An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis.
about
Comprehensive analysis of interactions between the Src-associated protein in mitosis of 68 kDa and the human Src-homology 3 proteomeHost heterogeneous ribonucleoprotein K (hnRNP K) as a potential target to suppress hepatitis B virus replication.Ablation of the Sam68 RNA binding protein protects mice from age-related bone lossSik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its RNA binding abilityMetastatic Lymph Node 51, a novel nucleo-cytoplasmic protein overexpressed in breast cancerRegulation of FynT function by dual domain docking on PAG/CbpFunctional interaction between c-Src and its mitotic target, Sam 68E1B 55-kilodalton-associated protein: a cellular protein with RNA-binding activity implicated in nucleocytoplasmic transport of adenovirus and cellular mRNAsThe role of a lymphoid-restricted, Grb2-like SH3-SH2-SH3 protein in T cell receptor signalingp70 phosphorylation and binding to p56lck is an early event in interleukin-2-induced onset of cell cycle progression in T-lymphocytesRACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cellsA Ras-GTPase-activating protein SH3-domain-binding proteinA role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domainRole of the nucleophosmin (NPM) portion of the non-Hodgkin's lymphoma-associated NPM-anaplastic lymphoma kinase fusion protein in oncogenesisInteraction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in T cell receptor signalingThe WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modulesDeciphering the cross talk between hnRNP K and c-Src: the c-Src activation domain in hnRNP K is distinct from a second interaction siteMouse disabled (mDab1): a Src binding protein implicated in neuronal developmentA new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate.Regulation of CD44 alternative splicing by SRm160 and its potential role in tumor cell invasionc-Src-mediated phosphorylation of hnRNP K drives translational activation of specifically silenced mRNAsThe poly(C)-binding proteins: a multiplicity of functions and a search for mechanisms.Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1Sam68 enhances the cytoplasmic utilization of intron-containing RNA and is functionally regulated by the nuclear kinase Sik/BRK.The mouse poly(C)-binding protein exists in multiple isoforms and interacts with several RNA-binding proteinsMCG10, a novel p53 target gene that encodes a KH domain RNA-binding protein, is capable of inducing apoptosis and cell cycle arrest in G(2)-MMutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactionsAdhesion signaling by a novel mitotic substrate of src kinasesMet receptors induce Sam68-dependent cell migration by activation of alternate extracellular signal-regulated kinase family membersTec kinase associates with c-kit and is tyrosine phosphorylated and activated following stem cell factor bindingIdentification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domainsSam68 is required for both NF-κB activation and apoptosis signaling by the TNF receptorTNF-stimulated MAP kinase activation mediated by a Rho family GTPase signaling pathwaySam68 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 domainAssociation of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1Heterogeneous nuclear ribonucleoprotein K is a transcription factorThe interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn)Association of the vav proto-oncogene product with poly(rC)-specific RNA-binding proteinsDifferential effects of B cell receptor and B cell receptor-FcgammaRIIB1 engagement on docking of Csk to GTPase-activating protein (GAP)-associated p62
P2860
Q21134534-C08FEDD3-44ED-46EC-824A-51BAFB3B23B6Q21144733-D1280D04-3627-420C-AE79-E18F669DB7F6Q21145275-C03FD12F-AA32-41CB-B669-3CF9E38A9962Q22254678-F59BF4FD-8B58-46AA-936A-1CF3B37F194BQ24300187-4B773037-8F76-4725-B216-67F183742426Q24302122-978477B5-7A58-467F-8FF3-7C527D86BF85Q24306924-FE764CA3-2C68-430D-81E4-F2CAF30F7FAFQ24312647-7AD77180-25B8-4788-9DD1-5F6EF00383C5Q24312928-8507890B-3ECF-41D4-A19C-C7F315069A39Q24312993-BB70F6F9-ACE7-4796-B655-795388B64B20Q24315691-13F616C0-58AE-4997-BD59-7CA92B263749Q24316153-A62C572A-42D4-4CEA-8774-376CA54F1D0EQ24316330-98D6BC51-8895-4C4E-AE36-F59B3A8E29BCQ24317141-4B0EFC95-21FD-4D8E-8F89-86BBD5E0661AQ24322019-7159C682-E26C-4380-AEF2-1F67784CAB83Q24323939-77D97A4B-3E19-49CD-ABE0-6708A7A58DEFQ24337409-AAAEEC15-E6E7-403F-B744-DB7AB1519BE8Q24532070-34410C41-CA70-4427-BC36-F3FEE5B08CF7Q24533279-4D00ECF9-C58E-44B0-8ACE-1A6BA1377862Q24535552-BE63DC7A-5D56-4858-AB12-781500642990Q24537510-45B3C4A8-D0BD-4C42-B503-D4EEF4254767Q24540086-2F142FF2-18C4-4F47-9C55-2462F4B2AD83Q24540397-C433283E-3F83-41A2-BCC4-88717E6E6F43Q24540541-2A734D15-711B-41D9-A33B-80BEEE108AB7Q24548185-216C7DC7-AD25-4347-A23D-B4771B9C493AQ24552865-BD2F0FA4-12A5-46D6-8ED5-1034547004A7Q24568352-239DC33F-056F-4E27-9A1B-4F8217BF1577Q24594187-3446F06E-B02C-45A0-BC15-E05E27E4568CQ24606871-87EC8F21-4F85-4DB1-A375-0D77FC920413Q24607293-FB6218F5-ADCE-4A7D-BFD4-F9E766D89774Q24611670-4E5B197D-DB22-4D98-8161-151849823F6AQ24630120-3E45C3B5-1D06-46AD-ADFF-ABE2FC987BC8Q24634905-0FD7AEC2-69ED-45C1-9062-F596C8D5FC01Q24641891-AD1989E3-171B-4075-8DE1-9B71887C6D21Q24644556-DBFE9316-B1BE-42A4-9CD6-3A50FC80F89EQ24646917-8BD1052C-6B2C-4A99-9B57-FD57D015A852Q24649693-6D6BE8F7-9990-4EDC-9DF7-034034177369Q24651533-A3E9D5BE-8AA5-45DF-B0D2-5EF86767B1EBQ24652816-31455631-C835-4158-8560-DF3876B978C5Q24653005-42C73A80-275E-4C2C-B286-A908F0433F6E
P2860
An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis.
description
1994 nî lūn-bûn
@nan
1994 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis.
@ast
An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis.
@en
type
label
An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis.
@ast
An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis.
@en
prefLabel
An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis.
@ast
An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis.
@en
P356
P1433
P1476
An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis.
@en
P2093
Shalloway D
P2888
P304
P356
10.1038/368867A0
P407
P577
1994-04-01T00:00:00Z
P6179
1027123016