Transcription intermediary factor 1-beta Recombinant Protein | TRIM28 recombinant protein

Recombinant Human Transcription intermediary factor 1-beta protein

Cat. Num. AAA717118

• Gene Names: TRIM28; KAP1; TF1B; RNF96; TIF1B; PPP1R157
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Transcription intermediary factor 1-beta; Recombinant Human Transcription intermediary factor 1-beta protein; E3 SUMO-protein ligase TRIM28 (EC:6.3.2.-); KRAB-associated protein 1; KAP-1; KRAB-interacting protein 1; KRIP-1; Nuclear corepressor KAP-1; RING finger protein 96; Tripartite motif-containing protein 28; TRIM28 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 22-291aa; Partial
• Sequence: PGEGSAGGEKRSTAPSAAASASASAAASSPAGGGAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRV

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for TRIM28 recombinant protein

Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg)

Product Categories/Family for TRIM28 recombinant protein

Transcription

References

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Biotechnol. 24:1285-1292(2006) Chromatin relaxation in response to DNA double-strand breaks is modulated by a novel ATM- and KAP-1 dependent pathway.Ziv Y., Bielopolski D., Galanty Y., Lukas C., Taya Y., Schultz D.C., Lukas J., Bekker-Jensen S., Bartek J., Shiloh Y.Nat. Cell Biol. 8:870-876(2006) MAGE-A, mMage-b, and MAGE-C proteins form complexes with KAP1 and suppress p53-dependent apoptosis in MAGE-positive cell lines.Yang B., O'Herrin S.M., Wu J., Reagan-Shaw S., Ma Y., Bhat K.M., Gravekamp C., Setaluri V., Peters N., Hoffmann F.M., Peng H., Ivanov A.V., Simpson A.J., Longley B.J.Cancer Res. 67:9954-9962(2007) Doxorubicin down-regulates Kruppel-associated box domain-associated protein 1 sumoylation that relieves its transcription repression on p21WAF1/CIP1 in breast cancer MCF-7 cells.Lee Y.K., Thomas S.N., Yang A.J., Ann D.K.J. Biol. Chem. 282:1595-1606(2007) Regulation of E2F1 function by the nuclear corepressor KAP1.Wang C., Rauscher F.J. III, Cress W.D., Chen J.J. Biol. Chem. 282:29902-29909(2007) Role for KAP1 serine 824 phosphorylation and sumoylation/desumoylation switch in regulating KAP1-mediated transcriptional repression.Li X., Lee Y.K., Jeng J.C., Yen Y., Schultz D.C., Shih H.M., Ann D.K.J. Biol. Chem. 282:36177-36189(2007) Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.J. Proteome Res. 6:4150-4162(2007) PHD domain-mediated E3 ligase activity directs intramolecular sumoylation of an adjacent bromodomain required for gene silencing.Ivanov A.V., Peng H., Yurchenko V., Yap K.L., Negorev D.G., Schultz D.C., Psulkowski E., Fredericks W.J., White D.E., Maul G.G., Sadofsky M.J., Zhou M.M., Rauscher F.J. IIIMol. Cell 28:823-837(2007) ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.Science 316:1160-1166(2007) A novel GDNF-inducible gene, BMZF3, encodes a transcriptional repressor associated with KAP-1.Suzuki C., Murakumo Y., Kawase Y., Sato T., Morinaga T., Fukuda N., Enomoto A., Ichihara M., Takahashi M.Biochem. Biophys. Res. Commun. 366:226-232(2008) The novel protein complex with SMARCAD1/KIAA1122 binds to the vicinity of TSS.Okazaki N., Ikeda S., Ohara R., Shimada K., Yanagawa T., Nagase T., Ohara O., Koga H.J. Mol. Biol. 382:257-265(2008) Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. IIIJ. Proteome Res. 7:1346-1351(2008) Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.J. Proteome Res. 7:5167-5176(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification.Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.J. Biol. Chem. 285:19324-19329(2010) Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways.Gilmore-Hebert M., Ramabhadran R., Stern D.F.Mol. Cancer Res. 8:1388-1398(2010) MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases.Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.Mol. Cell 39:963-974(2010) Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation.Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C.Nat. Cell Biol. 12:719-727(2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) SUMOylation of the transcriptional co-repressor KAP1 is regulated by the serine and threonine phosphatase PP1.Li X., Lin H.H., Chen H., Xu X., Shih H.M., Ann D.K.Sci. Signal. 3:RA32-RA32(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) Tripartite motif-containing protein 28 is a small ubiquitin-related modifier E3 ligase and negative regulator of IFN regulatory factor 7.Liang Q., Deng H., Li X., Wu X., Tang Q., Chang T.H., Peng H., Rauscher F.J. III, Ozato K., Zhu F.J. Immunol. 187:4754-4763(2011) Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1.Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E.Mol. Cell 42:285-296(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) Novel activity of KRAB domain that functions to reinforce nuclear localization of KRAB-containing zinc finger proteins by interacting with KAP1.Wang W., Cai J., Wu Y., Hu L., Chen Z., Hu J., Chen Z., Li W., Guo M., Huang Z.Cell. Mol. Life Sci. 70:3947-3958(2013) Cutting Edge a novel, human-specific interacting protein couples FOXP3 to a chromatin-remodeling complex that contains KAP1/TRIM28.Huang C., Martin S., Pfleger C., Du J., Buckner J.H., Bluestone J.A., Riley J.L., Ziegler S.F.J. Immunol. 190:4470-4473(2013) Senataxin, defective in the neurodegenerative disorder ataxia with oculomotor apraxia 2, lies at the interface of transcription and the DNA damage response.Yuce O., West S.C.Mol. Cell. Biol. 33:406-417(2013) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Solution structure of the PHD domain from the KAP-1 corepressor structural determinants for PHD, RING and LIM zinc-binding domains.Capili A.D., Schultz D.C., Rauscher F.J. III, Borden K.L.EMBO J. 20:165-177(2001) Structural insights into human KAP1 PHD finger-bromodomain and its role in gene silencing.Zeng L., Yap K.L., Ivanov A.V., Wang X., Mujtaba S., Plotnikova O., Rauscher F.J. III, Zhou M.M.Nat. Struct. Mol. Biol. 15:626-633(2008) Crystal structure of ms1043.RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bankPatterns of somatic mutation in human cancer genomes.Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.Nature 446:153-158(2007) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 5032179
• NCBI GeneID: 10155
• NCBI Accession #: NP_005753.1
• NCBI GenBank Nucleotide #: NM_005762.2
• UniProt Accession #: Q13263; O00677; Q7Z632; Q93040; Q96IM1
• Molecular Weight: 55.8 kDa
• NCBI Official Full Name: transcription intermediary factor 1-beta
• NCBI Official Synonym Full Names: tripartite motif containing 28
• NCBI Official Symbol: TRIM28
• NCBI Official Synonym Symbols: KAP1; TF1B; RNF96; TIF1B; PPP1R157
• NCBI Protein Information: transcription intermediary factor 1-beta
• UniProt Protein Name: Transcription intermediary factor 1-beta
• Protein Family: Transcription intermediary factor
• UniProt Gene Name: TRIM28
• UniProt Synonym Gene Names: KAP1; RNF96; TIF1B; TIF1-beta; KAP-1; KRIP-1
• UniProt Entry Name: TIF1B_HUMAN

NCBI Description

The protein encoded by this gene mediates transcriptional control by interaction with the Kruppel-associated box repression domain found in many transcription factors. The protein localizes to the nucleus and is thought to associate with specific chromatin regions. The protein is a member of the tripartite motif family. This tripartite motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. [provided by RefSeq, Jul 2008]

Uniprot Description

TIF1B: an atypical protein kinase that functions as a transcriptional coactivator. Mediates transcriptional regulation by interaction with the Kruppel-associated box (KRAB) repression domain found in many transcription factors. Binds to the negative regulatory domain of c-Myb and negatively regulates the c-Myb-dependent trans-activation. Localizes to the nucleus and is thought to associate with specific chromatin regions. Phosphorylated in an ATM-dependent manner following double-strand breaks. Its phosphorylation in response to DNA damage leads to chromatin relaxation. A member of the tripartite motif family. The tripartite motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region.

Protein type: Transcription, coactivator/corepressor; Protein kinase, atypical; Ubiquitin ligase; Ligase; Nuclear receptor co-regulator; EC 6.3.2.-; Kinase, protein; Ubiquitin conjugating system; ATYPICAL group; TIF1 family

Chromosomal Location of Human Ortholog: 19q13.4

Cellular Component: nuclear heterochromatin; nucleoplasm; nucleus

Molecular Function: DNA binding; ligase activity; protein binding; protein kinase activity; sequence-specific DNA binding; transcription corepressor activity; transcription factor activity; ubiquitin protein ligase binding; ubiquitin-protein ligase activity; zinc ion binding

Biological Process: convergent extension involved in axis elongation; DNA methylation during embryonic development; DNA repair; embryo implantation; epithelial to mesenchymal transition; gene expression; innate immune response; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; positive regulation of DNA repair; positive regulation of transcription factor import into nucleus; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; protein amino acid autophosphorylation; protein oligomerization; protein sumoylation; protein ubiquitination; transcription initiation from RNA polymerase II promoter