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P01286

- SLIB_HUMAN

UniProt

P01286 - SLIB_HUMAN

Protein

Somatoliberin

Gene

GHRH

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

    GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone.

    GO - Molecular functioni

    1. growth hormone-releasing hormone activity Source: BHF-UCL
    2. growth hormone-releasing hormone receptor binding Source: BHF-UCL

    GO - Biological processi

    1. adenohypophysis development Source: BHF-UCL
    2. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: BHF-UCL
    3. cAMP-mediated signaling Source: BHF-UCL
    4. cell-cell signaling Source: ProtInc
    5. growth hormone secretion Source: MGI
    6. positive regulation of cAMP biosynthetic process Source: BHF-UCL
    7. positive regulation of cell proliferation Source: BHF-UCL
    8. positive regulation of circadian sleep/wake cycle, REM sleep Source: BHF-UCL
    9. positive regulation of growth hormone secretion Source: BHF-UCL
    10. positive regulation of insulin-like growth factor receptor signaling pathway Source: BHF-UCL
    11. positive regulation of multicellular organism growth Source: BHF-UCL
    12. response to food Source: BHF-UCL

    Enzyme and pathway databases

    ReactomeiREACT_18377. Glucagon-type ligand receptors.
    REACT_19327. G alpha (s) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Somatoliberin
    Alternative name(s):
    Growth hormone-releasing factor
    Short name:
    GRF
    Growth hormone-releasing hormone
    Short name:
    GHRH
    Somatocrinin
    Somatorelin
    INN: Sermorelin
    Gene namesi
    Name:GHRH
    Synonyms:GHRF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:4265. GHRH.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: BHF-UCL
    2. extracellular space Source: BHF-UCL
    3. terminal bouton Source: BHF-UCL

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Pharmaceutical usei

    Available under the names Groliberin (Pharmacia) or Somatrel (Ferring). Also available under the name Geref (Serono). Geref is a synthetic acetylated form of residues 1 to 29 of GHRH. Used for the treatment of growth hormone deficiency.

    Organism-specific databases

    PharmGKBiPA28675.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 31111 PublicationPRO_0000011438Add
    BLAST
    Peptidei32 – 7544SomatoliberinPRO_0000011439Add
    BLAST
    Propeptidei78 – 10831PRO_0000011440Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751Leucine amide1 Publication

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues

    Proteomic databases

    PaxDbiP01286.
    PRIDEiP01286.

    PTM databases

    PhosphoSiteiP01286.

    Expressioni

    Gene expression databases

    BgeeiP01286.
    CleanExiHS_GHRH.
    GenevestigatoriP01286.

    Interactioni

    Protein-protein interaction databases

    BioGridi108958. 1 interaction.
    IntActiP01286. 2 interactions.
    MINTiMINT-8090632.
    STRINGi9606.ENSP00000237527.

    Structurei

    3D structure databases

    ProteinModelPortaliP01286.
    SMRiP01286. Positions 32-59, 78-104.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glucagon family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG47924.
    HOGENOMiHOG000115417.
    HOVERGENiHBG004478.
    InParanoidiP01286.
    KOiK05260.
    OrthoDBiEOG7WQ7VQ.
    PhylomeDBiP01286.
    TreeFamiTF353187.

    Family and domain databases

    InterProiIPR000532. Glucagon_GIP_secretin_VIP.
    [Graphical view]
    PfamiPF00123. Hormone_2. 1 hit.
    [Graphical view]
    SMARTiSM00070. GLUCA. 1 hit.
    [Graphical view]
    PROSITEiPS00260. GLUCAGON. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P01286-1) [UniParc]FASTAAdd to Basket

    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

    MPLWVFFFVI LTLSNSSHCS PPPPLTLRMR RYADAIFTNS YRKVLGQLSA    50
    RKLLQDIMSR QQGESNQERG ARARLGRQVD SMWAEQKQME LESILVALLQ 100
    KHSRNSQG 108
    Length:108
    Mass (Da):12,447
    Last modified:July 21, 1986 - v1
    Checksum:i366AE05383488C53
    GO
    Isoform 2 (identifier: P01286-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         103-103: Missing.

    Show »
    Length:107
    Mass (Da):12,360
    Checksum:i74432263093C5367
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti92 – 921E → D in CAA24955. (PubMed:6415488)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321Y → C.
    Corresponds to variant rs17787698 [ dbSNP | Ensembl ].
    VAR_049185
    Natural varianti75 – 751L → F.
    Corresponds to variant rs4988492 [ dbSNP | Ensembl ].
    VAR_024328

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei103 – 1031Missing in isoform 2. 2 PublicationsVSP_023146

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29177 Genomic DNA. No translation available.
    L00137
    , L00134, L00135, L00136 Genomic DNA. Translation: AAA52608.1.
    L00137
    , L00134, L00135, L00136 Genomic DNA. Translation: AAA52609.1.
    AL031659 Genomic DNA. Translation: CAB41762.2.
    AL031659 Genomic DNA. Translation: CAI42673.1.
    BC098109 mRNA. Translation: AAH98109.1.
    BC098161 mRNA. Translation: AAH98161.1.
    BC099727 mRNA. Translation: AAH99727.1.
    X00094 mRNA. Translation: CAA24955.1.
    X00094 mRNA. Translation: CAA24956.1.
    CCDSiCCDS13292.1. [P01286-1]
    CCDS54460.1. [P01286-2]
    PIRiA21902. RHHUS.
    RefSeqiNP_001171660.1. NM_001184731.1. [P01286-2]
    NP_066567.1. NM_021081.4. [P01286-1]
    UniGeneiHs.37023.

    Genome annotation databases

    EnsembliENST00000237527; ENSP00000237527; ENSG00000118702. [P01286-1]
    ENST00000373611; ENSP00000362713; ENSG00000118702. [P01286-2]
    ENST00000373614; ENSP00000362716; ENSG00000118702. [P01286-1]
    GeneIDi2691.
    KEGGihsa:2691.
    UCSCiuc002xgr.3. human. [P01286-1]
    uc002xgt.3. human. [P01286-2]

    Polymorphism databases

    DMDMi134521.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Growth hormone releasing hormone entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29177 Genomic DNA. No translation available.
    L00137
    , L00134 , L00135 , L00136 Genomic DNA. Translation: AAA52608.1 .
    L00137
    , L00134 , L00135 , L00136 Genomic DNA. Translation: AAA52609.1 .
    AL031659 Genomic DNA. Translation: CAB41762.2 .
    AL031659 Genomic DNA. Translation: CAI42673.1 .
    BC098109 mRNA. Translation: AAH98109.1 .
    BC098161 mRNA. Translation: AAH98161.1 .
    BC099727 mRNA. Translation: AAH99727.1 .
    X00094 mRNA. Translation: CAA24955.1 .
    X00094 mRNA. Translation: CAA24956.1 .
    CCDSi CCDS13292.1. [P01286-1 ]
    CCDS54460.1. [P01286-2 ]
    PIRi A21902. RHHUS.
    RefSeqi NP_001171660.1. NM_001184731.1. [P01286-2 ]
    NP_066567.1. NM_021081.4. [P01286-1 ]
    UniGenei Hs.37023.

    3D structure databases

    ProteinModelPortali P01286.
    SMRi P01286. Positions 32-59, 78-104.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108958. 1 interaction.
    IntActi P01286. 2 interactions.
    MINTi MINT-8090632.
    STRINGi 9606.ENSP00000237527.

    PTM databases

    PhosphoSitei P01286.

    Polymorphism databases

    DMDMi 134521.

    Proteomic databases

    PaxDbi P01286.
    PRIDEi P01286.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000237527 ; ENSP00000237527 ; ENSG00000118702 . [P01286-1 ]
    ENST00000373611 ; ENSP00000362713 ; ENSG00000118702 . [P01286-2 ]
    ENST00000373614 ; ENSP00000362716 ; ENSG00000118702 . [P01286-1 ]
    GeneIDi 2691.
    KEGGi hsa:2691.
    UCSCi uc002xgr.3. human. [P01286-1 ]
    uc002xgt.3. human. [P01286-2 ]

    Organism-specific databases

    CTDi 2691.
    GeneCardsi GC20M035880.
    HGNCi HGNC:4265. GHRH.
    MIMi 139190. gene.
    neXtProti NX_P01286.
    PharmGKBi PA28675.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47924.
    HOGENOMi HOG000115417.
    HOVERGENi HBG004478.
    InParanoidi P01286.
    KOi K05260.
    OrthoDBi EOG7WQ7VQ.
    PhylomeDBi P01286.
    TreeFami TF353187.

    Enzyme and pathway databases

    Reactomei REACT_18377. Glucagon-type ligand receptors.
    REACT_19327. G alpha (s) signalling events.

    Miscellaneous databases

    GenomeRNAii 2691.
    NextBioi 10640.
    PROi P01286.
    SOURCEi Search...

    Gene expression databases

    Bgeei P01286.
    CleanExi HS_GHRH.
    Genevestigatori P01286.

    Family and domain databases

    InterProi IPR000532. Glucagon_GIP_secretin_VIP.
    [Graphical view ]
    Pfami PF00123. Hormone_2. 1 hit.
    [Graphical view ]
    SMARTi SM00070. GLUCA. 1 hit.
    [Graphical view ]
    PROSITEi PS00260. GLUCAGON. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of cDNA for the precursor of human growth hormone-releasing factor, somatocrinin."
      Gubler U., Monahan J.J., Lomedico P.T., Bhatt R.S., Collier K.J., Hoffman B.J., Boehlen P., Esch F., Ling N., Zeytin F., Brazeau P., Poonian M.S., Gage L.P.
      Proc. Natl. Acad. Sci. U.S.A. 80:4311-4314(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. "Gene encoding human growth hormone-releasing factor precursor: structure, sequence, and chromosomal assignment."
      Mayo K.E., Cerelli G.M., Lebo R.V., Bruce B.D., Rosenfeld M.G., Evans R.M.
      Proc. Natl. Acad. Sci. U.S.A. 82:63-67(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 AND 2).
    5. "Expression-cloning and sequence of a cDNA encoding human growth hormone-releasing factor."
      Mayo K.E., Vale W., Rivier J., Rosenfeld M.G., Evans R.M.
      Nature 306:86-88(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-101.
    6. "Growth hormone-releasing factor from a human pancreatic tumor that caused acromegaly."
      Guillemin R., Brazeau P., Boehlen P., Esch F., Ling N., Wehrenberg W.B.
      Science 218:585-587(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-75, AMIDATION AT LEU-75.
    7. "Solution conformations of human growth hormone releasing factor: comparison of the restrained molecular dynamics and distance geometry methods for a system without long-range distance data."
      Bruenger A.T., Clore G.M., Gronenborn A.M., Karplus M.
      Protein Eng. 1:399-406(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 32-60.
    8. "Solution structure of human growth hormone releasing factor. Combined use of circular dichroism and nuclear magnetic resonance spectroscopy."
      Clore G.M., Martin S.R., Gronenborn A.M.
      J. Mol. Biol. 191:553-561(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 32-60.

    Entry informationi

    Entry nameiSLIB_HUMAN
    AccessioniPrimary (citable) accession number: P01286
    Secondary accession number(s): Q4KN10, Q5JYR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3