about
Fibronectin 1Erb-b2 receptor tyrosine kinase 2Bone morphogenetic protein 4Spleen tyrosine kinaseTransforming growth factor, beta receptor IIIFibroblast growth factor receptor 2Interleukin 1 betaLYN proto-oncogene, Src family tyrosine kinaseProtein tyrosine phosphatase non-receptor type 6APAF1 interacting proteinEPH receptor B1TNF receptor associated factor 7Family with sequence similarity 83 member DRAS relatedRAS guanyl releasing protein 1Cellular communication network factor 1EPH receptor A2EPH receptor A7ROS proto-oncogene 1, receptor tyrosine kinaseTIAM Rac1 associated GEF 1Serine/threonine/tyrosine interacting proteinNIMA related kinase 10Protein arginine methyltransferase 5Glutathione S-transferase pi 1CEA cell adhesion molecule 1Fibroblast growth factor receptor substrate 2Glutathione S-transferase, pi 1Cellular communication network factor 1T-lymphoma invasion and metastasis-inducing protein 1RAS guanyl releasing protein 1Endothelin converting enzyme 1Family with sequence similarity 83, member DCarcinoembryonic antigen-related cell adhesion molecule 1Corticotropin releasing hormone receptor 2Rho guanine nucleotide exchange factor 5Eph receptor A2Eph receptor A7Eph receptor B1Fibroblast growth factor receptor substrate 2Protein arginine N-methyltransferase 5
P682
Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1Activating mutations in RRAS underlie a phenotype within the RASopathy spectrum and contribute to leukaemogenesisConserved oncogenic behavior of the FAM83 family regulates MAPK signaling in human cancerEndosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptorLigand targeting of EphA2 enhances keratinocyte adhesion and differentiation via desmoglein 1Ligand binding induces Cbl-dependent EphB1 receptor degradation through the lysosomal pathwayPseudophosphatase STYX modulates cell-fate decisions and cell migration by spatiotemporal regulation of ERK1/2Structural analysis of autoinhibition in the Ras-specific exchange factor RasGRP1TIM, a Dbl-related protein, regulates cell shape and cytoskeletal organization in a Rho-dependent mannerPKHD1 gene silencing may cause cell abnormal proliferation through modulation of intracellular calcium in autosomal recessive polycystic kidney diseaseALL1 fusion proteins induce deregulation of EphA7 and ERK phosphorylation in human acute leukemiasIL-1β promotes malignant transformation and tumor aggressiveness in oral cancer.De Novo Missense Variants in TRAF7 Cause Developmental Delay, Congenital Anomalies, and Dysmorphic FeaturesA YWHAZ Variant Associated With Cardiofaciocutaneous Syndrome Activates the RAF-ERK Pathway
P921
Q14819493-A8CA5C47-E0E7-423D-B1FA-C281A61B937CQ14877504-D712D853-BBF3-4952-9320-3603D1E74E0EQ14903410-4EF7AE51-9FCB-4CD9-ADD3-CCB47FA545FFQ14907340-5A9FB5EF-233F-4899-AE9E-6565E5FB695CQ14911566-FF44C162-8AEA-415B-94F9-8B58E23DFA82Q14911646-BB546628-3B6F-460D-B85C-48725E7429A4Q14916414-86480F38-F032-48B6-AB28-893AC523288EQ15331919-35FDE345-4C4B-45C4-8F04-79BB2DE5913CQ21100543-D0A8165D-9FF1-4297-82A5-E569E68C0519Q21100690-86747E3A-49D8-49E9-BAFD-E4CDB0A32082Q21101194-D45CC6A9-8541-4749-A242-2FDC830DA8A5Q21104649-97E8EF02-3E4B-490C-A922-BD66BB8BCACAQ21105985-3FEB679E-BBCB-480A-877B-A478E5301DFFQ21109002-878816C2-0269-41C3-B90F-4F203ACD601FQ21110951-4A2CF96D-6B40-47A4-AE6A-131A1BD486B5Q21114247-BCCD50DA-9D42-4C39-ABFA-52B232B80BA7Q21114359-DD7AC997-5FE6-47A0-BCB6-00D9F3208C16Q21114364-DF80034A-694B-4779-B93B-E8D791E0271FQ21120491-9AB05614-4AFC-4ED1-842E-3BD4FB0C19B6Q21123942-7F25AB7E-0DE4-477C-8A88-A64E7B56016CQ21124582-327BE58A-B7F5-4113-B5DB-0D593C384BC5Q21124582-AB53486B-1A04-4BE6-AE49-71D65177DAE9Q21124826-533F8E3F-3E12-490B-9B3B-25D97DF93B2EQ21130994-50D3163A-F34D-4E60-B4B2-E3BCD71AF5CBQ21171798-1E3C76C4-BF6C-41E0-86B7-121656F86985Q21171950-341F0709-B35F-483A-A0B0-3D35527654B7Q21172873-D79390A1-7594-4002-BD92-14F460178EB6Q21433642-3605A8A0-B72F-4388-9FA3-53ED1DF2FBBCQ21494338-EF3FE967-D531-4F90-9A72-083DD5FA598DQ21495013-4923353C-6246-479E-86C9-037F1359EA19Q21495799-80A86A04-9806-4FCE-8689-26A439A7E70FQ21497547-C74C9DE4-BC4C-418E-908B-9EF4BB3CFE4DQ21497704-3F89E124-7FBF-4DDA-BFB2-905DA31F85AAQ21499241-71AF5FD5-4171-4466-AD72-1C1ACF1A5F96Q21499359-016E0132-3C95-4379-859A-84D4829DB994Q21971920-4A3AE124-577F-47F9-9394-15901E46FC89Q21979768-1BF2058C-E032-45A5-97BC-09607F05F954Q21979768-D248B49F-DD6C-45DB-8C29-DF37E109FF5BQ21979773-C8721963-0059-4D78-93C3-8254AAA8190FQ21981351-05D7664F-CB83-4A2D-8B43-D63B4F4124EC
P682
Q24290967-B2031CB4-C084-4E90-AFA2-B63709E843C1Q24294030-0995DFE5-2AE0-4A56-B573-C7B044C9ABE1Q24294761-323A432D-E810-40A1-9290-E846CCEDBA94Q24297204-484BD7F3-B012-4C40-AF42-7C8AF18C2F4FQ24300682-90CF27AF-3536-44DF-985C-66C68760547FQ24301313-9BA133A4-02BF-41D7-9D75-4EA658079DF4Q24307792-A5AF32B6-3870-4910-B58B-06BC3FE8BA9AQ24313621-3A124818-F000-4F29-A62F-1C3500E5DF2FQ24322063-659DDBA3-463B-4B3F-8073-7E23429C422BQ24324618-6C970E54-9C18-43D8-9EAC-AB9C9E21F630Q24338588-81578F6E-D1C6-4AF5-8602-237735EA3BBDQ30981861-2A350F43-6F20-4054-92D7-49DE2A3CEB50Q57761594-610ABAB2-9AEA-4234-8C08-E5CD71C68CA9Q64066695-A8EFD5BE-24AC-4FE2-A787-EB40C5B5BA9E
P921
description
Any process that modulates the ...... by the ERK1 and ERK2 cascade.
@en
biologisch proces
@nl
name
regulation of ERK1 and ERK2 cascade
@en
type
label
regulation of ERK1 and ERK2 cascade
@en
altLabel
GO:0070372
@en
regulation of ERK1 and ERK2 signaling pathway
@en
regulation of ERK1 and ERK2 signalling pathway
@en
regulation of ERK1/2 cascade
@en
prefLabel
regulation of ERK1 and ERK2 cascade
@en
P2888
P686
GO:0070372