cytoscape-spread
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The Spread physics simulation layout for Cytoscape.js
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elements: [{"data":{"id":"SCN3B","altered":0,"rank":182,"cited":7,"uniprotdesc":"Modulates channel gating kinetics. Causes uniquepersistent sodium currents. Inactivates the sodium channel openingmore slowly than the subunit beta-1. Its association withneurofascin may target the sodium channels to the nodes of Ranvierof developing axons and retain these channels at the nodes inmature myelinated axons (By similarity). ","isseed":false,"uniprot":"Q9NY72","isvalid":true,"importance":3},"position":{"x":761.9856964961891,"y":668.5312433983302},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"EDN2","altered":0,"rank":105,"cited":159,"uniprotdesc":"Endothelins are endothelium-derived vasoconstrictorpeptides.","isseed":false,"uniprot":"P20800","isvalid":true,"importance":3},"position":{"x":555.3167768572546,"y":948.6800832323651},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"HIRA","altered":0,"rank":148,"cited":53,"uniprotdesc":"Cooperates with ASF1A to promote replication-independentchromatin assembly. Required for the periodic repression ofhistone gene transcription during the cell cycle. Required for theformation of senescence-associated heterochromatin foci (SAHF) andefficient senescence-associated cell cycle exit.","isseed":false,"uniprot":"P54198","isvalid":true,"importance":3},"position":{"x":201.53321183626772,"y":588.7944080506556},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"AURKA","altered":0,"rank":94,"cited":228,"uniprotdesc":"Mitotic serine/threonine kinases that contributes to theregulation of cell cycle progression. Associates with thecentrosome and the spindle microtubules during mitosis and plays acritical role in various mitotic events including theestablishment of mitotic spindle, centrosome duplication,centrosome separation as well as maturation, chromosomalalignment, spindle assembly checkpoint, and cytokinesis. Requiredfor initial activation of CDK1 at centrosomes. Phosphorylatesnumerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1,TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymeraseactivity. Required for normal axon formation. Plays a role inmicrotubule remodeling during neurite extension. Important formicrotubule formation and/or stabilization. Also acts as a keyregulatory component of the p53/TP53 pathway, and particularly thecheckpoint-response pathways critical for oncogenic transformationof cells, by phosphorylating and stabilizing p53/TP53.Phosphorylates its own inhibitors, the protein phosphatase type 1(PP1) isoforms, to inhibit their activity. Necessary for propercilia disassembly prior to mitosis. ","isseed":false,"uniprot":"O14965","isvalid":true,"importance":3},"position":{"x":765.8265370658187,"y":480.08406503564606},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"AURKB","altered":0,"rank":142,"cited":62,"uniprotdesc":"Serine/threonine-protein kinase component of thechromosomal passenger complex (CPC), a complex that acts as a keyregulator of mitosis. The CPC complex has essential functions atthe centromere in ensuring correct chromosome alignment andsegregation and is required for chromatin-induced microtubulestabilization and spindle assembly. Involved in the bipolarattachment of spindle microtubules to kinetochores and is a keyregulator for the onset of cytokinesis during mitosis. Requiredfor central/midzone spindle assembly and cleavage furrowformation. Key component of the cytokinesis checkpoint, a processrequired to delay abscission to prevent both premature resolutionof intercellular chromosome bridges and accumulation of DNAdamage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring untilabscission checkpoint signaling is terminated at late cytokinesis(PubMed:22422861, PubMed:24814515). AURKB phosphorylates the CPCcomplex subunits BIRC5/survivin, CDCA8/borealin and INCENP.Phosphorylation of INCENP leads to increased AURKB activity. Otherknown AURKB substrates involved in centromeric functions andmitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1,VIM/vimentin, GSG2/Haspin, and histone H3. A positive feedbackloop involving GSG2 and AURKB contributes to localization of CPCto centromeres. Phosphorylation of VIM controls vimentin filamentsegregation in cytokinetic process, whereas histone H3 isphosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10phand H3S28ph, respectively). A positive feedback between GSG2 andAURKB contributes to CPC localization. AURKB is also required forkinetochore localization of BUB1 and SGOL1. Phosphorylation ofp53/TP53 negatively regulates its transcriptional activity. Keyregulator of active promoters in resting B- and T-lymphocytes:acts by mediating phosphorylation of H3S28ph at active promotersin resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitinationof histone H2A and enhancing binding and activity of the USP16deubiquitinase at transcribed genes. ","isseed":false,"uniprot":"Q96GD4","isvalid":true,"importance":3},"position":{"x":885.1284743216676,"y":513.4723232390118},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"BDNF","altered":0,"rank":6,"cited":5546,"uniprotdesc":"During development, promotes the survival anddifferentiation of selected neuronal populations of the peripheraland central nervous systems. Participates in axonal growth,pathfinding and in the modulation of dendritic growth andmorphology. Major regulator of synaptic transmission andplasticity at adult synapses in many regions of the CNS. Theversatility of BDNF is emphasized by its contribution to a rangeof adaptive neuronal responses including long-term potentiation(LTP), long-term depression (LTD), certain forms of short-termsynaptic plasticity, as well as homeostatic regulation ofintrinsic neuronal excitability. ","isseed":false,"uniprot":"P23560","isvalid":true,"importance":3},"position":{"x":500.41861485138065,"y":310.3342006937938},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"SERPINE1","altered":0,"rank":5,"cited":7063,"uniprotdesc":"Serine protease inhibitor. This inhibitor acts as 'bait'for tissue plasminogen activator, urokinase, protein C andmatriptase-3/TMPRSS7. Its rapid interaction with PLAT may functionas a major control point in the regulation of fibrinolysis.","isseed":false,"uniprot":"P05121","isvalid":true,"importance":3},"position":{"x":634.3028867500421,"y":813.6957604211618},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"FAS","altered":0,"rank":38,"cited":1011,"uniprotdesc":"Receptor for TNFSF6/FASLG. The adapter molecule FADDrecruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolyticactivation which initiates the subsequent cascade of caspases(aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheraltolerance, in the antigen-stimulated suicide of mature T-cells, orboth. The secreted isoforms 2 to 6 block apoptosis (in vitro).","isseed":false,"uniprot":"P25445","isvalid":true,"importance":3},"position":{"x":769.9224356618503,"y":287.86878583378393},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"CCNA2","altered":0,"rank":50,"cited":660,"uniprotdesc":"Essential for the control of the cell cycle at the G1/S(start) and the G2/M (mitosis) transitions.","isseed":false,"uniprot":"P20248","isvalid":true,"importance":3},"position":{"x":297.278002843864,"y":361.90291244587445},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"S100A2","altered":0,"rank":110,"cited":151,"uniprotdesc":"May function as calcium sensor and modulator,contributing to cellular calcium signaling. May function byinteracting with other proteins, such as TPR-containing proteins,and indirectly play a role in many physiological processes. Mayalso play a role in suppressing tumor cell growth.","isseed":false,"uniprot":"P29034","isvalid":true,"importance":3},"position":{"x":950,"y":522.8952873980897},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"H1F0","altered":0,"rank":179,"cited":8,"uniprotdesc":"Histones H1 are necessary for the condensation ofnucleosome chains into higher-order structures. The H1F0 histonesare found in cells that are in terminal stages of differentiationor that have low rates of cell division.","isseed":false,"uniprot":"P07305","isvalid":true,"importance":3},"position":{"x":406.729974699731,"y":765.219321874992},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"BCL2L14","altered":0,"rank":193,"cited":3,"uniprotdesc":"Plays a role in apoptosis.","isseed":false,"uniprot":"Q9BZR8","isvalid":true,"importance":3},"position":{"x":694.7508500363929,"y":257.77336898915996},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"YY1","altered":0,"rank":40,"cited":894,"uniprotdesc":"Multifunctional transcription factor that exhibitspositive and negative control on a large number of cellular andviral genes by binding to sites overlapping the transcriptionstart site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; somegenes have been shown to contain a longer binding motif allowingenhanced binding; the initial CG dinucleotide can be methylatedgreatly reducing the binding affinity. The effect on transcriptionregulation is depending upon the context in which it binds anddiverse mechanisms of action include direct activation orrepression, indirect activation or repression via cofactorrecruitment, or activation or repression by disruption of bindingsites or conformational DNA changes. Its activity is regulated bytranscription factors and cytoplasmic proteins that have beenshown to abrogate or completely inhibit YY1-mediated activation orrepression. For example, it acts as a repressor in absence ofadenovirus E1A protein but as an activator in its presence. Actssynergistically with the SMAD1 and SMAD4 in bone morphogeneticprotein (BMP)-mediated cardiac-specific gene expression(PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiacactivating regions. May play an important role in development anddifferentiation. Proposed to recruit the PRC2/EED-EZH2 complex totarget genes that are transcriptional repressed. Involved in DNArepair. In vitro, binds to DNA recombination intermediatestructures (Holliday junctions). Proposed core component of the chromatin remodelingINO80 complex which is involved in transcriptional regulation, DNAreplication and probably DNA repair; proposed to target the INO80complex to YY1-responsive elements.","isseed":false,"uniprot":"P25490","isvalid":true,"importance":3},"position":{"x":582.1174682492191,"y":414.9164664022851},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"SKP2","altered":0,"rank":56,"cited":571,"uniprotdesc":"Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediatesthe ubiquitination and subsequent proteasomal degradation oftarget proteins involved in cell cycle progression, signaltransduction and transcription. Specifically recognizesphosphorylated CDKN1B/p27kip and is involved in regulation of G1/Stransition. Degradation of CDKN1B/p27kip also requires CKS1.Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9,RAG2, FOXO1, UBP43, and probably MYC, TOB1 and TAL1. Degradationof TAL1 also requires STUB1. Recognizes CDKN1A in association withCCNE1 or CCNE2 and CDK2. Promotes ubiquitination and destructionof CDH1 in a CK1-Dependent Manner, thereby regulating cellmigration. ","isseed":false,"uniprot":"Q13309","isvalid":true,"importance":3},"position":{"x":503.974780035297,"y":142.59242611594001},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"MAPK1","altered":0,"rank":2,"cited":17194,"uniprotdesc":"Serine/threonine kinase which acts as an essentialcomponent of the MAP kinase signal transduction pathway.MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an importantrole in the MAPK/ERK cascade. They participate also in a signalingcascade initiated by activated KIT and KITLG/SCF. Depending on thecellular context, the MAPK/ERK cascade mediates diverse biologicalfunctions such as cell growth, adhesion, survival anddifferentiation through the regulation of transcription,translation, cytoskeletal rearrangements. The MAPK/ERK cascadeplays also a role in initiation and regulation of meiosis,mitosis, and postmitotic functions in differentiated cells byphosphorylating a number of transcription factors. About 160substrates have already been discovered for ERKs. Many of thesesubstrates are localized in the nucleus, and seem to participatein the regulation of transcription upon stimulation. However,other substrates are found in the cytosol as well as in othercellular organelles, and those are responsible for processes suchas translation, mitosis and apoptosis. Moreover, the MAPK/ERKcascade is also involved in the regulation of the endosomaldynamics, including lysosome processing and endosome cyclingthrough the perinuclear recycling compartment (PNRC); as well asin the fragmentation of the Golgi apparatus during mitosis. Thesubstrates include transcription factors (such as ATF2, BCL6,ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such asCANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators ofapoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG),regulators of translation (such as EIF4EBP1) and a variety ofother signaling-related molecules (like ARHGEF2, DCC, FRS2 orGRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2,RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2,RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases(such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates whichenable the propagation the MAPK/ERK signal to additional cytosolicand nuclear targets, thereby extending the specificity of thecascade. Mediates phosphorylation of TPR in respons to EGFstimulation. May play a role in the spindle assembly checkpoint.Phosphorylates PML and promotes its interaction with PIN1, leadingto PML degradation.Acts as a transcriptional repressor. Binds to a[GC]AAA[GC] consensus sequence. Repress the expression ofinterferon gamma-induced genes. Seems to bind to the promoter ofCCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 andSTAT1. Transcriptional activity is independent of kinase activity.","isseed":false,"uniprot":"P28482","isvalid":true,"importance":3},"position":{"x":455.25652704229003,"y":762.2566633032843},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"JUN","altered":0,"rank":8,"cited":4888,"uniprotdesc":"Transcription factor that recognizes and binds to theenhancer heptamer motif 5'-TGA[CG]TCA-3'. Promotes activity ofNR5A1 when phosphorylated by HIPK3 leading to increasedsteroidogenic gene expression upon cAMP signaling pathwaystimulation. ","isseed":false,"uniprot":"P05412","isvalid":true,"importance":3},"position":{"x":280.796000276297,"y":743.5925876837853},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"RGCC","altered":0,"rank":200,"cited":0,"uniprotdesc":"Modulates the activity of cell cycle-specific kinases.Enhances CDK1 activity. May contribute to the regulation of thecell cycle. May inhibit growth of glioma cells by promoting arrestof mitotic progression at the G2/M transition. Fibrogenic factorcontributing to the pathogenesis of renal fibrosis throughfibroblast activation. ","isseed":false,"uniprot":"Q9H4X1","isvalid":true,"importance":3},"position":{"x":511.8072177195267,"y":244.53538451611672},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"MAPK3","altered":0,"rank":1,"cited":21385,"uniprotdesc":"Serine/threonine kinase which acts as an essentialcomponent of the MAP kinase signal transduction pathway.MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an importantrole in the MAPK/ERK cascade. They participate also in a signalingcascade initiated by activated KIT and KITLG/SCF. Depending on thecellular context, the MAPK/ERK cascade mediates diverse biologicalfunctions such as cell growth, adhesion, survival anddifferentiation through the regulation of transcription,translation, cytoskeletal rearrangements. The MAPK/ERK cascadeplays also a role in initiation and regulation of meiosis,mitosis, and postmitotic functions in differentiated cells byphosphorylating a number of transcription factors. About 160substrates have already been discovered for ERKs. Many of thesesubstrates are localized in the nucleus, and seem to participatein the regulation of transcription upon stimulation. However,other substrates are found in the cytosol as well as in othercellular organelles, and those are responsible for processes suchas translation, mitosis and apoptosis. Moreover, the MAPK/ERKcascade is also involved in the regulation of the endosomaldynamics, including lysosome processing and endosome cyclingthrough the perinuclear recycling compartment (PNRC); as well asin the fragmentation of the Golgi apparatus during mitosis. Thesubstrates include transcription factors (such as ATF2, BCL6,ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such asCANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators ofapoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG),regulators of translation (such as EIF4EBP1) and a variety ofother signaling-related molecules (like ARHGEF2, FRS2 or GRB10).Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2,RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2,RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases(such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates whichenable the propagation the MAPK/ERK signal to additional cytosolicand nuclear targets, thereby extending the specificity of thecascade. ","isseed":false,"uniprot":"P27361","isvalid":true,"importance":3},"position":{"x":584.1270254748321,"y":833.0411995474743},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"MAPK9","altered":0,"rank":48,"cited":706,"uniprotdesc":"Serine/threonine-protein kinase involved in variousprocesses such as cell proliferation, differentiation, migration,transformation and programmed cell death. Extracellular stimulisuch as proinflammatory cytokines or physical stress stimulate thestress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK)signaling pathway. In this cascade, two dual specificity kinasesMAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2.In turn, MAPK9/JNK2 phosphorylates a number of transcriptionfactors, primarily components of AP-1 such as JUN and ATF2 andthus regulates AP-1 transcriptional activity. In response tooxidative or ribotoxic stresses, inhibits rRNA synthesis byphosphorylating and inactivating the RNA polymerase 1-specifictranscription initiation factor RRN3. Promotes stressed cellapoptosis by phosphorylating key regulatory factors including TP53and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarizeddifferentiation of T-helper cells into Th1 cells. Upon T-cellreceptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7and MAP3K7/TAK1 to regulate JUN protein levels. Plays an importantrole in the osmotic stress-induced epithelial tight-junctionsdisruption. When activated, promotes beta-catenin/CTNNB1degradation and inhibits the canonical Wnt signaling pathway.Participates also in neurite growth in spiral ganglion neurons.Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a rolein the regulation of the circadian clock (PubMed:22441692).MAPK9 isoforms display different binding patterns:alpha-1 and alpha-2 preferentially bind to JUN, whereas beta-1 andbeta-2 bind to ATF2. However, there is no correlation betweenbinding and phosphorylation, which is achieved at about the sameefficiency by all isoforms. JUNB is not a substrate for JNK2alpha-2, and JUND binds only weakly to it.","isseed":false,"uniprot":"P45984","isvalid":true,"importance":3},"position":{"x":682.2368360272419,"y":882.8755069202153},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"MAPK8","altered":0,"rank":26,"cited":2270,"uniprotdesc":"Serine/threonine-protein kinase involved in variousprocesses such as cell proliferation, differentiation, migration,transformation and programmed cell death. Extracellular stimulisuch as proinflammatory cytokines or physical stress stimulate thestress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK)signaling pathway. In this cascade, two dual specificity kinasesMAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1.In turn, MAPK8/JNK1 phosphorylates a number of transcriptionfactors, primarily components of AP-1 such as JUN, JDP2 and ATF2and thus regulates AP-1 transcriptional activity. Phosphorylatesthe replication licensing factor CDT1, inhibiting the interactionbetween CDT1 and the histone H4 acetylase HBO1 to replicationorigins. Loss of this interaction abrogates the acetylationrequired for replication initiation. Promotes stressed cellapoptosis by phosphorylating key regulatory factors includingp53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 andMAPK9 are required for polarized differentiation of T-helper cellsinto Th1 cells. Contributes to the survival of erythroid cells byphosphorylating the antagonist of cell death BAD upon EPOstimulation. Mediates starvation-induced BCL2 phosphorylation,BCL2 dissociation from BECN1, and thus activation of autophagy.Phosphorylates STMN2 and hence regulates microtubule dynamics,controlling neurite elongation in cortical neurons. In thedeveloping brain, through its cytoplasmic activity on STMN2,negatively regulates the rate of exit from multipolar stage and ofradial migration from the ventricular zone. Phosphorylates severalother substrates including heat shock factor protein 4 (HSF4), thedeacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates theCLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulationof the circadian clock (PubMed:22441692).JNK1 isoforms display different binding patterns: beta-1preferentially binds to c-Jun, whereas alpha-1, alpha-2, and beta-2 have a similar low level of binding to both c-Jun or ATF2.However, there is no correlation between binding andphosphorylation, which is achieved at about the same efficiency byall isoforms.","isseed":false,"uniprot":"P45983","isvalid":true,"importance":3},"position":{"x":336.5801981438756,"y":429.9095502765703},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"PRDM1","altered":0,"rank":106,"cited":159,"uniprotdesc":"Transcriptional repressor that binds specifically to thePRDI element in the promoter of the beta-interferon gene(PubMed:1851123). Drives the maturation of B-lymphocytes into Igsecreting cells (PubMed:12626569). ","isseed":false,"uniprot":"O75626","isvalid":true,"importance":3},"position":{"x":485.4655057645014,"y":945.6121533057524},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"EIF2AK2","altered":0,"rank":68,"cited":429,"uniprotdesc":"IFN-induced dsRNA-dependent serine/threonine-proteinkinase which plays a key role in the innate immune response toviral infection and is also involved in the regulation of signaltransduction, apoptosis, cell proliferation and differentiation.Exerts its antiviral activity on a wide range of DNA and RNAviruses including hepatitis C virus (HCV), hepatitis B virus(HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1).Inhibits viral replication via phosphorylation of the alphasubunit of eukaryotic initiation factor 2 (EIF2S1), thisphosphorylation impairs the recycling of EIF2S1 between successiverounds of initiation leading to inhibition of translation whicheventually results in shutdown of cellular and viral proteinsynthesis. Also phosphorylates other substrates includingp53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral proteinUS11. In addition to serine/threonine-protein kinase activity,also has tyrosine-protein kinase activity and phosphorylates CDK1at 'Tyr-4' upon DNA damage, facilitating its ubiquitination andproteosomal degradation. Either as an adapter protein and/or viaits kinase activity, can regulate various signaling pathways (p38MAP kinase, NF-kappa-B and insulin signaling pathways) andtranscription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved inthe expression of genes encoding proinflammatory cytokines andIFNs. Activates the NF-kappa-B pathway via interaction with IKBKBand TRAF family of proteins and activates the p38 MAP kinasepathway via interaction with MAP2K6. Can act as both a positiveand negative regulator of the insulin signaling pathway (ISP).Negatively regulates ISP by inducing the inhibitoryphosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5Awhich activates FOXO1, which in turn up-regulates the expressionof insulin receptor substrate 2 (IRS2). Can regulate NLRP3inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 andNLRC4 inflammasomes. Can trigger apoptosis via FADD-mediatedactivation of CASP8. Plays a role in the regulation of thecytoskeleton by binding to gelsolin (GSN), sequestering theprotein in an inactive conformation away from actin.","isseed":false,"uniprot":"P19525","isvalid":true,"importance":3},"position":{"x":569.1493957644504,"y":882.7180903184712},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"HSPA1A","altered":0,"rank":33,"cited":1596,"uniprotdesc":"In cooperation with other chaperones, Hsp70s stabilizepreexistent proteins against aggregation and mediate the foldingof newly translated polypeptides in the cytosol as well as withinorganelles. These chaperones participate in all these processesthrough their ability to recognize nonnative conformations ofother proteins. They bind extended peptide segments with a nethydrophobic character exposed by polypeptides during translationand membrane translocation, or following stress-induced damage. Incase of rotavirus A infection, serves as a post-attachmentreceptor for the virus to facilitate entry into the cell.","isseed":false,"uniprot":"P08107","isvalid":true,"importance":3},"position":{"x":291.719976843528,"y":579.9811430972651},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"CHEK1","altered":0,"rank":47,"cited":727,"uniprotdesc":"Serine/threonine-protein kinase which is required forcheckpoint-mediated cell cycle arrest and activation of DNA repairin response to the presence of DNA damage or unreplicated DNA. Mayalso negatively regulate cell cycle progression during unperturbedcell cycles. This regulation is achieved by a number of mechanismsthat together help to preserve the integrity of the genome.Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds toand phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation ofCDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at'Ser-216' creates binding sites for 14-3-3 proteins which inhibitCDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis ofCDC25A. Phosphorylation of CDC25A at 'Ser-76' primes the proteinfor subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88'by NEK11, which is required for polyubiquitination and degradationof CDCD25A. Inhibition of CDC25 leads to increased inhibitorytyrosine phosphorylation of CDK-cyclin complexes and blocks cellcycle progression. Also phosphorylates NEK6. Binds to andphosphorylates RAD51 at 'Thr-309', which promotes the release ofRAD51 from BRCA2 and enhances the association of RAD51 withchromatin, thereby promoting DNA repair by homologousrecombination. Phosphorylates multiple sites within the C-terminusof TP53, which promotes activation of TP53 by acetylation andpromotes cell cycle arrest and suppression of cellularproliferation. Also promotes repair of DNA cross-links throughphosphorylation of FANCE. Binds to and phosphorylates TLK1 at'Ser-743', which prevents the TLK1-dependent phosphorylation ofthe chromatin assembly factor ASF1A. This may enhance chromatinassembly both in the presence or absence of DNA damage. May alsoplay a role in replication fork maintenance through regulation ofPCNA. May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones.Phosphorylates histone H3.1 (to form H3T11ph), which leads toepigenetic inhibition of a subset of genes. May also phosphorylateRB1 to promote its interaction with the E2F family oftranscription factors and subsequent cell cycle arrest.Isoform 2: Endogenous repressor of isoform 1, interactswith, and antagonizes CHK1 to promote the S to G2/M phasetransition.","isseed":false,"uniprot":"O14757","isvalid":true,"importance":3},"position":{"x":220.1524689166021,"y":814.1513597603264},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"STK17A","altered":0,"rank":176,"cited":11,"uniprotdesc":"Acts as a positive regulator of apoptosis. Also acts asa regulator of cellular reactive oxygen species.","isseed":false,"uniprot":"Q9UEE5","isvalid":true,"importance":3},"position":{"x":428.40132786854133,"y":235.4470639516396},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"CHEK2","altered":0,"rank":42,"cited":859,"uniprotdesc":"Serine/threonine-protein kinase which is required forcheckpoint-mediated cell cycle arrest, activation of DNA repairand apoptosis in response to the presence of DNA double-strandbreaks. May also negatively regulate cell cycle progression duringunperturbed cell cycles. Following activation, phosphorylatesnumerous effectors preferentially at the consensus sequence [L-X-R-X-X-S/T]. Regulates cell cycle checkpoint arrest throughphosphorylation of CDC25A, CDC25B and CDC25C, inhibiting theiractivity. Inhibition of CDC25 phosphatase activity leads toincreased inhibitory tyrosine phosphorylation of CDK-cyclincomplexes and blocks cell cycle progression. May alsophosphorylate NEK6 which is involved in G2/M cell cycle arrest.Regulates DNA repair through phosphorylation of BRCA2, enhancingthe association of RAD51 with chromatin which promotes DNA repairby homologous recombination. Also stimulates the transcription ofgenes involved in DNA repair (including BRCA2) through thephosphorylation and activation of the transcription factor FOXM1.Regulates apoptosis through the phosphorylation of p53/TP53, MDM4and PML. Phosphorylation of p53/TP53 at 'Ser-20' by CHEK2 mayalleviate inhibition by MDM2, leading to accumulation of activep53/TP53. Phosphorylation of MDM4 may also reduce degradation ofp53/TP53. Also controls the transcription of pro-apoptotic genesthrough phosphorylation of the transcription factor E2F1. Tumorsuppressor, it may also have a DNA damage-independent function inmitotic spindle assembly by phosphorylating BRCA1. Its absence maybe a cause of the chromosomal instability observed in some cancercells. ","isseed":false,"uniprot":"O96017","isvalid":true,"importance":3},"position":{"x":556.6585149681805,"y":677.8506468486836},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"BDKRB2","altered":0,"rank":109,"cited":151,"uniprotdesc":"Receptor for bradykinin. It is associated with Gproteins that activate a phosphatidylinositol-calcium secondmessenger system.","isseed":false,"uniprot":"P30411","isvalid":true,"importance":3},"position":{"x":629.791361528527,"y":936.0631456104647},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"LIF","altered":0,"rank":14,"cited":3270,"uniprotdesc":"LIF has the capacity to induce terminal differentiationin leukemic cells. Its activities include the induction ofhematopoietic differentiation in normal and myeloid leukemiacells, the induction of neuronal cell differentiation, and thestimulation of acute-phase protein synthesis in hepatocytes.","isseed":false,"uniprot":"P15018","isvalid":true,"importance":3},"position":{"x":659.0903263182183,"y":497.9004799357725},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"VRK1","altered":0,"rank":120,"cited":97,"uniprotdesc":"Serine/threonine kinase involved in Golgi disassemblyduring the cell cycle: following phosphorylation by PLK3 duringmitosis, required to induce Golgi fragmentation. Acts by mediatingphosphorylation of downstream target protein. Phosphorylates 'Thr-18' of p53/TP53 and may thereby prevent the interaction betweenp53/TP53 and MDM2. Phosphorylates casein and histone H3.Phosphorylates BANF1: disrupts its ability to bind DNA, reducesits binding to LEM domain-containing proteins and causes itsrelocalization from the nucleus to the cytoplasm. PhosphorylatesATF2 which activates its transcriptional activity.","isseed":false,"uniprot":"Q99986","isvalid":true,"importance":3},"position":{"x":491.08155176356354,"y":847.0627953347798},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"RCHY1","altered":0,"rank":121,"cited":96,"uniprotdesc":"Mediates E3-dependent ubiquitination and proteasomaldegradation of target proteins, including p53/TP53, P73, HDAC1 andCDKN1B. Preferentially acts on tetrameric p53/TP53.Monoubiquitinates the translesion DNA polymerase POLH. Contributesto the regulation of the cell cycle progression. Increases ARtranscription factor activity. ","isseed":false,"uniprot":"Q96PM5","isvalid":true,"importance":3},"position":{"x":349.49513723436206,"y":771.4426953107417},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"SPP1","altered":0,"rank":20,"cited":2743,"uniprotdesc":"Binds tightly to hydroxyapatite. Appears to form anintegral part of the mineralized matrix. Probably important tocell-matrix interaction.Acts as a cytokine involved in enhancing production ofinterferon-gamma and interleukin-12 and reducing production ofinterleukin-10 and is essential in the pathway that leads to typeI immunity. ","isseed":false,"uniprot":"P10451","isvalid":true,"importance":3},"position":{"x":806.8861831099688,"y":833.6687776783972},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"COL18A1","altered":0,"rank":157,"cited":30,"uniprotdesc":"COLA18A probably plays a major role in determining theretinal structure as well as in the closure of the neural tube.Endostatin potently inhibits endothelial cellproliferation and angiogenesis. May inhibit angiogenesis bybinding to the heparan sulfate proteoglycans involved in growthfactor signaling.","isseed":false,"uniprot":"P39060","isvalid":true,"importance":3},"position":{"x":357.6472681750301,"y":333.6772210883497},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"CREBBP","altered":0,"rank":24,"cited":2442,"uniprotdesc":"Acetylates histones, giving a specific tag fortranscriptional activation. Also acetylates non-histone proteins,like NCOA3 and FOXO1. Binds specifically to phosphorylated CREBand enhances its transcriptional activity toward cAMP-responsivegenes. Acts as a coactivator of ALX1 in the presence of EP300.Acts as a circadian transcriptional coactivator which enhances theactivity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers.","isseed":false,"uniprot":"Q92793","isvalid":true,"importance":3},"position":{"x":541.0862850211842,"y":281.53821992566566},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"FDXR","altered":0,"rank":147,"cited":54,"uniprotdesc":"Serves as the first electron transfer protein in all themitochondrial P450 systems. Including cholesterol side chaincleavage in all steroidogenic tissues, steroid 11-betahydroxylation in the adrenal cortex, 25-OH-vitamin D3-24hydroxylation in the kidney, and sterol C-27 hydroxylation in theliver.","isseed":false,"uniprot":"P22570","isvalid":true,"importance":3},"position":{"x":50,"y":552.9723385624237},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"SMYD2","altered":0,"rank":175,"cited":12,"uniprotdesc":"Protein-lysine N-methyltransferase that methylates bothhistones and non-histone proteins, including p53/TP53 and RB1.Specifically methylates histone H3 'Lys-4' (H3K4me) anddimethylates histone H3 'Lys-36' (H3K36me2). Shows even highermethyltransferase activity on p53/TP53. Monomethylates 'Lys-370'of p53/TP53, leading to decreased DNA-binding activity andsubsequent transcriptional regulation activity of p53/TP53.Monomethylates RB1 at 'Lys-860'. ","isseed":false,"uniprot":"Q9NRG4","isvalid":true,"importance":3},"position":{"x":320.04894775109074,"y":214.10074865886835},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"ATR","altered":0,"rank":52,"cited":628,"uniprotdesc":"Serine/threonine protein kinase which activatescheckpoint signaling upon genotoxic stresses such as ionizingradiation (IR), ultraviolet light (UV), or DNA replicationstalling, thereby acting as a DNA damage sensor. Recognizes thesubstrate consensus sequence [ST]-Q. Phosphorylates BRCA1, CHEK1,MCM2, RAD17, RPA2, SMC1 and p53/TP53, which collectively inhibitDNA replication and mitosis and promote DNA repair, recombinationand apoptosis. Phosphorylates 'Ser-139' of histone variantH2AX/H2AFX at sites of DNA damage, thereby regulating DNA damageresponse mechanism. Required for FANCD2 ubiquitination. Criticalfor maintenance of fragile site stability and efficient regulationof centrosome duplication. ","isseed":false,"uniprot":"Q13535","isvalid":true,"importance":3},"position":{"x":718.2890027190751,"y":616.8179054559004},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"HGF","altered":0,"rank":4,"cited":7554,"uniprotdesc":"Potent mitogen for mature parenchymal hepatocyte cells,seems to be a hepatotrophic factor, and acts as a growth factorfor a broad spectrum of tissues and cell types. Activating ligandfor the receptor tyrosine kinase MET by binding to it andpromoting its dimerization. ","isseed":false,"uniprot":"P14210","isvalid":true,"importance":3},"position":{"x":108.21311953587619,"y":752.7468908105759},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"ATM","altered":0,"rank":25,"cited":2298,"uniprotdesc":"Serine/threonine protein kinase which activatescheckpoint signaling upon double strand breaks (DSBs), apoptosisand genotoxic stresses such as ionizing ultraviolet A light (UVA),thereby acting as a DNA damage sensor. Recognizes the substrateconsensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histonevariant H2AX/H2AFX at double strand breaks (DSBs), therebyregulating DNA damage response mechanism. Also plays a role inpre-B cell allelic exclusion, a process leading to expression of asingle immunoglobulin heavy chain allele to enforce clonality andmonospecific recognition by the B-cell antigen receptor (BCR)expressed on individual B-lymphocytes. After the introduction ofDNA breaks by the RAG complex on one immunoglobulin allele, actsby mediating a repositioning of the second allele topericentromeric heterochromatin, preventing accessibility to theRAG complex and recombination of the second allele. Also involvedin signal transduction and cell cycle control. May function as atumor suppressor. Necessary for activation of ABL1 and SAPK.Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1,CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. May play a role invesicle and/or protein transport. Could play a role in T-celldevelopment, gonad and neurological function. Plays a role inreplication-dependent histone mRNA degradation. Binds DNA ends.Phosphorylation of DYRK2 in nucleus in response to genotoxicstress prevents its MDM2-mediated ubiquitination and subsequentproteasome degradation. Phosphorylates ATF2 which stimulates itsfunction in DNA damage response. ","isseed":false,"uniprot":"Q13315","isvalid":true,"importance":3},"position":{"x":447.77537187107083,"y":711.5773414669369},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"EPHA2","altered":0,"rank":154,"cited":35,"uniprotdesc":"Receptor tyrosine kinase which binds promiscuouslymembrane-bound ephrin-A family ligands residing on adjacent cells,leading to contact-dependent bidirectional signaling intoneighboring cells. The signaling pathway downstream of thereceptor is referred to as forward signaling while the signalingpathway downstream of the ephrin ligand is referred to as reversesignaling. Activated by the ligand ephrin-A1/EFNA1 regulatesmigration, integrin-mediated adhesion, proliferation anddifferentiation of cells. Regulates cell adhesion anddifferentiation through DSG1/desmoglein-1 and inhibition of theERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May alsoparticipate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration.During development, may function in distinctive aspects of patternformation and subsequently in development of several fetaltissues. Involved for instance in angiogenesis, in early hindbraindevelopment and epithelial proliferation and branchingmorphogenesis during mammary gland development. Engaged by theligand ephrin-A5/EFNA5 may regulate lens fiber cells shape andinteractions and be important for lens transparency developmentand maintenance. With ephrin-A2/EFNA2 may play a role in boneremodeling through regulation of osteoclastogenesis andosteoblastogenesis. ","isseed":false,"uniprot":"P29317","isvalid":true,"importance":3},"position":{"x":169.8249954191063,"y":752.5176803275788},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"PCNA","altered":0,"rank":12,"cited":3811,"uniprotdesc":"Auxiliary protein of DNA polymerase delta and isinvolved in the control of eukaryotic DNA replication byincreasing the polymerase's processibility during elongation ofthe leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loadedonto DNA in order to be able to stimulate APEX2. Plays a key rolein DNA damage response (DDR) by being conveniently positioned atthe replication fork to coordinate DNA replication with DNA repairand DNA damage tolerance pathways. Acts as a loading platform torecruit DDR proteins that allow completion of DNA replicationafter DNA damage and promote postreplication repair:Monoubiquitinated PCNA leads to recruitment of translesion (TLS)polymerases, while 'Lys-63'-linked polyubiquitination of PCNA isinvolved in error-free pathway and employs recombinationmechanisms to synthesize across the lesion.","isseed":false,"uniprot":"P12004","isvalid":true,"importance":3},"position":{"x":393.7139913950467,"y":279.007133040323},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"GRK5","altered":0,"rank":135,"cited":74,"uniprotdesc":"Serine/threonine kinase that phosphorylatespreferentially the activated forms of a variety of G-protein-coupled receptors (GPCRs). Such receptor phosphorylation initiatesbeta-arrestin-mediated receptor desensitization, internalization,and signaling events leading to their down-regulation.Phosphorylates a variety of GPCRs, including adrenergic receptors,muscarinic acetylcholine receptors (more specifically Gi-coupledM2/M4 subtypes), dopamine receptors and opioid receptors. Inaddition to GPCRs, also phosphorylates various substrates: Hsc70-interacting protein/ST13, TP53/p53, HDAC5, and arrestin-1/ARRB1.Phosphorylation of ARRB1 by GRK5 inhibits G-protein independentMAPK1/MAPK3 signaling downstream of 5HT4-receptors.Phosphorylation of HDAC5, a repressor of myocyte enhancer factor 2(MEF2) leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription. Phosphorylation of TP53/p53, a crucialtumor suppressor, inhibits TP53/p53-mediated apoptosis.Phosphorylation of ST13 regulates internalization of the chemokinereceptor. Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor, LRP6 during Wnt signaling (in vitro).","isseed":false,"uniprot":"P34947","isvalid":true,"importance":3},"position":{"x":767.8516929832432,"y":617.2360347281034},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"STEAP3","altered":0,"rank":155,"cited":32,"uniprotdesc":"Endosomal ferrireductase required for efficienttransferrin-dependent iron uptake in erythroid cells. Participatesin erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Canalso reduce of Cu(2+) to Cu(1+), suggesting that it participatesin copper homeostasis. Uses NADP(+) as acceptor. May play a roledownstream of p53/TP53 to interface apoptosis and cell cycleprogression. Indirectly involved in exosome secretion byfacilitating the secretion of proteins such as TCTP.","isseed":false,"uniprot":"Q658P3","isvalid":true,"importance":3},"position":{"x":522.1918220260616,"y":761.4329566582309},"group":"nodes","removed":false,"selected":false,"selectable":true,"locked":false,"grabbed":false,"grabbable":true,"classes":""},{"data":{"id":"NUAK1","altered":0,"rank":149,"cited":48,"uniprotdesc":"Serine/threonine-protein kinase involved in variousprocesses such as cell adhesion, regulation of cell ploidy andsenescence, cell proliferation and tumor progression.Phosphorylates ATM, CASP6, LATS1, PPP1R12A and p53/TP53. Acts as aregulator of cellular senescence and cellular ploidy by mediatingphosphorylation of 'Ser-464' of LATS1, thereby controlling itsstability. Controls cell adhesion by regulating activity of themyosin protein phosphatase 1 (PP1) complex. Acts by med