Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
RGD ISO annotations to rat from other mammalian species
Mutation of the SHP-2 binding site in growth hormone (GH) receptor prolongs GH-promoted tyrosyl phosphorylation of GH receptor, JAK2, and STAT5B.
Autoregulation of growth hormone receptor and growth hormone binding protein transcripts in brain and peripheral tissues of the rat.
Activation of the Jak/Stat signal transduction pathway in GH-treated rat osteoblast-like cells in culture.
In rats with sepsis, the acute fall in IGF-I is associated with an increase in circulating growth hormone-binding protein levels.
Growth hormone receptor interaction with Jak proteins differs between tissues.
Localization and regulation of the growth hormone receptor and growth hormone-binding protein in the rat growth plate.
Interaction of the growth hormone receptor with cytokine-induced Src homology domain 2 protein in rat adipocytes.
Growth hormone insensitivity of rats under the endotoxemic condition.
Pro-inflammatory cytokines IL-1 beta and TNF-alpha reduce growth hormone receptor mRNA concentration in cultivated rat hepatocytes after stimulation with growth hormone.
Alteration of gene expression profiles in skeletal muscle of rats exposed to microgravity during a spaceflight.
Protective effects of recombinant human growth hormone on cirrhotic rats.
Spatial distribution of growth hormone receptor, insulin-like growth factor-I receptor and apoptotic chondrocytes during growth plate development.
Distinct neuronal growth hormone receptor ligand specificity in the rat brain.
Parenteral versus enteral nutrition: effect on serum cytokines and the hepatic expression of mRNA of suppressor of cytokine signaling proteins, insulin-like growth factor-1 and the growth hormone receptor in rodent sepsis.
Insulin regulation of growth hormone receptor gene expression: involvement of both the PI-3 kinase and MEK/ERK signaling pathways.
Regulation of rat growth hormone receptor gene expression.
Domains of the growth hormone receptor required for association and activation of JAK2 tyrosine kinase.
JAK2 phosphorylation of Irs-1/2
Falcon (Edison Scientific Literature) deep research report for rat Ghr (growth hormone receptor, UniProt P16310)
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GHR is a single-pass class I/type I cytokine receptor whose core molecular
function is to bind circulating growth hormone and transduce that signal
into intracellular phosphorylation cascades, inducing hepatic IGF-1 and
other GH-responsive genes.
"GHR is a cell-surface receptor whose primary function is **to bind circulating growth hormone (GH) and transduce that extracellular hormonal signal into intracellular phosphorylation cascades and gene regulation**, notably including induction of hepatic **IGF-1** and many other GH-responsive genes"
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GHR has no intrinsic kinase activity; its intracellular Box1 (and Box2)
proline-rich region recruits and couples to JAK2, the principal JAK kinase
for GHR.
"GHR lacks intrinsic kinase activity; instead its intracellular **Box1** (and Box2) region is central for recruiting/coupling to **JAK2**"
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Activated JAK2 phosphorylates receptor tyrosines and activates STAT5a/b
(dominant), STAT1, and STAT3, which translocate to the nucleus to regulate
transcription, defining the JAK-STAT output of GHR.
"JAK2 phosphorylates receptor tyrosines and activates **STAT5a/STAT5b** (dominant), as well as **STAT1** and **STAT3**, which dimerize and translocate to the nucleus to regulate transcription"
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Current mechanistic models hold that GHR is a preformed homodimer at the
cell surface, activated by GH-induced conformational rearrangement rather
than de novo ligand-induced dimerization.
"GHR exists as a **preformed homodimer** at the cell surface"
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A soluble growth hormone-binding protein (GHBP) corresponds to the GHR
extracellular domain and binds GH with receptor-like affinity, modulating
GH bioavailability in circulation.
"A **soluble GH-binding protein (GHBP)** corresponds to the **extracellular domain** of GHR and binds GH with receptor-like affinity"
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GHR outputs are branch-specific: canonical JAK2-STAT5 signaling can be
genetically uncoupled from an alternative LYN-ERK1/2 pathway, with Box1
mutations preventing JAK2 activation while preserving LYN activity.
"GHR signaling can be partitioned into canonical **JAK2–STAT5** versus an alternative **LYN–ERK1/2** pathway"
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GH signaling is tightly constrained by negative feedback: STAT5 induces
SOCS2, which binds phosphorylated GHR tyrosines and recruits an E3
ubiquitin ligase complex driving GHR internalization and degradation.
"STAT5 induces SOCS2 expression, and **SOCS2** can bind phosphorylated GHR tyrosines"
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The expert synthesis casts rat Ghr as a non-enzymatic cytokine receptor
whose central biochemical role is to organize and activate JAK2 at the
plasma membrane in response to GH binding.
"rat Ghr encodes a non-enzymatic cytokine receptor whose central biochemical role is to organize and activate JAK2 at the plasma membrane in response to GH binding"