P01241 (SOMA_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 153.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Somatotropin Alternative name(s): Growth hormone Short name=GH Short name=GH-N Growth hormone 1 Pituitary growth hormone | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 217 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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. |
| Subunit structure | Monomer, dimer, trimer, tetramer and pentamer, disulfide-linked or non-covalently associated, in homopolymeric and heteropolymeric combinations. Can also form a complex either with GHBP or with the alpha2-macroglobulin complex. |
| Subcellular location | |
| Involvement in disease | Defects in GH1 are a cause of growth hormone deficiency isolated type 1A (IGHD1A) [MIM:262400]; also known as pituitary dwarfism I. IGHD1A is an autosomal recessive deficiency of GH which causes short stature. IGHD1A patients have an absence of GH with severe dwarfism and often develop anti-GH antibodies when given exogenous GH. Ref.19 Defects in GH1 are a cause of growth hormone deficiency isolated type 1B (IGHD1B) [MIM:612781]; also known as dwarfism of Sindh. IGHD1B is an autosomal recessive deficiency of GH which causes short stature. IGHD1B patients have low but detectable levels of GH. Dwarfism is less severe than in IGHD1A and patients usually respond well to exogenous GH. Defects in GH1 are the cause of Kowarski syndrome (KWKS) [MIM:262650]; also known as pituitary dwarfism VI. Ref.28 Ref.31 Ref.38 Defects in GH1 are a cause of growth hormone deficiency isolated type 2 (IGHD2) [MIM:173100]. IGHD2 is an autosomal dominant deficiency of GH which causes short stature. Clinical severity is variable. Patients have a positive response and immunologic tolerance to growth hormone therapy. |
| Pharmaceutical use | Available under the names Nutropin or Protropin (Genentech), Norditropin (Novo Nordisk), Genotropin (Pharmacia Upjohn), Humatrope (Eli Lilly) and Saizen or Serostim (Serono). Used for the treatment of growth hormone deficiency and for Turner's syndrome. |
| Miscellaneous | Circulating GH shows a great heterogeneity due to alternative splicing, differential post-translational modifications of monomeric forms, oligomerization, optional binding to 2 different GH-binding proteins, and potentially proteolytic processing. |
| Sequence similarities | Belongs to the somatotropin/prolactin family. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| GHR | P10912 | 3 | EBI-1026046,EBI-286316 |
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1 (identifier: P01241-1) Also known as: 22 kDa; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: P01241-2) Also known as: 20 kDa variant; The sequence of this isoform differs from the canonical sequence as follows: 58-72: Missing. | ||||||
| Isoform 3 (identifier: P01241-3) The sequence of this isoform differs from the canonical sequence as follows: 111-148: Missing. | ||||||
| Isoform 4 (identifier: P01241-4) The sequence of this isoform differs from the canonical sequence as follows: 117-162: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 26 | 26 | Ref.10 Ref.11 Ref.13 Ref.16 | |||||||||||||||||||||||||||
| Chain | 27 – 217 | 191 | Somatotropin | PRO_0000032988 | ||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||
| Metal binding | 44 | 1 | Zinc By similarity | |||||||||||||||||||||||||||
| Metal binding | 200 | 1 | Zinc By similarity | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Modified residue | 132 | 1 | Phosphoserine Ref.20 Ref.22 | |||||||||||||||||||||||||||
| Modified residue | 163 | 1 | Deamidated glutamine; by deterioration Ref.18 | |||||||||||||||||||||||||||
| Modified residue | 176 | 1 | Phosphoserine Ref.20 Ref.22 | |||||||||||||||||||||||||||
| Modified residue | 178 | 1 | Deamidated asparagine; by deterioration Ref.18 | |||||||||||||||||||||||||||
| Disulfide bond | 79 ↔ 191 | Ref.11 | ||||||||||||||||||||||||||||
| Disulfide bond | 208 ↔ 215 | |||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||
| Alternative sequence | 58 – 72 | 15 | Missing in isoform 2. | VSP_006200 | ||||||||||||||||||||||||||
| Alternative sequence | 111 – 148 | 38 | Missing in isoform 3. | VSP_006201 | ||||||||||||||||||||||||||
| Alternative sequence | 117 – 162 | 46 | Missing in isoform 4. | VSP_006202 | ||||||||||||||||||||||||||
| Natural variant | 3 | 1 | T → A in IGHD1B; could be a neutral polymorphism. Ref.30 Ref.35 Ref.36 Corresponds to variant rs2001345 [ dbSNP | Ensembl ]. | VAR_011917 | ||||||||||||||||||||||||||
| Natural variant | 16 | 1 | L → P in IGHD1B; suppresses secretion. Ref.35 | VAR_015801 | ||||||||||||||||||||||||||
| Natural variant | 37 | 1 | D → N in IGHD1B. Ref.35 | VAR_015802 | ||||||||||||||||||||||||||
| Natural variant | 42 | 1 | R → C in IGHD1B; reduced secretion. Ref.35 | VAR_015803 | ||||||||||||||||||||||||||
| Natural variant | 53 | 1 | T → I in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.35 | VAR_015804 | ||||||||||||||||||||||||||
| Natural variant | 67 | 1 | K → R in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.35 | VAR_015805 | ||||||||||||||||||||||||||
| Natural variant | 73 | 1 | N → D in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.35 | VAR_015806 | ||||||||||||||||||||||||||
| Natural variant | 79 | 1 | C → S in short stature; idiopathic autosomal; affects binding affinity of GH for GHR and the potency of GH to activate the JAK2/STAT5 signaling pathway. Ref.37 | VAR_032702 | ||||||||||||||||||||||||||
| Natural variant | 97 | 1 | S → F in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.35 | VAR_015807 | ||||||||||||||||||||||||||
| Natural variant | 100 | 1 | E → K in IGHD1B. Ref.35 | VAR_015808 | ||||||||||||||||||||||||||
| Natural variant | 103 | 1 | R → C in KWKS; loss of activity; no difference in the binding affinity or bioactivity between wild-type and mutant; no difference found in the extent of subcellular localization within endoplasmic reticulum Golgi or secretory vesicles between wild-type and mutant; reduced capability of the mutant to induce GHR/GHBP gene transcription rate when compared to wild-type. Ref.28 Ref.38 | VAR_015809 | ||||||||||||||||||||||||||
| Natural variant | 105 | 1 | S → C. Ref.32 Corresponds to variant rs6174 [ dbSNP | Ensembl ]. | VAR_011918 | ||||||||||||||||||||||||||
| Natural variant | 117 | 1 | Q → L in IGHD1B; reduced secretion. Ref.35 | VAR_015810 | ||||||||||||||||||||||||||
| Natural variant | 134 | 1 | S → C in IGHD1B. Ref.35 | VAR_015811 | ||||||||||||||||||||||||||
| Natural variant | 134 | 1 | S → R in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.35 | VAR_015812 | ||||||||||||||||||||||||||
| Natural variant | 136 | 1 | V → I. Ref.35 Ref.36 Corresponds to variant rs5388 [ dbSNP | Ensembl ]. | VAR_011919 | ||||||||||||||||||||||||||
| Natural variant | 138 | 1 | D → G in KWKS; loss of activity. Ref.31 | VAR_015813 | ||||||||||||||||||||||||||
| Natural variant | 201 | 1 | T → A in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.35 | VAR_015814 | ||||||||||||||||||||||||||
| Natural variant | 205 | 1 | I → M in short stature; idiopathic autosomal. Ref.36 | VAR_032703 | ||||||||||||||||||||||||||
| Natural variant | 209 | 1 | R → H in IGHD2. Ref.30 Ref.34 | VAR_015815 | ||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||
| Sequence conflict | 35 | 1 | L → P in CAA23778. Ref.1 | |||||||||||||||||||||||||||
| Sequence conflict | 40 | 1 | M → S in CAA23779. Ref.3 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Helix | 33 – 61 | 29 | ||||||||||||||||||||||||||||
| Helix | 64 – 72 | 9 | ||||||||||||||||||||||||||||
| Helix | 80 – 83 | 4 | ||||||||||||||||||||||||||||
| Helix | 90 – 94 | 5 | ||||||||||||||||||||||||||||
| Helix | 98 – 112 | 15 | ||||||||||||||||||||||||||||
| Helix | 115 – 119 | 5 | ||||||||||||||||||||||||||||
| Helix | 120 – 125 | 6 | ||||||||||||||||||||||||||||
| Helix | 133 – 153 | 21 | ||||||||||||||||||||||||||||
| Helix | 163 – 166 | 4 | ||||||||||||||||||||||||||||
| Helix | 182 – 210 | 29 | ||||||||||||||||||||||||||||
| Turn | 212 – 216 | 5 | ||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning and nucleotide sequence of the human growth hormone structural gene." Roskam W., Rougeon F. Nucleic Acids Res. 7:305-320(1979) [PubMed: 386281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [2] | "Human growth hormone: complementary DNA cloning and expression in bacteria." Martial J.A., Hallewell R.A., Baxter J.D., Goodman H.M. Science 205:602-607(1979) [PubMed: 377496] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [3] | "Human growth hormone DNA sequence and mRNA structure: possible alternative splicing." Denoto F.M., Moore D.D., Goodman H.M. Nucleic Acids Res. 9:3719-3730(1981) [PubMed: 6269091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), POSSIBLE ALTERNATIVE SPLICING. |
| [4] | "The human growth hormone gene family: nucleotide sequences show recent divergence and predict a new polypeptide hormone." Seeburg P.H. DNA 1:239-249(1982) [PubMed: 7169009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [5] | "The human growth hormone locus: nucleotide sequence, biology, and evolution." Chen E.Y., Liao Y.C., Smith D.H., Barrera-Saldana H.A., Gelinas R.E., Seeburg P.H. Genomics 4:479-497(1989) [PubMed: 2744760] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [6] | "A novel gene expressed in human pituitary." Gu J., Huang Q.-H., Li N., Xu S.-H., Han Z.-G., Fu G., Chen Z. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Pituitary. |
| [7] | "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. Chen J.-L.Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Pituitary. |
| [8] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Pituitary. |
| [9] | "Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable." Gray G.L., Baldridge J.S., McKeown K.S., Heyneker H.L., Chang C.N. Gene 39:247-254(1985) [PubMed: 3912261] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-26. |
| [10] | "Human pituitary growth hormone. XIX. The primary structure of the hormone." Li C.H., Dixon J.S., Liu W.-K. Arch. Biochem. Biophys. 133:70-91(1969) [PubMed: 5810834] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-217. |
| [11] | "Human pituitary growth hormone. 32. The primary structure of the hormone: revision." Li C.H., Dixon J.S. Arch. Biochem. Biophys. 146:233-236(1971) [PubMed: 5144027] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-217, SEQUENCE REVISION. |
| [12] | "Sequence comparison of human pituitary growth hormone, human chorionic somatomammotropin, and ovine pituitary growth and lactogenic hormones." Bewley T.A., Dixon J.S., Li C.H. Int. J. Pept. Protein Res. 4:281-287(1972) [PubMed: 4675454] [Abstract] Cited for: SEQUENCE REVISION. |
| [13] | "Revised primary structure for human growth hormone." Niall H.D. Nature New Biol. 230:90-91(1971) [PubMed: 5279046] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-61 AND 102-124. |
| [14] | "Sequences of pituitary and placental lactogenic and growth hormones: evolution from a primordial peptide by gene reduplication." Niall H.D., Hogan M.L., Sauer R., Rosenblum I.Y., Greenwood F.C. Proc. Natl. Acad. Sci. U.S.A. 68:866-869(1971) [PubMed: 5279528] [Abstract] Cited for: SEQUENCE REVISION TO 119-120 AND 157-159. |
| [15] | "The chemistry of the human lactogenic hormones." Niall H.D. (In) Griffiths K. (eds.); Prolactin and carcinogenesis, Proc. fourth tenovus workshop prolactin, pp.13-20, Alpha Omega Alpha Press, Cardiff (1972) Cited for: SEQUENCE REVISION. |
| [16] | "The 20,000 molecular weight variant of human growth hormone. Preparation and some physical and chemical properties." Chapman G.E., Rogers K.M., Brittain T., Bradshaw R.A., Bates O.J., Turner C., Cary P.D., Crane-Robinson C. J. Biol. Chem. 256:2395-2401(1981) [PubMed: 7462247] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-79 (ISOFORM 2). |
| [17] | "The 20,000-dalton variant of human growth hormone: location of the amino acid deletions." Lewis U.J., Bonewald L.F., Lewis L.J. Biochem. Biophys. Res. Commun. 92:511-516(1980) [PubMed: 7356479] [Abstract] Cited for: PROTEIN SEQUENCE OF 46-80 (ISOFORM 2). |
| [18] | "Altered proteolytic cleavage of human growth hormone as a result of deamidation." Lewis U.J., Singh R.N., Bonewald L.F., Seavey B.K. J. Biol. Chem. 256:11645-11650(1981) [PubMed: 7028740] [Abstract] Cited for: DEAMIDATION AT GLN-163 AND ASN-178. |
| [19] | "A new mutation causing inherited growth hormone deficiency: a compound heterozygote of a 6.7 kb deletion and a two base deletion in the third exon of the GH-1 gene." Igarashi Y., Ogawa M., Kamijo T., Iwatani N., Nishi Y., Kohno H., Masumura T., Koga J. Hum. Mol. Genet. 2:1073-1074(1993) [PubMed: 8364549] [Abstract] Cited for: INVOLVEMENT IN IGHD1A. |
| [20] | "Identification and characterization of phosphorylated proteins in the human pituitary." Giorgianni F., Beranova-Giorgianni S., Desiderio D.M. Proteomics 4:587-598(2004) [PubMed: 14997482] [Abstract] Cited for: PHOSPHORYLATION AT SER-132 AND SER-176. Tissue: Pituitary. |
| [21] | "Growth hormone heterogeneity in human pituitary and plasma." Baumann G. Horm. Res. 51 Suppl. 1:2-6(1999) [PubMed: 10393484] [Abstract] Cited for: REVIEW. |
| [22] | "Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-176, MASS SPECTROMETRY. Tissue: Pituitary. |
| [23] | "Prediction of the three-dimensional structure of human growth hormone." Cohen F.E., Kuntz I.D. Proteins 2:162-166(1987) [PubMed: 3447173] [Abstract] Cited for: 3D-STRUCTURE MODELING. |
| [24] | "Human growth hormone and extracellular domain of its receptor: crystal structure of the complex." de Vos A.M., Ultsch M., Kossiakoff A.A. Science 255:306-312(1992) [PubMed: 1549776] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). |
| [25] | "The X-ray structure of a growth hormone-prolactin receptor complex." Somers W., Ultsch M., de Vos A.M., Kossiakoff A.A. Nature 372:478-481(1994) [PubMed: 7984244] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). |
| [26] | "The crystal-structure of wild-type growth-hormone at 2.5-A resolution." Chantalat L., Chirgadze N.Y., Jones N., Korber F., Navaza J., Pavlovsk A.G., Wlodawer A. Protein Pept. Lett. 2:333-340(1995) Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). |
| [27] | "Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9-A resolution." Sundstroem M., Lundqvist T., Roedin J., Giebel L.B., Milligan D., Norstedt G. J. Biol. Chem. 271:32197-32203(1996) [PubMed: 8943276] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). |
| [28] | "Short stature caused by a mutant growth hormone." Takahashi Y., Kaji H., Okimura Y., Goji K., Abe H., Chihara K. N. Engl. J. Med. 334:432-436(1996) [PubMed: 8552145] [Abstract] Cited for: VARIANT KWKS CYS-103. |
| [29] | Erratum Takahashi Y., Kaji H., Okimura Y., Goji K., Abe H., Chihara K. N. Engl. J. Med. 334:1207-1207(1996) |
| [30] | "Detection of growth hormone gene defects by dideoxy fingerprinting (ddF)." Miyata I., Cogan J.D., Prince M.A., Kamijo T., Ogawa M., Phillips J.A. III Endocr. J. 44:149-154(1997) [PubMed: 9152628] [Abstract] Cited for: VARIANT IGHD1B ALA-3, VARIANT IGHD2 HIS-209. |
| [31] | "Biologically inactive growth hormone caused by an amino acid substitution." Takahashi Y., Shirono H., Arisaka O., Takahashi K., Yagi T., Koga J., Kaji H., Okimura Y., Abe H., Tanaka T., Chihara K. J. Clin. Invest. 100:1159-1165(1997) [PubMed: 9276733] [Abstract] Cited for: VARIANT KWKS GLY-138. |
| [32] | "Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed: 10391209] [Abstract] Cited for: VARIANT CYS-105. |
| [33] | Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999) |
| [34] | "Autosomal dominant GH deficiency due to an Arg183His GH-1 gene mutation: clinical and molecular evidence of impaired regulated GH secretion." Deladoey J., Stocker P., Mullis P.E. J. Clin. Endocrinol. Metab. 86:3941-3947(2001) [PubMed: 11502836] [Abstract] Cited for: VARIANT IGHD2 HIS-209. |
| [35] | "Novel mutations of the growth hormone 1 (GH1) gene disclosed by modulation of the clinical selection criteria for individuals with short stature." Millar D.S., Lewis M.D., Horan M., Newsway V., Easter T.E., Gregory J.W., Fryklund L., Norin M., Crowne E.C., Davies S.J., Edwards P., Kirk J., Waldron K., Smith P.J., Phillips J.A. III, Scanlon M.F., Krawczak M., Cooper D.N., Procter A.M. Hum. Mutat. 21:424-440(2003) [PubMed: 12655557] [Abstract] Cited for: VARIANTS IGHD1B ALA-3; PRO-16; ASN-37; CYS-42; ILE-53; ARG-67; ASP-73; PHE-97; LYS-100; LEU-117; CYS-134; ARG-134 AND ALA-201, VARIANT ILE-136. |
| [36] | "A novel dysfunctional growth hormone variant (Ile179Met) exhibits a decreased ability to activate the extracellular signal-regulated kinase pathway." Lewis M.D., Horan M., Millar D.S., Newsway V., Easter T.E., Fryklund L., Gregory J.W., Norin M., Del Valle C.-J., Lopez-Siguero J.P., Canete R., Lopez-Canti L.F., Diaz-Torrado N., Espino R., Ulied A., Scanlon M.F., Procter A.M., Cooper D.N. J. Clin. Endocrinol. Metab. 89:1068-1075(2004) [PubMed: 15001589] [Abstract] Cited for: VARIANT SHORT STATURE MET-205, VARIANTS ALA-3 AND ILE-136. |
| [37] | "Short stature caused by a biologically inactive mutant growth hormone (GH-C53S)." Besson A., Salemi S., Deladoeey J., Vuissoz J.-M., Eble A., Bidlingmaier M., Buergi S., Honegger U., Flueck C., Mullis P.E. J. Clin. Endocrinol. Metab. 90:2493-2499(2005) [PubMed: 15713716] [Abstract] Cited for: VARIANT SHORT STATURE SER-79, CHARACTERIZATION OF VARIANT SHORT STATURE SER-79. |
| [38] | "Evaluation of the biological activity of a growth hormone (GH) mutant (R77C) and its impact on GH responsiveness and stature." Petkovic V., Besson A., Thevis M., Lochmatter D., Eble A., Fluck C.E., Mullis P.E. J. Clin. Endocrinol. Metab. 92:2893-2901(2007) [PubMed: 17519310] [Abstract] Cited for: CHARACTERIZATION OF VARIANT KWKS CYS-103. |
| + | Additional computationally mapped references. |
Web resources
| GeneReviews |
| Wikipedia Growth hormone entry |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| EMBL GenBank DDBJ | V00519 mRNA. Translation: CAA23778.1. V00520 Genomic DNA. Translation: CAA23779.1. M13438 Genomic DNA. Translation: AAA98618.1. J03071 Genomic DNA. Translation: AAA52549.1. AF185611 mRNA. Translation: AAG09699.1. AF110644 mRNA. Translation: AAD48584.1. BC062475 mRNA. Translation: AAH62475.1. BC075012 mRNA. Translation: AAH75012.1. BC075013 mRNA. Translation: AAH75013.1. BC090045 mRNA. Translation: AAH90045.1. M14398 mRNA. Translation: AAA52554.1. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| IPI | IPI00000889. IPI00218282. IPI00218283. IPI00218284. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PIR | STHU. A93731. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| RefSeq | NP_000506.2. NM_000515.3. NP_072053.1. NM_022559.2. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| UniGene | Hs.655229. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P01241. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| SMR | P01241. Positions 27-216. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| DIP | DIP-1022N. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| IntAct | P01241. 3 interactions. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| STRING | P01241. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PhosphoSite | P01241. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Polymorphism databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| DMDM | 134703. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PRIDE | P01241. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Ensembl | ENST00000323322; ENSP00000312673; ENSG00000189162. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GeneID | 2688. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| KEGG | hsa:2688. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| UCSC | uc002jdi.1. human. uc002jdj.1. human. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| CTD | 2688. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GeneCards | GC17M061994. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HGNC | HGNC:4261. GH1. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HPA | CAB025646. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| MIM | 139250. gene. 173100. phenotype. 262400. phenotype. 262650. phenotype. 612781. phenotype. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| neXtProt | NX_P01241. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Orphanet | 231662. Isolated growth hormone deficiency type IA. 231679. Isolated growth hormone deficiency type II. 629. Short stature due to growth hormone qualitative anomaly. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| eggNOG | prNOG10755. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HOVERGEN | HBG011318. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| InParanoid | P01241. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PhylomeDB | P01241. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reactome | REACT_6900. Immune System. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ArrayExpress | P01241. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Bgee | P01241. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| CleanEx | HS_GH1. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Genevestigator | P01241. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GermOnline | ENSG00000189162. Homo sapiens. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| InterPro | IPR009079. 4_helix_cytokine-like_core. IPR012351. 4_helix_cytokine_core. IPR001400. Somatotropin. IPR018116. Somatotropin_CS. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Gene3D | G3DSA:1.20.1250.10. 4_helix_cytokine_core. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| KO | K05438. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PANTHER | PTHR11417. Somatotropin. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Pfam | PF00103. Hormone_1. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PRINTS | PR00836. SOMATOTROPIN. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| SUPFAM | SSF47266. 4_helix_cytokine. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PROSITE | PS00266. SOMATOTROPIN_1. 1 hit. PS00338. SOMATOTROPIN_2. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Other | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| NextBio | 10614. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Entry information
| Entry name | SOMA_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P01241 Secondary accession number(s): Q14405 Q9UNL5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 17 Human chromosome 17: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with