RIPK1 | ENSG00000137275 | NCBI 8737

Details for: RIPK1

Gene ID: 8737

Symbol: RIPK1

Ensembl ID: ENSG00000137275

Description: receptor interacting serine/threonine kinase 1

Associated with

Apoptosis
(R-HSA-109581)
Casp8 activity is inhibited
(R-HSA-5218900)
Caspase activation via death receptors in the presence of ligand
(R-HSA-140534)
Caspase activation via extrinsic apoptotic signalling pathway
(R-HSA-5357769)
Cytosolic sensors of pathogen-associated dna
(R-HSA-1834949)
Ddx58/ifih1-mediated induction of interferon-alpha/beta
(R-HSA-168928)
Death receptor signaling
(R-HSA-73887)
Defective ripk1-mediated regulated necrosis
(R-HSA-9693928)
Deubiquitination
(R-HSA-5688426)
Dimerization of procaspase-8
(R-HSA-69416)
Disease
(R-HSA-1643685)
Diseases of programmed cell death
(R-HSA-9645723)
Ikk complex recruitment mediated by rip1
(R-HSA-937041)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Innate immune system
(R-HSA-168249)
Ion channel transport
(R-HSA-983712)
Metabolism of proteins
(R-HSA-392499)
Microbial modulation of ripk1-mediated regulated necrosis
(R-HSA-9686347)
Myd88-independent tlr4 cascade
(R-HSA-166166)
Nf-kb activation through fadd/rip-1 pathway mediated by caspase-8 and -10
(R-HSA-933543)
Ovarian tumor domain proteases
(R-HSA-5689896)
Post-translational protein modification
(R-HSA-597592)
Potential therapeutics for sars
(R-HSA-9679191)
Programmed cell death
(R-HSA-5357801)
Regulated necrosis
(R-HSA-5218859)
Regulation by c-flip
(R-HSA-3371378)
Regulation of necroptotic cell death
(R-HSA-5675482)
Regulation of tnfr1 signaling
(R-HSA-5357905)
Rip-mediated nfkb activation via zbp1
(R-HSA-1810476)
Ripk1-mediated regulated necrosis
(R-HSA-5213460)
Sars-cov-1 infection
(R-HSA-9678108)
Sars-cov-1-host interactions
(R-HSA-9692914)
Sars-cov-1-mediated effects on programmed cell death
(R-HSA-9692913)
Sars-cov infections
(R-HSA-9679506)
Signal transduction
(R-HSA-162582)
Stimuli-sensing channels
(R-HSA-2672351)
Ticam1, rip1-mediated ikk complex recruitment
(R-HSA-168927)
Tlr3-mediated ticam1-dependent programmed cell death
(R-HSA-9013957)
Tnfr1-induced nf-kappa-b signaling pathway
(R-HSA-5357956)
Tnfr1-induced proapoptotic signaling
(R-HSA-5357786)
Tnf signaling
(R-HSA-75893)
Toll-like receptor cascades
(R-HSA-168898)
Toll like receptor 3 (tlr3) cascade
(R-HSA-168164)
Toll like receptor 4 (tlr4) cascade
(R-HSA-166016)
Transport of small molecules
(R-HSA-382551)
Trif (ticam1)-mediated tlr4 signaling
(R-HSA-937061)
Trif-mediated programmed cell death
(R-HSA-2562578)
Trp channels
(R-HSA-3295583)
Ub-specific processing proteases
(R-HSA-5689880)
Viral infection pathways
(R-HSA-9824446)
Zbp1(dai) mediated induction of type i ifns
(R-HSA-1606322)
Apoptotic process
(GO:0006915)
Atp binding
(GO:0005524)
Chromatin remodeling
(GO:0006338)
Death domain binding
(GO:0070513)
Death receptor binding
(GO:0005123)
Histone h2as1 kinase activity
(GO:0044024)
Identical protein binding
(GO:0042802)
Inflammatory response
(GO:0006954)
Intracellular signal transduction
(GO:0035556)
Jun kinase kinase kinase activity
(GO:0004706)
Mapk cascade
(GO:0000165)
Negative regulation of apoptotic process
(GO:0043066)
Negative regulation of canonical nf-kappab signal transduction
(GO:0043124)
Peptidyl-serine autophosphorylation
(GO:0036289)
Positive regulation of apoptotic process
(GO:0043065)
Positive regulation of canonical nf-kappab signal transduction
(GO:0043123)
Positive regulation of gene expression
(GO:0010628)
Positive regulation of inflammatory response
(GO:0050729)
Positive regulation of interleukin-8 production
(GO:0032757)
Positive regulation of jnk cascade
(GO:0046330)
Positive regulation of macrophage differentiation
(GO:0045651)
Positive regulation of necroptotic process
(GO:0060545)
Positive regulation of neuron apoptotic process
(GO:0043525)
Positive regulation of nf-kappab transcription factor activity
(GO:0051092)
Positive regulation of programmed cell death
(GO:0043068)
Positive regulation of protein phosphorylation
(GO:0001934)
Positive regulation of transcription by rna polymerase ii
(GO:0045944)
Positive regulation of tumor necrosis factor production
(GO:0032760)
Protein-containing complex binding
(GO:0044877)
Protein autophosphorylation
(GO:0046777)
Protein binding
(GO:0005515)
Protein catabolic process
(GO:0030163)
Protein homodimerization activity
(GO:0042803)
Protein kinase activity
(GO:0004672)
Protein serine/threonine kinase activity
(GO:0004674)
Protein serine kinase activity
(GO:0106310)
Response to oxidative stress
(GO:0006979)
Response to tumor necrosis factor
(GO:0034612)
Signaling adaptor activity
(GO:0035591)
Tumor necrosis factor-mediated signaling pathway
(GO:0033209)
Ubiquitin protein ligase binding
(GO:0031625)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 184.3194
Cell Significance Index: -28.6700
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 114.3732
Cell Significance Index: -29.0100
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 61.7835
Cell Significance Index: -25.1000
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 26.3736
Cell Significance Index: -25.1800
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 23.9992
Cell Significance Index: -29.5900
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 10.6613
Cell Significance Index: -28.5600
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 7.5392
Cell Significance Index: -29.7500
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 7.0618
Cell Significance Index: -21.6900
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 6.7258
Cell Significance Index: -14.7200
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 1.2094
Cell Significance Index: 16.5000
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 1.0612
Cell Significance Index: 212.8700
Cell Name: ON midget ganglion cell (CL4033046)
Fold Change: 1.0403
Cell Significance Index: 13.1300
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.7858
Cell Significance Index: 85.4800
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.7751
Cell Significance Index: 153.8300
Cell Name: preadipocyte (CL0002334)
Fold Change: 0.7588
Cell Significance Index: 14.8100
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.7352
Cell Significance Index: 44.1400
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.6899
Cell Significance Index: 52.9400
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.6877
Cell Significance Index: 17.1900
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.6298
Cell Significance Index: 225.8900
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.6245
Cell Significance Index: 13.5300
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.6148
Cell Significance Index: 17.7200
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.6099
Cell Significance Index: 31.6800
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.4889
Cell Significance Index: 48.3600
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.4182
Cell Significance Index: 377.6200
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.2920
Cell Significance Index: 52.6400
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.2914
Cell Significance Index: 35.8300
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.2462
Cell Significance Index: 11.1600
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.2329
Cell Significance Index: 6.5100
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: 0.2135
Cell Significance Index: 3.0700
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.1940
Cell Significance Index: 36.9200
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 0.1908
Cell Significance Index: 9.9400
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.1740
Cell Significance Index: 76.9400
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.1733
Cell Significance Index: 8.0800
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.1665
Cell Significance Index: 11.5200
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.1574
Cell Significance Index: 5.5300
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.1550
Cell Significance Index: 4.1400
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.1057
Cell Significance Index: 73.1100
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.0891
Cell Significance Index: 56.5900
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 0.0822
Cell Significance Index: 4.6100
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.0741
Cell Significance Index: 40.5000
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0567
Cell Significance Index: 106.8300
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.0515
Cell Significance Index: 79.3300
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: 0.0498
Cell Significance Index: 1.2800
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.0332
Cell Significance Index: 2.0900
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.0298
Cell Significance Index: 54.8900
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.0293
Cell Significance Index: 5.0000
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.0232
Cell Significance Index: 3.1900
Cell Name: odontoblast (CL0000060)
Fold Change: 0.0232
Cell Significance Index: 2.9700
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.0224
Cell Significance Index: 30.4000
Cell Name: Hofbauer cell (CL3000001)
Fold Change: 0.0193
Cell Significance Index: 0.1600
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.0176
Cell Significance Index: 7.9800
Cell Name: fibroblast of cardiac tissue (CL0002548)
Fold Change: -0.0097
Cell Significance Index: -0.1400
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0125
Cell Significance Index: -9.2500
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.0179
Cell Significance Index: -2.6000
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0209
Cell Significance Index: -13.0400
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0219
Cell Significance Index: -16.0800
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.0282
Cell Significance Index: -0.6000
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0341
Cell Significance Index: -25.8400
Cell Name: Purkinje cell (CL0000121)
Fold Change: -0.0352
Cell Significance Index: -0.7700
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0413
Cell Significance Index: -23.3000
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.0467
Cell Significance Index: -2.8700
Cell Name: sebum secreting cell (CL0000317)
Fold Change: -0.0503
Cell Significance Index: -3.5600
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.0626
Cell Significance Index: -1.7100
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.0695
Cell Significance Index: -14.6400
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.0805
Cell Significance Index: -5.4200
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.0839
Cell Significance Index: -24.1500
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0946
Cell Significance Index: -9.6600
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.0984
Cell Significance Index: -11.4700
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.1002
Cell Significance Index: -4.4300
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: -0.1182
Cell Significance Index: -13.9400
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.1211
Cell Significance Index: -13.8200
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: -0.1233
Cell Significance Index: -5.8000
Cell Name: lactocyte (CL0002325)
Fold Change: -0.1253
Cell Significance Index: -16.1900
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.1321
Cell Significance Index: -15.1400
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -0.1413
Cell Significance Index: -5.3500
Cell Name: early pro-B cell (CL0002046)
Fold Change: -0.1428
Cell Significance Index: -9.2200
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: -0.1798
Cell Significance Index: -3.7300
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.1890
Cell Significance Index: -5.0700
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.2044
Cell Significance Index: -10.3300
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.2327
Cell Significance Index: -17.3400
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.2491
Cell Significance Index: -25.9400
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -0.2764
Cell Significance Index: -1.6700
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.2874
Cell Significance Index: -4.9300
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: -0.3062
Cell Significance Index: -2.8200
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: -0.3115
Cell Significance Index: -5.2500
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.3157
Cell Significance Index: -25.0000
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.3448
Cell Significance Index: -21.1400
Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
Fold Change: -0.3722
Cell Significance Index: -7.9000
Cell Name: BEST4+ enteroycte (CL4030026)
Fold Change: -0.4083
Cell Significance Index: -6.1500
Cell Name: OFF midget ganglion cell (CL4033047)
Fold Change: -0.4226
Cell Significance Index: -5.2700
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.4361
Cell Significance Index: -10.6400
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: -0.4424
Cell Significance Index: -6.5300
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: -0.4652
Cell Significance Index: -13.2800
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.4988
Cell Significance Index: -26.1900
Cell Name: cortical interneuron (CL0008031)
Fold Change: -0.4991
Cell Significance Index: -11.9700
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: -0.5012
Cell Significance Index: -14.7200
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.5053
Cell Significance Index: -16.1900
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.5100
Cell Significance Index: -14.6200
Cell Name: corneal epithelial cell (CL0000575)
Fold Change: -0.5550
Cell Significance Index: -7.9000
Cell Name: VIP GABAergic cortical interneuron (CL4023016)
Fold Change: -0.5559
Cell Significance Index: -11.1600

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** RIPK1 is a serine/threonine kinase that belongs to the receptor-interacting protein (RIP) family. It is characterized by its ability to interact with death receptors, leading to the activation of caspases and subsequent apoptosis. RIPK1 also participates in necroptosis, a form of programmed cell death that is distinct from apoptosis. The protein exhibits a unique ability to bind and regulate various signaling molecules, including TRAF6, FADD, and ZBP1. RIPK1's activity is tightly regulated by post-translational modifications, including phosphorylation and ubiquitination. **Pathways and Functions** RIPK1 is involved in multiple signaling pathways, including: 1. **Apoptosis**: RIPK1 interacts with death receptors, leading to the activation of caspases and apoptosis. 2. **Necroptosis**: RIPK1 participates in necroptosis, a form of programmed cell death that is distinct from apoptosis. 3. **Inflammation**: RIPK1 regulates the production of pro-inflammatory cytokines, such as TNF-α and IL-8. 4. **Immune response**: RIPK1 interacts with immune receptors, including TLR3 and TLR4, leading to the activation of signaling pathways. 5. **Cell survival**: RIPK1 regulates cell survival pathways, including the PI3K/AKT and MAPK/ERK signaling cascades. RIPK1's functions can be broadly categorized into three main areas: 1. **Apoptosis regulation**: RIPK1 regulates apoptosis by interacting with death receptors and activating caspases. 2. **Inflammation regulation**: RIPK1 regulates inflammation by modulating the production of pro-inflammatory cytokines. 3. **Cell survival regulation**: RIPK1 regulates cell survival by interacting with signaling molecules that promote cell survival. **Clinical Significance** RIPK1's dysregulation has been implicated in various diseases, including: 1. **Cancer**: RIPK1's dysregulation is associated with cancer progression and metastasis. 2. **Neurodegenerative disorders**: RIPK1's dysregulation is associated with neurodegenerative disorders, such as Alzheimer's disease and Parkinson's disease. 3. **Inflammatory conditions**: RIPK1's dysregulation is associated with inflammatory conditions, such as rheumatoid arthritis and atherosclerosis. 4. **Infectious diseases**: RIPK1's dysregulation is associated with infectious diseases, such as SARS-CoV-1 infection. In conclusion, RIPK1 is a critical protein kinase that plays a significant role in regulating apoptosis, necroptosis, and inflammation. Its dysregulation has been implicated in various diseases, highlighting the importance of RIPK1 in maintaining tissue homeostasis and responding to pathogen-associated molecular patterns. Further research is needed to fully understand RIPK1's functions and its role in human disease.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Receptor-interacting serine/threonine-protein kinase 1

Genular Protein ID: 3334010426

Symbol: RIPK1_HUMAN

Name: Receptor-interacting serine/threonine-protein kinase 1

UniProtKB Accession Codes:

Q13546 A0AV89 B2RAG1 B4E3F9 Q13180 Q59H33

Database IDs:

Citations:

PubMed ID: 8612133

Title: TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex.

PubMed ID: 8612133

DOI: 10.1016/s1074-7613(00)80252-6

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 14574404

Title: The DNA sequence and analysis of human chromosome 6.

PubMed ID: 14574404

DOI: 10.1038/nature02055

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7538908

Title: RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death.

PubMed ID: 7538908

DOI: 10.1016/0092-8674(95)90072-1

PubMed ID: 9044836

Title: CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP.

PubMed ID: 9044836

PubMed ID: 10521396

Title: Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis.

PubMed ID: 10521396

DOI: 10.1101/gad.13.19.2514

PubMed ID: 10356400

Title: The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation.

PubMed ID: 10356400

DOI: 10.1093/emboj/18.11.3044

PubMed ID: 10358032

Title: RIP3, a novel apoptosis-inducing kinase.

PubMed ID: 10358032

DOI: 10.1074/jbc.274.24.16871

PubMed ID: 10409763

Title: The Epstein-Barr virus oncoprotein latent membrane protein 1 engages the tumor necrosis factor receptor-associated proteins TRADD and receptor-interacting protein (RIP) but does not induce apoptosis or require RIP for NF-kappaB activation.

PubMed ID: 10409763

DOI: 10.1128/mcb.19.8.5759

PubMed ID: 9927690

Title: Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis.

PubMed ID: 9927690

DOI: 10.1073/pnas.96.3.1042

PubMed ID: 11101870

Title: Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule.

PubMed ID: 11101870

DOI: 10.1038/82732

PubMed ID: 11116146

Title: The epidermal growth factor receptor engages receptor interacting protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to activate NF-kappa B. Identification of a novel receptor-tyrosine kinase signalosome.

PubMed ID: 11116146

DOI: 10.1074/jbc.m008458200

PubMed ID: 11854271

Title: A novel zinc finger protein interacts with receptor-interacting protein (RIP) and inhibits tumor necrosis factor (TNF)- and IL1-induced NF-kappa B activation.

PubMed ID: 11854271

DOI: 10.1074/jbc.m108675200

PubMed ID: 11734559

Title: Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3.

PubMed ID: 11734559

DOI: 10.1074/jbc.m109488200

PubMed ID: 15144186

Title: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.

PubMed ID: 15144186

DOI: 10.1021/ac035352d

PubMed ID: 14754897

Title: ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor of NFkappaB activation.

PubMed ID: 14754897

DOI: 10.1074/jbc.m309491200

PubMed ID: 15310755

Title: AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation.

PubMed ID: 15310755

DOI: 10.1074/jbc.m407617200

PubMed ID: 15258597

Title: De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling.

PubMed ID: 15258597

DOI: 10.1038/nature02794

PubMed ID: 16127453

Title: IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction.

PubMed ID: 16127453

DOI: 10.1038/ni1243

PubMed ID: 16603398

Title: Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO.

PubMed ID: 16603398

DOI: 10.1016/j.molcel.2006.03.026

PubMed ID: 17703191

Title: Essential role for TAX1BP1 in the termination of TNF-alpha-, IL-1- and LPS-mediated NF-kappaB and JNK signaling.

PubMed ID: 17703191

DOI: 10.1038/sj.emboj.7601823

PubMed ID: 17301840

Title: RIP1, a kinase on the crossroads of a cell's decision to live or die.

PubMed ID: 17301840

DOI: 10.1038/sj.cdd.4402085

PubMed ID: 17389591

Title: RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation.

PubMed ID: 17389591

DOI: 10.1074/jbc.m701148200

PubMed ID: 17449468

Title: RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation.

PubMed ID: 17449468

DOI: 10.1074/jbc.m701913200

PubMed ID: 18450452

Title: CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation.

PubMed ID: 18450452

DOI: 10.1016/j.cub.2008.04.017

PubMed ID: 18408713

Title: Identification of RIP1 kinase as a specific cellular target of necrostatins.

PubMed ID: 18408713

DOI: 10.1038/nchembio.83

PubMed ID: 18442983

Title: Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1.

PubMed ID: 18442983

DOI: 10.1074/jbc.c800051200

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19524513

Title: Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation.

PubMed ID: 19524513

DOI: 10.1016/j.cell.2009.05.037

PubMed ID: 19524512

Title: Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha.

PubMed ID: 19524512

DOI: 10.1016/j.cell.2009.05.021

Title: Response: CARP1 regulates induction of NF-kappaB by TNFalpha.

DOI: 10.1016/j.cub.2008.11.041

PubMed ID: 20354226

Title: The role of the kinases RIP1 and RIP3 in TNF-induced necrosis.

PubMed ID: 20354226

DOI: 10.1126/scisignal.3115re4

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21455173

Title: Linear ubiquitination prevents inflammation and regulates immune signalling.

PubMed ID: 21455173

DOI: 10.1038/nature09816

PubMed ID: 21931591

Title: cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).

PubMed ID: 21931591

DOI: 10.1371/journal.pone.0022356

PubMed ID: 22265414

Title: The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways.

PubMed ID: 22265414

DOI: 10.1016/j.cell.2011.11.030

PubMed ID: 21887730

Title: Control of NOD2 and Rip2-dependent innate immune activation by GEF-H1.

PubMed ID: 21887730

DOI: 10.1002/ibd.21851

PubMed ID: 22858542

Title: Intrinsic cleavage of receptor-interacting protein kinase-1 by caspase-6.

PubMed ID: 22858542

DOI: 10.1038/cdd.2012.98

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24144979

Title: Ubiquitination-deubiquitination by the TRIM27-USP7 complex regulates tumor necrosis factor alpha-induced apoptosis.

PubMed ID: 24144979

DOI: 10.1128/mcb.00465-13

PubMed ID: 23955153

Title: Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains.

PubMed ID: 23955153

DOI: 10.1038/nature12436

PubMed ID: 24130170

Title: SH3RF2 functions as an oncogene by mediating PAK4 protein stability.

PubMed ID: 24130170

DOI: 10.1093/carcin/bgt338

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25459879

Title: The two faces of receptor interacting protein kinase-1.

PubMed ID: 25459879

DOI: 10.1016/j.molcel.2014.11.001

PubMed ID: 25736436

Title: WDFY1 mediates TLR3/4 signaling by recruiting TRIF.

PubMed ID: 25736436

DOI: 10.15252/embr.201439637

PubMed ID: 25674983

Title: Herpes simplex virus suppresses necroptosis in human cells.

PubMed ID: 25674983

DOI: 10.1016/j.chom.2015.01.003

PubMed ID: 28659487

Title: Mumps virus SH protein inhibits NF-kappaB activation by interacting with tumor necrosis factor receptor 1, interleukin-1 receptor 1, and Toll-like receptor 3 complexes.

PubMed ID: 28659487

DOI: 10.1128/jvi.01037-17

PubMed ID: 29883609

Title: PELI1 selectively targets kinase-active RIP3 for ubiquitylation-dependent proteasomal degradation.

PubMed ID: 29883609

DOI: 10.1016/j.molcel.2018.05.016

PubMed ID: 29440439

Title: Death-domain dimerization-mediated activation of RIPK1 controls necroptosis and RIPK1-dependent apoptosis.

PubMed ID: 29440439

DOI: 10.1073/pnas.1722013115

PubMed ID: 30026316

Title: Biallelic RIPK1 mutations in humans cause severe immunodeficiency, arthritis, and intestinal inflammation.

PubMed ID: 30026316

DOI: 10.1126/science.aar2641

PubMed ID: 31457011

Title: Ripoptocide - A Spark for Inflammation.

PubMed ID: 31457011

DOI: 10.3389/fcell.2019.00163

PubMed ID: 30988283

Title: Serine 25 phosphorylation inhibits RIPK1 kinase-dependent cell death in models of infection and inflammation.

PubMed ID: 30988283

DOI: 10.1038/s41467-019-09690-0

PubMed ID: 32657447

Title: A unique bacterial tactic to circumvent the cell death crosstalk induced by blockade of caspase-8.

PubMed ID: 32657447

DOI: 10.15252/embj.2020104469

PubMed ID: 35831301

Title: Grb2 interacts with necrosome components and is involved in rasfonin-induced necroptosis.

PubMed ID: 35831301

DOI: 10.1038/s41420-022-01106-1

PubMed ID: 23473668

Title: Structural basis of RIP1 inhibition by necrostatins.

PubMed ID: 23473668

DOI: 10.1016/j.str.2013.01.016

PubMed ID: 29681455

Title: The structure of the necrosome RIPK1-RIPK3 core, a human hetero-amyloid signaling complex.

PubMed ID: 29681455

DOI: 10.1016/j.cell.2018.03.032

PubMed ID: 30979585

Title: Structural and functional insights into host death domains inactivation by the bacterial arginine GlcNAcyltransferase effector.

PubMed ID: 30979585

DOI: 10.1016/j.molcel.2019.03.028

PubMed ID: 17344846

Title: Patterns of somatic mutation in human cancer genomes.

PubMed ID: 17344846

DOI: 10.1038/nature05610

PubMed ID: 31827281

Title: Mutations that prevent caspase cleavage of RIPK1 cause autoinflammatory disease.

PubMed ID: 31827281

DOI: 10.1038/s41586-019-1828-5

PubMed ID: 31827280

Title: A dominant autoinflammatory disease caused by non-cleavable variants of RIPK1.

PubMed ID: 31827280

DOI: 10.1038/s41586-019-1830-y

Sequence Information:

Length: 671
Mass: 75931
Checksum: 976E2428D525A9B2
Sequence:

MQPDMSLNVI KMKSSDFLES AELDSGGFGK VSLCFHRTQG LMIMKTVYKG PNCIEHNEAL 
LEEAKMMNRL RHSRVVKLLG VIIEEGKYSL VMEYMEKGNL MHVLKAEMST PLSVKGRIIL 
EIIEGMCYLH GKGVIHKDLK PENILVDNDF HIKIADLGLA SFKMWSKLNN EEHNELREVD 
GTAKKNGGTL YYMAPEHLND VNAKPTEKSD VYSFAVVLWA IFANKEPYEN AICEQQLIMC 
IKSGNRPDVD DITEYCPREI ISLMKLCWEA NPEARPTFPG IEEKFRPFYL SQLEESVEED 
VKSLKKEYSN ENAVVKRMQS LQLDCVAVPS SRSNSATEQP GSLHSSQGLG MGPVEESWFA 
PSLEHPQEEN EPSLQSKLQD EANYHLYGSR MDRQTKQQPR QNVAYNREEE RRRRVSHDPF 
AQQRPYENFQ NTEGKGTAYS SAASHGNAVH QPSGLTSQPQ VLYQNNGLYS SHGFGTRPLD 
PGTAGPRVWY RPIPSHMPSL HNIPVPETNY LGNTPTMPFS SLPPTDESIK YTIYNSTGIQ 
IGAYNYMEIG GTSSSLLDST NTNFKEEPAA KYQAIFDNTT SLTDKHLDPI RENLGKHWKN 
CARKLGFTQS QIDEIDHDYE RDGLKEKVYQ MLQKWVMREG IKGATVGKLA QALHQCSRID 
LLSSLIYVSQ N

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: RIPK1

Associated with

Cells (max top 100)

Other Information

TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. PubMed ID: 8612133

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The DNA sequence and analysis of human chromosome 6. PubMed ID: 14574404

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. PubMed ID: 7538908

CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP. PubMed ID: 9044836

Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. PubMed ID: 10521396

The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. PubMed ID: 10356400

RIP3, a novel apoptosis-inducing kinase. PubMed ID: 10358032

The Epstein-Barr virus oncoprotein latent membrane protein 1 engages the tumor necrosis factor receptor-associated proteins TRADD and receptor-interacting protein (RIP) but does not induce apoptosis or require RIP for NF-kappaB activation. PubMed ID: 10409763

Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis. PubMed ID: 9927690

Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. PubMed ID: 11101870

The epidermal growth factor receptor engages receptor interacting protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to activate NF-kappa B. Identification of a novel receptor-tyrosine kinase signalosome. PubMed ID: 11116146

A novel zinc finger protein interacts with receptor-interacting protein (RIP) and inhibits tumor necrosis factor (TNF)- and IL1-induced NF-kappa B activation. PubMed ID: 11854271

Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3. PubMed ID: 11734559

Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. PubMed ID: 15144186

ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor of NFkappaB activation. PubMed ID: 14754897

AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation. PubMed ID: 15310755

De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling. PubMed ID: 15258597

IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. PubMed ID: 16127453

Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. PubMed ID: 16603398

Essential role for TAX1BP1 in the termination of TNF-alpha-, IL-1- and LPS-mediated NF-kappaB and JNK signaling. PubMed ID: 17703191

RIP1, a kinase on the crossroads of a cell's decision to live or die. PubMed ID: 17301840

RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation. PubMed ID: 17389591

RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation. PubMed ID: 17449468

CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation. PubMed ID: 18450452

Identification of RIP1 kinase as a specific cellular target of necrostatins. PubMed ID: 18408713

Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1. PubMed ID: 18442983

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. PubMed ID: 19524513

Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. PubMed ID: 19524512

Response: CARP1 regulates induction of NF-kappaB by TNFalpha.

The role of the kinases RIP1 and RIP3 in TNF-induced necrosis. PubMed ID: 20354226

Initial characterization of the human central proteome. PubMed ID: 21269460

Linear ubiquitination prevents inflammation and regulates immune signalling. PubMed ID: 21455173

cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4). PubMed ID: 21931591

The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. PubMed ID: 22265414

Control of NOD2 and Rip2-dependent innate immune activation by GEF-H1. PubMed ID: 21887730

Intrinsic cleavage of receptor-interacting protein kinase-1 by caspase-6. PubMed ID: 22858542

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

Ubiquitination-deubiquitination by the TRIM27-USP7 complex regulates tumor necrosis factor alpha-induced apoptosis. PubMed ID: 24144979

Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains. PubMed ID: 23955153

SH3RF2 functions as an oncogene by mediating PAK4 protein stability. PubMed ID: 24130170

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

The two faces of receptor interacting protein kinase-1. PubMed ID: 25459879

WDFY1 mediates TLR3/4 signaling by recruiting TRIF. PubMed ID: 25736436

Herpes simplex virus suppresses necroptosis in human cells. PubMed ID: 25674983

Mumps virus SH protein inhibits NF-kappaB activation by interacting with tumor necrosis factor receptor 1, interleukin-1 receptor 1, and Toll-like receptor 3 complexes. PubMed ID: 28659487

PELI1 selectively targets kinase-active RIP3 for ubiquitylation-dependent proteasomal degradation. PubMed ID: 29883609

Death-domain dimerization-mediated activation of RIPK1 controls necroptosis and RIPK1-dependent apoptosis. PubMed ID: 29440439

Biallelic RIPK1 mutations in humans cause severe immunodeficiency, arthritis, and intestinal inflammation. PubMed ID: 30026316

Ripoptocide - A Spark for Inflammation. PubMed ID: 31457011

Serine 25 phosphorylation inhibits RIPK1 kinase-dependent cell death in models of infection and inflammation. PubMed ID: 30988283

A unique bacterial tactic to circumvent the cell death crosstalk induced by blockade of caspase-8. PubMed ID: 32657447

Grb2 interacts with necrosome components and is involved in rasfonin-induced necroptosis. PubMed ID: 35831301

Structural basis of RIP1 inhibition by necrostatins. PubMed ID: 23473668

The structure of the necrosome RIPK1-RIPK3 core, a human hetero-amyloid signaling complex. PubMed ID: 29681455

Structural and functional insights into host death domains inactivation by the bacterial arginine GlcNAcyltransferase effector. PubMed ID: 30979585

Patterns of somatic mutation in human cancer genomes. PubMed ID: 17344846

Mutations that prevent caspase cleavage of RIPK1 cause autoinflammatory disease. PubMed ID: 31827281

A dominant autoinflammatory disease caused by non-cleavable variants of RIPK1. PubMed ID: 31827280