Regulation of transcription by a protein methyltransferase
about
AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptorInterplay among coactivator-associated arginine methyltransferase 1, CBP, and CIITA in IFN-gamma-inducible MHC-II gene expressionTranscriptional activation of human matrix metalloproteinase-9 gene expression by multiple co-activatorsRelationships of the antiproliferative proteins BTG1 and BTG2 with CAF1, the human homolog of a component of the yeast CCR4 transcriptional complex: involvement in estrogen receptor alpha signaling pathwayIdentification of functional domains involved in BTG1 cell localizationIdentification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM)Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1Tumor formation and inactivation of RIZ1, an Rb-binding member of a nuclear protein-methyltransferase superfamilyThe novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificityCrosstalk between C/EBPbeta phosphorylation, arginine methylation, and SWI/SNF/Mediator implies an indexing transcription factor codeIdentification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alphaDifferential use of functional domains by coiled-coil coactivator in its synergistic coactivator function with beta-catenin or GRIP1The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcriptionTranscription factors and nuclear receptors interact with the SWI/SNF complex through the BAF60c subunitThe ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptorsSIP, a novel ankyrin repeat containing protein, sequesters steroid receptor coactivators in the cytoplasmRibosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)ZNF366 is an estrogen receptor corepressor that acts through CtBP and histone deacetylasesPromiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behaviorHuman SFMBT is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a ligand-dependent coactivator for retinoic acid receptorTDRD3 is an effector molecule for arginine-methylated histone marksGAS, a new glutamate-rich protein, interacts differentially with SRCs and is involved in oestrogen receptor functionH3R42me2a is a histone modification with positive transcriptional effectsPRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificityCARM1 methylates chromatin remodeling factor BAF155 to enhance tumor progression and metastasisProtein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosisActivating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteinsNuclear receptor coactivator thyroid hormone receptor-binding protein (TRBP) interacts with and stimulates its associated DNA-dependent protein kinasePhysical association between the histone acetyl transferase CBP and a histone methyl transferaseMethylation at arginine 17 of histone H3 is linked to gene activationPABP1 identified as an arginine methyltransferase substrate using high-density protein arraysNegative regulation of transcription by the type II arginine methyltransferase PRMT5The arginine-1493 residue in QRRGRTGR1493G motif IV of the hepatitis C virus NS3 helicase domain is essential for NS3 protein methylation by the protein arginine methyltransferase 1.A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3Targeting of SWI/SNF chromatin remodelling complexes to estrogen-responsive genes.Identification of a transcriptionally active peroxisome proliferator-activated receptor alpha -interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator.Jun dimerization protein 2 functions as a progesterone receptor N-terminal domain coactivator.The function of TIF2/GRIP1 in mouse reproduction is distinct from those of SRC-1 and p/CIP.Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1
P2860
Q22254314-7358EB16-F6DB-4135-BF56-E2B77526BCDFQ22330787-F1159EBF-59C3-45EE-9C8D-5CB826117664Q24289430-93AA9A8D-C768-4E07-A25D-DA2D3C176185Q24290687-1E0E91B4-6C84-4063-AC1A-14D679332679Q24291357-9019BD39-6A3E-4158-B70B-BB1BC8FB03ECQ24291422-30B4E102-306E-4E1C-BE3E-406AB2161D94Q24291581-E77BCB77-7B4F-4F9F-AE45-1BA76927E3C2Q24291648-F339A1FD-001C-4999-B5EB-87EBCD0D0422Q24291936-25714C06-7668-4D46-9C67-859C880AF2CCQ24297811-DF6D7129-7E85-439D-BB2A-83EACE52A840Q24298570-4FF7B6BC-014C-4871-AB37-596C59CC6E7AQ24298632-0FF53F7B-7832-4AD4-BB6A-64DE2742F6E8Q24301763-0144228E-AE34-4175-B515-6805CF7D4B72Q24303852-3AAD4F53-02B1-42C6-B053-520D25CCF01EQ24304094-869658B4-9915-4A6B-812A-35A09465BF1CQ24304823-EB82FCC3-6F79-4C4D-B2A4-C7EB51400129Q24306650-22BB4DF4-E73A-4A27-AA26-0FFF1A6D59D6Q24312025-4777939C-F397-4834-939E-82446271A7FDQ24314981-40137A44-E9E5-4809-9CCF-EC8903EFA4BFQ24315668-13C3A9D4-B57D-453D-A57D-731375F3D55EQ24316341-CF7094E9-99E5-49F7-A39B-15FB1A75D0B7Q24318709-CE05C226-AD1C-43EC-903C-7675C5ED3E21Q24318938-F1974117-B64D-498B-8228-CD3998467294Q24319807-367906B2-0D40-4F0C-82B0-40EE5365B758Q24320263-5041EE64-D765-455B-AE0D-E090547A655CQ24320341-25375835-A2DA-4A68-B7C8-07B0E236D6ECQ24322824-E7BD916F-AE29-49F2-8BD2-C71E4640699FQ24336785-BADD7527-0673-464B-8973-DF4FA37CAFA5Q24338427-58C3A6C8-7CE2-410A-A62E-DD0BC7156F31Q24522491-E8397FCB-DB0D-4747-8201-5041EB746974Q24522543-5741954A-A08A-4A9B-A3C4-15597BB6DBD9Q24522567-23D9151B-3204-427D-8E4C-EE7B63379353Q24522638-3BA8919D-D14D-4DB4-A7F8-975E26247540Q24529559-F32A60BB-4985-49AD-81BD-9D6D2A0DDEC6Q24531253-46D47C7C-379F-456B-8796-E99C16EF86A9Q24534273-66622E18-FE81-4A8E-BB47-3A4FDD50E542Q24535680-A45CAB4E-D987-4CA6-B084-41697578FED0Q24537624-1B309F7D-20C6-483B-925A-5554A8E61C8DQ24537671-D3158BA1-6DE6-4A73-A3C3-8298638B1FEAQ24540397-7B751ED5-2215-4380-AC67-41AC8085D5D9
P2860
Regulation of transcription by a protein methyltransferase
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Regulation of transcription by a protein methyltransferase
@ast
Regulation of transcription by a protein methyltransferase
@en
Regulation of transcription by a protein methyltransferase
@nl
type
label
Regulation of transcription by a protein methyltransferase
@ast
Regulation of transcription by a protein methyltransferase
@en
Regulation of transcription by a protein methyltransferase
@nl
prefLabel
Regulation of transcription by a protein methyltransferase
@ast
Regulation of transcription by a protein methyltransferase
@en
Regulation of transcription by a protein methyltransferase
@nl
P2093
P3181
P1433
P1476
Regulation of transcription by a protein methyltransferase
@en
P2093
B T Schurter
M R Stallcup
P304
P3181
P356
10.1126/SCIENCE.284.5423.2174
P407
P577
1999-06-25T00:00:00Z