ID SOMA_HUMAN Reviewed; 217 AA. AC P01241; A6NEF6; Q14405; Q16631; Q5EB53; Q9HBZ1; Q9UMJ7; Q9UNL5; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 2. DT 13-FEB-2019, entry version 217. DE RecName: Full=Somatotropin; DE AltName: Full=Growth hormone; DE Short=GH; DE Short=GH-N; DE AltName: Full=Growth hormone 1; DE AltName: Full=Pituitary growth hormone; DE Flags: Precursor; GN Name=GH1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=386281; DOI=10.1093/nar/7.2.305; RA Roskam W., Rougeon F.; RT "Molecular cloning and nucleotide sequence of the human growth hormone RT structural gene."; RL Nucleic Acids Res. 7:305-320(1979). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=377496; DOI=10.1126/science.377496; RA Martial J.A., Hallewell R.A., Baxter J.D., Goodman H.M.; RT "Human growth hormone: complementary DNA cloning and expression in RT bacteria."; RL Science 205:602-607(1979). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND POSSIBLE RP ALTERNATIVE SPLICING. RX PubMed=6269091; DOI=10.1093/nar/9.15.3719; RA Denoto F.M., Moore D.D., Goodman H.M.; RT "Human growth hormone DNA sequence and mRNA structure: possible RT alternative splicing."; RL Nucleic Acids Res. 9:3719-3730(1981). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7169009; DOI=10.1089/dna.1.1982.1.239; RA Seeburg P.H.; RT "The human growth hormone gene family: nucleotide sequences show RT recent divergence and predict a new polypeptide hormone."; RL DNA 1:239-249(1982). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2744760; DOI=10.1016/0888-7543(89)90271-1; RA Chen E.Y., Liao Y.C., Smith D.H., Barrera-Saldana H.A., Gelinas R.E., RA Seeburg P.H.; RT "The human growth hormone locus: nucleotide sequence, biology, and RT evolution."; RL Genomics 4:479-497(1989). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Pituitary; RA Gu J., Huang Q.-H., Li N., Xu S.-H., Han Z.-G., Fu G., Chen Z.; RT "A novel gene expressed in human pituitary."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=18473352; DOI=10.1002/humu.20767; RA Sedman L., Padhukasahasram B., Kelgo P., Laan M.; RT "Complex signatures of locus-specific selective pressures and gene RT conversion on human growth hormone/chorionic somatomammotropin RT genes."; RL Hum. Mutat. 29:1181-1193(2008). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in RT the human lineage."; RL Nature 440:1045-1049(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Pituitary; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal RT axis and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5). RC TISSUE=Pituitary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-26. RX PubMed=3912261; DOI=10.1016/0378-1119(85)90319-1; RA Gray G.L., Baldridge J.S., McKeown K.S., Heyneker H.L., Chang C.N.; RT "Periplasmic production of correctly processed human growth hormone in RT Escherichia coli: natural and bacterial signal sequences are RT interchangeable."; RL Gene 39:247-254(1985). RN [13] RP PROTEIN SEQUENCE OF 27-217. RX PubMed=5810834; DOI=10.1016/0003-9861(69)90489-5; RA Li C.H., Dixon J.S., Liu W.-K.; RT "Human pituitary growth hormone. XIX. The primary structure of the RT hormone."; RL Arch. Biochem. Biophys. 133:70-91(1969). RN [14] RP PROTEIN SEQUENCE OF 27-217, AND SEQUENCE REVISION. RX PubMed=5144027; DOI=10.1016/S0003-9861(71)80060-7; RA Li C.H., Dixon J.S.; RT "Human pituitary growth hormone. 32. The primary structure of the RT hormone: revision."; RL Arch. Biochem. Biophys. 146:233-236(1971). RN [15] RP SEQUENCE REVISION. RX PubMed=4675454; RA Bewley T.A., Dixon J.S., Li C.H.; RT "Sequence comparison of human pituitary growth hormone, human RT chorionic somatomammotropin, and ovine pituitary growth and lactogenic RT hormones."; RL Int. J. Pept. Protein Res. 4:281-287(1972). RN [16] RP PROTEIN SEQUENCE OF 27-61 AND 102-124. RX PubMed=5279046; RA Niall H.D.; RT "Revised primary structure for human growth hormone."; RL Nature New Biol. 230:90-91(1971). RN [17] RP SEQUENCE REVISION TO 119-120 AND 157-159. RX PubMed=5279528; DOI=10.1073/pnas.68.4.866; RA Niall H.D., Hogan M.L., Sauer R., Rosenblum I.Y., Greenwood F.C.; RT "Sequences of pituitary and placental lactogenic and growth hormones: RT evolution from a primordial peptide by gene reduplication."; RL Proc. Natl. Acad. Sci. U.S.A. 68:866-869(1971). RN [18] RP SEQUENCE REVISION. RA Niall H.D.; RT "The chemistry of the human lactogenic hormones."; RL (In) Griffiths K. (eds.); RL Prolactin and carcinogenesis, Proc. fourth tenovus workshop prolactin, RL pp.13-20, Alpha Omega Alpha Press, Cardiff (1972). RN [19] RP PROTEIN SEQUENCE OF 27-79 (ISOFORM 2). RX PubMed=7462247; RA Chapman G.E., Rogers K.M., Brittain T., Bradshaw R.A., Bates O.J., RA Turner C., Cary P.D., Crane-Robinson C.; RT "The 20,000 molecular weight variant of human growth hormone. RT Preparation and some physical and chemical properties."; RL J. Biol. Chem. 256:2395-2401(1981). RN [20] RP PROTEIN SEQUENCE OF 46-80 (ISOFORM 2). RX PubMed=7356479; DOI=10.1016/0006-291X(80)90363-0; RA Lewis U.J., Bonewald L.F., Lewis L.J.; RT "The 20,000-dalton variant of human growth hormone: location of the RT amino acid deletions."; RL Biochem. Biophys. Res. Commun. 92:511-516(1980). RN [21] RP DEAMIDATION AT GLN-163 AND ASN-178. RX PubMed=7028740; RA Lewis U.J., Singh R.N., Bonewald L.F., Seavey B.K.; RT "Altered proteolytic cleavage of human growth hormone as a result of RT deamidation."; RL J. Biol. Chem. 256:11645-11650(1981). RN [22] RP INVOLVEMENT IN IGHD1A. RX PubMed=8364549; DOI=10.1093/hmg/2.7.1073; RA Igarashi Y., Ogawa M., Kamijo T., Iwatani N., Nishi Y., Kohno H., RA Masumura T., Koga J.; RT "A new mutation causing inherited growth hormone deficiency: a RT compound heterozygote of a 6.7 kb deletion and a two base deletion in RT the third exon of the GH-1 gene."; RL Hum. Mol. Genet. 2:1073-1074(1993). RN [23] RP PHOSPHORYLATION AT SER-132 AND SER-176. RC TISSUE=Pituitary; RX PubMed=14997482; DOI=10.1002/pmic.200300584; RA Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.; RT "Identification and characterization of phosphorylated proteins in the RT human pituitary."; RL Proteomics 4:587-598(2004). RN [24] RP REVIEW. RX PubMed=10393484; DOI=10.1159/000053128; RA Baumann G.; RT "Growth hormone heterogeneity in human pituitary and plasma."; RL Horm. Res. 51 Suppl. 1:2-6(1999). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Pituitary; RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x; RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; RT "Phosphoproteomic analysis of the human pituitary."; RL Pituitary 9:109-120(2006). RN [26] RP 3D-STRUCTURE MODELING. RX PubMed=3447173; DOI=10.1002/prot.340020209; RA Cohen F.E., Kuntz I.D.; RT "Prediction of the three-dimensional structure of human growth RT hormone."; RL Proteins 2:162-166(1987). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=1549776; DOI=10.1126/science.1549776; RA de Vos A.M., Ultsch M., Kossiakoff A.A.; RT "Human growth hormone and extracellular domain of its receptor: RT crystal structure of the complex."; RL Science 255:306-312(1992). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RX PubMed=7984244; DOI=10.1038/372478a0; RA Somers W., Ultsch M., de Vos A.M., Kossiakoff A.A.; RT "The X-ray structure of a growth hormone-prolactin receptor complex."; RL Nature 372:478-481(1994). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RA Chantalat L., Chirgadze N.Y., Jones N., Korber F., Navaza J., RA Pavlovsk A.G., Wlodawer A.; RT "The crystal-structure of wild-type growth-hormone at 2.5-A RT resolution."; RL Protein Pept. Lett. 2:333-340(1995). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=8943276; DOI=10.1074/jbc.271.50.32197; RA Sundstroem M., Lundqvist T., Roedin J., Giebel L.B., Milligan D., RA Norstedt G.; RT "Crystal structure of an antagonist mutant of human growth hormone, RT G120R, in complex with its receptor at 2.9-A resolution."; RL J. Biol. Chem. 271:32197-32203(1996). RN [31] RP VARIANT KWKS CYS-103. RX PubMed=8552145; DOI=10.1056/NEJM199602153340704; RA Takahashi Y., Kaji H., Okimura Y., Goji K., Abe H., Chihara K.; RT "Short stature caused by a mutant growth hormone."; RL N. Engl. J. Med. 334:432-436(1996). RN [32] RP ERRATUM. RA Takahashi Y., Kaji H., Okimura Y., Goji K., Abe H., Chihara K.; RL N. Engl. J. Med. 334:1207-1207(1996). RN [33] RP VARIANT ALA-3, AND VARIANT IGHD2 HIS-209. RX PubMed=9152628; DOI=10.1507/endocrj.44.149; RA Miyata I., Cogan J.D., Prince M.A., Kamijo T., Ogawa M., RA Phillips J.A. III; RT "Detection of growth hormone gene defects by dideoxy fingerprinting RT (ddF)."; RL Endocr. J. 44:149-154(1997). RN [34] RP VARIANT KWKS GLY-138. RX PubMed=9276733; DOI=10.1172/JCI119627; RA Takahashi Y., Shirono H., Arisaka O., Takahashi K., Yagi T., Koga J., RA Kaji H., Okimura Y., Abe H., Tanaka T., Chihara K.; RT "Biologically inactive growth hormone caused by an amino acid RT substitution."; RL J. Clin. Invest. 100:1159-1165(1997). RN [35] RP VARIANT CYS-105. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [36] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). RN [37] RP VARIANT IGHD2 HIS-209. RX PubMed=11502836; DOI=10.1210/jcem.86.8.7723; RA Deladoey J., Stocker P., Mullis P.E.; RT "Autosomal dominant GH deficiency due to an Arg183His GH-1 gene RT mutation: clinical and molecular evidence of impaired regulated GH RT secretion."; RL J. Clin. Endocrinol. Metab. 86:3941-3947(2001). RN [38] RP VARIANTS IGHD1B PRO-16; ASN-37; CYS-42; ILE-53; ARG-67; ASP-73; RP PHE-97; LYS-100; LEU-117; CYS-134; ARG-134 AND ALA-201, AND VARIANTS RP ALA-3 AND ILE-136. RX PubMed=12655557; DOI=10.1002/humu.10168; RA Millar D.S., Lewis M.D., Horan M., Newsway V., Easter T.E., RA Gregory J.W., Fryklund L., Norin M., Crowne E.C., Davies S.J., RA Edwards P., Kirk J., Waldron K., Smith P.J., Phillips J.A. III, RA Scanlon M.F., Krawczak M., Cooper D.N., Procter A.M.; RT "Novel mutations of the growth hormone 1 (GH1) gene disclosed by RT modulation of the clinical selection criteria for individuals with RT short stature."; RL Hum. Mutat. 21:424-440(2003). RN [39] RP VARIANT SHORT STATURE MET-205, AND VARIANTS ALA-3 AND ILE-136. RX PubMed=15001589; DOI=10.1210/jc.2003-030652; RA Lewis M.D., Horan M., Millar D.S., Newsway V., Easter T.E., RA Fryklund L., Gregory J.W., Norin M., Del Valle C.-J., RA Lopez-Siguero J.P., Canete R., Lopez-Canti L.F., Diaz-Torrado N., RA Espino R., Ulied A., Scanlon M.F., Procter A.M., Cooper D.N.; RT "A novel dysfunctional growth hormone variant (Ile179Met) exhibits a RT decreased ability to activate the extracellular signal-regulated RT kinase pathway."; RL J. Clin. Endocrinol. Metab. 89:1068-1075(2004). RN [40] RP VARIANT SHORT STATURE SER-79, AND CHARACTERIZATION OF VARIANT SHORT RP STATURE SER-79. RX PubMed=15713716; DOI=10.1210/jc.2004-1838; RA Besson A., Salemi S., Deladoeey J., Vuissoz J.-M., Eble A., RA Bidlingmaier M., Buergi S., Honegger U., Flueck C., Mullis P.E.; RT "Short stature caused by a biologically inactive mutant growth hormone RT (GH-C53S)."; RL J. Clin. Endocrinol. Metab. 90:2493-2499(2005). RN [41] RP CHARACTERIZATION OF VARIANT KWKS CYS-103. RX PubMed=17519310; DOI=10.1210/jc.2006-2238; RA Petkovic V., Besson A., Thevis M., Lochmatter D., Eble A., Fluck C.E., RA Mullis P.E.; RT "Evaluation of the biological activity of a growth hormone (GH) mutant RT (R77C) and its impact on GH responsiveness and stature."; RL J. Clin. Endocrinol. Metab. 92:2893-2901(2007). CC -!- FUNCTION: Plays an important role in growth control. Its major CC role in stimulating body growth is to stimulate the liver and CC other tissues to secrete IGF-1. It stimulates both the CC differentiation and proliferation of myoblasts. It also stimulates CC amino acid uptake and protein synthesis in muscle and other CC tissues. CC -!- SUBUNIT: Monomer, dimer, trimer, tetramer and pentamer, disulfide- CC linked or non-covalently associated, in homopolymeric and CC heteropolymeric combinations. Can also form a complex either with CC GHBP or with the alpha2-macroglobulin complex. CC -!- INTERACTION: CC P10912:GHR; NbExp=3; IntAct=EBI-1026046, EBI-286316; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=22 kDa; CC IsoId=P01241-1; Sequence=Displayed; CC Name=2; Synonyms=20 kDa variant; CC IsoId=P01241-2; Sequence=VSP_006200; CC Name=3; CC IsoId=P01241-3; Sequence=VSP_006201; CC Name=4; CC IsoId=P01241-4; Sequence=VSP_006202; CC Name=5; CC IsoId=P01241-5; Sequence=VSP_045642; CC Note=No experimental confirmation available.; CC -!- DISEASE: Growth hormone deficiency, isolated, 1A (IGHD1A) CC [MIM:262400]: An autosomal recessive, severe deficiency of growth CC hormone leading to dwarfism. Patients often develop antibodies to CC administered growth hormone. {ECO:0000269|PubMed:8364549}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: Growth hormone deficiency, isolated, 1B (IGHD1B) CC [MIM:612781]: An autosomal recessive deficiency of growth hormone CC leading to short stature. Patients have low but detectable levels CC of growth hormone, significantly retarded bone age, and a positive CC response and immunologic tolerance to growth hormone therapy. CC {ECO:0000269|PubMed:12655557}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Kowarski syndrome (KWKS) [MIM:262650]: A syndrome CC clinically characterized by short stature associated with CC bioinactive growth hormone, normal or slightly increased growth CC hormone secretion, pathologically low insulin-like growth factor 1 CC levels, and normal catch-up growth on growth hormone replacement CC therapy. {ECO:0000269|PubMed:17519310, ECO:0000269|PubMed:8552145, CC ECO:0000269|PubMed:9276733}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Growth hormone deficiency, isolated, 2 (IGHD2) CC [MIM:173100]: An autosomal dominant deficiency of growth hormone CC leading to short stature. Clinical severity is variable. Patients CC have a positive response and immunologic tolerance to growth CC hormone therapy. {ECO:0000269|PubMed:11502836, CC ECO:0000269|PubMed:9152628}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- PHARMACEUTICAL: Available under the names Nutropin or Protropin CC (Genentech), Norditropin (Novo Nordisk), Genotropin (Pharmacia CC Upjohn), Humatrope (Eli Lilly) and Saizen or Serostim (Serono). CC Used for the treatment of growth hormone deficiency and for CC Turner's syndrome. CC -!- MISCELLANEOUS: Circulating GH shows a great heterogeneity due to CC alternative splicing, differential post-translational CC modifications of monomeric forms, oligomerization, optional CC binding to 2 different GH-binding proteins, and potentially CC proteolytic processing. CC -!- SIMILARITY: Belongs to the somatotropin/prolactin family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Growth hormone entry; CC URL="https://en.wikipedia.org/wiki/Growth_hormone"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; V00519; CAA23778.1; -; mRNA. DR EMBL; V00520; CAA23779.1; -; Genomic_DNA. DR EMBL; M13438; AAA98618.1; -; Genomic_DNA. DR EMBL; J03071; AAA52549.1; -; Genomic_DNA. DR EMBL; AF185611; AAG09699.1; -; mRNA. DR EMBL; AF110644; AAD48584.1; -; mRNA. DR EMBL; EU421712; ABZ88713.1; -; Genomic_DNA. DR EMBL; AC127029; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471109; EAW94233.1; -; Genomic_DNA. DR EMBL; BC062475; AAH62475.1; -; mRNA. DR EMBL; BC075012; AAH75012.1; -; mRNA. DR EMBL; BC075013; AAH75013.1; -; mRNA. DR EMBL; BC090045; AAH90045.1; -; mRNA. DR EMBL; CD106566; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M14398; AAA52554.1; -; mRNA. DR CCDS; CCDS11653.1; -. [P01241-1] DR CCDS; CCDS11654.1; -. [P01241-5] DR CCDS; CCDS45760.1; -. [P01241-2] DR PIR; A93731; STHU. DR RefSeq; NP_000506.2; NM_000515.4. [P01241-1] DR RefSeq; NP_072053.1; NM_022559.3. [P01241-2] DR RefSeq; NP_072054.1; NM_022560.3. [P01241-5] DR UniGene; Hs.655229; -. DR PDB; 1A22; X-ray; 2.60 A; A=27-217. DR PDB; 1AXI; X-ray; 2.10 A; A=27-217. DR PDB; 1BP3; X-ray; 2.90 A; A=27-217. DR PDB; 1HGU; X-ray; 2.50 A; A=27-217. DR PDB; 1HUW; X-ray; 2.00 A; A=27-217. DR PDB; 1HWG; X-ray; 2.50 A; A=27-217. DR PDB; 1HWH; X-ray; 2.90 A; A=27-217. DR PDB; 1KF9; X-ray; 2.60 A; A/D=27-217. DR PDB; 3HHR; X-ray; 2.80 A; A=27-216. DR PDBsum; 1A22; -. DR PDBsum; 1AXI; -. DR PDBsum; 1BP3; -. DR PDBsum; 1HGU; -. DR PDBsum; 1HUW; -. DR PDBsum; 1HWG; -. DR PDBsum; 1HWH; -. DR PDBsum; 1KF9; -. DR PDBsum; 3HHR; -. DR ProteinModelPortal; P01241; -. DR SMR; P01241; -. DR BioGrid; 108955; 6. DR DIP; DIP-1022N; -. DR IntAct; P01241; 4. DR STRING; 9606.ENSP00000312673; -. DR iPTMnet; P01241; -. DR PhosphoSitePlus; P01241; -. DR BioMuta; GH1; -. DR PaxDb; P01241; -. DR PeptideAtlas; P01241; -. DR PRIDE; P01241; -. DR ProteomicsDB; 51353; -. DR ProteomicsDB; 51354; -. [P01241-2] DR ProteomicsDB; 51355; -. [P01241-3] DR ProteomicsDB; 51356; -. [P01241-4] DR Ensembl; ENST00000323322; ENSP00000312673; ENSG00000259384. [P01241-1] DR Ensembl; ENST00000351388; ENSP00000343791; ENSG00000259384. [P01241-5] DR Ensembl; ENST00000458650; ENSP00000408486; ENSG00000259384. [P01241-2] DR GeneID; 2688; -. DR KEGG; hsa:2688; -. DR UCSC; uc002jdi.4; human. [P01241-1] DR CTD; 2688; -. DR DisGeNET; 2688; -. DR EuPathDB; HostDB:ENSG00000259384.6; -. DR GeneCards; GH1; -. DR HGNC; HGNC:4261; GH1. DR HPA; HPA043715; -. DR MalaCards; GH1; -. DR MIM; 139250; gene. DR MIM; 173100; phenotype. DR MIM; 262400; phenotype. DR MIM; 262650; phenotype. DR MIM; 612781; phenotype. DR neXtProt; NX_P01241; -. DR OpenTargets; ENSG00000259384; -. DR Orphanet; 231662; Isolated growth hormone deficiency type IA. DR Orphanet; 231671; Isolated growth hormone deficiency type IB. DR Orphanet; 231679; Isolated growth hormone deficiency type II. DR Orphanet; 629; Short stature due to growth hormone qualitative anomaly. DR PharmGKB; PA171; -. DR eggNOG; ENOG410IFR6; Eukaryota. DR eggNOG; ENOG4111HU8; LUCA. DR GeneTree; ENSGT00730000111012; -. DR HOGENOM; HOG000068443; -. DR HOVERGEN; HBG011318; -. DR InParanoid; P01241; -. DR KO; K05438; -. DR OMA; TYLRVMK; -. DR OrthoDB; 1190548at2759; -. DR PhylomeDB; P01241; -. DR TreeFam; TF332592; -. DR Reactome; R-HSA-1170546; Prolactin receptor signaling. DR Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin. DR Reactome; R-HSA-982772; Growth hormone receptor signaling. DR SABIO-RK; P01241; -. DR SignaLink; P01241; -. DR SIGNOR; P01241; -. DR ChiTaRS; GH1; human. DR EvolutionaryTrace; P01241; -. DR GenomeRNAi; 2688; -. DR PRO; PR:P01241; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; ENSG00000259384; Expressed in 94 organ(s), highest expression level in adenohypophysis. DR ExpressionAtlas; P01241; baseline and differential. DR Genevisible; P01241; HS. DR GO; GO:0031904; C:endosome lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0070195; C:growth hormone receptor complex; IDA:CAFA. DR GO; GO:0008083; F:growth factor activity; IPI:BHF-UCL. DR GO; GO:0005131; F:growth hormone receptor binding; IDA:MGI. DR GO; GO:0005179; F:hormone activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005148; F:prolactin receptor binding; IDA:AgBase. DR GO; GO:0048513; P:animal organ development; IBA:GO_Central. DR GO; GO:0070977; P:bone maturation; IDA:BHF-UCL. DR GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; TAS:Reactome. DR GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; IDA:BHF-UCL. DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IDA:MGI. DR GO; GO:0045927; P:positive regulation of growth; IBA:GO_Central. DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0043406; P:positive regulation of MAP kinase activity; TAS:BHF-UCL. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IDA:BHF-UCL. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL. DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL. DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:BHF-UCL. DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL. DR GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL. DR GO; GO:0031667; P:response to nutrient levels; IBA:GO_Central. DR InterPro; IPR009079; 4_helix_cytokine-like_core. DR InterPro; IPR001400; Somatotropin/Prolactin. DR InterPro; IPR018116; Somatotropin_CS. DR PANTHER; PTHR11417; PTHR11417; 1. DR Pfam; PF00103; Hormone_1; 1. DR PRINTS; PR00836; SOMATOTROPIN. DR SUPFAM; SSF47266; SSF47266; 1. DR PROSITE; PS00266; SOMATOTROPIN_1; 1. DR PROSITE; PS00338; SOMATOTROPIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disease mutation; Disulfide bond; Dwarfism; KW Hormone; Metal-binding; Pharmaceutical; Phosphoprotein; Polymorphism; KW Reference proteome; Secreted; Signal; Zinc. FT SIGNAL 1 26 {ECO:0000269|PubMed:5144027, FT ECO:0000269|PubMed:5279046, FT ECO:0000269|PubMed:5810834}. FT CHAIN 27 217 Somatotropin. FT /FTId=PRO_0000032988. FT METAL 44 44 Zinc. {ECO:0000250}. FT METAL 200 200 Zinc. {ECO:0000250}. FT MOD_RES 132 132 Phosphoserine. FT {ECO:0000269|PubMed:14997482}. FT MOD_RES 163 163 Deamidated glutamine; by deterioration. FT {ECO:0000269|PubMed:7028740}. FT MOD_RES 176 176 Phosphoserine. FT {ECO:0000269|PubMed:14997482}. FT MOD_RES 178 178 Deamidated asparagine; by deterioration. FT {ECO:0000269|PubMed:7028740}. FT DISULFID 79 191 {ECO:0000269|PubMed:5144027}. FT DISULFID 208 215 FT VAR_SEQ 58 97 Missing (in isoform 5). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_045642. FT VAR_SEQ 58 72 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_006200. FT VAR_SEQ 111 148 Missing (in isoform 3). FT {ECO:0000303|Ref.6}. FT /FTId=VSP_006201. FT VAR_SEQ 117 162 Missing (in isoform 4). FT {ECO:0000303|PubMed:10931946}. FT /FTId=VSP_006202. FT VARIANT 3 3 T -> A (found in patients with isolated FT growth hormone deficiency; FT dbSNP:rs2001345). FT {ECO:0000269|PubMed:12655557, FT ECO:0000269|PubMed:15001589, FT ECO:0000269|PubMed:9152628}. FT /FTId=VAR_011917. FT VARIANT 16 16 L -> P (in IGHD1B; suppresses secretion). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015801. FT VARIANT 37 37 D -> N (in IGHD1B). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015802. FT VARIANT 42 42 R -> C (in IGHD1B; reduced secretion; FT dbSNP:rs71640273). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015803. FT VARIANT 53 53 T -> I (in IGHD1B; reduced ability to FT activate the JAK/STAT pathway). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015804. FT VARIANT 67 67 K -> R (in IGHD1B; reduced ability to FT activate the JAK/STAT pathway). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015805. FT VARIANT 73 73 N -> D (in IGHD1B; reduced ability to FT activate the JAK/STAT pathway; FT dbSNP:rs71640276). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015806. FT VARIANT 79 79 C -> S (in short stature; idiopathic FT autosomal; affects binding affinity of GH FT for GHR and the potency of GH to activate FT the JAK2/STAT5 signaling pathway; FT dbSNP:rs137853222). FT {ECO:0000269|PubMed:15713716}. FT /FTId=VAR_032702. FT VARIANT 97 97 S -> F (in IGHD1B; reduced ability to FT activate the JAK/STAT pathway). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015807. FT VARIANT 100 100 E -> K (in IGHD1B). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015808. FT VARIANT 103 103 R -> C (in KWKS; no effect on GHR FT signaling pathway; does not affect FT interaction with GHR; results in a FT stronger interaction with GHBP; does not FT affect subcellular location; FT dbSNP:rs137853220). FT {ECO:0000269|PubMed:17519310, FT ECO:0000269|PubMed:8552145}. FT /FTId=VAR_015809. FT VARIANT 105 105 S -> C (in dbSNP:rs6174). FT {ECO:0000269|PubMed:10391209}. FT /FTId=VAR_011918. FT VARIANT 117 117 Q -> L (in IGHD1B; reduced secretion). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015810. FT VARIANT 134 134 S -> C (in IGHD1B). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015811. FT VARIANT 134 134 S -> R (in IGHD1B; reduced ability to FT activate the JAK/STAT pathway). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015812. FT VARIANT 136 136 V -> I (in dbSNP:rs5388). FT {ECO:0000269|PubMed:12655557, FT ECO:0000269|PubMed:15001589}. FT /FTId=VAR_011919. FT VARIANT 138 138 D -> G (in KWKS; loss of activity; FT dbSNP:rs137853221). FT {ECO:0000269|PubMed:9276733}. FT /FTId=VAR_015813. FT VARIANT 201 201 T -> A (in IGHD1B; reduced ability to FT activate the JAK/STAT pathway). FT {ECO:0000269|PubMed:12655557}. FT /FTId=VAR_015814. FT VARIANT 205 205 I -> M (in short stature; idiopathic FT autosomal; dbSNP:rs148474991). FT {ECO:0000269|PubMed:15001589}. FT /FTId=VAR_032703. FT VARIANT 209 209 R -> H (in IGHD2; dbSNP:rs137853223). FT {ECO:0000269|PubMed:11502836, FT ECO:0000269|PubMed:9152628}. FT /FTId=VAR_015815. FT CONFLICT 35 35 L -> P (in Ref. 1; CAA23778). FT {ECO:0000305}. FT CONFLICT 40 40 M -> S (in Ref. 3; CAA23779). FT {ECO:0000305}. FT HELIX 32 61 {ECO:0000244|PDB:1HUW}. FT HELIX 64 72 {ECO:0000244|PDB:1HUW}. FT HELIX 73 75 {ECO:0000244|PDB:1HGU}. FT TURN 80 83 {ECO:0000244|PDB:1HUW}. FT HELIX 90 94 {ECO:0000244|PDB:1HUW}. FT HELIX 98 110 {ECO:0000244|PDB:1HUW}. FT TURN 111 114 {ECO:0000244|PDB:1HUW}. FT HELIX 115 119 {ECO:0000244|PDB:1HUW}. FT HELIX 120 125 {ECO:0000244|PDB:1HUW}. FT TURN 129 133 {ECO:0000244|PDB:1HUW}. FT HELIX 136 154 {ECO:0000244|PDB:1HUW}. FT HELIX 163 166 {ECO:0000244|PDB:1AXI}. FT STRAND 178 180 {ECO:0000244|PDB:1HGU}. FT HELIX 182 209 {ECO:0000244|PDB:1HUW}. FT TURN 212 216 {ECO:0000244|PDB:1AXI}. SQ SEQUENCE 217 AA; 24847 MW; 72CC15AF4ED1C51A CRC64; MATGSRTSLL LAFGLLCLPW LQEGSAFPTI PLSRLFDNAM LRAHRLHQLA FDTYQEFEEA YIPKEQKYSF LQNPQTSLCF SESIPTPSNR EETQQKSNLE LLRISLLLIQ SWLEPVQFLR SVFANSLVYG ASDSNVYDLL KDLEEGIQTL MGRLEDGSPR TGQIFKQTYS KFDTNSHNDD ALLKNYGLLY CFRKDMDKVE TFLRIVQCRS VEGSCGF //