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Protein

Growth hormone receptor

Gene

GHR

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

Functioni

Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to the JAK2/STAT5 pathway (By similarity).By similarity
The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling.
Isoform 2 up-regulates the production of GHBP and acts as a negative inhibitor of GH signaling.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei345Required for endocytosis and down-regulationBy similarity1

GO - Molecular functioni

  • cytokine receptor activity Source: InterPro
  • growth factor binding Source: BHF-UCL
  • peptide hormone binding Source: BHF-UCL
  • proline-rich region binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • protein kinase binding Source: BHF-UCL

GO - Biological processi

  • 2-oxoglutarate metabolic process Source: BHF-UCL
  • activation of JAK2 kinase activity Source: BHF-UCL
  • activation of MAPK activity Source: BHF-UCL
  • allantoin metabolic process Source: BHF-UCL
  • cellular response to hormone stimulus Source: BHF-UCL
  • citrate metabolic process Source: BHF-UCL
  • creatine metabolic process Source: BHF-UCL
  • creatinine metabolic process Source: BHF-UCL
  • endocytosis Source: UniProtKB-KW
  • fatty acid metabolic process Source: BHF-UCL
  • growth hormone receptor signaling pathway Source: BHF-UCL
  • insulin-like growth factor receptor signaling pathway Source: BHF-UCL
  • isoleucine metabolic process Source: BHF-UCL
  • JAK-STAT cascade Source: BHF-UCL
  • JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
  • multicellular organism metabolic process Source: BHF-UCL
  • oxaloacetate metabolic process Source: BHF-UCL
  • positive regulation of multicellular organism growth Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of Stat5 protein Source: BHF-UCL
  • receptor internalization Source: BHF-UCL
  • regulation of multicellular organism growth Source: BHF-UCL
  • response to cycloheximide Source: BHF-UCL
  • response to estradiol Source: BHF-UCL
  • succinate metabolic process Source: BHF-UCL
  • taurine metabolic process Source: BHF-UCL
  • valine metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000112964-MONOMER.
ReactomeiR-HSA-1170546. Prolactin receptor signaling.
R-HSA-982772. Growth hormone receptor signaling.
SignaLinkiP10912.
SIGNORiP10912.

Names & Taxonomyi

Protein namesi
Recommended name:
Growth hormone receptor
Short name:
GH receptor
Alternative name(s):
Somatotropin receptor
Cleaved into the following chain:
Growth hormone-binding protein
Short name:
GH-binding protein
Short name:
GHBP
Alternative name(s):
Serum-binding protein
Gene namesi
Name:GHR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:4263. GHR.

Subcellular locationi

Isoform 2 :
Growth hormone-binding protein :
  • Secreted

  • Note: Complexed to a substantial fraction of circulating GH.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 264ExtracellularSequence analysisAdd BLAST246
Transmembranei265 – 288HelicalSequence analysisAdd BLAST24
Topological domaini289 – 638CytoplasmicSequence analysisAdd BLAST350

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • growth hormone receptor complex Source: BHF-UCL
  • integral component of membrane Source: BHF-UCL
  • integral component of plasma membrane Source: BHF-UCL
  • intracellular Source: GOC
  • plasma membrane Source: Reactome
  • receptor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Laron syndrome (LARS)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:262500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01842656C → S in LARS. 1 Publication1
Natural variantiVAR_01842758S → L in LARS. 1 Publication1
Natural variantiVAR_01842868W → R in LARS. 1 Publication1
Natural variantiVAR_00270989R → K in LARS. 1 Publication1
Natural variantiVAR_002710114F → S in LARS; loss of ability to bind ligand. 2 PublicationsCorresponds to variant rs121909357dbSNPEnsembl.1
Natural variantiVAR_002711143V → A in LARS. 1
Natural variantiVAR_018429149P → Q in LARS; disrupts GH binding. 2 PublicationsCorresponds to variant rs121909365dbSNPEnsembl.1
Natural variantiVAR_002712162V → D in LARS. 1 Publication1
Natural variantiVAR_002713170D → H in LARS; abolishes receptor homodimerization. 2 PublicationsCorresponds to variant rs121909366dbSNPEnsembl.1
Natural variantiVAR_018431171I → T in LARS; almost completely abolishes GH-binding at cell surface: 53% binding to membrane fractions. 1 PublicationCorresponds to variant rs121909367dbSNPEnsembl.1
Natural variantiVAR_018432172Q → P in LARS; almost completely abolishes GH-binding at cell surface and in membrane fractions. 1 PublicationCorresponds to variant rs121909368dbSNPEnsembl.1
Natural variantiVAR_018433173V → G in LARS; almost completely abolishes GH-binding at cell surface: 26% binding to membrane fractions. 1 PublicationCorresponds to variant rs121909369dbSNPEnsembl.1
Natural variantiVAR_002714179R → C in LARS and GHIP. 2 PublicationsCorresponds to variant rs121909362dbSNPEnsembl.1
Natural variantiVAR_018434226Y → C in LARS. 1 Publication1
Natural variantiVAR_002715229R → G in LARS. 1 Publication1
Natural variantiVAR_018435244S → I in LARS. 1 Publication1
Natural variantiVAR_018436262D → N in LARS. 1 Publication1
Natural variantiVAR_013939440C → F in LARS. 2 PublicationsCorresponds to variant rs6182dbSNPEnsembl.1
Growth hormone insensitivity, partial (GHIP)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:604271
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00270862E → K in GHIP. 1 PublicationCorresponds to variant rs121909361dbSNPEnsembl.1
Natural variantiVAR_002714179R → C in LARS and GHIP. 2 PublicationsCorresponds to variant rs121909362dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi260E → A: No change in shedding activity: No change in hormone binding. 1 Publication1
Mutagenesisi261E → A: No change in shedding activity: No change in hormone binding. 1 Publication1
Mutagenesisi262D → A: No change in shedding activity: No change in hormone binding. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi2690.
MalaCardsiGHR.
MIMi143890. phenotype.
262500. phenotype.
604271. phenotype.
OpenTargetsiENSG00000112964.
Orphaneti633. Laron syndrome.
314802. Short stature due to partial GHR deficiency.
PharmGKBiPA28674.

Chemistry databases

ChEMBLiCHEMBL1976.
DrugBankiDB00082. Pegvisomant.
DB00052. Somatropin recombinant.

Polymorphism and mutation databases

BioMutaiGHR.
DMDMi121180.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000001095719 – 638Growth hormone receptorAdd BLAST620
ChainiPRO_000001095819 – 256Growth hormone-binding proteinBy similarityAdd BLAST238

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi46N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi56 ↔ 661 Publication
Disulfide bondi101 ↔ 1121 Publication
Glycosylationi115N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi126 ↔ 1401 Publication
Glycosylationi156N-linked (GlcNAc...)Sequence analysis1
Glycosylationi161N-linked (GlcNAc...)Sequence analysis1
Glycosylationi200N-linked (GlcNAc...)Sequence analysis1
Modified residuei341PhosphoserineCombined sources1

Post-translational modificationi

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).By similarity
On GH binding, phosphorylated on tyrosine residues in the cytoplasmic domain by JAK2.By similarity
On ligand binding, ubiquitinated on lysine residues in the cytoplasmic domain. This ubiquitination is not sufficient for GHR internalization (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP10912.
PaxDbiP10912.
PeptideAtlasiP10912.
PRIDEiP10912.

PTM databases

iPTMnetiP10912.
PhosphoSitePlusiP10912.

Miscellaneous databases

PMAP-CutDBP10912.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiENSG00000112964.
CleanExiHS_GHR.
ExpressionAtlasiP10912. baseline and differential.
GenevisibleiP10912. HS.

Interactioni

Subunit structurei

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.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
DUSP7Q168292EBI-286316,EBI-1265847
GH1P012413EBI-286316,EBI-1026046
NCK1P163333EBI-286316,EBI-389883
Ncoa6Q9JLI42EBI-286316,EBI-286271From a different organism.
PTPN1P180315EBI-286316,EBI-968788
PTPN2P177068EBI-286316,EBI-984930
PTPN3P260454EBI-286316,EBI-1047946
PTPN9P433782EBI-286316,EBI-742898
PTPRBP234673EBI-286316,EBI-1265766
PTPRHQ9HD434EBI-286316,EBI-1267176
PTPRJQ129132EBI-286316,EBI-2264500

GO - Molecular functioni

  • growth factor binding Source: BHF-UCL
  • proline-rich region binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • protein kinase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108957. 41 interactors.
DIPiDIP-630N.
IntActiP10912. 23 interactors.
MINTiMINT-1528703.
STRINGi9606.ENSP00000230882.

Structurei

Secondary structure

1638
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi53 – 62Combined sources10
Beta strandi64 – 68Combined sources5
Beta strandi83 – 88Combined sources6
Turni93 – 96Combined sources4
Turni104 – 107Combined sources4
Beta strandi111 – 114Combined sources4
Helixi116 – 118Combined sources3
Beta strandi121 – 131Combined sources11
Beta strandi134 – 142Combined sources9
Helixi143 – 146Combined sources4
Beta strandi153 – 159Combined sources7
Beta strandi167 – 176Combined sources10
Turni183 – 186Combined sources4
Beta strandi190 – 198Combined sources9
Beta strandi210 – 221Combined sources12
Beta strandi226 – 234Combined sources9
Beta strandi240 – 243Combined sources4
Beta strandi247 – 249Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A22X-ray2.60B19-256[»]
1AXIX-ray2.10B19-254[»]
1HWGX-ray2.50B/C19-255[»]
1HWHX-ray2.90B19-255[»]
1KF9X-ray2.60B/C/E/F19-256[»]
2AEWX-ray2.70A/B47-251[»]
3HHRX-ray2.80B/C50-254[»]
DisProtiDP00033.
ProteinModelPortaliP10912.
SMRiP10912.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10912.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini151 – 254Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST104

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni260 – 262Required for ADAM17-mediated proteolysisBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi240 – 244WSXWS motif5
Motifi297 – 305Box 1 motif9
Motifi340 – 349UbE motif10

Domaini

The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
The box 1 motif is required for JAK interaction and/or activation.
The extracellular domain is the ligand-binding domain representing the growth hormone-binding protein (GHBP).
The ubiquitination-dependent endocytosis motif (UbE) is required for recruitment of the ubiquitin conjugation system on to the receptor and for its internalization.

Sequence similaritiesi

Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFQI. Eukaryota.
ENOG410XTHJ. LUCA.
GeneTreeiENSGT00530000063112.
HOGENOMiHOG000015773.
HOVERGENiHBG005836.
InParanoidiP10912.
KOiK05080.
PhylomeDBiP10912.
TreeFamiTF330851.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR025871. GHBP.
IPR015152. Growth/epo_recpt_lig-bind.
IPR013783. Ig-like_fold.
IPR003528. Long_hematopoietin_rcpt_CS.
[Graphical view]
PfamiPF09067. EpoR_lig-bind. 1 hit.
PF00041. fn3. 1 hit.
PF12772. GHBP. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 1 hit.
PS01352. HEMATOPO_REC_L_F1. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P10912-1) [UniParc]FASTAAdd to basket
Also known as: GHRfl

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
MDLWQLLLTL ALAGSSDAFS GSEATAAILS RAPWSLQSVN PGLKTNSSKE
60 70 80 90 100
PKFTKCRSPE RETFSCHWTD EVHHGTKNLG PIQLFYTRRN TQEWTQEWKE
110 120 130 140 150
CPDYVSAGEN SCYFNSSFTS IWIPYCIKLT SNGGTVDEKC FSVDEIVQPD
160 170 180 190 200
PPIALNWTLL NVSLTGIHAD IQVRWEAPRN ADIQKGWMVL EYELQYKEVN
210 220 230 240 250
ETKWKMMDPI LTTSVPVYSL KVDKEYEVRV RSKQRNSGNY GEFSEVLYVT
260 270 280 290 300
LPQMSQFTCE EDFYFPWLLI IIFGIFGLTV MLFVFLFSKQ QRIKMLILPP
310 320 330 340 350
VPVPKIKGID PDLLKEGKLE EVNTILAIHD SYKPEFHSDD SWVEFIELDI
360 370 380 390 400
DEPDEKTEES DTDRLLSSDH EKSHSNLGVK DGDSGRTSCC EPDILETDFN
410 420 430 440 450
ANDIHEGTSE VAQPQRLKGE ADLLCLDQKN QNNSPYHDAC PATQQPSVIQ
460 470 480 490 500
AEKNKPQPLP TEGAESTHQA AHIQLSNPSS LSNIDFYAQV SDITPAGSVV
510 520 530 540 550
LSPGQKNKAG MSQCDMHPEM VSLCQENFLM DNAYFCEADA KKCIPVAPHI
560 570 580 590 600
KVESHIQPSL NQEDIYITTE SLTTAAGRPG TGEHVPGSEM PVPDYTSIHI
610 620 630
VQSPQGLILN ATALPLPDKE FLSSCGYVST DQLNKIMP
Length:638
Mass (Da):71,500
Last modified:July 1, 1989 - v1
Checksum:iEAF77EADE4787822
GO
Isoform 2 (identifier: P10912-2) [UniParc]FASTAAdd to basket
Also known as: GHRtr, GHR1-279

The sequence of this isoform differs from the canonical sequence as follows:
     292-297: RIKMLI → SSSSKD
     298-638: Missing.

Show »
Length:297
Mass (Da):34,109
Checksum:iF690295F6BB01AC8
GO
Isoform 3 (identifier: P10912-3) [UniParc]FASTAAdd to basket
Also known as: GHR1-277

The sequence of this isoform differs from the canonical sequence as follows:
     292-294: RIK → KEN
     295-638: Missing.

Show »
Length:294
Mass (Da):33,889
Checksum:i0E85069AC8F6FDBF
GO
Isoform 4 (identifier: P10912-4) [UniParc]FASTAAdd to basket
Also known as: GHRd3

The sequence of this isoform differs from the canonical sequence as follows:
     24-24: A → D
     25-46: Missing.

Note: Arises by species-specific retrovirus-mediated alternative splice mimicry.
Show »
Length:616
Mass (Da):69,237
Checksum:i5F12CD731F49E1F1
GO

Polymorphismi

Genetic variation in GHR may act as phenotype modifier in familial hypercholesterolemia [MIMi:143890] patients carrying a mutation in the LDLR gene.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01842656C → S in LARS. 1 Publication1
Natural variantiVAR_01842758S → L in LARS. 1 Publication1
Natural variantiVAR_00270862E → K in GHIP. 1 PublicationCorresponds to variant rs121909361dbSNPEnsembl.1
Natural variantiVAR_01842868W → R in LARS. 1 Publication1
Natural variantiVAR_00270989R → K in LARS. 1 Publication1
Natural variantiVAR_002710114F → S in LARS; loss of ability to bind ligand. 2 PublicationsCorresponds to variant rs121909357dbSNPEnsembl.1
Natural variantiVAR_002711143V → A in LARS. 1
Natural variantiVAR_018429149P → Q in LARS; disrupts GH binding. 2 PublicationsCorresponds to variant rs121909365dbSNPEnsembl.1
Natural variantiVAR_002712162V → D in LARS. 1 Publication1
Natural variantiVAR_020002162V → F.Corresponds to variant rs6413484dbSNPEnsembl.1
Natural variantiVAR_018430162V → I Found in a patient with idiopathic short stature; unknown pathological significance. 1 PublicationCorresponds to variant rs6413484dbSNPEnsembl.1
Natural variantiVAR_002713170D → H in LARS; abolishes receptor homodimerization. 2 PublicationsCorresponds to variant rs121909366dbSNPEnsembl.1
Natural variantiVAR_018431171I → T in LARS; almost completely abolishes GH-binding at cell surface: 53% binding to membrane fractions. 1 PublicationCorresponds to variant rs121909367dbSNPEnsembl.1
Natural variantiVAR_018432172Q → P in LARS; almost completely abolishes GH-binding at cell surface and in membrane fractions. 1 PublicationCorresponds to variant rs121909368dbSNPEnsembl.1
Natural variantiVAR_018433173V → G in LARS; almost completely abolishes GH-binding at cell surface: 26% binding to membrane fractions. 1 PublicationCorresponds to variant rs121909369dbSNPEnsembl.1
Natural variantiVAR_002714179R → C in LARS and GHIP. 2 PublicationsCorresponds to variant rs121909362dbSNPEnsembl.1
Natural variantiVAR_013937179R → H.1 PublicationCorresponds to variant rs6181dbSNPEnsembl.1
Natural variantiVAR_018434226Y → C in LARS. 1 Publication1
Natural variantiVAR_002715229R → G in LARS. 1 Publication1
Natural variantiVAR_013938229R → H Found in a patient with idiopathic short stature; unknown pathological significance. 2 PublicationsCorresponds to variant rs6177dbSNPEnsembl.1
Natural variantiVAR_002716242E → D Found in a patient with idiopathic short stature; unknown pathological significance. 1 PublicationCorresponds to variant rs45588036dbSNPEnsembl.1
Natural variantiVAR_018435244S → I in LARS. 1 Publication1
Natural variantiVAR_018436262D → N in LARS. 1 Publication1
Natural variantiVAR_013939440C → F in LARS. 2 PublicationsCorresponds to variant rs6182dbSNPEnsembl.1
Natural variantiVAR_032704465E → K.Corresponds to variant rs34283856dbSNPEnsembl.1
Natural variantiVAR_013940495P → T.1 PublicationCorresponds to variant rs6183dbSNPEnsembl.1
Natural variantiVAR_013941544I → L Polymorphism with a modifier effect on plasma HDL cholesterol levels in familial hypercholesterolemia patients. 3 PublicationsCorresponds to variant rs6180dbSNPEnsembl.1
Natural variantiVAR_013942579P → T.1 PublicationCorresponds to variant rs6184dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01022524A → D in isoform 4. 1 Publication1
Alternative sequenceiVSP_01022625 – 46Missing in isoform 4. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_010227292 – 297RIKMLI → SSSSKD in isoform 2. 3 Publications6
Alternative sequenceiVSP_010229292 – 294RIK → KEN in isoform 3. 1 Publication3
Alternative sequenceiVSP_010230295 – 638Missing in isoform 3. 1 PublicationAdd BLAST344
Alternative sequenceiVSP_010228298 – 638Missing in isoform 2. 3 PublicationsAdd BLAST341

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06562 mRNA. Translation: CAA29808.1.
M28466
, M28458, M28459, M28460, M28461, M28462, M28463, M28464, M28465 Genomic DNA. Translation: AAA52555.1.
AJ278681 Genomic DNA. Translation: CAC06613.1.
CCDSiCCDS3940.1. [P10912-1]
CCDS56364.1. [P10912-4]
PIRiA33991.
RefSeqiNP_000154.1. NM_000163.4. [P10912-1]
NP_001229328.1. NM_001242399.2.
NP_001229329.1. NM_001242400.2. [P10912-1]
NP_001229330.1. NM_001242401.3. [P10912-1]
NP_001229331.1. NM_001242402.2. [P10912-1]
NP_001229332.1. NM_001242403.2. [P10912-1]
NP_001229333.1. NM_001242404.2. [P10912-1]
NP_001229334.1. NM_001242405.2. [P10912-1]
NP_001229335.1. NM_001242406.2. [P10912-1]
NP_001229389.1. NM_001242460.1. [P10912-4]
NP_001229391.1. NM_001242462.1.
UniGeneiHs.125180.
Hs.684632.
Hs.688223.

Genome annotation databases

EnsembliENST00000230882; ENSP00000230882; ENSG00000112964. [P10912-1]
ENST00000357703; ENSP00000350335; ENSG00000112964. [P10912-4]
ENST00000537449; ENSP00000442206; ENSG00000112964. [P10912-1]
ENST00000612382; ENSP00000478332; ENSG00000112964. [P10912-1]
ENST00000612626; ENSP00000479846; ENSG00000112964. [P10912-1]
ENST00000615111; ENSP00000478291; ENSG00000112964. [P10912-1]
ENST00000618088; ENSP00000482373; ENSG00000112964. [P10912-1]
GeneIDi2690.
KEGGihsa:2690.
UCSCiuc003jmt.4. human. [P10912-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06562 mRNA. Translation: CAA29808.1.
M28466
, M28458, M28459, M28460, M28461, M28462, M28463, M28464, M28465 Genomic DNA. Translation: AAA52555.1.
AJ278681 Genomic DNA. Translation: CAC06613.1.
CCDSiCCDS3940.1. [P10912-1]
CCDS56364.1. [P10912-4]
PIRiA33991.
RefSeqiNP_000154.1. NM_000163.4. [P10912-1]
NP_001229328.1. NM_001242399.2.
NP_001229329.1. NM_001242400.2. [P10912-1]
NP_001229330.1. NM_001242401.3. [P10912-1]
NP_001229331.1. NM_001242402.2. [P10912-1]
NP_001229332.1. NM_001242403.2. [P10912-1]
NP_001229333.1. NM_001242404.2. [P10912-1]
NP_001229334.1. NM_001242405.2. [P10912-1]
NP_001229335.1. NM_001242406.2. [P10912-1]
NP_001229389.1. NM_001242460.1. [P10912-4]
NP_001229391.1. NM_001242462.1.
UniGeneiHs.125180.
Hs.684632.
Hs.688223.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A22X-ray2.60B19-256[»]
1AXIX-ray2.10B19-254[»]
1HWGX-ray2.50B/C19-255[»]
1HWHX-ray2.90B19-255[»]
1KF9X-ray2.60B/C/E/F19-256[»]
2AEWX-ray2.70A/B47-251[»]
3HHRX-ray2.80B/C50-254[»]
DisProtiDP00033.
ProteinModelPortaliP10912.
SMRiP10912.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108957. 41 interactors.
DIPiDIP-630N.
IntActiP10912. 23 interactors.
MINTiMINT-1528703.
STRINGi9606.ENSP00000230882.

Chemistry databases

ChEMBLiCHEMBL1976.
DrugBankiDB00082. Pegvisomant.
DB00052. Somatropin recombinant.

PTM databases

iPTMnetiP10912.
PhosphoSitePlusiP10912.

Polymorphism and mutation databases

BioMutaiGHR.
DMDMi121180.

Proteomic databases

EPDiP10912.
PaxDbiP10912.
PeptideAtlasiP10912.
PRIDEiP10912.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000230882; ENSP00000230882; ENSG00000112964. [P10912-1]
ENST00000357703; ENSP00000350335; ENSG00000112964. [P10912-4]
ENST00000537449; ENSP00000442206; ENSG00000112964. [P10912-1]
ENST00000612382; ENSP00000478332; ENSG00000112964. [P10912-1]
ENST00000612626; ENSP00000479846; ENSG00000112964. [P10912-1]
ENST00000615111; ENSP00000478291; ENSG00000112964. [P10912-1]
ENST00000618088; ENSP00000482373; ENSG00000112964. [P10912-1]
GeneIDi2690.
KEGGihsa:2690.
UCSCiuc003jmt.4. human. [P10912-1]

Organism-specific databases

CTDi2690.
DisGeNETi2690.
GeneCardsiGHR.
HGNCiHGNC:4263. GHR.
MalaCardsiGHR.
MIMi143890. phenotype.
262500. phenotype.
600946. gene.
604271. phenotype.
neXtProtiNX_P10912.
OpenTargetsiENSG00000112964.
Orphaneti633. Laron syndrome.
314802. Short stature due to partial GHR deficiency.
PharmGKBiPA28674.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFQI. Eukaryota.
ENOG410XTHJ. LUCA.
GeneTreeiENSGT00530000063112.
HOGENOMiHOG000015773.
HOVERGENiHBG005836.
InParanoidiP10912.
KOiK05080.
PhylomeDBiP10912.
TreeFamiTF330851.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000112964-MONOMER.
ReactomeiR-HSA-1170546. Prolactin receptor signaling.
R-HSA-982772. Growth hormone receptor signaling.
SignaLinkiP10912.
SIGNORiP10912.

Miscellaneous databases

ChiTaRSiGHR. human.
EvolutionaryTraceiP10912.
GeneWikiiGrowth_hormone_receptor.
GenomeRNAii2690.
PMAP-CutDBP10912.
PROiP10912.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000112964.
CleanExiHS_GHR.
ExpressionAtlasiP10912. baseline and differential.
GenevisibleiP10912. HS.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR025871. GHBP.
IPR015152. Growth/epo_recpt_lig-bind.
IPR013783. Ig-like_fold.
IPR003528. Long_hematopoietin_rcpt_CS.
[Graphical view]
PfamiPF09067. EpoR_lig-bind. 1 hit.
PF00041. fn3. 1 hit.
PF12772. GHBP. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 1 hit.
PS01352. HEMATOPO_REC_L_F1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGHR_HUMAN
AccessioniPrimary (citable) accession number: P10912
Secondary accession number(s): Q9HCX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 199 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 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.