protein

Recombinant Human E3 ubiquitin-protein ligase TRIM21

MBS952632

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human E3 ubiquitin-protein ligase TRIM21

E3 ubiquitin-protein ligase TRIM21

2 kDa Ro protein; 52 kDa ribonucleoprotein autoantigen Ro/SS-A; RING finger protein 81; Ro(SS-A); Sjoegren syndrome type A antigen; SS-A; Tripartite motif-containing protein 21

E3 ubiquitin-protein ligase TRIM21; E3 ubiquitin-protein ligase TRIM21; E3 ubiquitin-protein ligase TRIM21; tripartite motif containing 21; 52 kDa Ro protein; 52 kDa ribonucleoprotein autoantigen Ro/SS-A; RING finger protein 81; Ro(SS-A); Sjoegren syndrome type A antigen; SS-A; Tripartite motif-containing protein 21

TRIM21

TRIM21; TRIM21; SSA; RO52; SSA1; RNF81; Ro/SSA; RNF81; RO52; SSA1; SS-A

RO52_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1-475

398

MASAARLTMMWEEVTCPICLDPFVEPVSIECGHSFCQEC
ISQVGKGGGSVCPVCRQRFLLKNLRPNRQLANMVNNLKE
ISQEAREGTQGERCAVHGERLHLFCEKDGKALCWVCAQS
RKHRDHAMVPLEEAAQEYQEKLQVALGELRRKQELAEKL
EVEIAIKRADWKKTVETQKSRIHAEFVQQKNFLVEEEQR
QLQELEKDEREQLRILGEKEAKLAQQSQALQELISELDR
RCHSSALELLQEVIIVLERSE

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Epigenetics and Nuclear Signaling

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs. 2

Protein heterogeneity in the human Ro/SSA ribonucleoproteins. The 52- and 60-kD Ro/SSA autoantigens are encoded by separate genes.Itoh K., Itoh Y., Frank M.B.J. Clin. Invest. 87:177-186(1991) Molecular definition and sequence motifs of the 52-kD component of human SS-A/Ro autoantigen.Chan E.K., Hamel J.C., Buyon J.P., Tan E.M.J. Clin. Invest. 87:68-76(1991) The location of a disease-associated polymorphism and genomic structure of the human 52-kDa Ro/SSA locus (SSA1) .Tsugu H., Horowitz R., Gibson N., Frank M.B.Genomics 24:541-548(1994) Structural differences between the human and mouse 52-kD Ro autoantigens associated with poorly conserved autoantibody activity across species.Keech C.L., Gordon T.P., McCluskey J.Clin. Exp. Immunol. 104:255-263(1996) A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region.Bepler G., O'Briant K.C., Kim Y.-C., Schreiber G., Pitterle D.M.Genomics 55:164-175(1999) Isolation of human Sjogren syndrome type A antigen cDNA clone from HEp-2 cells, isolate 1.Chen Y.-J., Fan Y.-H., Chiou S.-H.Human chromosome 11 DNA sequence and analysis including novel gene identification.Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.Nature 440:497-500(2006) 52-kD SS-A/Ro genomic structure and identification of an alternatively spliced transcript encoding a novel leucine zipper-minus autoantigen expressed in fetal and adult heart.Chan E.K., Di Donato F., Hamel J.C., Tseng C.E., Buyon J.P.J. Exp. Med. 182:983-992(1995) Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen.Cheng S.T., Nguyen T.Q., Yang Y.S., Capra J.D., Sontheimer R.D.J. Immunol. 156:4484-4491(1996) Association of stress proteins with autoantigens a possible mechanism for triggering autoimmunity?Purcell A.W., Todd A., Kinoshita G., Lynch T.A., Keech C.L., Gething M.J., Gordon T.P.Clin. Exp. Immunol. 132:193-200(2003) Autoantigen Ro52 is an E3 ubiquitin ligase.Wada K., Kamitani T.Biochem. Biophys. Res. Commun. 339:415-421(2006) Oncogenic protein UnpEL/Usp4 deubiquitinates Ro52 by its isopeptidase activity.Wada K., Tanji K., Kamitani T.Biochem. Biophys. Res. Commun. 339:731-736(2006) UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself.Wada K., Kamitani T.Biochem. Biophys. Res. Commun. 342:253-258(2006) Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein.Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M., Krek W.Mol. Cell. Biol. 26:5994-6004(2006) SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping activity.Yamochi T., Ohnuma K., Hosono O., Tanaka H., Kanai Y., Morimoto C.Biochem. Biophys. Res. Commun. 370:195-199(2008) The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but enters the nucleus upon cellular exposure to nitric oxide.Espinosa A., Oke V., Elfving A., Nyberg F., Covacu R., Wahren-Herlenius M.Exp. Cell Res. 314:3605-3613(2008) The E3 ubiquitin ligase Ro52 negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3.Higgs R., Ni Gabhann J., Ben Larbi N., Breen E.P., Fitzgerald K.A., Jefferies C.A.J. Immunol. 181:1780-1786(2008) Ro52 functionally interacts with IgG1 and regulates its quality control via the ERAD system.Takahata M., Bohgaki M., Tsukiyama T., Kondo T., Asaka M., Hatakeyama S.Mol. Immunol. 45:2045-2054(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) Ro52-mediated monoubiquitination of IKK{beta} down-regulates NF-{kappa}B signalling.Wada K., Niida M., Tanaka M., Kamitani T.J. Biochem. 146:821-832(2009) Extraordinary antigenicity of the human Ro52 autoantigen.Burbelo P.D., Ching K.H., Han B.L., Bush E.R., Reeves W.H., Iadarola M.J.Am. J. Transl. Res. 2:145-155(2010) Dynamic movements of Ro52 cytoplasmic bodies along microtubules.Tanaka M., Tanji K., Niida M., Kamitani T.Histochem. Cell Biol. 133:273-284(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) 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)

15208660

NP_003132.2

NM_003141.3

P19474

56.17kD

Adaptive Immune System Pathway (1269171); Antigen Processing: Ubiquitination Proteasome Degradation Pathway (1269193); Class I MHC Mediated Antigen Processing Presentation Pathway (1269192); Cytokine Signaling In Immune System Pathway (1269310); Cytosolic Sensors Of Pathogen-associated DNA Pathway (1269268); Immune System Pathway (1269170); Innate Immune System Pathway (1269203); Interferon Signaling Pathway (1269311); Interferon Gamma Signaling Pathway (1269314); Regulation Of Innate Immune Responses To Cytosolic DNA Pathway (1269277)

This gene encodes a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The encoded protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. RoSSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Alternatively spliced transcript variants for this gene have been described but the full-length nature of only one has been determined. [provided by RefSeq, Jul 2008]

TRIM21: E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)- like complex is shown to mediate ubiquitination of CDKN1B ('Thr- 187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin- mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2. Belongs to the TRIM/RBCC family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Ubiquitin ligase; Ubiquitin conjugating system; EC 6.3.2.-; Ligase. Chromosomal Location of Human Ortholog: 11p15.5. Cellular Component: autophagic vacuole; cytoplasm; cytoplasmic vesicle; cytosol; nucleus; ribonucleoprotein complex; SCF ubiquitin ligase complex. Molecular Function: DNA binding; identical protein binding; ligase activity; protein binding; RNA binding; ubiquitin-protein ligase activity; zinc ion binding. Biological Process: cell cycle; cytokine and chemokine mediated signaling pathway; inhibition of NF-kappaB transcription factor; innate immune response; negative regulation of viral transcription; positive regulation of autophagy; positive regulation of cell cycle; positive regulation of interferon type I production; positive regulation of transcription factor activity; positive regulation of virion penetration into host cell; protein autoubiquitination; protein destabilization; protein monoubiquitination; protein polyubiquitination; protein ubiquitination; regulation of interferon type I production

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180

0.05 mg (Baculovirus)

1260