Details for: Tgfb1i1
Associated with
Other Information
Genular Protein ID: 3622314646
Symbol: TGFI1_MOUSE
Name: Transforming growth factor beta-1-induced transcript 1 protein
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 7929412
Title: Characterization of the TGF beta 1-inducible hic-5 gene that encodes a putative novel zinc finger protein and its possible involvement in cellular senescence.
PubMed ID: 7929412
PubMed ID: 10831843
Title: Genomic structure and chromosomal mapping of the mouse hic-5 gene that encodes a focal adhesion protein.
PubMed ID: 10831843
PubMed ID: 16219310
Title: Identification and analysis of Hic-5/ARA55 isoforms: implications for integrin signaling and steroid hormone action.
PubMed ID: 16219310
PubMed ID: 16141072
Title: The transcriptional landscape of the mammalian genome.
PubMed ID: 16141072
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 9422762
Title: Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions.
PubMed ID: 9422762
PubMed ID: 9756887
Title: Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase.
PubMed ID: 9756887
PubMed ID: 9722648
Title: The LIM domains of hic-5 protein recognize specific DNA fragments in a zinc-dependent manner in vitro.
PubMed ID: 9722648
PubMed ID: 10092676
Title: Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain.
PubMed ID: 10092676
PubMed ID: 10330411
Title: Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: a role in cytoskeletal remodeling.
PubMed ID: 10330411
PubMed ID: 9858471
Title: Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin.
PubMed ID: 9858471
PubMed ID: 10649439
Title: Specific decrease in the level of Hic-5, a focal adhesion protein, during immortalization of mouse embryonic fibroblasts, and its association with focal adhesion kinase.
PubMed ID: 10649439
DOI: 10.1002/(sici)1097-4644(20000301)76:3<411::aid-jcb9>3.0.co;2-j
PubMed ID: 11134073
Title: Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion.
PubMed ID: 11134073
PubMed ID: 10848625
Title: Interaction of the tau2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix.
PubMed ID: 10848625
PubMed ID: 11437454
Title: Novel cell lines promote the discovery of genes involved in early heart development.
PubMed ID: 11437454
PubMed ID: 11546764
Title: Identification and characterization of hic-5/ARA55 as an hsp27 binding protein.
PubMed ID: 11546764
PubMed ID: 11463817
Title: Hic-5-reduced cell spreading on fibronectin: competitive effects between paxillin and Hic-5 through interaction with focal adhesion kinase.
PubMed ID: 11463817
PubMed ID: 11937715
Title: Possible involvement of hic-5, a focal adhesion protein, in the differentiation of C2C12 myoblasts.
PubMed ID: 11937715
DOI: 10.1247/csf.27.21
PubMed ID: 12153727
Title: Hic-5 interacts with GIT1 with a different binding mode from paxillin.
PubMed ID: 12153727
PubMed ID: 11779876
Title: The FXXLF motif mediates androgen receptor-specific interactions with coregulators.
PubMed ID: 11779876
PubMed ID: 11805099
Title: Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal adhesion adaptor proteins paxillin and Hic-5.
PubMed ID: 11805099
PubMed ID: 12177201
Title: The multiple LIM domain-containing adaptor protein Hic-5 synaptically colocalizes and interacts with the dopamine transporter.
PubMed ID: 12177201
PubMed ID: 12631731
Title: Hic-5 communicates between focal adhesions and the nucleus through oxidant-sensitive nuclear export signal.
PubMed ID: 12631731
PubMed ID: 14755691
Title: A LIM protein, Hic-5, functions as a potential coactivator for Sp1.
PubMed ID: 14755691
DOI: 10.1002/jcb.10754
PubMed ID: 16183059
Title: Tyrosine-phosphorylated Hic-5 inhibits epidermal growth factor-induced lamellipodia formation.
PubMed ID: 16183059
PubMed ID: 15687259
Title: Hic-5 regulates an epithelial program mediated by PPARgamma.
PubMed ID: 15687259
DOI: 10.1101/gad.1240705
PubMed ID: 15713747
Title: Uni-axial stretching regulates intracellular localization of Hic-5 expressed in smooth-muscle cells in vivo.
PubMed ID: 15713747
DOI: 10.1242/jcs.01683
PubMed ID: 16219691
Title: Regulation of paxillin family members during epithelial-mesenchymal transformation: a putative role for paxillin delta.
PubMed ID: 16219691
DOI: 10.1242/jcs.02615
PubMed ID: 16291758
Title: HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-driven transcription.
PubMed ID: 16291758
PubMed ID: 16624805
Title: ERK8 down-regulates transactivation of the glucocorticoid receptor through Hic-5.
PubMed ID: 16624805
PubMed ID: 16737959
Title: Oligomerizing potential of a focal adhesion LIM protein Hic-5 organizing a nuclear-cytoplasmic shuttling complex.
PubMed ID: 16737959
PubMed ID: 17233630
Title: Paxillin family members function as Csk-binding proteins that regulate Lyn activity in human and murine platelets.
PubMed ID: 17233630
DOI: 10.1042/bj20061618
PubMed ID: 17299801
Title: Hic-5 contributes to epithelial-mesenchymal transformation through a RhoA/ROCK-dependent pathway.
PubMed ID: 17299801
DOI: 10.1002/jcp.20991
PubMed ID: 17166536
Title: Hic-5/ARA55 a prostate stroma-specific AR coactivator.
PubMed ID: 17166536
PubMed ID: 21183079
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
PubMed ID: 21183079
Sequence Information:
- Length: 461
- Mass: 50101
- Checksum: 6AB15FFF466FEE73
- Sequence:
MEDLDALLSD LETTTSHMSR LGAPKERPPE TLTPPPPYGH QPQTGSGESS GTTGDKDHLY STVCKPRSPK PVAPVAPPFS SSSGVLGNGL CELDRLLQEL NATQFNITDE IMSQFPSSKM AEGEEKEDQS EDKSSPTVPP SPFPAPSKPS ATSATQELDR LMASLSDFRV QNHLPASGPP QPPAASPTRE GCPSPPGQTS KGSLDTMLGL LQSDLSRRGV PTQAKGLCGS CNKPIAGQVV TALGRAWHPE HFLCSGCSTT LGGSSFFEKD GAPFCPECYF ERFSPRCGFC NQPIRHKMVT ALGTHWHPEH FCCVSCGEPF GEEGFHEREG RPYCRRDFLQ LFAPRCQGCQ GPILDNYISA LSALWHPDCF VCRECLAPFS GGSFFEHEGR PLCENHFHAQ RGSLCATCGL PVTGRCVSAL GRRFHPDHFT CTFCLRPLTK GSFQERASKP YCQPCFLKLF G
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.