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Q9UBU3

- GHRL_HUMAN

UniProt

Q9UBU3 - GHRL_HUMAN

Protein

Appetite-regulating hormone

Gene

GHRL

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

    Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.
    Obestatin may be the ligand for GPR39. May have an appetite-reducing effect resulting in decreased food intake. May reduce gastric emptying activity and jejunal motility By similarity.By similarity

    GO - Molecular functioni

    1. ghrelin receptor binding Source: UniProtKB
    2. G-protein coupled receptor binding Source: UniProtKB
    3. growth hormone-releasing hormone activity Source: UniProtKB
    4. protein tyrosine kinase activator activity Source: UniProtKB

    GO - Biological processi

    1. actin polymerization or depolymerization Source: UniProtKB
    2. activation of MAPK activity Source: UniProtKB
    3. adult feeding behavior Source: HGNC
    4. cartilage development Source: UniProtKB
    5. cellular protein metabolic process Source: Reactome
    6. cortisol secretion Source: UniProtKB
    7. decidualization Source: UniProtKB
    8. dendrite development Source: MGI
    9. gastric acid secretion Source: Ensembl
    10. glucose metabolic process Source: UniProtKB
    11. G-protein coupled receptor signaling pathway Source: UniProtKB
    12. growth hormone secretion Source: HGNC
    13. hormone-mediated signaling pathway Source: HGNC
    14. negative regulation of angiogenesis Source: UniProtKB
    15. negative regulation of apoptotic process Source: UniProtKB
    16. negative regulation of circadian sleep/wake cycle, REM sleep Source: BHF-UCL
    17. negative regulation of endothelial cell proliferation Source: UniProtKB
    18. negative regulation of inflammatory response Source: UniProtKB
    19. negative regulation of insulin secretion Source: Ensembl
    20. negative regulation of interleukin-1 beta production Source: UniProtKB
    21. negative regulation of interleukin-6 biosynthetic process Source: UniProtKB
    22. negative regulation of locomotion Source: Ensembl
    23. negative regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
    24. positive regulation of appetite Source: HGNC
    25. positive regulation of circadian sleep/wake cycle, non-REM sleep Source: BHF-UCL
    26. positive regulation of corticotropin secretion Source: BHF-UCL
    27. positive regulation of cortisol secretion Source: BHF-UCL
    28. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    29. positive regulation of growth hormone receptor signaling pathway Source: BHF-UCL
    30. positive regulation of growth hormone secretion Source: BHF-UCL
    31. positive regulation of insulin secretion Source: UniProtKB
    32. positive regulation of multicellular organism growth Source: HGNC
    33. positive regulation of protein tyrosine kinase activity Source: GOC
    34. positive regulation of synapse assembly Source: MGI
    35. regulation of cell proliferation Source: UniProtKB
    36. regulation of excitatory postsynaptic membrane potential Source: Ensembl
    37. response to estrogen Source: UniProtKB
    38. response to hormone Source: UniProtKB

    Keywords - Molecular functioni

    Hormone

    Enzyme and pathway databases

    ReactomeiREACT_14819. Peptide ligand-binding receptors.
    REACT_18283. G alpha (q) signalling events.
    REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Appetite-regulating hormone
    Alternative name(s):
    Growth hormone secretagogue
    Growth hormone-releasing peptide
    Motilin-related peptide
    Protein M46
    Cleaved into the following 3 chains:
    Gene namesi
    Name:GHRL
    Synonyms:MTLRP
    ORF Names:UNQ524/PRO1066
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:18129. GHRL.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. endoplasmic reticulum lumen Source: Reactome
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: UniProtKB
    5. secretory granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671740.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23232 PublicationsAdd
    BLAST
    Peptidei24 – 5128Ghrelin-28PRO_0000019202Add
    BLAST
    Peptidei24 – 5027Ghrelin-27PRO_0000019203Add
    BLAST
    Propeptidei52 – 7524Removed in mature formPRO_0000019204Add
    BLAST
    Peptidei76 – 9823ObestatinBy similarityPRO_0000045140Add
    BLAST
    Propeptidei99 – 11719Removed in mature formBy similarityPRO_0000045141Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi26 – 261O-decanoyl serine; alternate2 Publications
    Lipidationi26 – 261O-octanoyl serine; alternate2 Publications
    Modified residuei98 – 981Leucine amideBy similarity

    Post-translational modificationi

    O-octanoylation or O-decanoylation is essential for ghrelin activity. The O-decanoylated forms Ghrelin-27-C10 and Ghrelin-28-C10 differ in the length of the carbon backbone of the carboxylic acid bound to Ser-26. A small fraction of ghrelin, ghrelin-28-C10:1, may be modified with a singly unsaturated carboxylic acid (PubMed:10604470).1 Publication
    Amidation of Leu-98 is essential for obestatin activity.By similarity

    Keywords - PTMi

    Amidation, Lipoprotein

    Proteomic databases

    PaxDbiQ9UBU3.
    PRIDEiQ9UBU3.

    PTM databases

    PhosphoSiteiQ9UBU3.

    Miscellaneous databases

    PMAP-CutDBQ9UBU3.

    Expressioni

    Tissue specificityi

    Highest level in stomach. All forms are found in serum as well. Other tissues compensate for the loss of ghrelin synthesis in the stomach following gastrectomy.1 Publication

    Gene expression databases

    ArrayExpressiQ9UBU3.
    BgeeiQ9UBU3.
    CleanExiHS_GHRL.
    GenevestigatoriQ9UBU3.

    Organism-specific databases

    HPAiCAB022731.
    HPA014246.

    Interactioni

    Protein-protein interaction databases

    BioGridi119706. 4 interactions.
    STRINGi9606.ENSP00000335074.

    Structurei

    Secondary structure

    1
    117
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 147
    Beta strandi17 – 248
    Beta strandi27 – 293
    Helixi30 – 356
    Beta strandi57 – 604
    Beta strandi63 – 708
    Beta strandi73 – 775
    Helixi90 – 934
    Helixi95 – 10410
    Helixi107 – 1159

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P7Xmodel-A1-117[»]
    ProteinModelPortaliQ9UBU3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the motilin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG45924.
    HOVERGENiHBG018522.
    InParanoidiQ9UBU3.
    KOiK05254.
    OMAiSLGTICS.
    OrthoDBiEOG741Z4K.
    PhylomeDBiQ9UBU3.
    TreeFamiTF336219.

    Family and domain databases

    InterProiIPR006737. Motilin_assoc.
    IPR006738. Motilin_ghrelin.
    IPR005441. Preproghrelin.
    [Graphical view]
    PANTHERiPTHR14122. PTHR14122. 1 hit.
    PfamiPF04643. Motilin_assoc. 1 hit.
    PF04644. Motilin_ghrelin. 1 hit.
    [Graphical view]
    PRINTSiPR01624. GHRELIN.

    Sequences (6)i

    Sequence statusi: Complete.

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

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UBU3-1) [UniParc]FASTAAdd to Basket

    Also known as: Ghrelin

    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

    MPSPGTVCSL LLLGMLWLDL AMAGSSFLSP EHQRVQQRKE SKKPPAKLQP    50
    RALAGWLRPE DGGQAEGAED ELEVRFNAPF DVGIKLSGVQ YQQHSQALGK 100
    FLQDILWEEA KEAPADK 117
    Length:117
    Mass (Da):12,911
    Last modified:May 1, 2000 - v1
    Checksum:i39C0572EBECA2755
    GO
    Isoform 2 (identifier: Q9UBU3-2) [UniParc]FASTAAdd to Basket

    Also known as: des-Gln14-ghrelin

    The sequence of this isoform differs from the canonical sequence as follows:
         37-37: Missing.

    Show »
    Length:116
    Mass (Da):12,783
    Checksum:iF0DEBEEE880DC951
    GO
    Isoform 3 (identifier: Q9UBU3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRVQ → MFTCWWSYLRSTLAAVPGEASRVQ

    Show »
    Length:105
    Mass (Da):11,784
    Checksum:i9E4000D6A0863F99
    GO
    Isoform 4 (identifier: Q9UBU3-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRVQ → MFTCWWSYLRSTLAAVPGEASRVQ
         37-37: Missing.

    Show »
    Length:104
    Mass (Da):11,656
    Checksum:i508946F0C415058F
    GO
    Isoform 5 (identifier: Q9UBU3-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-75: MPSPGTVCSL...EGAEDELEVR → MFTCWWSYLRSTLAAVPGEASRVQ

    Show »
    Length:66
    Mass (Da):7,460
    Checksum:i5001F0A57716C83D
    GO
    Isoform 6 (identifier: Q9UBU3-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         76-117: FNAPFDVGIKLSGVQYQQHSQALGKFLQDILWEEAKEAPADK → RPQPTSDRPQALLTSL

    Show »
    Length:91
    Mass (Da):9,972
    Checksum:iE7E532D32A3F8609
    GO

    Mass spectrometryi

    Molecular mass is 3398.9±0.3 Da from positions 24 - 51. Determined by ESI. Ghrelin-28-C10, O-decanoylated form.1 Publication
    Molecular mass is 3397.2±0.5 Da from positions 24 - 51. Determined by ESI. Ghrelin-28-C10:1, O-decenoylated form.1 Publication
    Molecular mass is 3371.3±0.1 Da from positions 24 - 51. Determined by ESI. Ghrelin-28-C8, O-octanoylated form.1 Publication
    Molecular mass is 3243.6±0.4 Da from positions 24 - 50. Determined by ESI. Ghrelin-27-C10, O-decanoylated form.1 Publication
    Molecular mass is 3214.6±0.6 Da from positions 24 - 50. Determined by ESI. Ghrelin-27-C8, O-octanoylated form.1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721L → M.1 Publication
    Corresponds to variant rs696217 [ dbSNP | Ensembl ].
    VAR_050095
    Natural varianti90 – 901Q → L.
    Corresponds to variant rs4684677 [ dbSNP | Ensembl ].
    VAR_029135

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7575MPSPG…ELEVR → MFTCWWSYLRSTLAAVPGEA SRVQ in isoform 5. 1 PublicationVSP_041438Add
    BLAST
    Alternative sequencei1 – 3636MPSPG…HQRVQ → MFTCWWSYLRSTLAAVPGEA SRVQ in isoform 3 and isoform 4. 1 PublicationVSP_041437Add
    BLAST
    Alternative sequencei37 – 371Missing in isoform 2 and isoform 4. 2 PublicationsVSP_003245
    Alternative sequencei76 – 11742FNAPF…APADK → RPQPTSDRPQALLTSL in isoform 6. 1 PublicationVSP_047642Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB029434 mRNA. Translation: BAA89371.1.
    AJ252278 mRNA. Translation: CAB65733.1.
    AF296558 Genomic DNA. Translation: AAG10300.1.
    EU072086 mRNA. Translation: ABV55189.1.
    EF549569 mRNA. Translation: ABQ40357.1.
    EF549571 mRNA. Translation: ABQ40358.1.
    EF549572 mRNA. Translation: ABQ40359.1.
    EF549573 mRNA. Translation: ABQ40360.1.
    EF549574 mRNA. Translation: ABQ40361.1.
    EF549575 mRNA. Translation: ABQ40362.1.
    EU072083 mRNA. Translation: ABV55186.1.
    EU072084 mRNA. Translation: ABV55187.1.
    EU072085 mRNA. Translation: ABV55188.1.
    EU072087 mRNA. Translation: ABV55190.1.
    AY184207 mRNA. Translation: AAO27351.1.
    AY359053 mRNA. Translation: AAQ89412.1.
    AC022384 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64074.1.
    CH471055 Genomic DNA. Translation: EAW64075.1.
    BC025791 mRNA. Translation: AAH25791.1.
    AB035700 mRNA. Translation: BAB19045.1.
    CCDSiCCDS33700.1. [Q9UBU3-1]
    CCDS46747.1. [Q9UBU3-5]
    CCDS46748.1. [Q9UBU3-3]
    CCDS46749.1. [Q9UBU3-4]
    CCDS46750.1. [Q9UBU3-2]
    PIRiA59316.
    RefSeqiNP_001128413.1. NM_001134941.1. [Q9UBU3-2]
    NP_001128416.1. NM_001134944.1. [Q9UBU3-3]
    NP_001128417.1. NM_001134945.1. [Q9UBU3-4]
    NP_001128418.1. NM_001134946.1. [Q9UBU3-5]
    NP_057446.1. NM_016362.3. [Q9UBU3-1]
    UniGeneiHs.590080.
    Hs.672979.

    Genome annotation databases

    EnsembliENST00000287656; ENSP00000287656; ENSG00000157017. [Q9UBU3-2]
    ENST00000335542; ENSP00000335074; ENSG00000157017. [Q9UBU3-1]
    ENST00000422159; ENSP00000405464; ENSG00000157017. [Q9UBU3-6]
    ENST00000429122; ENSP00000414819; ENSG00000157017. [Q9UBU3-1]
    ENST00000430179; ENSP00000399922; ENSG00000157017. [Q9UBU3-2]
    ENST00000437422; ENSP00000416768; ENSG00000157017. [Q9UBU3-3]
    ENST00000439975; ENSP00000403725; ENSG00000157017. [Q9UBU3-5]
    ENST00000449238; ENSP00000388145; ENSG00000157017. [Q9UBU3-4]
    ENST00000457360; ENSP00000391406; ENSG00000157017. [Q9UBU3-1]
    GeneIDi51738.
    KEGGihsa:51738.
    UCSCiuc010hdc.2. human. [Q9UBU3-5]
    uc010hde.2. human. [Q9UBU3-2]
    uc010hdf.2. human. [Q9UBU3-1]
    uc010hdj.2. human. [Q9UBU3-3]
    uc010hdk.2. human. [Q9UBU3-4]

    Polymorphism databases

    DMDMi17865471.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Protein Spotlight

    Gut feelings - Issue 66 of January 2006

    Wikipedia

    Ghrelin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB029434 mRNA. Translation: BAA89371.1 .
    AJ252278 mRNA. Translation: CAB65733.1 .
    AF296558 Genomic DNA. Translation: AAG10300.1 .
    EU072086 mRNA. Translation: ABV55189.1 .
    EF549569 mRNA. Translation: ABQ40357.1 .
    EF549571 mRNA. Translation: ABQ40358.1 .
    EF549572 mRNA. Translation: ABQ40359.1 .
    EF549573 mRNA. Translation: ABQ40360.1 .
    EF549574 mRNA. Translation: ABQ40361.1 .
    EF549575 mRNA. Translation: ABQ40362.1 .
    EU072083 mRNA. Translation: ABV55186.1 .
    EU072084 mRNA. Translation: ABV55187.1 .
    EU072085 mRNA. Translation: ABV55188.1 .
    EU072087 mRNA. Translation: ABV55190.1 .
    AY184207 mRNA. Translation: AAO27351.1 .
    AY359053 mRNA. Translation: AAQ89412.1 .
    AC022384 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64074.1 .
    CH471055 Genomic DNA. Translation: EAW64075.1 .
    BC025791 mRNA. Translation: AAH25791.1 .
    AB035700 mRNA. Translation: BAB19045.1 .
    CCDSi CCDS33700.1. [Q9UBU3-1 ]
    CCDS46747.1. [Q9UBU3-5 ]
    CCDS46748.1. [Q9UBU3-3 ]
    CCDS46749.1. [Q9UBU3-4 ]
    CCDS46750.1. [Q9UBU3-2 ]
    PIRi A59316.
    RefSeqi NP_001128413.1. NM_001134941.1. [Q9UBU3-2 ]
    NP_001128416.1. NM_001134944.1. [Q9UBU3-3 ]
    NP_001128417.1. NM_001134945.1. [Q9UBU3-4 ]
    NP_001128418.1. NM_001134946.1. [Q9UBU3-5 ]
    NP_057446.1. NM_016362.3. [Q9UBU3-1 ]
    UniGenei Hs.590080.
    Hs.672979.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P7X model - A 1-117 [» ]
    ProteinModelPortali Q9UBU3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119706. 4 interactions.
    STRINGi 9606.ENSP00000335074.

    Chemistry

    BindingDBi Q9UBU3.
    ChEMBLi CHEMBL1921664.

    PTM databases

    PhosphoSitei Q9UBU3.

    Polymorphism databases

    DMDMi 17865471.

    Proteomic databases

    PaxDbi Q9UBU3.
    PRIDEi Q9UBU3.

    Protocols and materials databases

    DNASUi 51738.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000287656 ; ENSP00000287656 ; ENSG00000157017 . [Q9UBU3-2 ]
    ENST00000335542 ; ENSP00000335074 ; ENSG00000157017 . [Q9UBU3-1 ]
    ENST00000422159 ; ENSP00000405464 ; ENSG00000157017 . [Q9UBU3-6 ]
    ENST00000429122 ; ENSP00000414819 ; ENSG00000157017 . [Q9UBU3-1 ]
    ENST00000430179 ; ENSP00000399922 ; ENSG00000157017 . [Q9UBU3-2 ]
    ENST00000437422 ; ENSP00000416768 ; ENSG00000157017 . [Q9UBU3-3 ]
    ENST00000439975 ; ENSP00000403725 ; ENSG00000157017 . [Q9UBU3-5 ]
    ENST00000449238 ; ENSP00000388145 ; ENSG00000157017 . [Q9UBU3-4 ]
    ENST00000457360 ; ENSP00000391406 ; ENSG00000157017 . [Q9UBU3-1 ]
    GeneIDi 51738.
    KEGGi hsa:51738.
    UCSCi uc010hdc.2. human. [Q9UBU3-5 ]
    uc010hde.2. human. [Q9UBU3-2 ]
    uc010hdf.2. human. [Q9UBU3-1 ]
    uc010hdj.2. human. [Q9UBU3-3 ]
    uc010hdk.2. human. [Q9UBU3-4 ]

    Organism-specific databases

    CTDi 51738.
    GeneCardsi GC03M010302.
    HGNCi HGNC:18129. GHRL.
    HPAi CAB022731.
    HPA014246.
    MIMi 605353. gene.
    neXtProti NX_Q9UBU3.
    PharmGKBi PA142671740.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45924.
    HOVERGENi HBG018522.
    InParanoidi Q9UBU3.
    KOi K05254.
    OMAi SLGTICS.
    OrthoDBi EOG741Z4K.
    PhylomeDBi Q9UBU3.
    TreeFami TF336219.

    Enzyme and pathway databases

    Reactomei REACT_14819. Peptide ligand-binding receptors.
    REACT_18283. G alpha (q) signalling events.
    REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.

    Miscellaneous databases

    GeneWikii Ghrelin.
    GenomeRNAii 51738.
    NextBioi 55808.
    PMAP-CutDB Q9UBU3.
    PROi Q9UBU3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBU3.
    Bgeei Q9UBU3.
    CleanExi HS_GHRL.
    Genevestigatori Q9UBU3.

    Family and domain databases

    InterProi IPR006737. Motilin_assoc.
    IPR006738. Motilin_ghrelin.
    IPR005441. Preproghrelin.
    [Graphical view ]
    PANTHERi PTHR14122. PTHR14122. 1 hit.
    Pfami PF04643. Motilin_assoc. 1 hit.
    PF04644. Motilin_ghrelin. 1 hit.
    [Graphical view ]
    PRINTSi PR01624. GHRELIN.
    ProtoNeti Search...

    Publicationsi

    1. "Ghrelin is a growth-hormone-releasing acylated peptide from stomach."
      Kojima M., Hosoda H., Date Y., Nakazato M., Matsuo H., Kangawa K.
      Nature 402:656-660(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ACYLATION AT SER-26.
      Tissue: Stomach.
    2. "Identification and characterization of a novel gastric peptide hormone: the motilin-related peptide."
      Tomasetto C., Karam S.M., Ribieras S., Masson R., Lefebvre O., Staub A., Alexander G., Chenard M.-P., Rio M.-C.
      Gastroenterology 119:395-405(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 24-33.
      Tissue: Stomach.
    3. "Genomic organization of the human Ghrelin gene."
      Wajnrajch M.P., Ten I.S., Gertner J.M., Leibel R.L.
      J. Endocr. Genet. 1:231-233(2000)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Structural divergence of human ghrelin. Identification of multiple ghrelin-derived molecules produced by post-translational processing."
      Hosoda H., Kojima M., Mizushima T., Shimizu S., Kangawa K.
      J. Biol. Chem. 278:64-70(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, ACYLATION AT SER-26, MASS SPECTROMETRY.
      Tissue: Stomach.
    5. "Revised genomic structure of the human ghrelin gene and identification of novel exons, alternative splice variants and natural antisense transcripts."
      Seim I., Collet C., Herington A.C., Chopin L.K.
      BMC Genomics 8:298-298(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
      Tissue: Heart, Kidney, Placenta and Stomach.
    6. "Identification and expression pattern of an exon 3-deleted proghrelin variant in the prostate."
      Jeffery P.L., Herington A.C., Chopin L.K.
      Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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] (ISOFORM 1), VARIANT MET-72.
      Tissue: Blood.
    11. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-38.
    12. "Ghrelin: discovery of the natural endogenous ligand for the growth hormone secretagogue receptor."
      Kojima M., Hosoda H., Matsuo H., Kangawa K.
      Trends Endocrinol. Metab. 12:118-122(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiGHRL_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBU3
    Secondary accession number(s): A8CF34
    , A8CF38, A8CF42, A8DN29, A8DN30, Q86YP8, Q8TAT9, Q9H3R3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 13, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 145 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

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

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3