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Q9UBU3

- GHRL_HUMAN

UniProt

Q9UBU3 - GHRL_HUMAN

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Protein

Appetite-regulating hormone

Gene

GHRL

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9UBU3.
CleanExiHS_GHRL.
ExpressionAtlasiQ9UBU3. baseline and differential.
GenevestigatoriQ9UBU3.

Organism-specific databases

HPAiCAB022731.
HPA014246.

Interactioni

Protein-protein interaction databases

BioGridi119706. 4 interactions.
STRINGi9606.ENSP00000335074.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000004064.
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

        10         20         30         40         50
MPSPGTVCSL LLLGMLWLDL AMAGSSFLSP EHQRVQQRKE SKKPPAKLQP
60 70 80 90 100
RALAGWLRPE DGGQAEGAED ELEVRFNAPF DVGIKLSGVQ YQQHSQALGK
110
FLQDILWEEA KEAPADK
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:
EMBLi
GenBanki
DDBJi
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.
UCSCiuc003bvj.1. human.
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]

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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 uc003bvj.1. human.
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.
GeneTreei ENSGT00390000004064.
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

Bgeei Q9UBU3.
CleanExi HS_GHRL.
ExpressionAtlasi Q9UBU3. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 147 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