P01241 (SOMA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names 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

Name:

GH1

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	Secreted.
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

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Dwarfism
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hormone
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological process	JAK-STAT cascade Inferred from direct assay. Source: BHF-UCL bone maturation Inferred from direct assay. Source: BHF-UCL glucose transport Inferred from direct assay. Source: MGI growth hormone receptor signaling pathway Inferred from direct assay. Source: BHF-UCL positive regulation of MAP kinase activity Traceable author statement. Source: BHF-UCL positive regulation of activation of JAK2 kinase activity Inferred from direct assay. Source: BHF-UCL positive regulation of insulin-like growth factor receptor signaling pathway Inferred from direct assay. Source: BHF-UCL positive regulation of multicellular organism growth Inferred from direct assay. Source: BHF-UCL positive regulation of phosphatidylinositol 3-kinase cascade Inferred from direct assay. Source: BHF-UCL positive regulation of tyrosine phosphorylation of Stat3 protein Inferred from direct assay. Source: BHF-UCL positive regulation of tyrosine phosphorylation of Stat5 protein Inferred from direct assay. Source: BHF-UCL response to estradiol stimulus Inferred from direct assay. Source: BHF-UCL
Cellular component	extracellular space Inferred from direct assay. Source: BHF-UCL
Molecular function	growth factor activity Inferred from physical interaction. Source: BHF-UCL growth hormone receptor binding Inferred from physical interaction Ref.24. Source: BHF-UCL hormone activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW prolactin receptor binding Inferred from physical interaction Ref.25. Source: BHF-UCL
Complete GO annotation...

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

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

217

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	Isoform 1 (22 kDa) [UniParc]. Last modified March 1, 1992. Version 2. Checksum: 72CC15AF4ED1C51A	FASTA	217	24,847
	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
	Isoform 2 (20 kDa variant) [UniParc]. Checksum: 65342A13E1856C5E	FASTA	202	22,992
	10 20 30 40 50 60 MATGSRTSLL LAFGLLCLPW LQEGSAFPTI PLSRLFDNAM LRAHRLHQLA FDTYQEFNPQ 70 80 90 100 110 120 TSLCFSESIP TPSNREETQQ KSNLELLRIS LLLIQSWLEP VQFLRSVFAN SLVYGASDSN 130 140 150 160 170 180 VYDLLKDLEE GIQTLMGRLE DGSPRTGQIF KQTYSKFDTN SHNDDALLKN YGLLYCFRKD 190 200 MDKVETFLRI VQCRSVEGSC GF
	Isoform 3 [UniParc]. Checksum: 0E875A91BE0B9B7E	FASTA	179	20,561
	10 20 30 40 50 60 MATGSRTSLL LAFGLLCLPW LQEGSAFPTI PLSRLFDNAM LRAHRLHQLA FDTYQEFEEA 70 80 90 100 110 120 YIPKEQKYSF LQNPQTSLCF SESIPTPSNR EETQQKSNLE LLRISLLLIQ TLMGRLEDGS 130 140 150 160 170 PRTGQIFKQT YSKFDTNSHN DDALLKNYGL LYCFRKDMDK VETFLRIVQC RSVEGSCGF
	Isoform 4 [UniParc]. Checksum: 9FA9013991FA9F28	FASTA	171	19,802
	10 20 30 40 50 60 MATGSRTSLL LAFGLLCLPW LQEGSAFPTI PLSRLFDNAM LRAHRLHQLA FDTYQEFEEA 70 80 90 100 110 120 YIPKEQKYSF LQNPQTSLCF SESIPTPSNR EETQQKSNLE LLRISLLLIQ SWLEPVQIFK 130 140 150 160 170 QTYSKFDTNS HNDDALLKNY GLLYCFRKDM DKVETFLRIV QCRSVEGSCG F

References

	« Hide 'large scale' referencesShow '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. , 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: 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

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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A22	X-ray	2.60	A	27-217	[»]
1AXI	X-ray	2.10	A	27-217	[»]
1BP3	X-ray	2.90	A	27-217	[»]
1HGU	X-ray	2.50	A	27-217	[»]
1HUW	X-ray	2.00	A	27-217	[»]
1HWG	X-ray	2.50	A	27-217	[»]
1HWH	X-ray	2.90	A	27-217	[»]
1KF9	X-ray	2.60	A/D	27-217	[»]
3HHR	X-ray	2.80	A	27-216	[»]

ProteinModelPortal

P01241.

SMR

P01241. Positions 27-216.

ModBase

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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

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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

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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

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Other

NextBio

10614.

SOURCE

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Entry information

Entry name

SOMA_HUMAN

Accession

Primary (citable) accession number: P01241
Secondary accession number(s): Q14405 , Q16631, Q5EB53, Q9HBZ1, Q9UMJ7, Q9UNL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 1, 1992
Last modified:	January 25, 2012
This is version 153 of the entry and version 2 of the sequence. [Complete 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.