positive regulation of peptidyl-tyrosine phosphorylation
about
CD44 molecule (Indian blood group)Insulin like growth factor 1Macrophage migration inhibitory factorReelinReelinInsulin IITransformation related protein 53AGTCholecystokininColony stimulating factor 3 (granulocyte)Insulin-like growth factor 1Adiponectin, C1Q and collagen domain containingCD36 moleculeEpidermal growth factorInterleukin 6CD4 antigenInterleukin 4C-abl oncogene 1, non-receptor tyrosine kinaseInsulin-like growth factor 2Mechanistic target of rapamycin kinaseInterleukin 5Leukemia inhibitory factorPrion proteinIntercellular adhesion molecule 15-hydroxytryptamine (serotonin) receptor 2ANeurotrophin 3Transforming growth factor, beta 1Interleukin 11Hepatocyte growth factorInterleukin 15Spleen tyrosine kinaseCD80 antigenGrowth hormone receptorTransforming growth factor alphaIntegrin beta 1 (fibronectin receptor beta)Angiopoietin 1Kit ligandIntegrin beta 3Ectonucleotide pyrophosphatase/phosphodiesterase 2Toll-like receptor 4
P682
Cripto-1 induces phosphatidylinositol 3'-kinase-dependent phosphorylation of AKT and glycogen synthase kinase 3beta in human cervical carcinoma cellsMelanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130casFunctional interaction between c-Abl and the p21-activated protein kinase gamma-PAKShedding of the interleukin-6 (IL-6) receptor (gp80) determines the ability of IL-6 to induce gp130 phosphorylation in human osteoblastsMultiple angiopoietin recombinant proteins activate the Tie1 receptor tyrosine kinase and promote its interaction with Tie2Tetraspanin CD81 is linked to ERK/MAPKinase signaling by Shc in liver tumor cellsMitogen-activated protein kinases and ribosomal S6 protein kinases are involved in signaling pathways shared by interleukin-11, interleukin-6, leukemia inhibitory factor, and oncostatin M in mouse 3T3-L1 cellsAngiopoietin-1-induced ubiquitylation of Tie2 by c-Cbl is required for internalization and degradationNeuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cellsAngiotensin II induces focal adhesion kinase/paxillin phosphorylation and cell migration in human umbilical vein endothelial cellsAlzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons.
P921
Q1056532-F42EF9EB-6D0D-4BDF-BE16-AD6324C2925AQ1263065-702ABA39-6350-403A-82BD-780D25F1E7E5Q133582-FF89498D-DA4D-4C23-8542-7642DE054ECEQ13561329-867F5C94-D629-4A1D-9657-9F62252E453CQ14331165-9910F0D3-5009-45DA-9E75-79B7DC98131DQ14762286-000C3BC5-8B3F-427F-8DEA-0C0E437E6D24Q14762286-572B362F-708A-4419-B4FC-0F8254FD5FAFQ14818136-46244B33-0BD3-4AAA-809A-A931FD135E41Q14859647-4B90DB24-45BA-42F8-BC5F-923AFC4A196AQ14862711-64EADF92-9EDE-400D-9BB0-D07EF7ED6B37Q14863144-19EA2B17-0953-41D2-BB35-9BDFD97979EAQ14863723-E8FD154A-28F1-467E-BB12-297AEF2AA879Q14864062-463D5BFB-2B65-4442-9722-E8D849326392Q14864583-4C6C80D3-CDB2-4431-9C40-4C364959F100Q14864699-3A166313-ED4D-4F93-8818-87A7EC117F39Q14865240-A1EA6F74-4093-4727-8D83-D3A13F655E74Q14865413-0C755916-DAF4-46BF-9209-81242C89FF3DQ14865961-1A018EBE-4FDB-42A0-B055-FDC99D985995Q14874000-F7C4B05C-A6E9-4AAE-BE50-9FFCB7F67725Q14874351-935F6171-551F-4F7C-9FFD-8D2A86346CE6Q14876092-3F55638B-34A1-494A-A4E0-56EB03B28CD2Q14877652-0304F8C2-0A49-4149-9E29-7838BEF7C19AQ14878799-0F8E0FD6-DF20-42BC-B6DF-8F08982359E7Q14881308-CCFB50AD-FD8B-4A7E-8D72-84F5412DDCD4Q14891112-C943F487-6BED-4CE3-8ADA-312D67807FABQ14891461-A4487C8F-2AB4-4B35-9702-B9943D358421Q14904572-DD44762E-A63A-4B65-8653-1EC35752CB88Q14904616-148C876D-1F37-456C-9507-7DB179AA7009Q14906034-16AD66CF-BA54-481D-B8BB-B2F0179545AFQ14906215-6C2C100D-CBB7-4F7D-B1F5-9DE3F2ADF894Q14907170-0679FF7B-8EEB-4B13-9AC7-A7EE57970AC0Q14907170-24B33477-B40F-4E5F-BE5A-ED205F7997EAQ14907340-58D12E08-D1D6-4667-B6E6-EE8EFA866141Q14907512-25AA5DF8-FB73-4FEE-8D96-0F958C2E5820Q14907634-5676A043-D85D-40E4-90B9-381D8AF8C68AQ14907634-90BA80E6-B915-4DE5-ADD1-67073CEFFC85Q14908040-A6FF2D10-9F6B-4E92-9251-EF36E2C2C619Q14912087-0FC7A623-A1E5-4A8A-9470-95C6F2447418Q14912180-7BBC1770-F753-46AA-BBA2-746D9CCD1975Q14912447-68CADB7C-9B54-4E47-861A-F36A2EA7BFA5
P682
Q22010560-1A05BF92-90B2-4991-9F11-D1A8DAD59190Q22010904-7FFCEB2B-0D69-4B9D-9B98-0C5AA7285BC0Q24290639-C3C1BFF7-7325-4E34-ADB5-7FEC197E059FQ24292420-3BC001CE-E5F2-4B8F-BB49-084CA5C5A8D9Q24300714-49EB385F-C8FF-4FC4-B06C-47181CF62D73Q24302000-00ABD99A-E3FA-4AD4-A41E-E9B1CA18389DQ24305084-1CC4FA86-670A-480F-941D-F58A47789824Q24336384-3BE37F21-D7B9-437E-832C-4711253BFF1DQ24337623-F344CAF3-4094-4B3D-8CB0-4550E34A5F8BQ24338186-EB2F37A8-5565-478E-B732-1485FBABA75EQ28771398-D89AA212-1BB1-4975-9A1D-5019899AD05D
P921
positive regulation of peptidyl-tyrosine phosphorylation
description
Any process that activates or ...... rylation of peptidyl-tyrosine.
@en
biologisch proces
@nl
name
positive regulation of peptidyl-tyrosine phosphorylation
@en
type
label
positive regulation of peptidyl-tyrosine phosphorylation
@en
altLabel
GO:0050731
@en
up regulation of peptidyl-tyrosine phosphorylation
@en
up-regulation of peptidyl-tyrosine phosphorylation
@en
upregulation of peptidyl-tyrosine phosphorylation
@en
prefLabel
positive regulation of peptidyl-tyrosine phosphorylation
@en
P2888
P686
GO:0050731