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Protein

Somatotropin

Gene

GH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441ZincBy similarity
Metal bindingi200 – 2001ZincBy similarity

GO - Molecular functioni

  • growth factor activity Source: BHF-UCL
  • growth hormone receptor binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • prolactin receptor binding Source: AgBase

GO - Biological processi

  • bone maturation Source: BHF-UCL
  • glucose transport Source: MGI
  • growth hormone receptor signaling pathway Source: BHF-UCL
  • JAK-STAT cascade Source: BHF-UCL
  • JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
  • positive regulation of activation of JAK2 kinase activity Source: BHF-UCL
  • positive regulation of insulin-like growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of JAK-STAT cascade Source: BHF-UCL
  • positive regulation of MAP kinase activity Source: BHF-UCL
  • positive regulation of multicellular organism growth Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of Stat5 protein Source: BHF-UCL
  • response to estradiol Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_111133. Growth hormone receptor signaling.
REACT_115697. Prolactin receptor signaling.
REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
SignaLinkiP01241.

Names & Taxonomyi

Protein namesi
Recommended name:
Somatotropin
Alternative name(s):
Growth hormone
Short name:
GH
Short name:
GH-N
Growth hormone 1
Pituitary growth hormone
Gene namesi
Name:GH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:4261. GH1.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • intracellular Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Growth hormone deficiency, isolated, 1A (IGHD1A)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive, severe deficiency of growth hormone leading to dwarfism. Patients often develop antibodies to administered growth hormone.

See also OMIM:262400
Growth hormone deficiency, isolated, 1B (IGHD1B)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:612781
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161L → P in IGHD1B; suppresses secretion. 1 Publication
VAR_015801
Natural varianti37 – 371D → N in IGHD1B. 1 Publication
VAR_015802
Natural varianti42 – 421R → C in IGHD1B; reduced secretion. 1 Publication
VAR_015803
Natural varianti53 – 531T → I in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015804
Natural varianti67 – 671K → R in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015805
Natural varianti73 – 731N → D in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015806
Natural varianti97 – 971S → F in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015807
Natural varianti100 – 1001E → K in IGHD1B. 1 Publication
VAR_015808
Natural varianti117 – 1171Q → L in IGHD1B; reduced secretion. 1 Publication
VAR_015810
Natural varianti134 – 1341S → C in IGHD1B. 1 Publication
VAR_015811
Natural varianti134 – 1341S → R in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015812
Natural varianti201 – 2011T → A in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015814
Kowarski syndrome (KWKS)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:262650
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031R → C in KWKS; the mutant fails to induce GHR signaling pathway; does not affect interaction with GHR; results in a stronger interaction with GHBP; does not affect subcellular location. 2 Publications
VAR_015809
Natural varianti138 – 1381D → G in KWKS; loss of activity. 1 Publication
VAR_015813
Growth hormone deficiency, isolated, 2 (IGHD2)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:173100
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091R → H in IGHD2. 2 Publications
VAR_015815

Pharmaceutical usei

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.

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi173100. phenotype.
262400. phenotype.
262650. phenotype.
612781. phenotype.
Orphaneti231662. 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.
PharmGKBiPA171.

Polymorphism and mutation databases

BioMutaiGH1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26263 PublicationsAdd
BLAST
Chaini27 – 217191SomatotropinPRO_0000032988Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi79 ↔ 1911 Publication
Modified residuei132 – 1321Phosphoserine1 Publication
Modified residuei163 – 1631Deamidated glutamine; by deterioration1 Publication
Modified residuei176 – 1761Phosphoserine1 Publication
Modified residuei178 – 1781Deamidated asparagine; by deterioration1 Publication
Disulfide bondi208 ↔ 215

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP01241.
PRIDEiP01241.

PTM databases

PhosphoSiteiP01241.

Expressioni

Gene expression databases

BgeeiP01241.
CleanExiHS_GH1.
ExpressionAtlasiP01241. baseline.
GenevisibleiP01241. HS.

Organism-specific databases

HPAiHPA043715.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
GHRP109123EBI-1026046,EBI-286316

Protein-protein interaction databases

BioGridi108955. 6 interactions.
DIPiDIP-1022N.
IntActiP01241. 3 interactions.
STRINGi9606.ENSP00000312673.

Structurei

Secondary structure

1
217
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 6130Combined sources
Helixi64 – 729Combined sources
Helixi73 – 753Combined sources
Turni80 – 834Combined sources
Helixi90 – 945Combined sources
Helixi98 – 11013Combined sources
Turni111 – 1144Combined sources
Helixi115 – 1195Combined sources
Helixi120 – 1256Combined sources
Turni129 – 1335Combined sources
Helixi136 – 15419Combined sources
Helixi163 – 1664Combined sources
Beta strandi178 – 1803Combined sources
Helixi182 – 20928Combined sources
Turni212 – 2165Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP01241.
SMRiP01241. Positions 27-216.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01241.

Family & Domainsi

Sequence similaritiesi

Belongs to the somatotropin/prolactin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG26152.
GeneTreeiENSGT00730000111012.
HOGENOMiHOG000068443.
HOVERGENiHBG011318.
InParanoidiP01241.
KOiK05438.
OMAiTYLRVMK.
OrthoDBiEOG7F7W9X.
PhylomeDBiP01241.
TreeFamiTF332592.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001400. Somatotropin.
IPR018116. Somatotropin_CS.
[Graphical view]
PANTHERiPTHR11417. PTHR11417. 1 hit.
PfamiPF00103. Hormone_1. 1 hit.
[Graphical view]
PRINTSiPR00836. SOMATOTROPIN.
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00266. SOMATOTROPIN_1. 1 hit.
PS00338. SOMATOTROPIN_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P01241-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MATGSRTSLL LAFGLLCLPW LQEGSAFPTI PLSRLFDNAM LRAHRLHQLA
60 70 80 90 100
FDTYQEFEEA YIPKEQKYSF LQNPQTSLCF SESIPTPSNR EETQQKSNLE
110 120 130 140 150
LLRISLLLIQ SWLEPVQFLR SVFANSLVYG ASDSNVYDLL KDLEEGIQTL
160 170 180 190 200
MGRLEDGSPR TGQIFKQTYS KFDTNSHNDD ALLKNYGLLY CFRKDMDKVE
210
TFLRIVQCRS VEGSCGF
Length:217
Mass (Da):24,847
Last modified:March 1, 1992 - v2
Checksum:i72CC15AF4ED1C51A
GO
Isoform 2 (identifier: P01241-2) [UniParc]FASTAAdd to basket

Also known as: 20 kDa variant

The sequence of this isoform differs from the canonical sequence as follows:
     58-72: Missing.

Show »
Length:202
Mass (Da):22,992
Checksum:i65342A13E1856C5E
GO
Isoform 3 (identifier: P01241-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     111-148: Missing.

Show »
Length:179
Mass (Da):20,561
Checksum:i0E875A91BE0B9B7E
GO
Isoform 4 (identifier: P01241-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-162: Missing.

Show »
Length:171
Mass (Da):19,802
Checksum:i9FA9013991FA9F28
GO
Isoform 5 (identifier: P01241-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-97: Missing.

Note: No experimental confirmation available.
Show »
Length:177
Mass (Da):20,201
Checksum:i399A85FF90C22721
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351L → P in CAA23778 (PubMed:386281).Curated
Sequence conflicti40 – 401M → S in CAA23779 (PubMed:6269091).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31T → A Found in patients with isolated growth hormone deficiency. 3 Publications
Corresponds to variant rs2001345 [ dbSNP | Ensembl ].
VAR_011917
Natural varianti16 – 161L → P in IGHD1B; suppresses secretion. 1 Publication
VAR_015801
Natural varianti37 – 371D → N in IGHD1B. 1 Publication
VAR_015802
Natural varianti42 – 421R → C in IGHD1B; reduced secretion. 1 Publication
VAR_015803
Natural varianti53 – 531T → I in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015804
Natural varianti67 – 671K → R in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015805
Natural varianti73 – 731N → D in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015806
Natural varianti79 – 791C → 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. 1 Publication
VAR_032702
Natural varianti97 – 971S → F in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015807
Natural varianti100 – 1001E → K in IGHD1B. 1 Publication
VAR_015808
Natural varianti103 – 1031R → C in KWKS; the mutant fails to induce GHR signaling pathway; does not affect interaction with GHR; results in a stronger interaction with GHBP; does not affect subcellular location. 2 Publications
VAR_015809
Natural varianti105 – 1051S → C.1 Publication
Corresponds to variant rs6174 [ dbSNP | Ensembl ].
VAR_011918
Natural varianti117 – 1171Q → L in IGHD1B; reduced secretion. 1 Publication
VAR_015810
Natural varianti134 – 1341S → C in IGHD1B. 1 Publication
VAR_015811
Natural varianti134 – 1341S → R in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015812
Natural varianti136 – 1361V → I.2 Publications
Corresponds to variant rs5388 [ dbSNP | Ensembl ].
VAR_011919
Natural varianti138 – 1381D → G in KWKS; loss of activity. 1 Publication
VAR_015813
Natural varianti201 – 2011T → A in IGHD1B; reduced ability to activate the JAK/STAT pathway. 1 Publication
VAR_015814
Natural varianti205 – 2051I → M in short stature; idiopathic autosomal. 1 Publication
VAR_032703
Natural varianti209 – 2091R → H in IGHD2. 2 Publications
VAR_015815

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 9740Missing in isoform 5. 1 PublicationVSP_045642Add
BLAST
Alternative sequencei58 – 7215Missing in isoform 2. 1 PublicationVSP_006200Add
BLAST
Alternative sequencei111 – 14838Missing in isoform 3. 1 PublicationVSP_006201Add
BLAST
Alternative sequencei117 – 16246Missing in isoform 4. 1 PublicationVSP_006202Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11653.1. [P01241-1]
CCDS11654.1. [P01241-5]
CCDS45760.1. [P01241-2]
PIRiA93731. STHU.
RefSeqiNP_000506.2. NM_000515.4. [P01241-1]
NP_072053.1. NM_022559.3. [P01241-2]
NP_072054.1. NM_022560.3. [P01241-5]
UniGeneiHs.655229.

Genome annotation databases

EnsembliENST00000323322; ENSP00000312673; ENSG00000259384.
ENST00000351388; ENSP00000343791; ENSG00000259384. [P01241-5]
GeneIDi2688.
KEGGihsa:2688.
UCSCiuc002jdj.3. human. [P01241-1]
uc002jdk.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Growth hormone entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11653.1. [P01241-1]
CCDS11654.1. [P01241-5]
CCDS45760.1. [P01241-2]
PIRiA93731. STHU.
RefSeqiNP_000506.2. NM_000515.4. [P01241-1]
NP_072053.1. NM_022559.3. [P01241-2]
NP_072054.1. NM_022560.3. [P01241-5]
UniGeneiHs.655229.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP01241.
SMRiP01241. Positions 27-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108955. 6 interactions.
DIPiDIP-1022N.
IntActiP01241. 3 interactions.
STRINGi9606.ENSP00000312673.

PTM databases

PhosphoSiteiP01241.

Polymorphism and mutation databases

BioMutaiGH1.

Proteomic databases

PaxDbiP01241.
PRIDEiP01241.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323322; ENSP00000312673; ENSG00000259384.
ENST00000351388; ENSP00000343791; ENSG00000259384. [P01241-5]
GeneIDi2688.
KEGGihsa:2688.
UCSCiuc002jdj.3. human. [P01241-1]
uc002jdk.3. human.

Organism-specific databases

CTDi2688.
GeneCardsiGC17M061994.
HGNCiHGNC:4261. GH1.
HPAiHPA043715.
MIMi139250. gene.
173100. phenotype.
262400. phenotype.
262650. phenotype.
612781. phenotype.
neXtProtiNX_P01241.
Orphaneti231662. 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.
PharmGKBiPA171.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG26152.
GeneTreeiENSGT00730000111012.
HOGENOMiHOG000068443.
HOVERGENiHBG011318.
InParanoidiP01241.
KOiK05438.
OMAiTYLRVMK.
OrthoDBiEOG7F7W9X.
PhylomeDBiP01241.
TreeFamiTF332592.

Enzyme and pathway databases

ReactomeiREACT_111133. Growth hormone receptor signaling.
REACT_115697. Prolactin receptor signaling.
REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
SignaLinkiP01241.

Miscellaneous databases

ChiTaRSiGH1. human.
EvolutionaryTraceiP01241.
GenomeRNAii2688.
NextBioi10614.
PROiP01241.
SOURCEiSearch...

Gene expression databases

BgeeiP01241.
CleanExiHS_GH1.
ExpressionAtlasiP01241. baseline.
GenevisibleiP01241. HS.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001400. Somatotropin.
IPR018116. Somatotropin_CS.
[Graphical view]
PANTHERiPTHR11417. PTHR11417. 1 hit.
PfamiPF00103. Hormone_1. 1 hit.
[Graphical view]
PRINTSiPR00836. SOMATOTROPIN.
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00266. SOMATOTROPIN_1. 1 hit.
PS00338. SOMATOTROPIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. 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. 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. 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. Cited for: VARIANT KWKS GLY-138.
  35. Cited for: VARIANT CYS-105.
  36. "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.
  37. "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.
  38. "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.
  39. Cited for: VARIANT SHORT STATURE SER-79, CHARACTERIZATION OF VARIANT SHORT STATURE SER-79.
  40. "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.

Entry informationi

Entry nameiSOMA_HUMAN
AccessioniPrimary (citable) accession number: P01241
Secondary accession number(s): A6NEF6
, Q14405, Q16631, Q5EB53, Q9HBZ1, Q9UMJ7, Q9UNL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 1992
Last modified: July 22, 2015
This is version 188 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.