Specificity | Medulla oblongata and hypothalamus |
Post translational modification | N/A |
Function | Stimulates prolactin (PRL) release and regulates the expression of prolactin through its receptor GPR10. May stimulate lactotrophs directly to secrete PRL |
Protein Length | 98 Amino acids |
Molecular weight | 10544 |
References | 1 PubMed abstract 9607765 |
Domain Name | N/A |
Hormone Name | Prolactin-releasing peptide PrRP20 |
Mature Hormone Sequence | RTPDINPAWYAGRGIRPVGRF |
Position of mature hormone in Pre-Hormone protein | 21 Residues from position (33-53) |
Receptor | Q4EW11
Detail in HMRbase |
Gene ID | 286856 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 10344 |
Swiss-prot Accession number | Q95MI6 (Sequence in FASTA format) |
Description | Corticoliberin precursor (Corticotropin-releasing factor) (CRF)(Corticotropin-releasing hormone). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the sauvagine/corticotropin-releasing factor/urotensin I family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | This hormone from hypothalamus regulates the release of corticotropin from pituitary gland |
Protein Length | 190 Amino acids |
Molecular weight | 20739 |
References | 1 Buchanan F.C., Thue T.D., Schmutz S.M.; "Sequence analysis of bovine corticotrophin-releasing hormone - acandidate gene for post-natal growth."; Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
|
Domain Name | CRF |
Hormone Name | Corticoliberin |
Mature Hormone Sequence | SQEPPISLDLTFHLLREVLEMTKADQLAQQAHXNRKLLDIA |
Position of mature hormone in Pre-Hormone protein | 41 Residues from position (148-188) |
Receptor | Q9BGU4
Detail in HMRbase |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 10347 |
Swiss-prot Accession number | Q9BDJ6 (Sequence in FASTA format) |
Description | Appetite-regulating hormone precursor (Growth hormone secretagogue)(Growth hormone-releasing peptide) (Motilin-related peptide)[Contains: Ghrelin; Obestatin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein (By similarity) |
Developmental Stage | N/A |
Similarity | Belongs to the motilin family. |
Tissue Specificity | N/A |
Post translational modification | O-n-octanoylation is essential for ghrelin activity (By similarity). Amidation of Leu-97 is essential for obestatin activity (By similarity). |
Function | Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation |
Protein Length | 116 Amino acids |
Molecular weight | 12793 |
References | 1 Kita K., Harada K., Yokota H.; Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
2 Li C., Lobo S., Wang Z., Fu A., Meng Y., Murdoch B., Hansen C.,Moore S.; "A full length genomic sequence of the bovine ghrelin gene."; Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. 3 Kojima M.; Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. |
Domain Name | Motilin_assoc Motilin_ghrelin |
Hormone Name | Ghrelin |
Mature Hormone Sequence | GSSFLSPEHQKLQRKEAKKPSGRLKPR |
Position of mature hormone in Pre-Hormone protein | 27 Residues from position (24-50) |
Receptor | Q9BDH9 Detail in HMRbase Q9N1F8 Detail in HMRbase Q9TUJ0 Detail in HMRbase Q9TUJ1 Detail in HMRbase |
Gene ID | 281192 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 10348 |
Swiss-prot Accession number | Q9BDJ6 (Sequence in FASTA format) |
Description | Appetite-regulating hormone precursor (Growth hormone secretagogue)(Growth hormone-releasing peptide) (Motilin-related peptide)[Contains: Ghrelin; Obestatin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein (By similarity) |
Developmental Stage | N/A |
Similarity | Belongs to the motilin family. |
Tissue Specificity | N/A |
Post translational modification | O-n-octanoylation is essential for ghrelin activity (By similarity). Amidation of Leu-97 is essential for obestatin activity (By similarity). |
Function | Obestatin may be the ligand for GPR39. May have an appetite-reducing effect resulting in decreased food intake. May reduce gastric emptying activity and jejunal motility |
Protein Length | 116 Amino acids |
Molecular weight | 12793 |
References | 1 Kita K., Harada K., Yokota H.; Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
2 Li C., Lobo S., Wang Z., Fu A., Meng Y., Murdoch B., Hansen C.,Moore S.; "A full length genomic sequence of the bovine ghrelin gene."; Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. 3 Kojima M.; Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. |
Domain Name | Motilin_assoc Motilin_ghrelin |
Hormone Name | Obestatin |
Mature Hormone Sequence | FNAPFNIGIKLAGAQSLQHGQTL |
Position of mature hormone in Pre-Hormone protein | 23 Residues from position (75-97) |
Receptor | Q9BDH9 Detail in HMRbase Q9N1F8 Detail in HMRbase Q9TUJ0 Detail in HMRbase Q9TUJ1 Detail in HMRbase |
Gene ID | 281192 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 10408 |
Swiss-prot Accession number | P03972 (Sequence in FASTA format) |
Description | Muellerian-inhibiting factor precursor (MIS) (Anti-Muellerian hormone)(AMH) (Muellerian-inhibiting substance). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the TGF-beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | This glycoprotein, produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. It is also able to inhibit the growth of tumors derived from tissues of Muellerian duct origin |
Protein Length | 575 Amino acids |
Molecular weight | 60624 |
References | 1 PubMed abstract 3754790 |
Domain Name | N/A |
Hormone Name | Muellerian-inhibiting factor |
Mature Hormone Sequence | REEVFSTSALPREQATGSGALIFQQAWDWPLSSLWLPGSPLDPLCLVTLHGSGNGSRAPLRVVGVLSSYEQAFLEAVRRTHWGLSDLTTFAVCPAGNGQPVLPHLQRLQAWLGEPGGRWLVVLHLEEVTWEPTPLLRFQEPPPGGASPPELALLVVYPGPGLEVTVTGAGLPGTQSLCLTADSDFLALVVDHPEGAWRRPGLALTLRRRGNGALLSTAQLQALLFGADSRCFTRKTPALLLLLPARSSAPMPAHGRLDLVPFPQPRASPEPEEAPPSADPFLETLTRLVRALAGPPARASPPRLALDPGALAGFPQGQVNLSDPAALERLLDGEEPLLLLLPPTAATTGVPATPQGPKSPLWAAGLARRVAAELQAVAAELRALPGLPPAAPPLLARLLALCPGNPDSPGGPLRALLLLKALQGLRAEWRGRERSGSARAQRSAGAAAADGPCALRELSVDLRAERSVLIPETYQANNCQGACGWPQSDRNPRYGNHVVLLLKMQARGATLARPPCCVPTAYTGKLLISLSEERISAHHVPNMVATECGCR |
Position of mature hormone in Pre-Hormone protein | 551 Residues from position (25-575) |
Receptor | N/A |
Gene ID | 280718 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10592 |
Swiss-prot Accession number | P09611 (Sequence in FASTA format) |
Description | Chorionic somatomammotropin hormone 1 precursor (Placental lactogen I)(BPLP-I). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the somatotropin/prolactin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | N/A |
Protein Length | 236 Amino acids |
Molecular weight | 26909 |
References | 1 PubMed abstract 2341410 2 PubMed abstract 3242594 3 PubMed abstract 2003877 |
Domain Name | Hormone_1 |
Hormone Name | Chorionic somatomammotropin hormone 1 |
Mature Hormone Sequence | VEDYAPYCKNQPGNCRIPLQSLFERATLVASNNYRLAREMFNEFNKQFGEGKNFTSKVINSCHTEFMTTPNNKEAAANTEDEALLRLVISLLHSWDEPLHQAVTELLHRNGASPDILARAKEIEDKTKVLLEGVEMIQKRVHPGEKKNEPYPVWSEKSSLTADDEDVRQTAFYRMFHCLHRDSSKISTYINLLKCRFTPC |
Position of mature hormone in Pre-Hormone protein | 200 Residues from position (37-236) |
Receptor | N/A |
Gene ID | 281097 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10593 |
Swiss-prot Accession number | P19159 (Sequence in FASTA format) |
Description | Chorionic somatomammotropin hormone 2 precursor (Placental lactogenII) (BPLP-II). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the somatotropin/prolactin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | N/A |
Protein Length | 238 Amino acids |
Molecular weight | 27714 |
References | 1 PubMed abstract 2341410 |
Domain Name | Hormone_1 |
Hormone Name | Chorionic somatomammotropin hormone 2 |
Mature Hormone Sequence | ISCPSCGPDMFVSLQKSLIDVFINAASLSHDFHNLSTIMFNEFDEKYAQGKLYYINATKSCHTNSFHTPEERDKAQQMNNEDLSKWTLVLLYSWNNPLYYLLLELRNMKNLSEAVISSAMEIENMSEKLQAFIESQFRKIIVPVLKMIHEVSDTWSRFSSMTFSDEDRSISEYYNLFYCLRRDSRKVDMYIKILTCRTRKTC |
Position of mature hormone in Pre-Hormone protein | 202 Residues from position (37-238) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10669 |
Swiss-prot Accession number | P01302 (Sequence in FASTA format) |
Description | Pancreatic prohormone precursor (Pancreatic polypeptide) (PP)[Contains: Pancreatic hormone; C-terminal peptide 1; C-terminalpeptide 2]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the NPY family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Pancreatic hormone is synthesized in pancreatic islets of Langerhans and acts as a regulator of pancreatic and gastrointestinal functions |
Protein Length | 131 Amino acids |
Molecular weight | 14376 |
References | 1 PubMed abstract 7831336 2 Chance R.E., Moon N.E., Johnson M.G.; (In) Jaffe B.M., Behrman H.R. (eds.);Methods of hormone radioimmunoassay (2nd ed.), pp.657-672, AcademicPress, New York and London (1979). 3 PubMed abstract 1734969 |
Domain Name | Hormone_3 |
Hormone Name | Pancreatic hormone |
Mature Hormone Sequence | APLEPEYPGDNATPEQMAQYAAELRRYINMLTRPRY |
Position of mature hormone in Pre-Hormone protein | 36 Residues from position (30-65) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | 1BBA 1LJV 1V1D |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10800 |
Swiss-prot Accession number | P01317 (Sequence in FASTA format) |
Description | Insulin precursor [Contains: Insulin B chain; Insulin A chain]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the insulin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver |
Protein Length | 105 Amino acids |
Molecular weight | 11393 |
References | 1 PubMed abstract 2456452 2 PubMed abstract 4928892 3 PubMed abstract 14886311 4 PubMed abstract 5545080 5 PubMed abstract 5105368 6 PubMed abstract 13032079 7 PubMed abstract 13249947 8 Smith G.D., Duax W.L., Dodson E.J., Dodson G.G., de Graaf R.A.G.,Reynolds C.D.; "The structure of des-Phe b1 bovine insulin."; Acta Crystallogr. B 38:3028-3032(1982). 9 PubMed abstract 9141131 |
Domain Name | Insulin |
Hormone Name | Insulin B chain |
Mature Hormone Sequence | FVNQHLCGSHLVEALYLVCGERGFFYTPKA |
Position of mature hormone in Pre-Hormone protein | 30 Residues from position (25-54) |
Receptor | N/A |
Gene ID | 280829 |
PDB ID | 1APH 1BPH 1CPH 1DPH 1HO0 1PID 2A3G 2BN1 2BN3 2INS |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10801 |
Swiss-prot Accession number | P01317 (Sequence in FASTA format) |
Description | Insulin precursor [Contains: Insulin B chain; Insulin A chain]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Mevtazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the insulin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver |
Protein Length | 105 Amino acids |
Molecular weight | 11393 |
References | 1 PubMed abstract 2456452 2 PubMed abstract 4928892 3 PubMed abstract 14886311 4 PubMed abstract 5545080 5 PubMed abstract 5105368 6 PubMed abstract 13032079 7 PubMed abstract 13249947 8 Smith G.D., Duax W.L., Dodson E.J., Dodson G.G., de Graaf R.A.G.,Reynolds C.D.; "The structure of des-Phe b1 bovine insulin."; Acta Crystallogr. B 38:3028-3032(1982). 9 PubMed abstract 9141131 |
Domain Name | Insulin |
Hormone Name | Insulin A chain |
Mature Hormone Sequence | GIVEQCCASVCSLYQLENYCN |
Position of mature hormone in Pre-Hormone protein | 21 Residues from position (85-105) |
Receptor | N/A |
Gene ID | 280829 |
PDB ID | 1APH 1BPH 1CPH 1DPH 1HO0 1PID 2A3G 2BN1 2BN3 2INS |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10915 |
Swiss-prot Accession number | P01175 (Sequence in FASTA format) |
Description | Oxytocin-neurophysin 1 precursor (OT-NPI) [Contains: Oxytocin(Ocytocin); Neurophysin 1]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the vasopressin/oxytocin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland |
Protein Length | 125 Amino acids |
Molecular weight | 12665 |
References | 1 PubMed abstract 3768139 2 PubMed abstract 6709064 3 PubMed abstract 6209133 4 PubMed abstract 13129273 5 Tuppy H., Michl H.; "About the chemical structure of oxytocin."; Monatsh. Chem. 84:1011-1020(1953). 6 PubMed abstract 670174 7 PubMed abstract 428540 8 PubMed abstract 2911588 9 PubMed abstract 3008332 |
Domain Name | Hormone_5 |
Hormone Name | Oxytocin |
Mature Hormone Sequence | CYIQNCPLG |
Position of mature hormone in Pre-Hormone protein | 9 Residues from position (20-28) |
Receptor | P56449
Detail in HMRbase |
Gene ID | 280888 |
PDB ID | 1L5C 1L5D 1XY1 1XY2 2HNU 2HNV 2HNW |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11033 |
Swiss-prot Accession number | P01260 (Sequence in FASTA format) |
Description | Calcitonin. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the calcitonin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones |
Protein Length | 32 Amino acids |
Molecular weight | 3596 |
References | 1 PubMed abstract 5259773 |
Domain Name | Calc_CGRP_IAPP |
Hormone Name | Calcitonin |
Mature Hormone Sequence | CSNLSTCVLSAYWKDLNNYHRFSGMGFGPETP |
Position of mature hormone in Pre-Hormone protein | 32 Residues from position (1-32) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11037 |
Swiss-prot Accession number | P01252 (Sequence in FASTA format) |
Description | Prothymosin alpha [Contains: Thymosin alpha-1]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Nucleus |
Developmental Stage | N/A |
Similarity | Belongs to the pro/parathymosin family. |
Tissue Specificity | N/A |
Post translational modification | Covalently linked to a small RNA of about 20 nucleotides (By similarity). |
Function | Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections |
Protein Length | 109 Amino acids |
Molecular weight | 11941 |
References | 1 PubMed abstract 2901823 2 PubMed abstract 762108 3 PubMed abstract 1426245 4 PubMed abstract 8485135 |
Domain Name | Prothymosin |
Hormone Name | Prothymosin alpha |
Mature Hormone Sequence | SDAAVDTSSEITTKDLKEKKEVVEEAENGREAPANGNANEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAATGKRAAEDDEDDDVDTKKQKTDEDD |
Position of mature hormone in Pre-Hormone protein | 109 Residues from position (2-110) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11038 |
Swiss-prot Accession number | P01252 (Sequence in FASTA format) |
Description | Prothymosin alpha [Contains: Thymosin alpha-1]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Nucleus |
Developmental Stage | N/A |
Similarity | Belongs to the pro/parathymosin family. |
Tissue Specificity | N/A |
Post translational modification | Covalently linked to a small RNA of about 20 nucleotides (By similarity). |
Function | It is a potent immunopotentiating agent |
Protein Length | 109 Amino acids |
Molecular weight | 11941 |
References | 1 PubMed abstract 2901823 2 PubMed abstract 762108 3 PubMed abstract 1426245 4 PubMed abstract 8485135 |
Domain Name | Prothymosin |
Hormone Name | Thymosin alpha-1 |
Mature Hormone Sequence | SDAAVDTSSEITTKDLKEKKEVVEEAEN |
Position of mature hormone in Pre-Hormone protein | 28 Residues from position (2-29) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11045 |
Swiss-prot Accession number | P21752 (Sequence in FASTA format) |
Description | Thymosin beta-10 (Thymosin beta-9) [Contains: Thymosin beta-8]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Cytoplasm |
Developmental Stage | N/A |
Similarity | Belongs to the thymosin beta family. |
Tissue Specificity | Distributed in numerous types of tissues, including thymus, spleen, lung, liver and muscle |
Post translational modification | N/A |
Function | Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization |
Protein Length | 42 Amino acids |
Molecular weight | 4805 |
References | 1 Gutierrez-Pabello J.A., Adams L.G.; "Bovine thymosin beta-10 full length cDNA sequence."; Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 6952223 3 PubMed abstract 3818171 4 Gallert B., Zarbock J., Voelter W., Holak T.A.; "A nuclear magnetic resonance and simulated annealing study ofthymosin beta-9 in solution."; (In) Schneider C.H., Eberles A.N. (eds.);Peptides 1992, pp.517-518, Escom Science Publishers, Leiden (1993). 5 PubMed abstract 9108730 |
Domain Name | Thymosin |
Hormone Name | Thymosin beta-10 |
Mature Hormone Sequence | ADKPDLGEINSFDKAKLKKTETQEKNTLPTKETIEQEKQAK |
Position of mature hormone in Pre-Hormone protein | 41 Residues from position (2-42) |
Receptor | N/A |
Gene ID | 282385 |
PDB ID | 1HJ0 |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11046 |
Swiss-prot Accession number | P21752 (Sequence in FASTA format) |
Description | Thymosin beta-10 (Thymosin beta-9) [Contains: Thymosin beta-8]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Cytoplasm |
Developmental Stage | N/A |
Similarity | Belongs to the thymosin beta family. |
Tissue Specificity | Distributed in numerous types of tissues, including thymus, spleen, lung, liver and muscle |
Post translational modification | N/A |
Function | Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization |
Protein Length | 42 Amino acids |
Molecular weight | 4805 |
References | 1 Gutierrez-Pabello J.A., Adams L.G.; "Bovine thymosin beta-10 full length cDNA sequence."; Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 6952223 3 PubMed abstract 3818171 4 Gallert B., Zarbock J., Voelter W., Holak T.A.; "A nuclear magnetic resonance and simulated annealing study ofthymosin beta-9 in solution."; (In) Schneider C.H., Eberles A.N. (eds.);Peptides 1992, pp.517-518, Escom Science Publishers, Leiden (1993). 5 PubMed abstract 9108730 |
Domain Name | Thymosin |
Hormone Name | Thymosin beta-8 |
Mature Hormone Sequence | ADKPDLGEINSFDKAKLKKTETQEKNTLPTKETIEQEKQ |
Position of mature hormone in Pre-Hormone protein | 39 Residues from position (2-40) |
Receptor | N/A |
Gene ID | 282385 |
PDB ID | 1HJ0 |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11055 |
Swiss-prot Accession number | P62326 (Sequence in FASTA format) |
Description | Thymosin beta-4 (T beta 4) [Contains: Hematopoietic system regulatorypeptide (Seraspenide)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Cytoplasm |
Developmental Stage | N/A |
Similarity | Belongs to the thymosin beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization |
Protein Length | 44 Amino acids |
Molecular weight | 5053 |
References | 1 Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.; "Analysis of sequences obtained from constructed full-length bovinecDNA libraries."; Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
2 Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. 3 PubMed abstract 6940133 4 PubMed abstract 2915977 5 PubMed abstract 2253778 6 PubMed abstract 1551869 7 PubMed abstract 2261438 8 PubMed abstract 8269922 |
Domain Name | Thymosin |
Hormone Name | Thymosin beta-4 |
Mature Hormone Sequence | SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES |
Position of mature hormone in Pre-Hormone protein | 43 Residues from position (2-44) |
Receptor | N/A |
Gene ID | 781334 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11079 |
Swiss-prot Accession number | P01272 (Sequence in FASTA format) |
Description | Glucagon precursor [Contains: Glicentin; Glicentin-related polypeptide(GRPP); Oxyntomodulin (OXY) (OXM); Glucagon; Glucagon-like peptide 1(GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-likepeptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract |
Post translational modification | Proglucagon is posttranslationally processed in a tissue- specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by posttranslational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). |
Function | Glicentin may modulate gastric acid secretion and gastro-pyloro-duodenal activity |
Protein Length | 180 Amino acids |
Molecular weight | 20944 |
References | 1 PubMed abstract 6577439 2 Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 3 PubMed abstract 5102927 4 PubMed abstract 12554744 5 PubMed abstract 12626323 6 PubMed abstract 10322410 7 PubMed abstract 10605628 8 PubMed abstract 6631957 |
Domain Name | Hormone_2 |
Hormone Name | Glicentin |
Mature Hormone Sequence | RSLQNTEEKSSSFPAPQTDPLGDPDQINEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNKNNIA |
Position of mature hormone in Pre-Hormone protein | 69 Residues from position (21-89) |
Receptor | N/A |
Gene ID | 280802 |
PDB ID | 1KX6 |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11080 |
Swiss-prot Accession number | P01272 (Sequence in FASTA format) |
Description | Glucagon precursor [Contains: Glicentin; Glicentin-related polypeptide(GRPP); Oxyntomodulin (OXY) (OXM); Glucagon; Glucagon-like peptide 1(GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-likepeptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract |
Post translational modification | Proglucagon is posttranslationally processed in a tissue- specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by posttranslational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). |
Function | Oxyntomodulin significantly reduces food intake |
Protein Length | 180 Amino acids |
Molecular weight | 20944 |
References | 1 PubMed abstract 6577439 2 Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 3 PubMed abstract 5102927 4 PubMed abstract 12554744 5 PubMed abstract 12626323 6 PubMed abstract 10322410 7 PubMed abstract 10605628 8 PubMed abstract 6631957 |
Domain Name | Hormone_2 |
Hormone Name | Oxyntomodulin |
Mature Hormone Sequence | HSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNKNNIA |
Position of mature hormone in Pre-Hormone protein | 37 Residues from position (53-89) |
Receptor | N/A |
Gene ID | 280802 |
PDB ID | 1KX6 |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11081 |
Swiss-prot Accession number | P01272 (Sequence in FASTA format) |
Description | Glucagon precursor [Contains: Glicentin; Glicentin-related polypeptide(GRPP); Oxyntomodulin (OXY) (OXM); Glucagon; Glucagon-like peptide 1(GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-likepeptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract |
Post translational modification | Proglucagon is posttranslationally processed in a tissue- specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by posttranslational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). |
Function | Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia |
Protein Length | 180 Amino acids |
Molecular weight | 20944 |
References | 1 PubMed abstract 6577439 2 Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 3 PubMed abstract 5102927 4 PubMed abstract 12554744 5 PubMed abstract 12626323 6 PubMed abstract 10322410 7 PubMed abstract 10605628 8 PubMed abstract 6631957 |
Domain Name | Hormone_2 |
Hormone Name | Glucagon |
Mature Hormone Sequence | HSQGTFTSDYSKYLDSRRAQDFVQWLMNT |
Position of mature hormone in Pre-Hormone protein | 29 Residues from position (53-81) |
Receptor | N/A |
Gene ID | 280802 |
PDB ID | 1KX6 |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11082 |
Swiss-prot Accession number | P01272 (Sequence in FASTA format) |
Description | Glucagon precursor [Contains: Glicentin; Glicentin-related polypeptide(GRPP); Oxyntomodulin (OXY) (OXM); Glucagon; Glucagon-like peptide 1(GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-likepeptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract |
Post translational modification | Proglucagon is posttranslationally processed in a tissue- specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by posttranslational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). |
Function | GLP-1 is a potent stimulator of glucose-dependent insulin release. Play important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Have growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferaton |
Protein Length | 180 Amino acids |
Molecular weight | 20944 |
References | 1 PubMed abstract 6577439 2 Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 3 PubMed abstract 5102927 4 PubMed abstract 12554744 5 PubMed abstract 12626323 6 PubMed abstract 10322410 7 PubMed abstract 10605628 8 PubMed abstract 6631957 |
Domain Name | Hormone_2 |
Hormone Name | Glucagon-like peptide 1 |
Mature Hormone Sequence | HDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG |
Position of mature hormone in Pre-Hormone protein | 37 Residues from position (92-128) |
Receptor | N/A |
Gene ID | 280802 |
PDB ID | 1KX6 |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11083 |
Swiss-prot Accession number | P01272 (Sequence in FASTA format) |
Description | Glucagon precursor [Contains: Glicentin; Glicentin-related polypeptide(GRPP); Oxyntomodulin (OXY) (OXM); Glucagon; Glucagon-like peptide 1(GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-likepeptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract |
Post translational modification | Proglucagon is posttranslationally processed in a tissue- specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by posttranslational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). |
Function | GLP-2 stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability |
Protein Length | 180 Amino acids |
Molecular weight | 20944 |
References | 1 PubMed abstract 6577439 2 Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 3 PubMed abstract 5102927 4 PubMed abstract 12554744 5 PubMed abstract 12626323 6 PubMed abstract 10322410 7 PubMed abstract 10605628 8 PubMed abstract 6631957 |
Domain Name | Hormone_2 |
Hormone Name | Glucagon-like peptide 2 |
Mature Hormone Sequence | HADGSFSDEMNTVLDSLATRDFINWLLQTKITD |
Position of mature hormone in Pre-Hormone protein | 33 Residues from position (146-178) |
Receptor | N/A |
Gene ID | 280802 |
PDB ID | 1KX6 |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11158 |
Swiss-prot Accession number | Q863C3 (Sequence in FASTA format) |
Description | Gastrin-releasing peptide precursor (GRP) [Contains: Neuromedin-C(GRP-10) (GRP-(18-27))] (Fragment). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the bombesin/neuromedin-B/ranatensin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | GRP stimulates gastrin release as well as other gastrointestinal hormones |
Protein Length | 126 Amino acids |
Molecular weight | 13840 |
References | 1 Budipitojo T., Sasaki T., Cruzana M.B.C., Kitamura N., Yamada J.; "Molecular cloning of cDNA encoding an endometrial gastrin-releasingpeptide (GRP) of cow."; Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2755876 |
Domain Name | Bombesin |
Hormone Name | Gastrin-releasing peptide |
Mature Hormone Sequence | APVTAGRGGALAKMYTRGNHWAVGHLM |
Position of mature hormone in Pre-Hormone protein | 27 Residues from position (24-50) |
Receptor | N/A |
Gene ID | 615323 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11164 |
Swiss-prot Accession number | P41520 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | The precursor cleaved by enzymes to produce a number of active cholecystokinins. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion |
Protein Length | 115 Amino acids |
Molecular weight | 12835 |
References | 1 Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2217909 3 PubMed abstract 4011954 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-18 |
Mature Hormone Sequence | LDPSHRISDRDYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 18 Residues from position (86-103) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 617510 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11258 |
Swiss-prot Accession number | P01190 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
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. |
Function | Beta-endorphin is an endogenous opiate |
Protein Length | 265 Amino acids |
Molecular weight | 29260 |
References | 1 PubMed abstract 221818 2 PubMed abstract 6249166 3 PubMed abstract 6263630 4 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 5 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 6 PubMed abstract 216007 7 PubMed abstract 7274457 8 PubMed abstract 13642798 9 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 10 PubMed abstract 4344689 11 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 12 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 13 PubMed abstract 13348631 14 PubMed abstract 1065904 15 PubMed abstract 4030947 16 PubMed abstract 2266117 17 PubMed abstract 221818 18 PubMed abstract 6249166 19 PubMed abstract 6263630 20 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 21 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 22 PubMed abstract 216007 23 PubMed abstract 7274457 24 PubMed abstract 13642798 25 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 26 PubMed abstract 4344689 27 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 28 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 29 PubMed abstract 13348631 30 PubMed abstract 1065904 31 PubMed abstract 4030947 32 PubMed abstract 2266117 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Beta-endorphin |
Mature Hormone Sequence | YGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ |
Position of mature hormone in Pre-Hormone protein | 31 Residues from position (235-265) |
Receptor | P47798
Detail in HMRbase |
Gene ID | 281416 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11259 |
Swiss-prot Accession number | P01190 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
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. |
Function | MSH (melanocyte-stimulating hormone) increases the pigmentation of skin by increasing melanin production in melanocytes |
Protein Length | 265 Amino acids |
Molecular weight | 29260 |
References | 1 PubMed abstract 221818 2 PubMed abstract 6249166 3 PubMed abstract 6263630 4 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 5 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 6 PubMed abstract 216007 7 PubMed abstract 7274457 8 PubMed abstract 13642798 9 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 10 PubMed abstract 4344689 11 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 12 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 13 PubMed abstract 13348631 14 PubMed abstract 1065904 15 PubMed abstract 4030947 16 PubMed abstract 2266117 17 PubMed abstract 221818 18 PubMed abstract 6249166 19 PubMed abstract 6263630 20 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 21 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 22 PubMed abstract 216007 23 PubMed abstract 7274457 24 PubMed abstract 13642798 25 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 26 PubMed abstract 4344689 27 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 28 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 29 PubMed abstract 13348631 30 PubMed abstract 1065904 31 PubMed abstract 4030947 32 PubMed abstract 2266117 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Melanotropin gamma (Gamma-MSH) |
Mature Hormone Sequence | YVMGHFRWDRF |
Position of mature hormone in Pre-Hormone protein | 11 Residues from position (77-87) |
Receptor | P47798
Detail in HMRbase |
Gene ID | 281416 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11260 |
Swiss-prot Accession number | P01190 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
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. |
Function | ACTH stimulates the adrenal glands to release cortisol |
Protein Length | 265 Amino acids |
Molecular weight | 29260 |
References | 1 PubMed abstract 221818 2 PubMed abstract 6249166 3 PubMed abstract 6263630 4 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 5 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 6 PubMed abstract 216007 7 PubMed abstract 7274457 8 PubMed abstract 13642798 9 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 10 PubMed abstract 4344689 11 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 12 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 13 PubMed abstract 13348631 14 PubMed abstract 1065904 15 PubMed abstract 4030947 16 PubMed abstract 2266117 17 PubMed abstract 221818 18 PubMed abstract 6249166 19 PubMed abstract 6263630 20 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 21 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 22 PubMed abstract 216007 23 PubMed abstract 7274457 24 PubMed abstract 13642798 25 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 26 PubMed abstract 4344689 27 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 28 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 29 PubMed abstract 13348631 30 PubMed abstract 1065904 31 PubMed abstract 4030947 32 PubMed abstract 2266117 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Corticotropin |
Mature Hormone Sequence | SYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAQAFPLEF |
Position of mature hormone in Pre-Hormone protein | 39 Residues from position (132-170) |
Receptor | P47798
Detail in HMRbase |
Gene ID | 281416 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11261 |
Swiss-prot Accession number | P01190 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
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. |
Function | MSH (melanocyte-stimulating hormone) increases the pigmentation of skin by increasing melanin production in melanocytes |
Protein Length | 265 Amino acids |
Molecular weight | 29260 |
References | 1 PubMed abstract 221818 2 PubMed abstract 6249166 3 PubMed abstract 6263630 4 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 5 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 6 PubMed abstract 216007 7 PubMed abstract 7274457 8 PubMed abstract 13642798 9 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 10 PubMed abstract 4344689 11 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 12 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 13 PubMed abstract 13348631 14 PubMed abstract 1065904 15 PubMed abstract 4030947 16 PubMed abstract 2266117 17 PubMed abstract 221818 18 PubMed abstract 6249166 19 PubMed abstract 6263630 20 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 21 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 22 PubMed abstract 216007 23 PubMed abstract 7274457 24 PubMed abstract 13642798 25 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 26 PubMed abstract 4344689 27 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 28 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 29 PubMed abstract 13348631 30 PubMed abstract 1065904 31 PubMed abstract 4030947 32 PubMed abstract 2266117 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Melanotropin alpha (Alpha-MSH) |
Mature Hormone Sequence | SYSMEHFRWGKPV |
Position of mature hormone in Pre-Hormone protein | 13 Residues from position (132-144) |
Receptor | P47798
Detail in HMRbase |
Gene ID | 281416 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11262 |
Swiss-prot Accession number | P01190 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
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. |
Function | Stimulates melanocytes to produce melanin. It performs lipid-mobilizing functions such as lipolysis and steroidogenesis. |
Protein Length | 265 Amino acids |
Molecular weight | 29260 |
References | 1 PubMed abstract 221818 2 PubMed abstract 6249166 3 PubMed abstract 6263630 4 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 5 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 6 PubMed abstract 216007 7 PubMed abstract 7274457 8 PubMed abstract 13642798 9 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 10 PubMed abstract 4344689 11 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 12 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 13 PubMed abstract 13348631 14 PubMed abstract 1065904 15 PubMed abstract 4030947 16 PubMed abstract 2266117 17 PubMed abstract 221818 18 PubMed abstract 6249166 19 PubMed abstract 6263630 20 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 21 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 22 PubMed abstract 216007 23 PubMed abstract 7274457 24 PubMed abstract 13642798 25 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 26 PubMed abstract 4344689 27 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 28 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 29 PubMed abstract 13348631 30 PubMed abstract 1065904 31 PubMed abstract 4030947 32 PubMed abstract 2266117 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Lipotropin beta (Beta-LPH) |
Mature Hormone Sequence | ELTGERLEQARGPEAQAESAAARAELEYGLVAEAEAEAAEKKDSGPYKMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ |
Position of mature hormone in Pre-Hormone protein | 93 Residues from position (173-265) |
Receptor | P47798
Detail in HMRbase |
Gene ID | 281416 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11263 |
Swiss-prot Accession number | P01190 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
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. |
Function | Stimulates melanocytes to produce melanin. It performs lipid-mobilizing functions such as lipolysis and steroidogenesis. |
Protein Length | 265 Amino acids |
Molecular weight | 29260 |
References | 1 PubMed abstract 221818 2 PubMed abstract 6249166 3 PubMed abstract 6263630 4 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 5 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 6 PubMed abstract 216007 7 PubMed abstract 7274457 8 PubMed abstract 13642798 9 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 10 PubMed abstract 4344689 11 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 12 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 13 PubMed abstract 13348631 14 PubMed abstract 1065904 15 PubMed abstract 4030947 16 PubMed abstract 2266117 17 PubMed abstract 221818 18 PubMed abstract 6249166 19 PubMed abstract 6263630 20 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 21 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 22 PubMed abstract 216007 23 PubMed abstract 7274457 24 PubMed abstract 13642798 25 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 26 PubMed abstract 4344689 27 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 28 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 29 PubMed abstract 13348631 30 PubMed abstract 1065904 31 PubMed abstract 4030947 32 PubMed abstract 2266117 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Lipotropin gamma (Gamma-LPH) |
Mature Hormone Sequence | ELTGERLEQARGPEAQAESAAARAELEYGLVAEAEAEAAEKKDSGPYKMEHFRWGSPPKD |
Position of mature hormone in Pre-Hormone protein | 60 Residues from position (173-232) |
Receptor | P47798
Detail in HMRbase |
Gene ID | 281416 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11264 |
Swiss-prot Accession number | P01190 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
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. |
Function | MSH (melanocyte-stimulating hormone) increases the pigmentation of skin by increasing melanin production in melanocytes |
Protein Length | 265 Amino acids |
Molecular weight | 29260 |
References | 1 PubMed abstract 221818 2 PubMed abstract 6249166 3 PubMed abstract 6263630 4 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 5 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 6 PubMed abstract 216007 7 PubMed abstract 7274457 8 PubMed abstract 13642798 9 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 10 PubMed abstract 4344689 11 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 12 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 13 PubMed abstract 13348631 14 PubMed abstract 1065904 15 PubMed abstract 4030947 16 PubMed abstract 2266117 17 PubMed abstract 221818 18 PubMed abstract 6249166 19 PubMed abstract 6263630 20 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 21 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 22 PubMed abstract 216007 23 PubMed abstract 7274457 24 PubMed abstract 13642798 25 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 26 PubMed abstract 4344689 27 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 28 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 29 PubMed abstract 13348631 30 PubMed abstract 1065904 31 PubMed abstract 4030947 32 PubMed abstract 2266117 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Melanotropin beta (Beta-MSH) |
Mature Hormone Sequence | DSGPYKMEHFRWGSPPKD |
Position of mature hormone in Pre-Hormone protein | 18 Residues from position (215-232) |
Receptor | P47798
Detail in HMRbase |
Gene ID | 281416 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11265 |
Swiss-prot Accession number | P01190 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
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. |
Function | Met-enkephalin is an endogenous opiate |
Protein Length | 265 Amino acids |
Molecular weight | 29260 |
References | 1 PubMed abstract 221818 2 PubMed abstract 6249166 3 PubMed abstract 6263630 4 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 5 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 6 PubMed abstract 216007 7 PubMed abstract 7274457 8 PubMed abstract 13642798 9 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 10 PubMed abstract 4344689 11 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 12 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 13 PubMed abstract 13348631 14 PubMed abstract 1065904 15 PubMed abstract 4030947 16 PubMed abstract 2266117 17 PubMed abstract 221818 18 PubMed abstract 6249166 19 PubMed abstract 6263630 20 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 21 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 22 PubMed abstract 216007 23 PubMed abstract 7274457 24 PubMed abstract 13642798 25 Li C.H., Dixon J.S., Chung D.; "Isolation of melatonin, the pineal gland factor that lightensmelanocytes."; J. Am. Chem. Soc. 80:2587-2588(1958). 26 PubMed abstract 4344689 27 Pankov Y.A.; "Primary structure of the bovine beta-lipotropic hormone."; Vopr. Med. Khim. 19:330-332(1973). 28 Geschwind I.I., Li C.H., Barnafi L.; "The isolation and structure of a melanocyte-stimulating hormone frombovine pituitary glands."; J. Am. Chem. Soc. 79:1003-1004(1957). 29 PubMed abstract 13348631 30 PubMed abstract 1065904 31 PubMed abstract 4030947 32 PubMed abstract 2266117 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Met-enkephalin |
Mature Hormone Sequence | YGGFM |
Position of mature hormone in Pre-Hormone protein | 5 Residues from position (235-239) |
Receptor | P47798
Detail in HMRbase |
Gene ID | 281416 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11301 |
Swiss-prot Accession number | P01217 (Sequence in FASTA format) |
Description | Glycoprotein hormones alpha chain precursor (Anterior pituitaryglycoprotein hormones common subunit alpha) (Follitropin alpha chain)(Follicle-stimulating hormone alpha chain) (FSH-alpha) (Lutropin alphachain) (Luteinizing hormone alpha chain) (LSH-alpha) (Thyrotropinalpha chain) (Thyroid-stimulating hormone alpha chain) (TSH-alpha). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glycoprotein hormones subunit alpha family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | N/A |
Protein Length | 120 Amino acids |
Molecular weight | 13616 |
References | 1 PubMed abstract 6314263 2 PubMed abstract 6688736 3 PubMed abstract 6187740 4 PubMed abstract 5101174 5 PubMed abstract 5101175 6 PubMed abstract 5107231 7 PubMed abstract 4854483 8 PubMed abstract 6314263 9 PubMed abstract 6688736 10 PubMed abstract 6187740 11 PubMed abstract 5101174 12 PubMed abstract 5101175 13 PubMed abstract 5107231 14 PubMed abstract 4854483 |
Domain Name | Hormone_6 |
Hormone Name | Glycoprotein hormones alpha chain |
Mature Hormone Sequence | FPDGEFTMQGCPECKLKENKYFSKPDAPIYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKAFTKATVMGNVRVENHTECHCSTCYYHKS |
Position of mature hormone in Pre-Hormone protein | 96 Residues from position (25-120) |
Receptor | P35376 Detail in HMRbase Q28005 Detail in HMRbase Q27987 Detail in HMRbase |
Gene ID | 280749 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11306 |
Swiss-prot Accession number | P01223 (Sequence in FASTA format) |
Description | Thyrotropin subunit beta precursor (Thyroid-stimulating hormonesubunit beta) (TSH-beta) (TSH-B) (Thyrotropin beta chain). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the glycoprotein hormones subunit beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Indispensable for the control of thyroid structure and metabolism |
Protein Length | 138 Amino acids |
Molecular weight | 15624 |
References | 1 PubMed abstract 6325416 2 PubMed abstract 5101174 3 PubMed abstract 5101173 4 PubMed abstract 8670056 |
Domain Name | Cys_knot |
Hormone Name | Thyroid-stimulating hormone subunit beta (TSH-B) (Thyrotropin beta chain) |
Mature Hormone Sequence | FCIPTEYMMHVERKECAYCLTINTTVCAGYCMTRDVNGKLFLPKYALSQDVCTYRDFMYKTAEIPGCPRHVTPYFSYPVAISCKCGKCNTDYSDCIHEAIKTNYCTKPQKSY |
Position of mature hormone in Pre-Hormone protein | 112 Residues from position (21-132) |
Receptor | Q27987
Detail in HMRbase |
Gene ID | 281552 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11317 |
Swiss-prot Accession number | P01239 (Sequence in FASTA format) |
Description | Prolactin precursor (PRL). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the somatotropin/prolactin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Prolactin acts primarily on the mammary gland by promoting lactation |
Protein Length | 229 Amino acids |
Molecular weight | 25793 |
References | 1 PubMed abstract 6274859 2 Cao X., Huang S.Z., Ren Z.R., Zeng Y.T.; Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. 3 PubMed abstract 6299665 4 PubMed abstract 6897772 5 Rubtsov P.M., Oganesyan R.G., Gorbulev V.G., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones. II. Possible polymorphism ofpreprolactin in cattle. Data of molecular cloning."; Mol. Biol. (Mosk.) 22:117-127(1988). 6 PubMed abstract 4608931 7 PubMed abstract 5507606 8 PubMed abstract 8250856 |
Domain Name | Hormone_1 |
Hormone Name | Prolactin |
Mature Hormone Sequence | TPVCPNGPGNCQVSLRDLFDRAVMVSHYIHDLSSEMFNEFDKRYAQGKGFITMALNSCHTSSLPTPEDKEQAQQTHHEVLMSLILGLLRSWNDPLYHLVTEVRGMKGAPDAILSRAIEIEEENKRLLEGMEMIFGQVIPGAKETEPYPVWSGLPSLQTKDEDARYSAFYNLLHCLRRDSSKIDTYLKLLNCRIIYNNNC |
Position of mature hormone in Pre-Hormone protein | 199 Residues from position (31-229) |
Receptor | Q28172
Detail in HMRbase |
Gene ID | 280901 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11321 |
Swiss-prot Accession number | P01246 (Sequence in FASTA format) |
Description | Somatotropin precursor (Growth hormone). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the somatotropin/prolactin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues |
Protein Length | 217 Amino acids |
Molecular weight | 24558 |
References | 1 PubMed abstract 6893197 2 PubMed abstract 6296767 3 PubMed abstract 6303731 4 PubMed abstract 6357899 5 Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,Zhvirblis G.S., Skryabin K.G., Baev A.A.; "Genetic engineering of peptide hormones."; Mol. Biol. (Mosk.) 19:226-235(1985). 6 Mauro S.M.Z., Ferro M.I.T., Macari M., Ferro J.A.; "The complete sequence of a cDNA encoding the bovine growth hormone."; Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. 7 Javadmanesh A., Nassiry M., Eftekhari Shahrudi F., Basami M.; "Cloning the cDNA of bovine growth hormone gene in E. coli."; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 8 PubMed abstract 4584625 9 PubMed abstract 4580883 10 PubMed abstract 3899556 11 PubMed abstract 4856718 12 PubMed abstract 5579941 13 PubMed abstract 1123321 14 PubMed abstract 2021631 |
Domain Name | Hormone_1 |
Hormone Name | Growth hormone (Somatotropin) (GH) |
Mature Hormone Sequence | AFPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDGTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF |
Position of mature hormone in Pre-Hormone protein | 191 Residues from position (27-217) |
Receptor | O46600
Detail in HMRbase |
Gene ID | 280804 |
PDB ID | 1BST |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11326 |
Swiss-prot Accession number | P01268 (Sequence in FASTA format) |
Description | Parathyroid hormone precursor (Parathyrin) (PTH). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the parathyroid hormone family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion |
Protein Length | 115 Amino acids |
Molecular weight | 12980 |
References | 1 PubMed abstract 388425 2 PubMed abstract 6170060 3 PubMed abstract 6185374 4 PubMed abstract 6086460 5 PubMed abstract 4522780 6 PubMed abstract 5531031 7 PubMed abstract 5275384 8 PubMed abstract 4322265 9 PubMed abstract 10623601 |
Domain Name | Parathyroid |
Hormone Name | Parathyroid hormone (Parathyrin) (PTH) |
Mature Hormone Sequence | AVSEIQFMHNLGKHLSSMERVEWLRKKLQDVHNFVALGASIAYRDGSSQRPRKKEDNVLVESHQKSLGEADKADVDVLIKAKPQ |
Position of mature hormone in Pre-Hormone protein | 84 Residues from position (32-115) |
Receptor | Q1LZF7
Detail in HMRbase |
Gene ID | 280903 |
PDB ID | 1ZWC |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11350 |
Swiss-prot Accession number | P01352 (Sequence in FASTA format) |
Description | Gastrin precursor [Contains: Big gastrin (Gastrin 34) (G34); Gastrin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine |
Protein Length | 104 Amino acids |
Molecular weight | 11573 |
References | 1 PubMed abstract 2608050 2 PubMed abstract 1773057 3 PubMed abstract 5665711 |
Domain Name | Gastrin |
Hormone Name | Big gastrin |
Mature Hormone Sequence | QLGLQDPPHMVADLSKKQGPWVEEEEAAYGWMDF |
Position of mature hormone in Pre-Hormone protein | 34 Residues from position (59-92) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 280800 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11351 |
Swiss-prot Accession number | P01352 (Sequence in FASTA format) |
Description | Gastrin precursor [Contains: Big gastrin (Gastrin 34) (G34); Gastrin]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine |
Protein Length | 104 Amino acids |
Molecular weight | 11573 |
References | 1 PubMed abstract 2608050 2 PubMed abstract 1773057 3 PubMed abstract 5665711 |
Domain Name | Gastrin |
Hormone Name | Gastrin |
Mature Hormone Sequence | QGPWVEEEEAAYGWMDF |
Position of mature hormone in Pre-Hormone protein | 17 Residues from position (76-92) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 280800 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11366 |
Swiss-prot Accession number | P04651 (Sequence in FASTA format) |
Description | Lutropin subunit beta precursor (Luteinizing hormone subunit beta)(LSH-beta) (LSH-B) (LH-B) (Lutropin beta chain). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the glycoprotein hormones subunit beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids |
Protein Length | 141 Amino acids |
Molecular weight | 15202 |
References | 1 PubMed abstract 2987241 2 PubMed abstract 3838746 3 PubMed abstract 4770795 |
Domain Name | Cys_knot |
Hormone Name | Luteinizing hormone subunit beta (LSH-B) (LH-B)(Lutropin subunit beta) |
Mature Hormone Sequence | SRGPLRPLCQPINATLAAEKEACPVCITFTTSICAGYCPSMKRVLPVILPPMPQRVCTYHELRFASVRLPGCPPGVDPMVSFPVALSCHCGPCRLSSTDCGGPRTQPLACDHPPLPDILFL |
Position of mature hormone in Pre-Hormone protein | 121 Residues from position (21-141) |
Receptor | Q28005
Detail in HMRbase |
Gene ID | 280839 786429 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11371 |
Swiss-prot Accession number | P04837 (Sequence in FASTA format) |
Description | Follitropin subunit beta precursor (Follicle-stimulating hormone betasubunit) (FSH-beta) (FSH-B) (Follitropin beta chain). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glycoprotein hormones subunit beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Stimulates development of follicle and spermatogenesis in the reproductive organs |
Protein Length | 129 Amino acids |
Molecular weight | 14713 |
References | 1 PubMed abstract 3092216 2 PubMed abstract 3096676 3 PubMed abstract 2840246 4 PubMed abstract 3092216 5 PubMed abstract 3096676 6 PubMed abstract 2840246 |
Domain Name | Cys_knot |
Hormone Name | Follicle-stimulating hormone beta subunit |
Mature Hormone Sequence | CELTNITITVEKEECGFCISINTTWCAGYCYTRDLVYRDPARPNIQKTCTFKELVYETVKVPGCAHHADSLYTYPVATECHCSKCDSDSTDCTVRGLGPSYCSFREIKE |
Position of mature hormone in Pre-Hormone protein | 109 Residues from position (21-129) |
Receptor | P35376
Detail in HMRbase |
Gene ID | 281171 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11432 |
Swiss-prot Accession number | P26917 (Sequence in FASTA format) |
Description | Somatostatin precursor [Contains: Somatostatin-28; Somatostatin-14]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the somatostatin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Somatostatin inhibits the release of somatotropin |
Protein Length | 116 Amino acids |
Molecular weight | 12689 |
References | 1 PubMed abstract 2899837 2 PubMed abstract 10100681 3 Morsci N.S., Schnabel R.D., Taylor J.F.; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 4 Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. |
Domain Name | Somatostatin |
Hormone Name | Somatostatin-28 |
Mature Hormone Sequence | SANSNPAMAPRERKAGCKNFFWKTFTSC |
Position of mature hormone in Pre-Hormone protein | 28 Residues from position (89-116) |
Receptor | P34993
Detail in HMRbase |
Gene ID | 280932 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11433 |
Swiss-prot Accession number | P26917 (Sequence in FASTA format) |
Description | Somatostatin precursor [Contains: Somatostatin-28; Somatostatin-14]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the somatostatin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Somatostatin inhibits the release of somatotropin |
Protein Length | 116 Amino acids |
Molecular weight | 12689 |
References | 1 PubMed abstract 2899837 2 PubMed abstract 10100681 3 Morsci N.S., Schnabel R.D., Taylor J.F.; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 4 Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. |
Domain Name | Somatostatin |
Hormone Name | Somatostatin-14 |
Mature Hormone Sequence | AGCKNFFWKTFTSC |
Position of mature hormone in Pre-Hormone protein | 14 Residues from position (103-116) |
Receptor | P34993
Detail in HMRbase |
Gene ID | 280932 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11445 |
Swiss-prot Accession number | P41520 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | The precursor cleaved by enzymes to produce a number of active cholecystokinins. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion |
Protein Length | 115 Amino acids |
Molecular weight | 12835 |
References | 1 Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2217909 3 PubMed abstract 4011954 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin |
Mature Hormone Sequence | QPMPHADPTGPRAQQAEEAPRRQLRAVPRVDDEPRAQLGALLARYIQQARKAPSGRMSVIKNLQSLDPSHRISDRDYMGWMDFGRRSAEEFEYTS |
Position of mature hormone in Pre-Hormone protein | 95 Residues from position (21-115) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 617510 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11446 |
Swiss-prot Accession number | P41520 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | The precursor cleaved by enzymes to produce a number of active cholecystokinins. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion |
Protein Length | 115 Amino acids |
Molecular weight | 12835 |
References | 1 Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2217909 3 PubMed abstract 4011954 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-58 |
Mature Hormone Sequence | AVPRVDDEPRAQLGALLARYIQQARKAPSGRMSVIKNLQSLDPSHRISDRDYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 58 Residues from position (46-103) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 617510 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11447 |
Swiss-prot Accession number | P41520 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | The precursor cleaved by enzymes to produce a number of active cholecystokinins. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion |
Protein Length | 115 Amino acids |
Molecular weight | 12835 |
References | 1 Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2217909 3 PubMed abstract 4011954 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-58 desnonopeptide |
Mature Hormone Sequence | AVPRVDDEPRAQLGALLARYIQQARKAPSGRMSVIKNLQSLDPSHRISD |
Position of mature hormone in Pre-Hormone protein | 49 Residues from position (46-94) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 617510 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11448 |
Swiss-prot Accession number | P41520 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | The precursor cleaved by enzymes to produce a number of active cholecystokinins. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion |
Protein Length | 115 Amino acids |
Molecular weight | 12835 |
References | 1 Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2217909 3 PubMed abstract 4011954 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-39 |
Mature Hormone Sequence | YIQQARKAPSGRMSVIKNLQSLDPSHRISDRDYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 39 Residues from position (65-103) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 617510 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11449 |
Swiss-prot Accession number | P41520 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | The precursor cleaved by enzymes to produce a number of active cholecystokinins. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion |
Protein Length | 115 Amino acids |
Molecular weight | 12835 |
References | 1 Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2217909 3 PubMed abstract 4011954 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-33 |
Mature Hormone Sequence | KAPSGRMSVIKNLQSLDPSHRISDRDYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 33 Residues from position (71-103) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 617510 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11450 |
Swiss-prot Accession number | P41520 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | The precursor cleaved by enzymes to produce a number of active cholecystokinins. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion |
Protein Length | 115 Amino acids |
Molecular weight | 12835 |
References | 1 Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2217909 3 PubMed abstract 4011954 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-25 |
Mature Hormone Sequence | VIKNLQSLDPSHRISDRDYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 25 Residues from position (79-103) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 617510 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11451 |
Swiss-prot Accession number | P41520 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | The precursor cleaved by enzymes to produce a number of active cholecystokinins. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion |
Protein Length | 115 Amino acids |
Molecular weight | 12835 |
References | 1 Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2217909 3 PubMed abstract 4011954 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-12 |
Mature Hormone Sequence | ISDRDYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 12 Residues from position (92-103) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 617510 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11452 |
Swiss-prot Accession number | P41520 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | The precursor cleaved by enzymes to produce a number of active cholecystokinins. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion |
Protein Length | 115 Amino acids |
Molecular weight | 12835 |
References | 1 Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2217909 3 PubMed abstract 4011954 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-8 |
Mature Hormone Sequence | DYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 8 Residues from position (96-103) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 617510 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11453 |
Swiss-prot Accession number | P41520 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | The precursor cleaved by enzymes to produce a number of active cholecystokinins. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion |
Protein Length | 115 Amino acids |
Molecular weight | 12835 |
References | 1 Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2217909 3 PubMed abstract 4011954 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-7 |
Mature Hormone Sequence | YMGWMDF |
Position of mature hormone in Pre-Hormone protein | 7 Residues from position (97-103) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 617510 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11454 |
Swiss-prot Accession number | P41520 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | The precursor cleaved by enzymes to produce a number of active cholecystokinins. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion |
Protein Length | 115 Amino acids |
Molecular weight | 12835 |
References | 1 Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2217909 3 PubMed abstract 4011954 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-5 |
Mature Hormone Sequence | GWMDF |
Position of mature hormone in Pre-Hormone protein | 5 Residues from position (99-103) |
Receptor | P79266
Detail in HMRbase |
Gene ID | 617510 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11493 |
Swiss-prot Accession number | P63292 (Sequence in FASTA format) |
Description | Somatoliberin precursor (Growth hormone-releasing factor) (GRF)(Growth hormone-releasing hormone) (GHRH). |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone |
Protein Length | 106 Amino acids |
Molecular weight | 12058 |
References | 1 Zhou P., Kazmer G.W., Yang X.; Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 6421287 |
Domain Name | Hormone_2 |
Hormone Name | Somatoliberin |
Mature Hormone Sequence | YADAIFTNSYRKVLGQLSARKLLQDIMNRQQGERNQEQGAKVRL |
Position of mature hormone in Pre-Hormone protein | 44 Residues from position (31-74) |
Receptor | Q9BDH9 Detail in HMRbase Q9N1F8 Detail in HMRbase Q9TUJ0 Detail in HMRbase Q9TUJ1 Detail in HMRbase |
Gene ID | 281191 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11522 |
Swiss-prot Accession number | P50595 (Sequence in FASTA format) |
Description | Leptin;Alternative Name: Obesity factor; Precursor |
Source organism | Bos taurus (Bovine) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;Pecora; Bovidae; Bovinae; Bos. |
Subcellular location | Secreted (Probable) |
Developmental Stage | N/A |
Similarity | Belongs to the leptin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | May function as part of a signaling pathway that acts to regulate the size of the body fat depot. An increase in the level of LEP may act directly or indirectly on the CNS to inhibit food intake and/or regulate energy expenditure as part of a homeostatic mechanism to maintain constancy of the adipose mass. |
Protein Length | 167 Amino acids |
Molecular weight | 18716 |
References | 1 PubMed abstract 10594237 2 PubMed abstract 14629116 3 PubMed abstract 16305752 4 PubMed abstract 8661738 |
Domain Name | Leptin |
Hormone Name | Leptin |
Mature Hormone Sequence | |
Position of mature hormone in Pre-Hormone protein | |
Receptor | Q32PD8 Detail in HMRbase Q3SYT0 Detail in HMRbase Q59HQ0 Detail in HMRbase Q5KQU4 Detail in HMRbase Q5KQU5 Detail in HMRbase |
Gene ID | 280836 |
PDB ID | 2A16 |
Drugpedia | wiki |
Comments |