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P01241 (SOMA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Somatotropin
Alternative name(s):
Growth hormone
Short name=GH
Short name=GH-N
Growth hormone 1
Pituitary growth hormone
Gene names
Name:GH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secreted.

Involvement in disease

Growth hormone deficiency, isolated, 1A (IGHD1A) [MIM:262400]: An autosomal recessive, severe deficiency of growth hormone leading to dwarfism. Patients often develop antibodies to administered growth hormone.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22

Growth hormone deficiency, isolated, 1B (IGHD1B) [MIM:612781]: An autosomal recessive deficiency of growth hormone leading to short stature. Patients have low but detectable levels of growth hormone, significantly retarded bone age, and a positive response and immunologic tolerance to growth hormone therapy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38

Kowarski syndrome (KWKS) [MIM:262650]: A syndrome clinically characterized by short stature associated with bioinactive growth hormone, normal or slightly increased growth hormone secretion, pathologically low insulin-like growth factor 1 levels, and normal catch-up growth on growth hormone replacement therapy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31 Ref.34 Ref.41

Growth hormone deficiency, isolated, 2 (IGHD2) [MIM:173100]: An autosomal dominant deficiency of growth hormone leading to short stature. Clinical severity is variable. Patients have a positive response and immunologic tolerance to growth hormone therapy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33 Ref.37

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

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dwarfism
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHormone
   PTMDisulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Inferred from direct assay PubMed 8063815. Source: BHF-UCL

JAK-STAT cascade involved in growth hormone signaling pathway

Traceable author statement. Source: Reactome

bone maturation

Inferred from direct assay PubMed 20110402. Source: BHF-UCL

glucose transport

Inferred from direct assay PubMed 9144201. Source: MGI

growth hormone receptor signaling pathway

Inferred from direct assay PubMed 8063815. Source: BHF-UCL

positive regulation of JAK-STAT cascade

Inferred from direct assay PubMed 8923468. Source: BHF-UCL

positive regulation of MAP kinase activity

Traceable author statement PubMed 8063815. Source: BHF-UCL

positive regulation of activation of JAK2 kinase activity

Inferred from direct assay PubMed 12552091PubMed 8063815. Source: BHF-UCL

positive regulation of insulin-like growth factor receptor signaling pathway

Inferred from direct assay PubMed 7565946. Source: BHF-UCL

positive regulation of multicellular organism growth

Inferred from direct assay PubMed 20110402PubMed 7565946. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 7782332. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 7782332. Source: BHF-UCL

positive regulation of tyrosine phosphorylation of Stat3 protein

Inferred from direct assay PubMed 12552091PubMed 8923468. Source: BHF-UCL

positive regulation of tyrosine phosphorylation of Stat5 protein

Inferred from direct assay PubMed 12552091PubMed 8923468. Source: BHF-UCL

response to estradiol

Inferred from direct assay PubMed 12552091. Source: BHF-UCL

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 11549663. Source: BHF-UCL

   Molecular_functiongrowth factor activity

Inferred from physical interaction PubMed 9360546. Source: BHF-UCL

growth hormone receptor binding

Inferred from physical interaction Ref.27PubMed 2825030. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

prolactin receptor binding

Inferred from physical interaction Ref.28. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GHRP109123EBI-1026046,EBI-286316

Alternative products

This entry describes 5 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.
Isoform 5 (identifier: P01241-5)

The sequence of this isoform differs from the canonical sequence as follows:
     58-97: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.13 Ref.14 Ref.16 Ref.19
Chain27 – 217191Somatotropin
PRO_0000032988

Sites

Metal binding441Zinc By similarity
Metal binding2001Zinc By similarity

Amino acid modifications

Modified residue1321Phosphoserine Ref.23
Modified residue1631Deamidated glutamine; by deterioration Ref.21
Modified residue1761Phosphoserine Ref.23
Modified residue1781Deamidated asparagine; by deterioration Ref.21
Disulfide bond79 ↔ 191 Ref.14
Disulfide bond208 ↔ 215

Natural variations

Alternative sequence58 – 9740Missing in isoform 5.
VSP_045642
Alternative sequence58 – 7215Missing in isoform 2.
VSP_006200
Alternative sequence111 – 14838Missing in isoform 3.
VSP_006201
Alternative sequence117 – 16246Missing in isoform 4.
VSP_006202
Natural variant31T → A Found in patients with isolated growth hormone deficiency. Ref.33 Ref.38 Ref.39
Corresponds to variant rs2001345 [ dbSNP | Ensembl ].
VAR_011917
Natural variant161L → P in IGHD1B; suppresses secretion. Ref.38
VAR_015801
Natural variant371D → N in IGHD1B. Ref.38
VAR_015802
Natural variant421R → C in IGHD1B; reduced secretion. Ref.38
VAR_015803
Natural variant531T → I in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.38
VAR_015804
Natural variant671K → R in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.38
VAR_015805
Natural variant731N → D in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.38
VAR_015806
Natural variant791C → 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.40
VAR_032702
Natural variant971S → F in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.38
VAR_015807
Natural variant1001E → K in IGHD1B. Ref.38
VAR_015808
Natural variant1031R → 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.31 Ref.41
VAR_015809
Natural variant1051S → C. Ref.35
Corresponds to variant rs6174 [ dbSNP | Ensembl ].
VAR_011918
Natural variant1171Q → L in IGHD1B; reduced secretion. Ref.38
VAR_015810
Natural variant1341S → C in IGHD1B. Ref.38
VAR_015811
Natural variant1341S → R in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.38
VAR_015812
Natural variant1361V → I. Ref.38 Ref.39
Corresponds to variant rs5388 [ dbSNP | Ensembl ].
VAR_011919
Natural variant1381D → G in KWKS; loss of activity. Ref.34
VAR_015813
Natural variant2011T → A in IGHD1B; reduced ability to activate the JAK/STAT pathway. Ref.38
VAR_015814
Natural variant2051I → M in short stature; idiopathic autosomal. Ref.39
VAR_032703
Natural variant2091R → H in IGHD2. Ref.33 Ref.37
VAR_015815

Experimental info

Sequence conflict351L → P in CAA23778. Ref.1
Sequence conflict401M → S in CAA23779. Ref.3

Secondary structure

........................... 217
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (22 kDa) [UniParc].

Last modified March 1, 1992. Version 2.
Checksum: 72CC15AF4ED1C51A

FASTA21724,847
        10         20         30         40         50         60 
MATGSRTSLL LAFGLLCLPW LQEGSAFPTI PLSRLFDNAM LRAHRLHQLA FDTYQEFEEA 

        70         80         90        100        110        120 
YIPKEQKYSF LQNPQTSLCF SESIPTPSNR EETQQKSNLE LLRISLLLIQ SWLEPVQFLR 

       130        140        150        160        170        180 
SVFANSLVYG ASDSNVYDLL KDLEEGIQTL MGRLEDGSPR TGQIFKQTYS KFDTNSHNDD 

       190        200        210 
ALLKNYGLLY CFRKDMDKVE TFLRIVQCRS VEGSCGF 

« Hide

Isoform 2 (20 kDa variant) [UniParc].

Checksum: 65342A13E1856C5E
Show »

FASTA20222,992
Isoform 3 [UniParc].

Checksum: 0E875A91BE0B9B7E
Show »

FASTA17920,561
Isoform 4 [UniParc].

Checksum: 9FA9013991FA9F28
Show »

FASTA17119,802
Isoform 5 [UniParc].

Checksum: 399A85FF90C22721
Show »

FASTA17720,201

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]"Complex signatures of locus-specific selective pressures and gene conversion on human growth hormone/chorionic somatomammotropin genes."
Sedman L., Padhukasahasram B., Kelgo P., Laan M.
Hum. Mutat. 29:1181-1193(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Pituitary.
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5).
Tissue: Pituitary.
[12]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-26.
[13]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-217.
[14]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-217, SEQUENCE REVISION.
[15]"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] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[16]"Revised primary structure for human growth hormone."
Niall H.D.
Nature New Biol. 230:90-91(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-61 AND 102-124.
[17]"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] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 119-120 AND 157-159.
[18]"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.
[19]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-79 (ISOFORM 2).
[20]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 46-80 (ISOFORM 2).
[21]"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] [Europe PMC] [Abstract]
Cited for: DEAMIDATION AT GLN-163 AND ASN-178.
[22]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN IGHD1A.
[23]"Identification and characterization of phosphorylated proteins in the human pituitary."
Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.
Proteomics 4:587-598(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-132 AND SER-176.
Tissue: Pituitary.
[24]"Growth hormone heterogeneity in human pituitary and plasma."
Baumann G.
Horm. Res. 51 Suppl. 1:2-6(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[25]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary.
[26]"Prediction of the three-dimensional structure of human growth hormone."
Cohen F.E., Kuntz I.D.
Proteins 2:162-166(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[27]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[28]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[29]"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).
[30]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[31]"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] [Europe PMC] [Abstract]
Cited for: VARIANT KWKS CYS-103.
[32]Erratum
Takahashi Y., Kaji H., Okimura Y., Goji K., Abe H., Chihara K.
N. Engl. J. Med. 334:1207-1207(1996)
[33]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-3, VARIANT IGHD2 HIS-209.
[34]"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] [Europe PMC] [Abstract]
Cited for: VARIANT KWKS GLY-138.
[35]"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] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-105.
[36]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)
[37]"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] [Europe PMC] [Abstract]
Cited for: VARIANT IGHD2 HIS-209.
[38]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS IGHD1B 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, VARIANTS ALA-3 AND ILE-136.
[39]"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] [Europe PMC] [Abstract]
Cited for: VARIANT SHORT STATURE MET-205, VARIANTS ALA-3 AND ILE-136.
[40]"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] [Europe PMC] [Abstract]
Cited for: VARIANT SHORT STATURE SER-79, CHARACTERIZATION OF VARIANT SHORT STATURE SER-79.
[41]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT KWKS CYS-103.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Growth hormone entry

Cross-references

Sequence databases

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.
EU421712 Genomic DNA. Translation: ABZ88713.1.
AC127029 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94233.1.
BC062475 mRNA. Translation: AAH62475.1.
BC075012 mRNA. Translation: AAH75012.1.
BC075013 mRNA. Translation: AAH75013.1.
BC090045 mRNA. Translation: AAH90045.1.
CD106566 mRNA. No translation available.
M14398 mRNA. Translation: AAA52554.1.
PIRSTHU. A93731.
RefSeqNP_000506.2. NM_000515.3.
NP_072053.1. NM_022559.2.
NP_072054.1. NM_022560.2.
XP_005257275.1. XM_005257218.2.
XP_005257276.1. XM_005257219.2.
UniGeneHs.655229.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A22X-ray2.60A27-217[»]
1AXIX-ray2.10A27-217[»]
1BP3X-ray2.90A27-217[»]
1HGUX-ray2.50A27-217[»]
1HUWX-ray2.00A27-217[»]
1HWGX-ray2.50A27-217[»]
1HWHX-ray2.90A27-217[»]
1KF9X-ray2.60A/D27-217[»]
3HHRX-ray2.80A27-216[»]
ProteinModelPortalP01241.
SMRP01241. Positions 27-216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108955. 6 interactions.
DIPDIP-1022N.
IntActP01241. 3 interactions.
STRING9606.ENSP00000312673.

PTM databases

PhosphoSiteP01241.

Proteomic databases

PaxDbP01241.
PRIDEP01241.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323322; ENSP00000312673; ENSG00000259384. [P01241-1]
ENST00000351388; ENSP00000343791; ENSG00000259384. [P01241-5]
ENST00000458650; ENSP00000408486; ENSG00000259384. [P01241-2]
GeneID2688.
KEGGhsa:2688.
UCSCuc002jdj.3. human. [P01241-1]
uc002jdk.3. human.

Organism-specific databases

CTD2688.
GeneCardsGC17M061994.
HGNCHGNC:4261. GH1.
HPACAB025646.
HPA043715.
MIM139250. gene.
173100. phenotype.
262400. phenotype.
262650. phenotype.
612781. phenotype.
neXtProtNX_P01241.
Orphanet231662. Isolated growth hormone deficiency type IA.
231671. Isolated growth hormone deficiency type IB.
231679. Isolated growth hormone deficiency type II.
629. Short stature due to growth hormone qualitative anomaly.
PharmGKBPA171.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26152.
HOVERGENHBG011318.
InParanoidP01241.
KOK05438.
OMACRRFVES.
OrthoDBEOG7F7W9X.
PhylomeDBP01241.
TreeFamTF332592.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_6900. Immune System.
SignaLinkP01241.

Gene expression databases

ArrayExpressP01241.
BgeeP01241.
CleanExHS_GH1.
GenevestigatorP01241.

Family and domain databases

Gene3D1.20.1250.10. 1 hit.
InterProIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001400. Somatotropin.
IPR018116. Somatotropin_CS.
[Graphical view]
PANTHERPTHR11417. PTHR11417. 1 hit.
PfamPF00103. Hormone_1. 1 hit.
[Graphical view]
PRINTSPR00836. SOMATOTROPIN.
SUPFAMSSF47266. SSF47266. 1 hit.
PROSITEPS00266. SOMATOTROPIN_1. 1 hit.
PS00338. SOMATOTROPIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGH1. human.
EvolutionaryTraceP01241.
GenomeRNAi2688.
NextBio10614.
PROP01241.
SOURCESearch...

Entry information

Entry nameSOMA_HUMAN
AccessionPrimary (citable) accession number: P01241
Secondary accession number(s): A6NEF6 expand/collapse secondary AC list , Q14405, Q16631, Q5EB53, Q9HBZ1, Q9UMJ7, Q9UNL5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM