P62 association with RNA is regulated by tyrosine phosphorylation.
about
The STAR RNA binding proteins GLD-1, QKI, SAM68 and SLM-2 bind bipartite RNA motifsSik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its RNA binding abilityThe splicing regulator Sam68 binds to a novel exonic splicing silencer and functions in SMN2 alternative splicing in spinal muscular atrophyA role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domainInteraction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in T cell receptor signalingStructure-function analysis of Qk1: a lethal point mutation in mouse quaking prevents homodimerization.c-Src-mediated phosphorylation of hnRNP K drives translational activation of specifically silenced mRNAsSam68 enhances the cytoplasmic utilization of intron-containing RNA and is functionally regulated by the nuclear kinase Sik/BRK.Adhesion signaling by a novel mitotic substrate of src kinasesSam68 regulates translation of target mRNAs in male germ cells, necessary for mouse spermatogenesisSelf-association of the single-KH-domain family members Sam68, GRP33, GLD-1, and Qk1: role of the KH domainThe interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn)Sam68 regulates a set of alternatively spliced exons during neurogenesisCharacterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1 is a Src substrate during mitosisThe RNA-binding protein Sam68 modulates the alternative splicing of Bcl-xSam68 exerts separable effects on cell cycle progression and apoptosisSAM68: Signal Transduction and RNA Metabolism in Human CancerStructural Basis for Homodimerization of the Src-associated during Mitosis, 68-kDa Protein (Sam68) Qua1 DomainThe STAR/GSG family protein rSLM-2 regulates the selection of alternative splice sitesArginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domainsEvidence for SH3 domain directed binding and phosphorylation of Sam68 by SrcSyk is required for BCR-mediated activation of p90Rsk, but not p70S6k, via a mitogen-activated protein kinase-independent pathway in B cellsHuman squamous-cell-carcinoma cell line (DJM-1) cells synthesize P-cadherin molecules via an elevation of extracellular calcium: calcium regulates P-cadherin-gene expression at the translational level via protein tyrosine phosphorylationIdentification of a Torpedo homolog of Sam68 that interacts with the synapse organizing protein rapsynp68 Sam is a substrate of the insulin receptor and associates with the SH2 domains of p85 PI3KSam68 associates with the SH3 domains of Grb2 recruiting GAP to the Grb2-SOS complex in insulin receptor signalingAn adaptor role for cytoplasmic Sam68 in modulating Src activity during cell polarization.Sam68 is tyrosine phosphorylated and recruited to signalling in peripheral blood mononuclear cells from HIV infected patients.Tr-kit promotes the formation of a multimolecular complex composed by Fyn, PLCgamma1 and Sam68.The K protein domain that recruits the interleukin 1-responsive K protein kinase lies adjacent to a cluster of c-Src and Vav SH3-binding sites. Implications that K protein acts as a docking platform.Premature translation of oskar in oocytes lacking the RNA-binding protein bicaudal-C.Signal transduction and post-transcriptional gene expression.Mechanisms of HGF/Met signaling to Brk and Sam68 in breast cancer progression.Selected glimpses into the activation and function of Src kinase.Regulation of eukaryotic translation by the RACK1 protein: a platform for signalling molecules on the ribosome.Phosphorylation of the Drosophila melanogaster RNA-binding protein HOW by MAPK/ERK enhances its dimerization and activityRegulation of mRNA stability in the nervous system and beyond.Gene regulation at the RNA layer: RNA binding proteins in intercellular signaling networks.Role of leptin as an immunomodulator of blood mononuclear cells: mechanisms of action.The role of potential splicing factors including RBMY, RBMX, hnRNPG-T and STAR proteins in spermatogenesis.
P2860
Q21263034-CFBD8978-E1E2-42E8-8E24-834F266B7885Q22254678-B2C3B181-B4C9-4749-A87F-9787E2CE08CEQ24301061-5973871D-0203-48A5-9619-39E72761DDBEQ24316330-BF88F154-51EC-4247-9C6A-B70671BFE85DQ24322019-D1666B96-F362-4951-B2AB-7737ECAD48F0Q24522616-55E2EC78-D3CA-4DD0-A6E1-85170DD73F64Q24537510-8E87DCA9-6252-438E-A8FF-09185F93F48CQ24540541-89F485D9-2BF5-48ED-BA83-5BAA32CE15D4Q24594187-51A9C599-FD27-4265-A6C4-F0D46888F09FQ24641891-4CD619DB-856E-49D9-8F9F-1FC32246CE71Q24644556-1763CAC6-9AB2-4125-BBEE-B1338FBDC145Q24651533-CA0E075A-309A-4291-9774-F7E239BCFBACQ24655267-7E74217A-AA4C-4EB9-9BCA-6B5DA2AC3336Q24673734-B4D694EF-4DE5-431A-AC9F-5CA5FBFCA8AEQ24683323-CE38CFDC-3D6E-40D3-A3B6-5FDE7BEB5F9AQ24793959-AA784651-0DB9-47D5-A186-CB07B92AE503Q26798149-EFC1283C-803E-43EF-9247-626CA2CB94C3Q27663266-9EBDC1A7-E3E3-4452-A60E-F24B52E816D5Q28140466-3CA890C9-DC69-4495-8231-3BE2DCEE8048Q28140712-4B71E117-E44F-4DA5-9CC8-C6824E2E9614Q28143349-645D4D6D-6D40-46D9-A431-EEF5B416D92EQ28243344-74CEB29A-2329-40ED-8A14-0EED852A97D7Q28253644-E9E59E92-E6D9-4BAD-8649-38AFE0AE97F0Q28287814-57D22942-D451-4107-A2B7-6DDA60969176Q28566032-C6AD0268-DD9A-4510-9904-D168BE11789EQ28576618-DE609CAE-DFFB-4B26-9774-DB8254B89C9BQ30157401-88A3F684-82CD-4B5F-B5A8-CEB1B88EBABDQ30160172-5ED617E3-02C7-4C32-8B3D-9EFAE9FA9FE9Q30164372-D8FF450B-F918-439A-9269-977B40BD8B12Q30192947-8BE4A6E2-C83A-4FAF-B6FD-A7EF1A17777BQ33776105-12539DB0-A8A1-4486-81EA-5CA5CD8A7086Q33999553-103FC997-E958-4EA9-832A-283A9D36D834Q34085432-A7F19F0C-63B9-4C3C-8142-65F29E5C7794Q34103644-D5C8EEFD-0594-4AF6-960F-317C73A5376DQ34166370-6A318C8A-1E32-40B2-8B54-426ADF5F8224Q34221070-5B1D6A36-3AD6-4A18-8141-7D9A1AF82C77Q34464736-482FED26-5D59-4DBC-8F9B-EF823509FFA7Q35112564-B3FD4988-88D7-4664-8A3C-1BBFB843AFE5Q35161166-16B1C587-62E0-44AA-B6C6-8581A9F2DD3EQ35982124-9D9149BA-E1FD-4E3F-A693-E14F6C352FC4
P2860
P62 association with RNA is regulated by tyrosine phosphorylation.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
P62 association with RNA is regulated by tyrosine phosphorylation.
@en
type
label
P62 association with RNA is regulated by tyrosine phosphorylation.
@en
prefLabel
P62 association with RNA is regulated by tyrosine phosphorylation.
@en
P2860
P356
P1476
P62 association with RNA is regulated by tyrosine phosphorylation
@en
P2093
P2860
P304
P356
10.1074/JBC.270.5.2010
P407
P50
P577
1995-02-01T00:00:00Z