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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Tripartite motif-containing protein 21''' also known as '''E3 ubiquitin-protein ligase TRIM21''' is a [[protein]] that in humans is encoded by the ''TRIM21'' [[gene]].<ref name="pmid8094596">{{cite journal |vauthors=Frank MB, Itoh K, Fujisaku A, Pontarotti P, Mattei MG, Neas BR | title = The mapping of the human 52-kD Ro/SSA autoantigen gene to human chromosome 11, and its polymorphisms | journal = Am J Hum Genet | volume = 52 | issue = 1 | pages = 183–91 |date=Mar 1993 | pmid = 8094596 | pmc = 1682114 | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TRIM21 tripartite motif-containing 21| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6737| accessdate = }}</ref> Alternatively spliced transcript variants for this gene have been described but the full-length nature of only one has been determined. It is expressed in most human tissues.<ref name="pmid21045130"/>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Structure ==
{{GNF_Protein_box
| image = PBB_Protein_TRIM21_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2iwg.
| PDB = {{PDB2|2iwg}}
| Name = Tripartite motif-containing 21
| HGNCid = 11312
| Symbol = TRIM21
| AltSymbols =; SSA; RNF81; RO52; SSA1
| OMIM = 109092
| ECnumber = 
| Homologene = 2365
| MGIid = 106657
| GeneAtlas_image1 = PBB_GE_TRIM21_204804_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0030529 |text = ribonucleoprotein complex}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6737
    | Hs_Ensembl = ENSG00000132109
    | Hs_RefseqProtein = NP_003132
    | Hs_RefseqmRNA = NM_003141
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 4362734
    | Hs_GenLoc_end = 4371502
    | Hs_Uniprot = P19474
    | Mm_EntrezGene = 20821
    | Mm_Ensembl = ENSMUSG00000030966
    | Mm_RefseqmRNA = XM_991802
    | Mm_RefseqProtein = XP_996896
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 102432657
    | Mm_GenLoc_end = 102439262
    | Mm_Uniprot = Q3U7K7
  }}
}}
'''Tripartite motif-containing 21''', also known as '''TRIM21''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TRIM21 tripartite motif-containing 21| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6737| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
TRIM21 is a member of the [[tripartite motif family|tripartite motif]] (TRIM) family. The TRIM motif includes three zinc-binding domains, a [[RING finger domain]], a B-box type 1 and a B-box type 2 [[zinc finger]], and a [[coiled coil]] region.<ref name="entrez"/>
{{PBB_Summary
 
| section_title =
== Function ==
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: TRIM21 tripartite motif-containing 21| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6737| accessdate = }}</ref>
 
}}
TRIM21 is an intracellular antibody effector in the [[intracellular antibody-mediated proteolysis]] pathway. It recognizes [[Fc-domain|Fc domain]]<ref name="pmid17400754">{{cite journal | vauthors = James LC, Keeble AH, Khan Z, Rhodes DA, Trowsdale J | title = Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 15 | pages = 6200–5 | year = 2007 | pmid = 17400754 | pmc = 1851072 | doi = 10.1073/pnas.0609174104 }}</ref> and binds to [[immunoglobulin G]] as well as [[immunoglobulin M]] on antibody marked non-enveloped virions which have infected the cell. Either by [[Ubiquitin|autoubiquitination]] or by ubiquitination of a cofactor, it is then responsible for directing the virions to the [[proteasome]]. TRIM21 itself is not degraded in the proteasome unlike both the viral capsid and the bound antibody.<ref name="pmid21045130">{{cite journal | vauthors = Mallery DL, McEwan WA, Bidgood SR, Towers GJ, Johnson CM, James LC | title = Antibodies mediate intracellular immunity through tripartite motif-containing 21 (TRIM21) | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 107 | issue = 46 | pages = 19985–90 | year = 2010 | pmid = 21045130 | pmc = 2993423 | doi = 10.1073/pnas.1014074107 }}</ref>
 
TRIM21 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.<ref name="entrez"/>
 
== Clinical significance ==
 
RoSSA interacts with autoantigens in patients with [[Sjögren's syndrome]] and [[systemic lupus erythematosus]].<ref name="entrez"/>
 
TRIM21 can be used to knockout specific proteins with their corresponding antibodies, a method known as Trim-Away. In this assay, TRIM21 and  antibodies are delivered into cells through [[electroporation]], and the targeted protein is degraded within a few minutes.<ref>{{cite journal | vauthors = Clift D, McEwan WA, Labzin LI, Konieczny V, Mogessie B, James LC, Schuh M | title = A Method for the Acute and Rapid Degradation of Endogenous Proteins | journal=Cell | doi=10.1016/j.cell.2017.10.033 | }}</ref>  


==References==
==References==
{{reflist|2}}
{{reflist}}
{{Clear}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | author=Jones SK |title=Ultraviolet radiation (UVR) induces cell-surface Ro/SSA antigen expression by human keratinocytes in vitro: a possible mechanism for the UVR induction of cutaneous lupus lesions |journal=Br. J. Dermatol. |volume=126 |issue= 6 |pages= 546–553 |year= 1992 |pmid= 1610705 |doi=10.1111/j.1365-2133.1992.tb00098.x }}
| citations =
*{{cite journal  |vauthors=Itoh K, Itoh Y, Frank MB |title=Protein heterogeneity in the human Ro/SSA ribonucleoproteins. The 52- and 60-kD Ro/SSA autoantigens are encoded by separate genes |journal=J. Clin. Invest. |volume=87 |issue= 1 |pages= 177–186 |year= 1991 |pmid= 1985094 |doi=10.1172/JCI114968  | pmc=295020 }}
*{{cite journal  | author=Jones SK |title=Ultraviolet radiation (UVR) induces cell-surface Ro/SSA antigen expression by human keratinocytes in vitro: a possible mechanism for the UVR induction of cutaneous lupus lesions. |journal=Br. J. Dermatol. |volume=126 |issue= 6 |pages= 546-53 |year= 1992 |pmid= 1610705 |doi=  }}
*{{cite journal  |vauthors=Chan EK, Hamel JC, Buyon JP, Tan EM |title=Molecular definition and sequence motifs of the 52-kD component of human SS-A/Ro autoantigen |journal=J. Clin. Invest. |volume=87 |issue= 1 |pages= 68–76 |year= 1991 |pmid= 1985112 |doi=10.1172/JCI115003  | pmc=294993 }}
*{{cite journal  | author=Itoh K, Itoh Y, Frank MB |title=Protein heterogeneity in the human Ro/SSA ribonucleoproteins. The 52- and 60-kD Ro/SSA autoantigens are encoded by separate genes. |journal=J. Clin. Invest. |volume=87 |issue= 1 |pages= 177-86 |year= 1991 |pmid= 1985094 |doi=  }}
*{{cite journal  | author=Miyagawa S |title=SSA/Ro antigen expression in simian virus 40-transformed human keratinocytes |journal=J. Invest. Dermatol. |volume=90 |issue= 3 |pages= 342–345 |year= 1988 |pmid= 2450143 |doi=10.1111/1523-1747.ep12456308 |name-list-format=vanc| author2=Okada N  | author3=Inagaki Y  | display-authors=3  | last4=Kitano  | first4=Yukio  | last5=Ueki  | first5=Hiroaki  | last6=Sakamoto  | first6=Kuniki  | last7=Steinberg  | first7=Mark L. }}
*{{cite journal  | author=Chan EK, Hamel JC, Buyon JP, Tan EM |title=Molecular definition and sequence motifs of the 52-kD component of human SS-A/Ro autoantigen. |journal=J. Clin. Invest. |volume=87 |issue= 1 |pages= 68-76 |year= 1991 |pmid= 1985112 |doi=  }}
*{{cite journal  | author=Chan EK |title=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 |journal=J. Exp. Med. |volume=182 |issue= 4 |pages= 983–992 |year= 1995 |pmid= 7561701 |doi=10.1084/jem.182.4.983  | pmc=2192297 |name-list-format=vanc| author2=Di Donato F  | author3=Hamel JC  | display-authors=3  | last4=Tseng | first4=CE  | last5=Buyon  | first5=JP }}
*{{cite journal  | author=Miyagawa S, Okada N, Inagaki Y, ''et al.'' |title=SSA/Ro antigen expression in simian virus 40-transformed human keratinocytes. |journal=J. Invest. Dermatol. |volume=90 |issue= 3 |pages= 342-5 |year= 1988 |pmid= 2450143 |doi= }}
*{{cite journal  |vauthors=Tsugu H, Horowitz R, Gibson N, Frank MB |title=The location of a disease-associated polymorphism and genomic structure of the human 52-kDa Ro/SSA locus (SSA1) |journal=Genomics |volume=24 |issue= 3 |pages= 541–548 |year= 1995 |pmid= 7713506 |doi= 10.1006/geno.1994.1664 }}
*{{cite journal | author=Chan EK, Di Donato F, Hamel JC, ''et al.'' |title=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. |journal=J. Exp. Med. |volume=182 |issue= 4 |pages= 983-92 |year= 1995 |pmid= 7561701 |doi=  }}
*{{cite journal  |vauthors=Frank MB, McCubbin VR, Heldermon C |title=Expression and DNA binding of the human 52 kDa Ro/SSA autoantigen |journal=Biochem. J. |volume=305 |issue= 2|pages= 359–62 |year= 1995 |pmid= 7832745 |doi= | pmc=1136368 }}
*{{cite journal  | author=Tsugu H, Horowitz R, Gibson N, Frank MB |title=The location of a disease-associated polymorphism and genomic structure of the human 52-kDa Ro/SSA locus (SSA1). |journal=Genomics |volume=24 |issue= 3 |pages= 541-8 |year= 1995 |pmid= 7713506 |doi= 10.1006/geno.1994.1664 }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–174 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Frank MB, McCubbin VR, Heldermon C |title=Expression and DNA binding of the human 52 kDa Ro/SSA autoantigen. |journal=Biochem. J. |volume=305 ( Pt 2) |issue=  |pages= 359-62 |year= 1995 |pmid= 7832745 |doi=  }}
*{{cite journal  |vauthors=Keech CL, Gordon TP, McCluskey J |title=Structural differences between the human and mouse 52-kD Ro autoantigens associated with poorly conserved autoantibody activity across species |journal=Clin. Exp. Immunol. |volume=104 |issue= 2 |pages= 255–263 |year= 1996 |pmid= 8625517 |doi=10.1046/j.1365-2249.1996.16726.x  | pmc=2200432  }}
*{{cite journal  | author=Frank MB, Itoh K, Fujisaku A, ''et al.'' |title=The mapping of the human 52-kD Ro/SSA autoantigen gene to human chromosome 11, and its polymorphisms. |journal=Am. J. Hum. Genet. |volume=52 |issue= 1 |pages= 183-91 |year= 1993 |pmid= 8094596 |doi= }}
*{{cite journal  |vauthors=Igarashi T, Itoh Y, Fukunaga Y, Yamamoto M |title=Stress-induced cell surface expression and antigenic alteration of the Ro/SSA autoantigen |journal=Autoimmunity |volume=22 |issue= 1 |pages= 33–42 |year= 1996 |pmid= 8882420 |doi=10.3109/08916939508995297 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | author=Suzuki Y |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–156 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |name-list-format=vanc| author2=Yoshitomo-Nakagawa K | author3=Maruyama K  | display-authors=3  | last4=Suyama  | first4=A  | last5=Sugano  | first5=S  }}
*{{cite journal  | author=Keech CL, Gordon TP, McCluskey J |title=Structural differences between the human and mouse 52-kD Ro autoantigens associated with poorly conserved autoantibody activity across species. |journal=Clin. Exp. Immunol. |volume=104 |issue= 2 |pages= 255-63 |year= 1996 |pmid= 8625517 |doi=  }}
*{{cite journal  | author=Bepler G |title=A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region |journal=Genomics |volume=55 |issue= 2 |pages= 164–175 |year= 1999 |pmid= 9933563 |doi= 10.1006/geno.1998.5659 |name-list-format=vanc| author2=O'briant KC  | author3=Kim YC  | display-authors=3  | last4=Schreiber  | first4=G  | last5=Pitterle  | first5=DM }}
*{{cite journal  | author=Igarashi T, Itoh Y, Fukunaga Y, Yamamoto M |title=Stress-induced cell surface expression and antigenic alteration of the Ro/SSA autoantigen. |journal=Autoimmunity |volume=22 |issue= 1 |pages= 33-42 |year= 1996 |pmid= 8882420 |doi= }}
*{{cite journal  | author=Tseng CE |title=mRNA and protein expression of SSA/Ro and SSB/La in human fetal cardiac myocytes cultured using a novel application of the Langendorff procedure |journal=Pediatr. Res. |volume=45 |issue= 2 |pages= 260–269 |year= 1999 |pmid= 10022600 |doi=10.1203/00006450-199902000-00018 |name-list-format=vanc| author2=Miranda E | author3=Di Donato F  | display-authors=3  | last4=Boutjdir  | first4=Mohamed  | last5=Rashbaum  | first5=William  | last6=Chan  | first6=Edward K. L.  | last7=Buyon  | first7=Jill P. }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | author=Fabini G |title=Analysis of the molecular composition of Ro ribonucleoprotein complexes. Identification of novel Y RNA-binding proteins |journal=Eur. J. Biochem. |volume=267 |issue= 9 |pages= 2778–2789 |year= 2000 |pmid= 10785401 |doi=10.1046/j.1432-1327.2000.01298.x |name-list-format=vanc| author2=Rutjes SA  | author3=Zimmermann C  | display-authors=3  | last4=Pruijn  | first4=Ger J. M.  | last5=Steiner  | first5=Gunter }}
*{{cite journal  | author=Bepler G, O'briant KC, Kim YC, ''et al.'' |title=A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region. |journal=Genomics |volume=55 |issue= 2 |pages= 164-75 |year= 1999 |pmid= 9933563 |doi= 10.1006/geno.1998.5659 }}
*{{cite journal  | author=Kurien BT |title=Autoantibody to the leucine zipper region of 52 kDa Ro/SSA binds native 60 kDa Ro/SSA: identification of a tertiary epitope with components from 60 kDa Ro/SSA and 52 kDa Ro/SSA |journal=Scand. J. Immunol. |volume=53 |issue= 3 |pages= 268–276 |year= 2001 |pmid= 11251884 |doi=10.1046/j.1365-3083.2001.00870.x  |name-list-format=vanc| author2=Chambers TL  | author3=Thomas PY  | display-authors=3  | last4=Frank  | first4=M. B.  | last5=Scofield  | first5=R. H.  }}
*{{cite journal | author=Tseng CE, Miranda E, Di Donato F, ''et al.'' |title=mRNA and protein expression of SSA/Ro and SSB/La in human fetal cardiac myocytes cultured using a novel application of the Langendorff procedure. |journal=Pediatr. Res. |volume=45 |issue= 2 |pages= 260-9 |year= 1999 |pmid= 10022600 |doi=  }}
*{{cite journal  | author=Reymond A |title=The tripartite motif family identifies cell compartments |journal=EMBO J. |volume=20 |issue= 9 |pages= 2140–2151 |year= 2001 |pmid= 11331580 |doi= 10.1093/emboj/20.9.2140  | pmc=125245  |name-list-format=vanc| author2=Meroni G  | author3=Fantozzi A  | display-authors=3  | last4=Merla  | first4=G  | last5=Cairo  | first5=S  | last6=Luzi  | first6=L  | last7=Riganelli  | first7=D  | last8=Zanaria  | first8=E  | last9=Messali  | first9=S }}
*{{cite journal  | author=Fabini G, Rutjes SA, Zimmermann C, ''et al.'' |title=Analysis of the molecular composition of Ro ribonucleoprotein complexes. Identification of novel Y RNA-binding proteins. |journal=Eur. J. Biochem. |volume=267 |issue= 9 |pages= 2778-89 |year= 2000 |pmid= 10785401 |doi=  }}
*{{cite journal  | author=Di Donato F |title=Interaction between 52 kDa SSA/Ro and deubiquitinating enzyme UnpEL: a clue to function |journal=Int. J. Biochem. Cell Biol. |volume=33 |issue= 9 |pages= 924–934 |year= 2001 |pmid= 11461834 |doi=10.1016/S1357-2725(01)00055-3  |name-list-format=vanc| author2=Chan EK  | author3=Askanase AD  | display-authors=3  | last4=Miranda-Carus  | first4=Maria-Eugenia  | last5=Buyon  | first5=Jill P  }}
*{{cite journal  | author=Kurien BT, Chambers TL, Thomas PY, ''et al.'' |title=Autoantibody to the leucine zipper region of 52 kDa Ro/SSA binds native 60 kDa Ro/SSA: identification of a tertiary epitope with components from 60 kDa Ro/SSA and 52 kDa Ro/SSA. |journal=Scand. J. Immunol. |volume=53 |issue= 3 |pages= 268-76 |year= 2001 |pmid= 11251884 |doi=  }}
*{{cite journal  |vauthors=Fukuda-Kamitani T, Kamitani T |title=Ubiquitination of Ro52 autoantigen |journal=Biochem. Biophys. Res. Commun. |volume=295 |issue= 4 |pages= 774–778 |year= 2002 |pmid= 12127959 |doi=10.1016/S0006-291X(02)00750-7  }}
*{{cite journal | author=Reymond A, Meroni G, Fantozzi A, ''et al.'' |title=The tripartite motif family identifies cell compartments. |journal=EMBO J. |volume=20 |issue= 9 |pages= 2140-51 |year= 2001 |pmid= 11331580 |doi= 10.1093/emboj/20.9.2140 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–16903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Di Donato F, Chan EK, Askanase AD, ''et al.'' |title=Interaction between 52 kDa SSA/Ro and deubiquitinating enzyme UnpEL: a clue to function. |journal=Int. J. Biochem. Cell Biol. |volume=33 |issue= 9 |pages= 924-34 |year= 2001 |pmid= 11461834 |doi= }}
*{{cite journal | author=Fukuda-Kamitani T, Kamitani T |title=Ubiquitination of Ro52 autoantigen. |journal=Biochem. Biophys. Res. Commun. |volume=295 |issue= 4 |pages= 774-8 |year= 2002 |pmid= 12127959 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{refend}}
 
{{PDB Gallery|geneid=6737}}
{{protein-stub}}
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Revision as of 08:53, 18 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Tripartite motif-containing protein 21 also known as E3 ubiquitin-protein ligase TRIM21 is a protein that in humans is encoded by the TRIM21 gene.[1][2] Alternatively spliced transcript variants for this gene have been described but the full-length nature of only one has been determined. It is expressed in most human tissues.[3]

Structure

TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING finger domain, a B-box type 1 and a B-box type 2 zinc finger, and a coiled coil region.[2]

Function

TRIM21 is an intracellular antibody effector in the intracellular antibody-mediated proteolysis pathway. It recognizes Fc domain[4] and binds to immunoglobulin G as well as immunoglobulin M on antibody marked non-enveloped virions which have infected the cell. Either by autoubiquitination or by ubiquitination of a cofactor, it is then responsible for directing the virions to the proteasome. TRIM21 itself is not degraded in the proteasome unlike both the viral capsid and the bound antibody.[3]

TRIM21 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.[2]

Clinical significance

RoSSA interacts with autoantigens in patients with Sjögren's syndrome and systemic lupus erythematosus.[2]

TRIM21 can be used to knockout specific proteins with their corresponding antibodies, a method known as Trim-Away. In this assay, TRIM21 and antibodies are delivered into cells through electroporation, and the targeted protein is degraded within a few minutes.[5]

References

  1. ↑ Frank MB, Itoh K, Fujisaku A, Pontarotti P, Mattei MG, Neas BR (Mar 1993). "The mapping of the human 52-kD Ro/SSA autoantigen gene to human chromosome 11, and its polymorphisms". Am J Hum Genet. 52 (1): 183–91. PMC 1682114. PMID 8094596.
  2. ↑ 2.0 2.1 2.2 2.3 "Entrez Gene: TRIM21 tripartite motif-containing 21".
  3. ↑ 3.0 3.1 Mallery DL, McEwan WA, Bidgood SR, Towers GJ, Johnson CM, James LC (2010). "Antibodies mediate intracellular immunity through tripartite motif-containing 21 (TRIM21)". Proceedings of the National Academy of Sciences of the United States of America. 107 (46): 19985–90. doi:10.1073/pnas.1014074107. PMC 2993423. PMID 21045130.
  4. ↑ James LC, Keeble AH, Khan Z, Rhodes DA, Trowsdale J (2007). "Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function". Proceedings of the National Academy of Sciences of the United States of America. 104 (15): 6200–5. doi:10.1073/pnas.0609174104. PMC 1851072. PMID 17400754.
  5. ↑ Clift D, McEwan WA, Labzin LI, Konieczny V, Mogessie B, James LC, Schuh M. "A Method for the Acute and Rapid Degradation of Endogenous Proteins". Cell. doi:10.1016/j.cell.2017.10.033.

Further reading

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