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Growth hormone receptor (GH receptor) (Somatotropin receptor) [Cleaved into: Growth hormone-binding protein (GH-binding protein) (GHBP) (Serum-binding protein)]

 GHR_HUMAN               Reviewed;         638 AA.
P10912; Q9HCX2;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
30-AUG-2017, entry version 205.
RecName: Full=Growth hormone receptor;
Short=GH receptor;
AltName: Full=Somatotropin receptor;
Contains:
RecName: Full=Growth hormone-binding protein;
Short=GH-binding protein;
Short=GHBP;
AltName: Full=Serum-binding protein;
Flags: Precursor;
Name=GHR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=2825030; DOI=10.1038/330537a0;
Leung D.W., Spencer S.A., Cachianes G., Hammonds R.G., Collins C.,
Henzel W.J., Barnard R., Waters M.J., Wood W.I.;
"Growth hormone receptor and serum binding protein: purification,
cloning and expression.";
Nature 330:537-543(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT LEU-544.
PubMed=2813379; DOI=10.1073/pnas.86.20.8083;
Godowski P.J., Leung D.W., Meacham L.R., Galgani J.P., Hellmiss R.,
Keret R., Rotwein P.S., Parks J.S., Laron Z., Wood W.I.;
"Characterization of the human growth hormone receptor gene and
demonstration of a partial gene deletion in two patients with Laron-
type dwarfism.";
Proc. Natl. Acad. Sci. U.S.A. 86:8083-8087(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Placenta;
PubMed=1569971; DOI=10.1210/mend.6.2.1569971;
Urbanek M., MacLeod J.N., Cooke N.E., Liebhaber S.A.;
"Expression of a human growth hormone (hGH) receptor isoform is
predicted by tissue-specific alternative splicing of exon 3 of the hGH
receptor gene transcript.";
Mol. Endocrinol. 6:279-287(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Liver;
PubMed=8855247; DOI=10.1073/pnas.93.20.10723;
Dastot F., Sobrier M.-L., Duquesnoy P., Duriez B., Goossens M.,
Amselem S.;
"Alternatively spliced forms in the cytoplasmic domain of the human
growth hormone (GH) receptor regulate its ability to generate a
soluble GH-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 93:10723-10728(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9360546; DOI=10.1210/jcem.82.11.4358;
Amit T., Bergman T., Dastot F., Youdim M.B.H., Amselem S.,
Hochberg Z.;
"A membrane-fixed, truncated isoform of the human growth hormone
receptor.";
J. Clin. Endocrinol. Metab. 82:3813-3817(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Liver;
PubMed=9058373; DOI=10.1210/mend.11.3.9901;
Ross R.J., Esposito N., Shen X.Y., Von Laue S., Chew S.L.,
Dobson P.R., Postel-Vinay M.-C., Finidori J.;
"A short isoform of the human growth hormone receptor functions as a
dominant negative inhibitor of the full-length receptor and generates
large amounts of binding protein.";
Mol. Endocrinol. 11:265-273(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-336.
Orlovsky I.V., Borovikova I.E., Rubtsov P.M.;
"Comparing of nucleotide sequences of alternatively spliced region of
mammalian growth hormone receptor genes.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[8]
CHARACTERIZATION (ISOFORM 4).
PubMed=8360189;
Urbanek M., Russell J.E., Cooke N.E., Liebhaber S.A.;
"Functional characterization of the alternatively spliced, placental
human growth hormone receptor.";
J. Biol. Chem. 268:19025-19032(1993).
[9]
MOLECULAR MECHANISM OF PRODUCTION (ISOFORM 4).
PubMed=10764769; DOI=10.1074/jbc.M001615200;
Pantel J., Machinis K., Sobrier M.-L., Duquesnoy P., Goossens M.,
Amselem S.;
"Species-specific alternative splice mimicry at the growth hormone
receptor locus revealed by the lineage of retroelements during primate
evolution.";
J. Biol. Chem. 275:18664-18669(2000).
[10]
DISULFIDE BONDS.
PubMed=2406245;
Fuh G., Mulkerrin M.G., Bass S., McFarland N., Brochier M.,
Bourrel J.H., Light D.R., Wells J.A.;
"The human growth hormone receptor. Secretion from Escherichia coli
and disulfide bonding pattern of the extracellular binding domain.";
J. Biol. Chem. 265:3111-3115(1990).
[11]
SITE CRITICAL TO PROTEOLYSIS, AND MUTAGENESIS OF GLU-260; GLU-261 AND
ASP-262.
PubMed=11785980; DOI=10.1006/bbrc.2001.6261;
Conte F., Salles J.P., Raynal P., Fernandez L., Molinas C., Tauber M.,
Bieth E.;
"Identification of a region critical for proteolysis of the human
growth hormone receptor.";
Biochem. Biophys. Res. Commun. 290:851-857(2002).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 19-254 IN COMPLEX WITH GROWTH
HORMONE.
PubMed=1549776; DOI=10.1126/science.1549776;
de Vos A.M., Ultsch M., Kossiakoff A.A.;
"Human growth hormone and extracellular domain of its receptor:
crystal structure of the complex.";
Science 255:306-312(1992).
[14]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-256 IN COMPLEX WITH GROWTH
HORMONE.
PubMed=8943276; DOI=10.1074/jbc.271.50.32197;
Sundstroem M., Lundqvist T., Roedin J., Giebel L.B., Milligan D.,
Norstedt G.;
"Crystal structure of an antagonist mutant of human growth hormone,
G120R, in complex with its receptor at 2.9-A resolution.";
J. Biol. Chem. 271:32197-32203(1996).
[15]
VARIANT LARS SER-114.
PubMed=2779634; DOI=10.1056/NEJM198910123211501;
Amselem S., Duquesnoy P., Attree O., Novelli G., Bousnina S.,
Postel-Vinay M.-C., Goossens M.;
"Laron dwarfism and mutations of the growth hormone-receptor gene.";
N. Engl. J. Med. 321:989-995(1989).
[16]
VARIANT LARS PHE-440.
PubMed=8421103; DOI=10.1210/jcem.76.1.8421103;
Kou K., Lajara R., Rotwein P.;
"Amino acid substitutions in the intracellular part of the growth
hormone receptor in a patient with the Laron syndrome.";
J. Clin. Endocrinol. Metab. 76:54-59(1993).
[17]
VARIANTS LARS LYS-89; GLN-149; ASP-162; CYS-179 AND GLY-229.
PubMed=8504296; DOI=10.1093/hmg/2.4.355;
Amselem S., Duquesnoy P., Duriez B., Dastot F., Sobrier M.-L.,
Valleix S., Goossens M.;
"Spectrum of growth hormone receptor mutations and associated
haplotypes in Laron syndrome.";
Hum. Mol. Genet. 2:355-359(1993).
[18]
CHARACTERIZATION OF VARIANT LARS SER-114.
PubMed=8450064; DOI=10.1172/JCI116304;
Edery M., Rozakis-Adcock M., Goujon L., Finidori J., Levi-Meyrueis C.,
Paly J., Djiane J., Postel-Vinay M.-C., Kelly P.A.;
"Lack of hormone binding in COS-7 cells expressing a mutated growth
hormone receptor found in Laron dwarfism.";
J. Clin. Invest. 91:838-844(1993).
[19]
VARIANT LARS HIS-170.
PubMed=8137822;
Duquesnoy P., Sobrier M.-L., Duriez B., Dastot F., Buchanan C.R.,
Savage M.O., Preece M.A., Craescu C.T., Blouquit Y., Goossens M.,
Amselem S.;
"A single amino acid substitution in the exoplasmic domain of the
human growth hormone (GH) receptor confers familial GH resistance
(Laron syndrome) with positive GH-binding activity by abolishing
receptor homodimerization.";
EMBO J. 13:1386-1395(1994).
[20]
VARIANTS GHIP LYS-62 AND CYS-179, AND VARIANTS HIS-229 AND ASP-242.
PubMed=7565946; DOI=10.1056/NEJM199510263331701;
Goddard A.D., Covello R., Luoh S.-M., Clackson T., Attie K.M.,
Gesundheit N., Rundle A.C., Wells J.A., Carlsson L.M.S.;
"Mutations of the growth hormone receptor in children with idiopathic
short stature.";
N. Engl. J. Med. 333:1093-1098(1995).
[21]
VARIANTS LARS SER-56; LEU-58 AND ARG-68.
PubMed=9024232; DOI=10.1210/jcem.82.2.3725;
Sobrier M.-L., Dastot F., Duquesnoy P., Kandemir N., Yordam N.,
Goossens M., Amselem S.;
"Nine novel growth hormone receptor gene mutations in patients with
Laron syndrome.";
J. Clin. Endocrinol. Metab. 82:435-437(1997).
[22]
VARIANT LARS GLN-149, AND CHARACTERIZATION OF VARIANT LARS GLN-149.
PubMed=9661642; DOI=10.1210/jcem.83.7.4954;
Walker J.L., Crock P.A., Behncken S.N., Rowlinson S.W.,
Nicholson L.M., Boulton T.J.C., Waters M.J.;
"A novel mutation affecting the interdomain link region of the growth
hormone receptor in a Vietnamese girl, and response to long-term
treatment with recombinant human insulin-like growth factor-I and
luteinizing hormone-releasing hormone analogue.";
J. Clin. Endocrinol. Metab. 83:2554-2561(1998).
[23]
VARIANT ILE-162.
PubMed=9814495; DOI=10.1210/jcem.83.11.5238;
Sanchez J.E., Perera E., Baumbach L., Cleveland W.W.;
"Growth hormone receptor mutations in children with idiopathic short
stature.";
J. Clin. Endocrinol. Metab. 83:4079-4083(1998).
[24]
VARIANTS LARS HIS-170; THR-171; PRO-172 AND GLY-173, AND
CHARACTERIZATION OF VARIANTS LARS THR-171; PRO-172 AND GLY-173.
PubMed=9851797; DOI=10.1210/jcem.83.12.5357;
Wojcik J., Berg M.A., Esposito N., Geffner M.E., Sakati N.,
Reiter E.O., Dower S., Francke U., Postel-Vinay M.-C., Finidori J.;
"Four contiguous amino acid substitutions, identified in patients with
Laron syndrome, differently affect the binding affinity and
intracellular trafficking of the growth hormone receptor.";
J. Clin. Endocrinol. Metab. 83:4481-4489(1998).
[25]
VARIANTS HIS-179; HIS-229; PHE-440; THR-495; LEU-544 AND THR-579.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[26]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[27]
VARIANTS LARS CYS-226 AND ASN-262.
PubMed=10870033; DOI=10.1530/eje.0.1430071;
Enberg B., Luthman H., Segnestam K., Ritzen E.M., Sundstroem M.,
Norstedt G.;
"Characterisation of novel missense mutations in the GH receptor gene
causing severe growth retardation.";
Eur. J. Endocrinol. 143:71-76(2000).
[28]
VARIANT LEU-544.
PubMed=12910492; DOI=10.1002/ajmg.a.20172;
Takada D., Ezura Y., Ono S., Iino Y., Katayama Y., Xin Y., Wu L.L.,
Larringa-Shum S., Stephenson S.H., Hunt S.C., Hopkins P.N., Emi M.;
"Growth hormone receptor variant (L526I) modifies plasma HDL
cholesterol phenotype in familial hypercholesterolemia: intra-familial
association study in an eight-generation hyperlipidemic kindred.";
Am. J. Med. Genet. A 121:136-140(2003).
[29]
VARIANT LARS ILE-244.
PubMed=14678285; DOI=10.1111/j.1365-2265.2004.01930.x;
Jorge A.A.L., Souza S.C.A.L., Arnhold I.J.P., Mendonca B.B.;
"The first homozygous mutation (S226I) in the highly-conserved WSXWS-
like motif of the GH receptor causing Laron syndrome: suppression of
GH secretion by GnRH analogue therapy not restored by
dihydrotestosterone administration.";
Clin. Endocrinol. (Oxf.) 60:36-40(2004).
-!- FUNCTION: Receptor for pituitary gland growth hormone involved in
regulating postnatal body growth. On ligand binding, couples to
the JAK2/STAT5 pathway (By similarity). {ECO:0000250}.
-!- FUNCTION: The soluble form (GHBP) acts as a reservoir of growth
hormone in plasma and may be a modulator/inhibitor of GH
signaling.
-!- FUNCTION: Isoform 2 up-regulates the production of GHBP and acts
as a negative inhibitor of GH signaling.
-!- SUBUNIT: On growth hormone (GH) binding, forms homodimers and
binds JAK2 via a box 1-containing domain. Binding to SOCS3
inhibits JAK2 activation, binding to CIS and SOCS2 inhibits STAT5
activation. Interacts with ADAM17. {ECO:0000250}.
-!- INTERACTION:
Q16829:DUSP7; NbExp=2; IntAct=EBI-286316, EBI-1265847;
P01241:GH1; NbExp=3; IntAct=EBI-286316, EBI-1026046;
P16333:NCK1; NbExp=3; IntAct=EBI-286316, EBI-389883;
Q9JLI4:Ncoa6 (xeno); NbExp=2; IntAct=EBI-286316, EBI-286271;
P18031:PTPN1; NbExp=5; IntAct=EBI-286316, EBI-968788;
P17706:PTPN2; NbExp=8; IntAct=EBI-286316, EBI-984930;
P26045:PTPN3; NbExp=4; IntAct=EBI-286316, EBI-1047946;
P43378:PTPN9; NbExp=2; IntAct=EBI-286316, EBI-742898;
P23467:PTPRB; NbExp=3; IntAct=EBI-286316, EBI-1265766;
Q9HD43:PTPRH; NbExp=4; IntAct=EBI-286316, EBI-1267176;
Q12913:PTPRJ; NbExp=2; IntAct=EBI-286316, EBI-2264500;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Note=On growth hormone binding, GHR is ubiquitinated,
internalized, down-regulated and transported into a degradative or
non-degradative pathway. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I
membrane protein. Note=Remains fixed to the cell membrane and is
not internalized.
-!- SUBCELLULAR LOCATION: Growth hormone-binding protein: Secreted.
Note=Complexed to a substantial fraction of circulating GH.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=GHRfl;
IsoId=P10912-1; Sequence=Displayed;
Name=2; Synonyms=GHRtr, GHR1-279;
IsoId=P10912-2; Sequence=VSP_010227, VSP_010228;
Name=3; Synonyms=GHR1-277;
IsoId=P10912-3; Sequence=VSP_010229, VSP_010230;
Name=4; Synonyms=GHRd3;
IsoId=P10912-4; Sequence=VSP_010225, VSP_010226;
Note=Arises by species-specific retrovirus-mediated alternative
splice mimicry.;
-!- TISSUE SPECIFICITY: Expressed in various tissues with high
expression in liver and skeletal muscle. Isoform 4 is
predominantly expressed in kidney, bladder, adrenal gland and
brain stem. Isoform 1 expression in placenta is predominant in
chorion and decidua. Isoform 4 is highly expressed in placental
villi. Isoform 2 is expressed in lung, stomach and muscle. Low
levels in liver.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- DOMAIN: The extracellular domain is the ligand-binding domain
representing the growth hormone-binding protein (GHBP).
-!- DOMAIN: The ubiquitination-dependent endocytosis motif (UbE) is
required for recruitment of the ubiquitin conjugation system on to
the receptor and for its internalization.
-!- PTM: The soluble form (GHBP) is produced by phorbol ester-promoted
proteolytic cleavage at the cell surface (shedding) by
ADAM17/TACE. Shedding is inhibited by growth hormone (GH) binding
to the receptor probably due to a conformational change in GHR
rendering the receptor inaccessible to ADAM17 (By similarity).
{ECO:0000250}.
-!- PTM: On GH binding, phosphorylated on tyrosine residues in the
cytoplasmic domain by JAK2. {ECO:0000250}.
-!- PTM: On ligand binding, ubiquitinated on lysine residues in the
cytoplasmic domain. This ubiquitination is not sufficient for GHR
internalization (By similarity). {ECO:0000250}.
-!- POLYMORPHISM: Genetic variation in GHR may act as phenotype
modifier in familial hypercholesterolemia [MIM:143890] patients
carrying a mutation in the LDLR gene.
-!- DISEASE: Laron syndrome (LARS) [MIM:262500]: A severe form of
growth hormone insensitivity characterized by growth impairment,
short stature, dysfunctional growth hormone receptor, and failure
to generate insulin-like growth factor I in response to growth
hormone. {ECO:0000269|PubMed:10870033,
ECO:0000269|PubMed:14678285, ECO:0000269|PubMed:2779634,
ECO:0000269|PubMed:8137822, ECO:0000269|PubMed:8421103,
ECO:0000269|PubMed:8450064, ECO:0000269|PubMed:8504296,
ECO:0000269|PubMed:9024232, ECO:0000269|PubMed:9661642,
ECO:0000269|PubMed:9851797}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Growth hormone insensitivity, partial (GHIP)
[MIM:604271]: A disease characterized by partial resistance to
growth hormone resulting in short stature. Short stature is
defined by a standing height more than 2 standard deviations below
the mean (or below the 2.5 percentile) for sex and chronological
age, compared with a well-nourished, healthy, genetically relevant
population. {ECO:0000269|PubMed:7565946}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
subfamily. {ECO:0000305}.
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EMBL; X06562; CAA29808.1; -; mRNA.
EMBL; M28466; AAA52555.1; -; Genomic_DNA.
EMBL; M28458; AAA52555.1; JOINED; Genomic_DNA.
EMBL; M28459; AAA52555.1; JOINED; Genomic_DNA.
EMBL; M28460; AAA52555.1; JOINED; Genomic_DNA.
EMBL; M28461; AAA52555.1; JOINED; Genomic_DNA.
EMBL; M28462; AAA52555.1; JOINED; Genomic_DNA.
EMBL; M28463; AAA52555.1; JOINED; Genomic_DNA.
EMBL; M28464; AAA52555.1; JOINED; Genomic_DNA.
EMBL; M28465; AAA52555.1; JOINED; Genomic_DNA.
EMBL; AJ278681; CAC06613.1; -; Genomic_DNA.
CCDS; CCDS3940.1; -. [P10912-1]
CCDS; CCDS56364.1; -. [P10912-4]
PIR; A33991; A33991.
RefSeq; NP_000154.1; NM_000163.4. [P10912-1]
RefSeq; NP_001229328.1; NM_001242399.2.
RefSeq; NP_001229329.1; NM_001242400.2. [P10912-1]
RefSeq; NP_001229330.1; NM_001242401.3. [P10912-1]
RefSeq; NP_001229331.1; NM_001242402.2. [P10912-1]
RefSeq; NP_001229332.1; NM_001242403.2. [P10912-1]
RefSeq; NP_001229333.1; NM_001242404.2. [P10912-1]
RefSeq; NP_001229334.1; NM_001242405.2. [P10912-1]
RefSeq; NP_001229335.1; NM_001242406.2. [P10912-1]
RefSeq; NP_001229389.1; NM_001242460.1. [P10912-4]
RefSeq; NP_001229391.1; NM_001242462.1.
UniGene; Hs.125180; -.
UniGene; Hs.684632; -.
UniGene; Hs.688223; -.
PDB; 1A22; X-ray; 2.60 A; B=19-256.
PDB; 1AXI; X-ray; 2.10 A; B=19-254.
PDB; 1HWG; X-ray; 2.50 A; B/C=19-255.
PDB; 1HWH; X-ray; 2.90 A; B=19-255.
PDB; 1KF9; X-ray; 2.60 A; B/C/E/F=19-256.
PDB; 2AEW; X-ray; 2.70 A; A/B=47-251.
PDB; 3HHR; X-ray; 2.80 A; B/C=50-254.
PDBsum; 1A22; -.
PDBsum; 1AXI; -.
PDBsum; 1HWG; -.
PDBsum; 1HWH; -.
PDBsum; 1KF9; -.
PDBsum; 2AEW; -.
PDBsum; 3HHR; -.
DisProt; DP00033; -.
ProteinModelPortal; P10912; -.
SMR; P10912; -.
BioGrid; 108957; 41.
DIP; DIP-630N; -.
ELM; P10912; -.
IntAct; P10912; 23.
MINT; MINT-1528703; -.
STRING; 9606.ENSP00000230882; -.
ChEMBL; CHEMBL1976; -.
DrugBank; DB00082; Pegvisomant.
DrugBank; DB00052; Somatropin recombinant.
iPTMnet; P10912; -.
PhosphoSitePlus; P10912; -.
BioMuta; GHR; -.
DMDM; 121180; -.
EPD; P10912; -.
PaxDb; P10912; -.
PeptideAtlas; P10912; -.
PRIDE; P10912; -.
Ensembl; ENST00000230882; ENSP00000230882; ENSG00000112964. [P10912-1]
Ensembl; ENST00000357703; ENSP00000350335; ENSG00000112964. [P10912-4]
Ensembl; ENST00000537449; ENSP00000442206; ENSG00000112964. [P10912-1]
Ensembl; ENST00000612382; ENSP00000478332; ENSG00000112964. [P10912-1]
Ensembl; ENST00000612626; ENSP00000479846; ENSG00000112964. [P10912-1]
Ensembl; ENST00000615111; ENSP00000478291; ENSG00000112964. [P10912-1]
Ensembl; ENST00000618088; ENSP00000482373; ENSG00000112964. [P10912-1]
GeneID; 2690; -.
KEGG; hsa:2690; -.
UCSC; uc003jmt.4; human. [P10912-1]
CTD; 2690; -.
DisGeNET; 2690; -.
GeneCards; GHR; -.
HGNC; HGNC:4263; GHR.
HPA; HPA045339; -.
HPA; HPA057705; -.
MalaCards; GHR; -.
MIM; 143890; phenotype.
MIM; 262500; phenotype.
MIM; 600946; gene.
MIM; 604271; phenotype.
neXtProt; NX_P10912; -.
OpenTargets; ENSG00000112964; -.
Orphanet; 633; Laron syndrome.
Orphanet; 314802; Short stature due to partial GHR deficiency.
PharmGKB; PA28674; -.
eggNOG; ENOG410IFQI; Eukaryota.
eggNOG; ENOG410XTHJ; LUCA.
GeneTree; ENSGT00530000063112; -.
HOGENOM; HOG000015773; -.
HOVERGEN; HBG005836; -.
InParanoid; P10912; -.
KO; K05080; -.
PhylomeDB; P10912; -.
TreeFam; TF330851; -.
Reactome; R-HSA-1170546; Prolactin receptor signaling.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
SignaLink; P10912; -.
SIGNOR; P10912; -.
ChiTaRS; GHR; human.
EvolutionaryTrace; P10912; -.
GeneWiki; Growth_hormone_receptor; -.
GenomeRNAi; 2690; -.
PMAP-CutDB; P10912; -.
PRO; PR:P10912; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000112964; -.
CleanEx; HS_GHR; -.
ExpressionAtlas; P10912; baseline and differential.
Genevisible; P10912; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0070195; C:growth hormone receptor complex; IDA:CAFA.
GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0000932; C:P-body; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
GO; GO:0019838; F:growth factor binding; IPI:BHF-UCL.
GO; GO:0017046; F:peptide hormone binding; IPI:BHF-UCL.
GO; GO:0070064; F:proline-rich region binding; ISS:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; ISS:BHF-UCL.
GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:BHF-UCL.
GO; GO:0042976; P:activation of Janus kinase activity; ISS:BHF-UCL.
GO; GO:0000187; P:activation of MAPK activity; ISS:BHF-UCL.
GO; GO:0000255; P:allantoin metabolic process; ISS:BHF-UCL.
GO; GO:0032870; P:cellular response to hormone stimulus; IMP:BHF-UCL.
GO; GO:0006101; P:citrate metabolic process; ISS:BHF-UCL.
GO; GO:0006600; P:creatine metabolic process; ISS:BHF-UCL.
GO; GO:0046449; P:creatinine metabolic process; ISS:BHF-UCL.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0006631; P:fatty acid metabolic process; ISS:BHF-UCL.
GO; GO:0060396; P:growth hormone receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0006549; P:isoleucine metabolic process; ISS:BHF-UCL.
GO; GO:0007259; P:JAK-STAT cascade; ISS:BHF-UCL.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; TAS:Reactome.
GO; GO:0044236; P:multicellular organism metabolic process; IMP:BHF-UCL.
GO; GO:0006107; P:oxaloacetate metabolic process; ISS:BHF-UCL.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:BHF-UCL.
GO; GO:0031623; P:receptor internalization; IDA:BHF-UCL.
GO; GO:0040014; P:regulation of multicellular organism growth; ISS:BHF-UCL.
GO; GO:0046898; P:response to cycloheximide; IDA:BHF-UCL.
GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL.
GO; GO:0006105; P:succinate metabolic process; ISS:BHF-UCL.
GO; GO:0019530; P:taurine metabolic process; ISS:BHF-UCL.
GO; GO:0006573; P:valine metabolic process; ISS:BHF-UCL.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR025871; GHBP.
InterPro; IPR015152; Growth/epo_recpt_lig-bind.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003528; Long_hematopoietin_rcpt_CS.
Pfam; PF09067; EpoR_lig-bind; 1.
Pfam; PF00041; fn3; 1.
Pfam; PF12772; GHBP; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 1.
PROSITE; PS01352; HEMATOPO_REC_L_F1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond; Dwarfism;
Endocytosis; Glycoprotein; Membrane; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 638 Growth hormone receptor.
/FTId=PRO_0000010957.
CHAIN 19 256 Growth hormone-binding protein.
{ECO:0000250}.
/FTId=PRO_0000010958.
TOPO_DOM 19 264 Extracellular. {ECO:0000255}.
TRANSMEM 265 288 Helical. {ECO:0000255}.
TOPO_DOM 289 638 Cytoplasmic. {ECO:0000255}.
DOMAIN 151 254 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 260 262 Required for ADAM17-mediated proteolysis.
{ECO:0000250}.
MOTIF 240 244 WSXWS motif.
MOTIF 297 305 Box 1 motif.
MOTIF 340 349 UbE motif.
SITE 345 345 Required for endocytosis and down-
regulation. {ECO:0000250}.
MOD_RES 341 341 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 56 66 {ECO:0000269|PubMed:2406245}.
DISULFID 101 112 {ECO:0000269|PubMed:2406245}.
DISULFID 126 140 {ECO:0000269|PubMed:2406245}.
VAR_SEQ 24 24 A -> D (in isoform 4).
{ECO:0000303|PubMed:1569971}.
/FTId=VSP_010225.
VAR_SEQ 25 46 Missing (in isoform 4).
{ECO:0000303|PubMed:1569971}.
/FTId=VSP_010226.
VAR_SEQ 292 297 RIKMLI -> SSSSKD (in isoform 2).
{ECO:0000303|PubMed:8855247,
ECO:0000303|PubMed:9058373,
ECO:0000303|PubMed:9360546}.
/FTId=VSP_010227.
VAR_SEQ 292 294 RIK -> KEN (in isoform 3).
{ECO:0000303|PubMed:9058373}.
/FTId=VSP_010229.
VAR_SEQ 295 638 Missing (in isoform 3).
{ECO:0000303|PubMed:9058373}.
/FTId=VSP_010230.
VAR_SEQ 298 638 Missing (in isoform 2).
{ECO:0000303|PubMed:8855247,
ECO:0000303|PubMed:9058373,
ECO:0000303|PubMed:9360546}.
/FTId=VSP_010228.
VARIANT 56 56 C -> S (in LARS).
{ECO:0000269|PubMed:9024232}.
/FTId=VAR_018426.
VARIANT 58 58 S -> L (in LARS).
{ECO:0000269|PubMed:9024232}.
/FTId=VAR_018427.
VARIANT 62 62 E -> K (in GHIP; dbSNP:rs121909361).
{ECO:0000269|PubMed:7565946}.
/FTId=VAR_002708.
VARIANT 68 68 W -> R (in LARS).
{ECO:0000269|PubMed:9024232}.
/FTId=VAR_018428.
VARIANT 89 89 R -> K (in LARS).
{ECO:0000269|PubMed:8504296}.
/FTId=VAR_002709.
VARIANT 114 114 F -> S (in LARS; loss of ability to bind
ligand; dbSNP:rs121909357).
{ECO:0000269|PubMed:2779634,
ECO:0000269|PubMed:8450064}.
/FTId=VAR_002710.
VARIANT 143 143 V -> A (in LARS).
/FTId=VAR_002711.
VARIANT 149 149 P -> Q (in LARS; disrupts GH binding;
dbSNP:rs121909365).
{ECO:0000269|PubMed:8504296,
ECO:0000269|PubMed:9661642}.
/FTId=VAR_018429.
VARIANT 162 162 V -> D (in LARS).
{ECO:0000269|PubMed:8504296}.
/FTId=VAR_002712.
VARIANT 162 162 V -> F (in dbSNP:rs6413484).
/FTId=VAR_020002.
VARIANT 162 162 V -> I (found in a patient with
idiopathic short stature; unknown
pathological significance;
dbSNP:rs6413484).
{ECO:0000269|PubMed:9814495}.
/FTId=VAR_018430.
VARIANT 170 170 D -> H (in LARS; abolishes receptor
homodimerization; dbSNP:rs121909366).
{ECO:0000269|PubMed:8137822,
ECO:0000269|PubMed:9851797}.
/FTId=VAR_002713.
VARIANT 171 171 I -> T (in LARS; almost completely
abolishes GH-binding at cell surface: 53%
binding to membrane fractions;
dbSNP:rs121909367).
{ECO:0000269|PubMed:9851797}.
/FTId=VAR_018431.
VARIANT 172 172 Q -> P (in LARS; almost completely
abolishes GH-binding at cell surface and
in membrane fractions;
dbSNP:rs121909368).
{ECO:0000269|PubMed:9851797}.
/FTId=VAR_018432.
VARIANT 173 173 V -> G (in LARS; almost completely
abolishes GH-binding at cell surface: 26%
binding to membrane fractions;
dbSNP:rs121909369).
{ECO:0000269|PubMed:9851797}.
/FTId=VAR_018433.
VARIANT 179 179 R -> C (in LARS and GHIP;
dbSNP:rs121909362).
{ECO:0000269|PubMed:7565946,
ECO:0000269|PubMed:8504296}.
/FTId=VAR_002714.
VARIANT 179 179 R -> H (in dbSNP:rs6181).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013937.
VARIANT 226 226 Y -> C (in LARS).
{ECO:0000269|PubMed:10870033}.
/FTId=VAR_018434.
VARIANT 229 229 R -> G (in LARS).
{ECO:0000269|PubMed:8504296}.
/FTId=VAR_002715.
VARIANT 229 229 R -> H (found in a patient with
idiopathic short stature; unknown
pathological significance; dbSNP:rs6177).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:7565946}.
/FTId=VAR_013938.
VARIANT 242 242 E -> D (found in a patient with
idiopathic short stature; unknown
pathological significance;
dbSNP:rs45588036).
{ECO:0000269|PubMed:7565946}.
/FTId=VAR_002716.
VARIANT 244 244 S -> I (in LARS).
{ECO:0000269|PubMed:14678285}.
/FTId=VAR_018435.
VARIANT 262 262 D -> N (in LARS).
{ECO:0000269|PubMed:10870033}.
/FTId=VAR_018436.
VARIANT 440 440 C -> F (in LARS; dbSNP:rs6182).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:8421103}.
/FTId=VAR_013939.
VARIANT 465 465 E -> K (in dbSNP:rs34283856).
/FTId=VAR_032704.
VARIANT 495 495 P -> T (in dbSNP:rs6183).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013940.
VARIANT 544 544 I -> L (polymorphism with a modifier
effect on plasma HDL cholesterol levels
in familial hypercholesterolemia
patients; dbSNP:rs6180).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:12910492,
ECO:0000269|PubMed:2813379}.
/FTId=VAR_013941.
VARIANT 579 579 P -> T (in dbSNP:rs6184).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013942.
MUTAGEN 260 260 E->A: No change in shedding activity: No
change in hormone binding.
{ECO:0000269|PubMed:11785980}.
MUTAGEN 261 261 E->A: No change in shedding activity: No
change in hormone binding.
{ECO:0000269|PubMed:11785980}.
MUTAGEN 262 262 D->A: No change in shedding activity: No
change in hormone binding.
{ECO:0000269|PubMed:11785980}.
STRAND 53 62 {ECO:0000244|PDB:1AXI}.
STRAND 64 68 {ECO:0000244|PDB:1AXI}.
STRAND 83 88 {ECO:0000244|PDB:1AXI}.
TURN 93 96 {ECO:0000244|PDB:1HWG}.
TURN 104 107 {ECO:0000244|PDB:3HHR}.
STRAND 111 114 {ECO:0000244|PDB:1AXI}.
HELIX 116 118 {ECO:0000244|PDB:1AXI}.
STRAND 121 131 {ECO:0000244|PDB:1AXI}.
STRAND 134 142 {ECO:0000244|PDB:1AXI}.
HELIX 143 146 {ECO:0000244|PDB:1AXI}.
STRAND 153 159 {ECO:0000244|PDB:1AXI}.
STRAND 167 176 {ECO:0000244|PDB:1AXI}.
TURN 183 186 {ECO:0000244|PDB:1AXI}.
STRAND 190 198 {ECO:0000244|PDB:1AXI}.
STRAND 210 221 {ECO:0000244|PDB:1AXI}.
STRAND 226 234 {ECO:0000244|PDB:1AXI}.
STRAND 240 243 {ECO:0000244|PDB:2AEW}.
STRAND 247 249 {ECO:0000244|PDB:1AXI}.
SEQUENCE 638 AA; 71500 MW; EAF77EADE4787822 CRC64;
MDLWQLLLTL ALAGSSDAFS GSEATAAILS RAPWSLQSVN PGLKTNSSKE PKFTKCRSPE
RETFSCHWTD EVHHGTKNLG PIQLFYTRRN TQEWTQEWKE CPDYVSAGEN SCYFNSSFTS
IWIPYCIKLT SNGGTVDEKC FSVDEIVQPD PPIALNWTLL NVSLTGIHAD IQVRWEAPRN
ADIQKGWMVL EYELQYKEVN ETKWKMMDPI LTTSVPVYSL KVDKEYEVRV RSKQRNSGNY
GEFSEVLYVT LPQMSQFTCE EDFYFPWLLI IIFGIFGLTV MLFVFLFSKQ QRIKMLILPP
VPVPKIKGID PDLLKEGKLE EVNTILAIHD SYKPEFHSDD SWVEFIELDI DEPDEKTEES
DTDRLLSSDH EKSHSNLGVK DGDSGRTSCC EPDILETDFN ANDIHEGTSE VAQPQRLKGE
ADLLCLDQKN QNNSPYHDAC PATQQPSVIQ AEKNKPQPLP TEGAESTHQA AHIQLSNPSS
LSNIDFYAQV SDITPAGSVV LSPGQKNKAG MSQCDMHPEM VSLCQENFLM DNAYFCEADA
KKCIPVAPHI KVESHIQPSL NQEDIYITTE SLTTAAGRPG TGEHVPGSEM PVPDYTSIHI
VQSPQGLILN ATALPLPDKE FLSSCGYVST DQLNKIMP


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