Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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RXFP1Relaxin receptor 1; Receptor for relaxins. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. Binding of the ligand may also activate a tyrosine kinase pathway that inhibits the activity of a phosphodiesterase that degrades cAMP; Belongs to the G-protein coupled receptor 1 family. (784 aa)    
Predicted Functional Partners:
RLN2
Relaxin A chain; Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. May be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix.
    
 0.999
RLN1
Relaxin A chain; Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. May be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix.
     
 0.995
RXFP3
Relaxin-3 receptor 1; Receptor for RNL3/relaxin-3. Binding of the ligand inhibit cAMP accumulation.
     
 0.989
RXFP4
Relaxin-3 receptor 2; High affinity receptor for INSL5. Also acts as receptor for RLN3/relaxin-3, as well as bradykinin and kallidin. Binding of the ligand inhibit cAMP accumulation; Belongs to the G-protein coupled receptor 1 family.
     
 0.983
RLN3
Relaxin-3 A chain; May play a role in neuropeptide signaling processes. Ligand for LGR7, relaxin-3 receptor-1 (GPCR135) and relaxin-3 receptor-2 (GPCR142); Belongs to the insulin family.
   
 
 0.972
INSL3
Insulin-like 3 A chain; Seems to play a role in testicular function. May be a trophic hormone with a role in testicular descent in fetal life. Is a ligand for LGR8 receptor; Belongs to the insulin family.
   
 
 0.971
GNAO1
Guanine nucleotide-binding protein G(o) subunit alpha; Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14; Belongs to the G-alpha family. G(i/o/t/z) subfamily.
   
 
 0.921
RXFP2
Relaxin receptor 2; Receptor for relaxin. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. May also be a receptor for Leydig insulin-like peptide (INSL3).
  
 
0.911
GNB1
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1; Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
   
 
 0.906
GNAS
Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas; Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein- coupled receptors (GPCRs). Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP. GNAS functions downstream of several GPCRs, including beta-adrenergic receptors. XLas isoforms interact with the same set of receptors as GNAS isoforms (By similarity).
     
 0.904
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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