TGFB1I1

Transforming growth factor beta 1 induced transcript 1
Identifiers
Symbols	TGFB1I1 ; ARA55; HIC-5; HIC5; TSC-5
External IDs	OMIM: 602353 MGI: 102784 HomoloGene: 7572 GeneCards: TGFB1I1 Gene
Gene ontology Molecular function • transcription coactivator activity • protein binding • zinc ion binding • Roundabout binding • androgen receptor binding • I-SMAD binding Cellular component • intracellular • cytoplasm • cytoskeleton • focal adhesion • nuclear matrix • extracellular matrix Biological process • transcription from RNA polymerase II promoter • cell adhesion • negative regulation of cell proliferation • response to heat • positive regulation of epithelial to mesenchymal transition • Wnt signaling pathway • morphogenesis of embryonic epithelium • positive regulation of transforming growth factor beta receptor signaling pathway • negative regulation of transforming growth factor beta receptor signaling pathway • androgen receptor signaling pathway • ubiquitin-dependent SMAD protein catabolic process • epithelial cell differentiation • cell fate commitment • negative regulation of fat cell differentiation • positive regulation of transcription, DNA-templated Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7041	21804
Ensembl	ENSG00000140682	ENSMUSG00000030782
UniProt	O43294	Q62219
RefSeq (mRNA)	NM_001042454	NM_001289550
RefSeq (protein)	NP_001035919	NP_001276479
Location (UCSC)	Chr 16: 31.47 – 31.48 Mb	Chr 7: 128.25 – 128.25 Mb
PubMed search

Transforming growth factor beta-1-induced transcript 1 protein is a protein that in humans is encoded by the TGFB1I1 gene.^[1][2]

Interactions

TGFB1I1 has been shown to interact with:

• Androgen receptor,^[3][4]
• Dopamine transporter^[5]
• Hsp27,^[6]
• PTK2B,^[1][3][7]
• PTK2,^[1][7][8] and
• PTPN12.^[9]

Model organisms

Model organisms have been used in the study of TGFB1I1 function. A conditional knockout mouse line called Tgfb1i1^{tm1b(KOMP)Wtsi} was generated at the Wellcome Trust Sanger Institute.^[10] Male and female animals underwent a standardized phenotypic screen^[11] to determine the effects of deletion.^{[12][13][14][15]} Additional screens performed: - In-depth immunological phenotyping^[16]

Tgfb1i1 knockout mouse phenotype

Characteristic	Phenotype
All data available at.[11][16]
Peripheral blood leukocytes 6 Weeks	Normal
Haematology 6 Weeks	Normal
Insulin	Normal
Homozygous viability at P14	Normal
Homozygous Fertility	Normal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Heart weight	Normal
Salmonella infection	Normal
Cytotoxic T Cell Function	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Bone Marrow Immunophenotyping	Normal
Epidermal Immune Composition	Normal
Influenza Challenge	Normal

See also

• Transcription coregulator

References

1. Matsuya M, Sasaki H, Aoto H, Mitaka T, Nagura K, Ohba T, Ishino M, Takahashi S, Suzuki R, Sasaki T (Jan 1998). "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions". The Journal of Biological Chemistry 273 (2): 1003–14. doi:10.1074/jbc.273.2.1003. PMID 9422762.
2. Fujimoto N, Yeh S, Kang HY, Inui S, Chang HC, Mizokami A, Chang C (Mar 1999). "Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate". The Journal of Biological Chemistry 274 (12): 8316–21. doi:10.1074/jbc.274.12.8316. PMID 10075738.
3. Wang X, Yang Y, Guo X, Sampson ER, Hsu CL, Tsai MY, Yeh S, Wu G, Guo Y, Chang C (May 2002). "Suppression of androgen receptor transactivation by Pyk2 via interaction and phosphorylation of the ARA55 coregulator". The Journal of Biological Chemistry 277 (18): 15426–31. doi:10.1074/jbc.M111218200. PMID 11856738.
4. He B, Minges JT, Lee LW, Wilson EM (Mar 2002). "The FXXLF motif mediates androgen receptor-specific interactions with coregulators". The Journal of Biological Chemistry 277 (12): 10226–35. doi:10.1074/jbc.M111975200. PMID 11779876.
5. Carneiro AM, Ingram SL, Beaulieu JM, Sweeney A, Amara SG, Thomas SM, Caron MG, Torres GE (Aug 2002). "The multiple LIM domain-containing adaptor protein Hic-5 synaptically colocalizes and interacts with the dopamine transporter". The Journal of Neuroscience 22 (16): 7045–54. PMID 12177201.
6. Jia Y, Ransom RF, Shibanuma M, Liu C, Welsh MJ, Smoyer WE (Oct 2001). "Identification and characterization of hic-5/ARA55 as an hsp27 binding protein". The Journal of Biological Chemistry 276 (43): 39911–8. doi:10.1074/jbc.M103510200. PMID 11546764.
7. Thomas SM, Hagel M, Turner CE (Jan 1999). "Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin". Journal of Cell Science 112 (2): 181–90. PMID 9858471.
8. Nishiya N, Tachibana K, Shibanuma M, Mashimo JI, Nose K (Aug 2001). "Hic-5-reduced cell spreading on fibronectin: competitive effects between paxillin and Hic-5 through interaction with focal adhesion kinase". Molecular and Cellular Biology 21 (16): 5332–45. doi:10.1128/MCB.21.16.5332-5345.2001. PMC 87257. PMID 11463817.
9. Nishiya N, Iwabuchi Y, Shibanuma M, Côté JF, Tremblay ML, Nose K (Apr 1999). "Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain". The Journal of Biological Chemistry 274 (14): 9847–53. doi:10.1074/jbc.274.14.9847. PMID 10092676.
10. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
11. "International Mouse Phenotyping Consortium".
12. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
13. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
14. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
15. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
16. "Infection and Immunity Immunophenotyping (3i) Consortium".

External links

• TGFB1I1 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
• NURSA C148

Further reading

• Yeh S, Sampson ER, Lee DK, Kim E, Hsu CL, Chen YL, Chang HC, Altuwaijri S, Huang KE, Chang C (Dec 2000). "Functional analysis of androgen receptor N-terminal and ligand binding domain interacting coregulators in prostate cancer". Journal of the Formosan Medical Association = Taiwan Yi Zhi 99 (12): 885–94. PMID 11155740.
• Heitzer MD, DeFranco DB (Feb 2007). "Hic-5/ARA55: a prostate stroma-specific AR coactivator". Steroids 72 (2): 218–20. doi:10.1016/j.steroids.2006.11.010. PMID 17166536.
• Wilson SE, Lloyd SA (Sep 1991). "Epidermal growth factor and its receptor, basic fibroblast growth factor, transforming growth factor beta-1, and interleukin-1 alpha messenger RNA production in human corneal endothelial cells". Investigative Ophthalmology & Visual Science 32 (10): 2747–56. PMID 1716619.
• Shibanuma M, Mashimo J, Kuroki T, Nose K (Oct 1994). "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". The Journal of Biological Chemistry 269 (43): 26767–74. PMID 7929412.
• Shibanuma M, Mochizuki E, Maniwa R, Mashimo J, Nishiya N, Imai S, Takano T, Oshimura M, Nose K (Mar 1997). "Induction of senescence-like phenotypes by forced expression of hic-5, which encodes a novel LIM motif protein, in immortalized human fibroblasts". Molecular and Cellular Biology 17 (3): 1224–35. doi:10.1128/mcb.17.3.1224. PMC 231847. PMID 9032249.
• Fujita H, Kamiguchi K, Cho D, Shibanuma M, Morimoto C, Tachibana K (Oct 1998). "Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase". The Journal of Biological Chemistry 273 (41): 26516–21. doi:10.1074/jbc.273.41.26516. PMID 9756887.
• Thomas SM, Hagel M, Turner CE (Jan 1999). "Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin". Journal of Cell Science 112 (2): 181–90. PMID 9858471.
• Nishiya N, Iwabuchi Y, Shibanuma M, Côté JF, Tremblay ML, Nose K (Apr 1999). "Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain". The Journal of Biological Chemistry 274 (14): 9847–53. doi:10.1074/jbc.274.14.9847. PMID 10092676.
• Turner CE, Brown MC, Perrotta JA, Riedy MC, Nikolopoulos SN, McDonald AR, Bagrodia S, Thomas S, Leventhal PS (May 1999). "Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling". The Journal of Cell Biology 145 (4): 851–63. doi:10.1083/jcb.145.4.851. PMC 2133183. PMID 10330411.
• Liu S, Thomas SM, Woodside DG, Rose DM, Kiosses WB, Pfaff M, Ginsberg MH (Dec 1999). "Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses". Nature 402 (6762): 676–81. doi:10.1038/45264. PMID 10604475.
• Yang L, Guerrero J, Hong H, DeFranco DB, Stallcup MR (Jun 2000). "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". Molecular Biology of the Cell 11 (6): 2007–18. doi:10.1091/mbc.11.6.2007. PMC 14899. PMID 10848625.
• Oda A, Ochs HD, Lasky LA, Spencer S, Ozaki K, Fujihara M, Handa M, Ikebuchi K, Ikeda H (May 2001). "CrkL is an adapter for Wiskott-Aldrich syndrome protein and Syk". Blood 97 (9): 2633–9. doi:10.1182/blood.V97.9.2633. PMID 11313252.
• Nishiya N, Tachibana K, Shibanuma M, Mashimo JI, Nose K (Aug 2001). "Hic-5-reduced cell spreading on fibronectin: competitive effects between paxillin and Hic-5 through interaction with focal adhesion kinase". Molecular and Cellular Biology 21 (16): 5332–45. doi:10.1128/MCB.21.16.5332-5345.2001. PMC 87257. PMID 11463817.
• Jia Y, Ransom RF, Shibanuma M, Liu C, Welsh MJ, Smoyer WE (Oct 2001). "Identification and characterization of hic-5/ARA55 as an hsp27 binding protein". The Journal of Biological Chemistry 276 (43): 39911–8. doi:10.1074/jbc.M103510200. PMID 11546764.
• Ting HJ, Yeh S, Nishimura K, Chang C (Jan 2002). "Supervillin associates with androgen receptor and modulates its transcriptional activity". Proceedings of the National Academy of Sciences of the United States of America 99 (2): 661–6. doi:10.1073/pnas.022469899. PMC 117362. PMID 11792840.
• Denhez F, Wilcox-Adelman SA, Baciu PC, Saoncella S, Lee S, French B, Neveu W, Goetinck PF (Apr 2002). "Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal adhesion adaptor proteins paxillin and Hic-5". The Journal of Biological Chemistry 277 (14): 12270–4. doi:10.1074/jbc.M110291200. PMID 11805099.
• Wang X, Yang Y, Guo X, Sampson ER, Hsu CL, Tsai MY, Yeh S, Wu G, Guo Y, Chang C (May 2002). "Suppression of androgen receptor transactivation by Pyk2 via interaction and phosphorylation of the ARA55 coregulator". The Journal of Biological Chemistry 277 (18): 15426–31. doi:10.1074/jbc.M111218200. PMID 11856738.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.