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P01241

- SOMA_HUMAN

UniProt

P01241 - SOMA_HUMAN

Protein

Somatotropin

Gene

GH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 2 (01 Mar 1992)
      Previous versions | rss
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    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

    1. growth factor activity Source: BHF-UCL
    2. growth hormone receptor binding Source: BHF-UCL
    3. metal ion binding Source: UniProtKB-KW
    4. prolactin receptor binding Source: BHF-UCL
    5. protein binding Source: IntAct

    GO - Biological processi

    1. bone maturation Source: BHF-UCL
    2. glucose transport Source: MGI
    3. growth hormone receptor signaling pathway Source: BHF-UCL
    4. JAK-STAT cascade Source: BHF-UCL
    5. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
    6. positive regulation of activation of JAK2 kinase activity Source: BHF-UCL
    7. positive regulation of insulin-like growth factor receptor signaling pathway Source: BHF-UCL
    8. positive regulation of JAK-STAT cascade Source: BHF-UCL
    9. positive regulation of MAP kinase activity Source: BHF-UCL
    10. positive regulation of multicellular organism growth Source: BHF-UCL
    11. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    12. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
    13. positive regulation of tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
    14. positive regulation of tyrosine phosphorylation of Stat5 protein Source: BHF-UCL
    15. response to estradiol Source: BHF-UCL

    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: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4261. GH1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: BHF-UCL

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti103 – 1031R → 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. 1 Publication
    VAR_015809
    Natural varianti138 – 1381D → G in KWKS; loss of activity. 1 Publication
    VAR_015813
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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

    ArrayExpressiP01241.
    BgeeiP01241.
    CleanExiHS_GH1.
    GenevestigatoriP01241.

    Organism-specific databases

    HPAiCAB025646.
    HPA043715.

    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 – 6130
    Helixi64 – 729
    Helixi73 – 753
    Turni80 – 834
    Helixi90 – 945
    Helixi98 – 11013
    Turni111 – 1144
    Helixi115 – 1195
    Helixi120 – 1256
    Turni129 – 1335
    Helixi136 – 15419
    Helixi163 – 1664
    Beta strandi178 – 1803
    Helixi182 – 20928
    Turni212 – 2165

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOVERGENiHBG011318.
    InParanoidiP01241.
    KOiK05438.
    OMAiDTNLRSD.
    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. Align

    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

    MATGSRTSLL LAFGLLCLPW LQEGSAFPTI PLSRLFDNAM LRAHRLHQLA    50
    FDTYQEFEEA YIPKEQKYSF LQNPQTSLCF SESIPTPSNR EETQQKSNLE 100
    LLRISLLLIQ SWLEPVQFLR SVFANSLVYG ASDSNVYDLL KDLEEGIQTL 150
    MGRLEDGSPR TGQIFKQTYS KFDTNSHNDD ALLKNYGLLY CFRKDMDKVE 200
    TFLRIVQCRS VEGSCGF 217
    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; 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. 1 Publication
    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:
    EMBL
    GenBank
    DDBJ
    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]
    XP_005257275.1. XM_005257218.2. [P01241-3]
    XP_005257276.1. XM_005257219.2. [P01241-4]
    UniGeneiHs.655229.

    Genome annotation databases

    EnsembliENST00000323322; ENSP00000312673; ENSG00000259384. [P01241-1]
    ENST00000351388; ENSP00000343791; ENSG00000259384. [P01241-5]
    ENST00000458650; ENSP00000408486; ENSG00000259384. [P01241-2]
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS11653.1. [P01241-1 ]
    CCDS11654.1. [P01241-5 ]
    CCDS45760.1. [P01241-2 ]
    PIRi A93731. STHU.
    RefSeqi NP_000506.2. NM_000515.4. [P01241-1 ]
    NP_072053.1. NM_022559.3. [P01241-2 ]
    NP_072054.1. NM_022560.3. [P01241-5 ]
    XP_005257275.1. XM_005257218.2. [P01241-3 ]
    XP_005257276.1. XM_005257219.2. [P01241-4 ]
    UniGenei Hs.655229.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P01241.
    SMRi P01241. Positions 27-216.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108955. 6 interactions.
    DIPi DIP-1022N.
    IntActi P01241. 3 interactions.
    STRINGi 9606.ENSP00000312673.

    PTM databases

    PhosphoSitei P01241.

    Proteomic databases

    PaxDbi P01241.
    PRIDEi P01241.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323322 ; ENSP00000312673 ; ENSG00000259384 . [P01241-1 ]
    ENST00000351388 ; ENSP00000343791 ; ENSG00000259384 . [P01241-5 ]
    ENST00000458650 ; ENSP00000408486 ; ENSG00000259384 . [P01241-2 ]
    GeneIDi 2688.
    KEGGi hsa:2688.
    UCSCi uc002jdj.3. human. [P01241-1 ]
    uc002jdk.3. human.

    Organism-specific databases

    CTDi 2688.
    GeneCardsi GC17M061994.
    HGNCi HGNC:4261. GH1.
    HPAi CAB025646.
    HPA043715.
    MIMi 139250. gene.
    173100. phenotype.
    262400. phenotype.
    262650. phenotype.
    612781. phenotype.
    neXtProti NX_P01241.
    Orphaneti 231662. 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.
    PharmGKBi PA171.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG26152.
    HOVERGENi HBG011318.
    InParanoidi P01241.
    KOi K05438.
    OMAi DTNLRSD.
    OrthoDBi EOG7F7W9X.
    PhylomeDBi P01241.
    TreeFami TF332592.

    Enzyme and pathway databases

    Reactomei REACT_111133. Growth hormone receptor signaling.
    REACT_115697. Prolactin receptor signaling.
    REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
    SignaLinki P01241.

    Miscellaneous databases

    ChiTaRSi GH1. human.
    EvolutionaryTracei P01241.
    GenomeRNAii 2688.
    NextBioi 10614.
    PROi P01241.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01241.
    Bgeei P01241.
    CleanExi HS_GH1.
    Genevestigatori P01241.

    Family and domain databases

    Gene3Di 1.20.1250.10. 1 hit.
    InterProi IPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR001400. Somatotropin.
    IPR018116. Somatotropin_CS.
    [Graphical view ]
    PANTHERi PTHR11417. PTHR11417. 1 hit.
    Pfami PF00103. Hormone_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00836. SOMATOTROPIN.
    SUPFAMi SSF47266. SSF47266. 1 hit.
    PROSITEi PS00266. SOMATOTROPIN_1. 1 hit.
    PS00338. SOMATOTROPIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 179 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