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Q9UBU3 (GHRL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Ghrelin-27
  2. Ghrelin-28
    Short name=Ghrelin
  3. Obestatin
Gene names
Name:GHRL
Synonyms:MTLRP
ORF Names:UNQ524/PRO1066
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Secreted.

Tissue specificity

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. Ref.4

Post-translational modification

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 (Ref.1).

Amidation of Leu-98 is essential for obestatin activity By similarity.

Sequence similarities

Belongs to the motilin family.

Mass spectrometry

Molecular mass is 3398.9±0.3 Da from positions 24 - 51. Determined by ESI. Ghrelin-28-C10, O-decanoylated form. Ref.4

Molecular mass is 3397.2±0.5 Da from positions 24 - 51. Determined by ESI. Ghrelin-28-C10:1, O-decenoylated form. Ref.4

Molecular mass is 3371.3±0.1 Da from positions 24 - 51. Determined by ESI. Ghrelin-28-C8, O-octanoylated form. Ref.4

Molecular mass is 3243.6±0.4 Da from positions 24 - 50. Determined by ESI. Ghrelin-27-C10, O-decanoylated form. Ref.4

Molecular mass is 3214.6±0.6 Da from positions 24 - 50. Determined by ESI. Ghrelin-27-C8, O-octanoylated form. Ref.4

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   Molecular functionHormone
   PTMAmidation
Lipoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

actin polymerization or depolymerization

Inferred from direct assay PubMed 15232612. Source: UniProtKB

activation of MAPK activity

Inferred from mutant phenotype PubMed 15350694. Source: UniProtKB

adult feeding behavior

Inferred from sequence or structural similarity. Source: HGNC

cartilage development

Non-traceable author statement PubMed 15576457. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

cortisol secretion

Non-traceable author statement PubMed 17201814. Source: UniProtKB

decidualization

Inferred from direct assay PubMed 17494105. Source: UniProtKB

dendrite development

Inferred from direct assay PubMed 16491079. Source: MGI

gastric acid secretion

Inferred from electronic annotation. Source: Ensembl

glucose metabolic process

Non-traceable author statement PubMed 17392603. Source: UniProtKB

growth hormone secretion

Traceable author statement PubMed 16511605. Source: HGNC

hormone-mediated signaling pathway

Traceable author statement PubMed 16511605. Source: HGNC

negative regulation of angiogenesis

Non-traceable author statement PubMed 15572208. Source: UniProtKB

negative regulation of apoptotic process

Inferred from direct assay PubMed 15158140. Source: UniProtKB

negative regulation of circadian sleep/wake cycle, REM sleep

Inferred from direct assay PubMed 18329818. Source: BHF-UCL

negative regulation of endothelial cell proliferation

Inferred from direct assay PubMed 15572208. Source: UniProtKB

negative regulation of inflammatory response

Inferred from direct assay PubMed 15232612. Source: UniProtKB

negative regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-1 beta production

Inferred from direct assay PubMed 15232612. Source: UniProtKB

negative regulation of interleukin-6 biosynthetic process

Inferred from direct assay PubMed 15232612. Source: UniProtKB

negative regulation of locomotion

Inferred from electronic annotation. Source: Ensembl

negative regulation of tumor necrosis factor biosynthetic process

Inferred from direct assay PubMed 15232612. Source: UniProtKB

positive regulation of appetite

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of circadian sleep/wake cycle, non-REM sleep

Inferred from direct assay PubMed 18329818. Source: BHF-UCL

positive regulation of corticotropin secretion

Inferred from direct assay PubMed 12566947. Source: BHF-UCL

positive regulation of cortisol secretion

Inferred from direct assay PubMed 12566947PubMed 18329818. Source: BHF-UCL

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of growth hormone receptor signaling pathway

Inferred by curator PubMed 12566947. Source: BHF-UCL

positive regulation of growth hormone secretion

Inferred from direct assay PubMed 12566947PubMed 18329818. Source: BHF-UCL

positive regulation of insulin secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of multicellular organism growth

Inferred by curator PubMed 16511605. Source: HGNC

positive regulation of protein tyrosine kinase activity

Inferred from mutant phenotype PubMed 15350694. Source: GOC

positive regulation of synapse assembly

Inferred from direct assay PubMed 16491079. Source: MGI

regulation of cell proliferation

Inferred from direct assay PubMed 15564328PubMed 16394173. Source: UniProtKB

regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from direct assay PubMed 15292338. Source: UniProtKB

response to hormone

Inferred from direct assay PubMed 15232612. Source: UniProtKB

   Cellular_componentaxon

Inferred from direct assay PubMed 17113048. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Inferred from direct assay PubMed 17392603. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 15039149PubMed 15531532. Source: UniProtKB

secretory granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionG-protein coupled receptor binding

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

ghrelin receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

growth hormone-releasing hormone activity

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

protein tyrosine kinase activator activity

Inferred from mutant phenotype PubMed 15350694. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UBU3-1)

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.
Isoform 2 (identifier: Q9UBU3-2)

Also known as: des-Gln14-ghrelin;

The sequence of this isoform differs from the canonical sequence as follows:
     37-37: Missing.
Isoform 3 (identifier: Q9UBU3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRVQ → MFTCWWSYLRSTLAAVPGEASRVQ
Isoform 4 (identifier: Q9UBU3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRVQ → MFTCWWSYLRSTLAAVPGEASRVQ
     37-37: Missing.
Isoform 5 (identifier: Q9UBU3-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: MPSPGTVCSL...EGAEDELEVR → MFTCWWSYLRSTLAAVPGEASRVQ
Isoform 6 (identifier: Q9UBU3-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.2 Ref.11
Peptide24 – 5128Ghrelin-28
PRO_0000019202
Peptide24 – 5027Ghrelin-27
PRO_0000019203
Propeptide52 – 7524Removed in mature form
PRO_0000019204
Peptide76 – 9823Obestatin By similarity
PRO_0000045140
Propeptide99 – 11719Removed in mature form By similarity
PRO_0000045141

Amino acid modifications

Modified residue981Leucine amide By similarity
Lipidation261O-decanoyl serine; alternate
Lipidation261O-octanoyl serine; alternate

Natural variations

Alternative sequence1 – 7575MPSPG…ELEVR → MFTCWWSYLRSTLAAVPGEA SRVQ in isoform 5.
VSP_041438
Alternative sequence1 – 3636MPSPG…HQRVQ → MFTCWWSYLRSTLAAVPGEA SRVQ in isoform 3 and isoform 4.
VSP_041437
Alternative sequence371Missing in isoform 2 and isoform 4.
VSP_003245
Alternative sequence76 – 11742FNAPF…APADK → RPQPTSDRPQALLTSL in isoform 6.
VSP_047642
Natural variant721L → M. Ref.10
Corresponds to variant rs696217 [ dbSNP | Ensembl ].
VAR_050095
Natural variant901Q → L.
Corresponds to variant rs4684677 [ dbSNP | Ensembl ].
VAR_029135

Secondary structure

.................... 117
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Ghrelin) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 39C0572EBECA2755

FASTA11712,911
        10         20         30         40         50         60 
MPSPGTVCSL LLLGMLWLDL AMAGSSFLSP EHQRVQQRKE SKKPPAKLQP RALAGWLRPE 

        70         80         90        100        110 
DGGQAEGAED ELEVRFNAPF DVGIKLSGVQ YQQHSQALGK FLQDILWEEA KEAPADK 

« Hide

Isoform 2 (des-Gln14-ghrelin) [UniParc].

Checksum: F0DEBEEE880DC951
Show »

FASTA11612,783
Isoform 3 [UniParc].

Checksum: 9E4000D6A0863F99
Show »

FASTA10511,784
Isoform 4 [UniParc].

Checksum: 508946F0C415058F
Show »

FASTA10411,656
Isoform 5 [UniParc].

Checksum: 5001F0A57716C83D
Show »

FASTA667,460
Isoform 6 [UniParc].

Checksum: E7E532D32A3F8609
Show »

FASTA919,972

References

« Hide 'large scale' references
[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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS33700.1. [Q9UBU3-1]
CCDS46747.1. [Q9UBU3-5]
CCDS46748.1. [Q9UBU3-3]
CCDS46749.1. [Q9UBU3-4]
CCDS46750.1. [Q9UBU3-2]
PIRA59316.
RefSeqNP_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]
UniGeneHs.590080.
Hs.672979.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P7Xmodel-A1-117[»]
ProteinModelPortalQ9UBU3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119706. 4 interactions.
STRING9606.ENSP00000335074.

Chemistry

BindingDBQ9UBU3.
ChEMBLCHEMBL1921664.

PTM databases

PhosphoSiteQ9UBU3.

Polymorphism databases

DMDM17865471.

Proteomic databases

PaxDbQ9UBU3.
PRIDEQ9UBU3.

Protocols and materials databases

DNASU51738.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287656; 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]
ENST00000449554; ENSP00000415521; ENSG00000157017. [Q9UBU3-2]
ENST00000450603; ENSP00000389192; ENSG00000157017. [Q9UBU3-1]
ENST00000457360; ENSP00000391406; ENSG00000157017. [Q9UBU3-1]
GeneID51738.
KEGGhsa:51738.
UCSCuc010hdc.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

CTD51738.
GeneCardsGC03M010302.
HGNCHGNC:18129. GHRL.
HPACAB022731.
HPA014246.
MIM605353. gene.
neXtProtNX_Q9UBU3.
PharmGKBPA142671740.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45924.
HOVERGENHBG018522.
InParanoidQ9UBU3.
KOK05254.
OMASLGTICS.
OrthoDBEOG741Z4K.
PhylomeDBQ9UBU3.
TreeFamTF336219.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9UBU3.
BgeeQ9UBU3.
CleanExHS_GHRL.
GenevestigatorQ9UBU3.

Family and domain databases

InterProIPR006737. Motilin_assoc.
IPR006738. Motilin_ghrelin.
IPR005441. Preproghrelin.
[Graphical view]
PANTHERPTHR14122. PTHR14122. 1 hit.
PfamPF04643. Motilin_assoc. 1 hit.
PF04644. Motilin_ghrelin. 1 hit.
[Graphical view]
PRINTSPR01624. GHRELIN.
ProtoNetSearch...

Other

GeneWikiGhrelin.
GenomeRNAi51738.
NextBio55808.
PMAP-CutDBQ9UBU3.
PROQ9UBU3.
SOURCESearch...

Entry information

Entry nameGHRL_HUMAN
AccessionPrimary (citable) accession number: Q9UBU3
Secondary accession number(s): A8CF34 expand/collapse secondary AC list , A8CF38, A8CF42, A8DN29, A8DN30, Q86YP8, Q8TAT9, Q9H3R3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM