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E3 ubiquitin-protein ligase TRIM21 (EC 2.3.2.27) (52 kDa Ro protein) (52 kDa ribonucleoprotein autoantigen Ro/SS-A) (RING finger protein 81) (RING-type E3 ubiquitin transferase TRIM21) (Ro(SS-A)) (Sjoegren syndrome type A antigen) (SS-A) (Tripartite motif-containing protein 21)

 RO52_HUMAN              Reviewed;         475 AA.
P19474; Q5XPV5; Q96RF8;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
22-NOV-2017, entry version 198.
RecName: Full=E3 ubiquitin-protein ligase TRIM21;
EC=2.3.2.27;
AltName: Full=52 kDa Ro protein;
AltName: Full=52 kDa ribonucleoprotein autoantigen Ro/SS-A;
AltName: Full=RING finger protein 81;
AltName: Full=RING-type E3 ubiquitin transferase TRIM21 {ECO:0000305};
AltName: Full=Ro(SS-A);
AltName: Full=Sjoegren syndrome type A antigen;
Short=SS-A;
AltName: Full=Tripartite motif-containing protein 21;
Name=TRIM21; Synonyms=RNF81, RO52, SSA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Thymocyte;
PubMed=1985094; DOI=10.1172/JCI114968;
Itoh K., Itoh Y., Frank M.B.;
"Protein heterogeneity in the human Ro/SSA ribonucleoproteins. The
52- and 60-kD Ro/SSA autoantigens are encoded by separate genes.";
J. Clin. Invest. 87:177-186(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT
ALA-52.
PubMed=1985112; DOI=10.1172/JCI115003;
Chan E.K., Hamel J.C., Buyon J.P., Tan E.M.;
"Molecular definition and sequence motifs of the 52-kD component of
human SS-A/Ro autoantigen.";
J. Clin. Invest. 87:68-76(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=7713506; DOI=10.1006/geno.1994.1664;
Tsugu H., Horowitz R., Gibson N., Frank M.B.;
"The location of a disease-associated polymorphism and genomic
structure of the human 52-kDa Ro/SSA locus (SSA1).";
Genomics 24:541-548(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8625517; DOI=10.1046/j.1365-2249.1996.16726.x;
Keech C.L., Gordon T.P., McCluskey J.;
"Structural differences between the human and mouse 52-kD Ro
autoantigens associated with poorly conserved autoantibody activity
across species.";
Clin. Exp. Immunol. 104:255-263(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-96.
PubMed=9933563; DOI=10.1006/geno.1998.5659;
Bepler G., O'Briant K.C., Kim Y.-C., Schreiber G., Pitterle D.M.;
"A 1.4-Mb high-resolution physical map and contig of chromosome
segment 11p15.5 and genes in the LOH11A metastasis suppressor
region.";
Genomics 55:164-175(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Chen Y.-J., Fan Y.-H., Chiou S.-H.;
"Isolation of human Sjogren syndrome type A antigen cDNA clone from
HEp-2 cells, isolate 1.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
PubMed=7561701; DOI=10.1084/jem.182.4.983;
Chan E.K., Di Donato F., Hamel J.C., Tseng C.E., Buyon J.P.;
"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.";
J. Exp. Med. 182:983-992(1995).
[10]
INTERACTION WITH CALR.
PubMed=8666824;
Cheng S.T., Nguyen T.Q., Yang Y.S., Capra J.D., Sontheimer R.D.;
"Calreticulin binds hYRNA and the 52-kDa polypeptide component of the
Ro/SS-A ribonucleoprotein autoantigen.";
J. Immunol. 156:4484-4491(1996).
[11]
INTERACTION WITH HSPA5.
PubMed=12699405; DOI=10.1046/j.1365-2249.2003.02153.x;
Purcell A.W., Todd A., Kinoshita G., Lynch T.A., Keech C.L.,
Gething M.J., Gordon T.P.;
"Association of stress proteins with autoantigens: a possible
mechanism for triggering autoimmunity?";
Clin. Exp. Immunol. 132:193-200(2003).
[12]
FUNCTION, AUTOUBIQUITINATION, AND MUTAGENESIS OF CYS-16.
PubMed=16297862; DOI=10.1016/j.bbrc.2005.11.029;
Wada K., Kamitani T.;
"Autoantigen Ro52 is an E3 ubiquitin ligase.";
Biochem. Biophys. Res. Commun. 339:415-421(2006).
[13]
FUNCTION, AND DEUBIQUITINATION BY USP4.
PubMed=16316627; DOI=10.1016/j.bbrc.2005.11.076;
Wada K., Tanji K., Kamitani T.;
"Oncogenic protein UnpEL/Usp4 deubiquitinates Ro52 by its isopeptidase
activity.";
Biochem. Biophys. Res. Commun. 339:731-736(2006).
[14]
FUNCTION, AUTOUBIQUITINATION, DEUBIQUITINATION BY USP4, AND
MUTAGENESIS OF CYS-16.
PubMed=16472766; DOI=10.1016/j.bbrc.2006.01.144;
Wada K., Kamitani T.;
"UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself.";
Biochem. Biophys. Res. Commun. 342:253-258(2006).
[15]
FUNCTION, AUTOUBIQUITINATION, INTERACTION WITH THE SCF(SKP2)-LIKE
COMPLEX, AND INTERACTION WITH SKP2; SKP1; CUL1 AND FBXW11.
PubMed=16880511; DOI=10.1128/MCB.01630-05;
Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M.,
Krek W.;
"Regulation of p27 degradation and S-phase progression by Ro52 RING
finger protein.";
Mol. Cell. Biol. 26:5994-6004(2006).
[16]
HOMOMERIZATION, AND SUBCELLULAR LOCATION.
PubMed=17156811; DOI=10.1016/j.virol.2006.10.035;
Li X., Gold B., O'hUigin C., Diaz-Griffero F., Song B., Si Z., Li Y.,
Yuan W., Stremlau M., Mische C., Javanbakht H., Scally M., Winkler C.,
Dean M., Sodroski J.;
"Unique features of TRIM5alpha among closely related human TRIM family
members.";
Virology 360:419-433(2007).
[17]
FUNCTION, INTERACTION WITH DCP2, AND SUBCELLULAR LOCATION.
PubMed=18361920; DOI=10.1016/j.bbrc.2008.03.075;
Yamochi T., Ohnuma K., Hosono O., Tanaka H., Kanai Y., Morimoto C.;
"SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping
activity.";
Biochem. Biophys. Res. Commun. 370:195-199(2008).
[18]
FUNCTION, SUBCELLULAR LOCATION, COILED-COIL DOMAIN, AND DOMAIN
B30.2/SPRY.
PubMed=18845142; DOI=10.1016/j.yexcr.2008.09.011;
Espinosa A., Oke V., Elfving A., Nyberg F., Covacu R.,
Wahren-Herlenius M.;
"The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but
enters the nucleus upon cellular exposure to nitric oxide.";
Exp. Cell Res. 314:3605-3613(2008).
[19]
FUNCTION, AND INTERACTION WITH IRF3.
PubMed=18641315; DOI=10.4049/jimmunol.181.3.1780;
Higgs R., Ni Gabhann J., Ben Larbi N., Breen E.P., Fitzgerald K.A.,
Jefferies C.A.;
"The E3 ubiquitin ligase Ro52 negatively regulates IFN-beta production
post-pathogen recognition by polyubiquitin-mediated degradation of
IRF3.";
J. Immunol. 181:1780-1786(2008).
[20]
FUNCTION, INTERACTION WITH VCP, AUTOUBIQUITINATION, AND SUBCELLULAR
LOCATION.
PubMed=18022694; DOI=10.1016/j.molimm.2007.10.023;
Takahata M., Bohgaki M., Tsukiyama T., Kondo T., Asaka M.,
Hatakeyama S.;
"Ro52 functionally interacts with IgG1 and regulates its quality
control via the ERAD system.";
Mol. Immunol. 45:2045-2054(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
FUNCTION, INTERACTION WITH IKBKB, AND MUTAGENESIS OF CYS-16.
PubMed=19675099; DOI=10.1093/jb/mvp127;
Wada K., Niida M., Tanaka M., Kamitani T.;
"Ro52-mediated monoubiquitination of IKK{beta} down-regulates
NF-{kappa}B signalling.";
J. Biochem. 146:821-832(2009).
[23]
ANTIGENICITY.
PubMed=20407604;
Burbelo P.D., Ching K.H., Han B.L., Bush E.R., Reeves W.H.,
Iadarola M.J.;
"Extraordinary antigenicity of the human Ro52 autoantigen.";
Am. J. Transl. Res. 2:145-155(2010).
[24]
SUBCELLULAR LOCATION.
PubMed=20013343; DOI=10.1007/s00418-009-0669-y;
Tanaka M., Tanji K., Niida M., Kamitani T.;
"Dynamic movements of Ro52 cytoplasmic bodies along microtubules.";
Histochem. Cell Biol. 133:273-284(2010).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
FUNCTION, INDUCTION BY IFNG, INTERACTION WITH MEFV; BECN1; GABARAP;
GABARAPL1; GABARAPL2; IRF3; MAP1LC3C; SQSTM1 AND ULK1, AND SUBCELLULAR
LOCATION.
PubMed=26347139; DOI=10.1083/jcb.201503023;
Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T.,
Deretic V.;
"TRIM-mediated precision autophagy targets cytoplasmic regulators of
innate immunity.";
J. Cell Biol. 210:973-989(2015).
-!- FUNCTION: 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. Involved in the regulation of innate immunity and the
inflammatory response in response to IFNG/IFN-gamma. Organizes
autophagic machinery by serving as a platform for the assembly of
ULK1, Beclin 1/BECN1 and ATG8 family members and recognizes
specific autophagy targets, thus coordinating target recognition
with assembly of the autophagic apparatus and initiation of
autophagy. Acts as an autophagy receptor for the degradation of
IRF3, hence attenuating type I interferon (IFN)-dependent immune
responses (PubMed:26347139). {ECO:0000269|PubMed:16297862,
ECO:0000269|PubMed:16316627, ECO:0000269|PubMed:16472766,
ECO:0000269|PubMed:16880511, ECO:0000269|PubMed:18022694,
ECO:0000269|PubMed:18361920, ECO:0000269|PubMed:18641315,
ECO:0000269|PubMed:18845142, ECO:0000269|PubMed:19675099,
ECO:0000269|PubMed:26347139}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homotrimer (PubMed:17156811) (PubMed:26347139). Interacts
(via C-terminus) with IRF8 (via C-terminus) (By similarity).
Component of a SCF(SKP2)-like complex containing CUL1, SKP1,
TRIM21 and SKP2. Interacts with CALR, CUL1, FBXW11, HSPA5, IKBKB,
IRF3, SKP1 and VCP. Interacts with SKP2; the interaction with SKP2
does not depend on an intact F-box domain. Interacts (via N-
terminus and C-terminus) with DCP2 (via N-terminus and C-
terminus). Interacts with ULK1, BECN1 and with ATG8 family
members, including GABARAP, GABARAPL1, GABARAPL2 and
MAP1LC3C/LC3C. Interacts with TRIM21 and SQSTM1/sequestosome 1.
Interacts with IRF3 (PubMed:26347139). {ECO:0000250,
ECO:0000269|PubMed:12699405, ECO:0000269|PubMed:16880511,
ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:18022694,
ECO:0000269|PubMed:18361920, ECO:0000269|PubMed:18641315,
ECO:0000269|PubMed:19675099, ECO:0000269|PubMed:26347139,
ECO:0000269|PubMed:8666824}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-81290, EBI-81290;
Q9BW85:CCDC94; NbExp=4; IntAct=EBI-81290, EBI-10300345;
Q13588:GRAP; NbExp=5; IntAct=EBI-81290, EBI-2847510;
Q8IZW8:TNS4; NbExp=4; IntAct=EBI-81290, EBI-7543499;
O75382:TRIM3; NbExp=4; IntAct=EBI-81290, EBI-2129889;
Q9HCM9:TRIM39; NbExp=4; IntAct=EBI-81290, EBI-739510;
Q9HCM9-2:TRIM39; NbExp=4; IntAct=EBI-81290, EBI-11523450;
Q99757:TXN2; NbExp=5; IntAct=EBI-81290, EBI-2932492;
Q7KZS0:UBE2I; NbExp=3; IntAct=EBI-81290, EBI-10180829;
Q9Y4E8:USP15; NbExp=3; IntAct=EBI-81290, EBI-1043104;
Q13107-1:USP4; NbExp=3; IntAct=EBI-81290, EBI-723305;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17156811,
ECO:0000269|PubMed:26347139}. Cytoplasmic vesicle, autophagosome
{ECO:0000269|PubMed:26347139}. Nucleus
{ECO:0000269|PubMed:17156811}. Cytoplasm, P-body. Note=Enters the
nucleus upon exposure to nitric oxide. Localizes to small dot- or
rod-like structures in the cytoplasm, called cytoplasmic bodies
(P-body) that are located underneath the plasma membrane and also
diffusely in the cytoplasm and are highly motil in cells.
Cytoplasmic bodies are located along the microtubules and do not
share the same cytoplasmic bodies with TRIM5. Colocalizes with
DCP2 in P-body.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Ro52alpha, 52alpha;
IsoId=P19474-1; Sequence=Displayed;
Name=2; Synonyms=Ro52beta, 52beta;
IsoId=P19474-2; Sequence=VSP_039627;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in fetal
and adult heart and fetal lung.
-!- INDUCTION: Up-regulated by isoform 2 of XBP1. Up-regulated by
IFNG/interferon-gamma, with a peak after 2-4 hours of treatment in
monocytes/macrophages. {ECO:0000269|PubMed:26347139}.
-!- DOMAIN: The coiled-coil is necessary for the cytoplasmic
localization. The B30.2/SPRY domain is necessary for the
cytoplasmic localization, the interaction with IRF3 and for the
IRF3-driven interferon beta promoter activity. The RING-type zinc
finger is necessary for ubiquitination and for the IRF3-driven
interferon beta promoter activity. Interacts with SKP2 and CUL1 in
a RING finger-independent manner. {ECO:0000269|PubMed:18845142}.
-!- PTM: Autoubiquitinated; does not lead to its proteasomal
degradation. Deubiquitinated by USP4; leading to its
stabilization. {ECO:0000269|PubMed:16297862,
ECO:0000269|PubMed:16316627, ECO:0000269|PubMed:16472766,
ECO:0000269|PubMed:16880511, ECO:0000269|PubMed:18022694}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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EMBL; M34551; AAA36581.1; -; mRNA.
EMBL; U01882; AAB87094.1; -; Genomic_DNA.
EMBL; M62800; AAA36651.1; -; mRNA.
EMBL; U13658; AAA79867.1; -; Genomic_DNA.
EMBL; U13657; AAA79867.1; JOINED; Genomic_DNA.
EMBL; AF391283; AAK76432.1; -; Genomic_DNA.
EMBL; AY742713; AAU89982.1; -; mRNA.
EMBL; AC009758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010861; AAH10861.1; -; mRNA.
CCDS; CCDS44525.1; -. [P19474-1]
PIR; A55642; A37241.
RefSeq; NP_003132.2; NM_003141.3. [P19474-1]
UniGene; Hs.532357; -.
PDB; 2IWG; X-ray; 2.35 A; B/E=287-465.
PDB; 5JPX; NMR; -; A=86-130.
PDBsum; 2IWG; -.
PDBsum; 5JPX; -.
ProteinModelPortal; P19474; -.
SMR; P19474; -.
BioGrid; 112615; 94.
IntAct; P19474; 56.
MINT; MINT-1462811; -.
STRING; 9606.ENSP00000254436; -.
iPTMnet; P19474; -.
PhosphoSitePlus; P19474; -.
BioMuta; TRIM21; -.
DMDM; 133250; -.
EPD; P19474; -.
MaxQB; P19474; -.
PaxDb; P19474; -.
PeptideAtlas; P19474; -.
PRIDE; P19474; -.
DNASU; 6737; -.
Ensembl; ENST00000254436; ENSP00000254436; ENSG00000132109. [P19474-1]
GeneID; 6737; -.
KEGG; hsa:6737; -.
UCSC; uc001lyy.2; human. [P19474-1]
CTD; 6737; -.
DisGeNET; 6737; -.
EuPathDB; HostDB:ENSG00000132109.9; -.
GeneCards; TRIM21; -.
HGNC; HGNC:11312; TRIM21.
HPA; CAB004566; -.
HPA; HPA005673; -.
MIM; 109092; gene.
neXtProt; NX_P19474; -.
OpenTargets; ENSG00000132109; -.
PharmGKB; PA36136; -.
eggNOG; KOG2177; Eukaryota.
eggNOG; ENOG4111G04; LUCA.
GeneTree; ENSGT00760000118893; -.
HOGENOM; HOG000234133; -.
HOVERGEN; HBG001357; -.
InParanoid; P19474; -.
KO; K10651; -.
OMA; CWVCSQS; -.
OrthoDB; EOG091G05W2; -.
PhylomeDB; P19474; -.
TreeFam; TF338674; -.
Reactome; R-HSA-1834941; STING mediated induction of host immune responses.
Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; P19474; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; P19474; -.
GeneWiki; TRIM21; -.
GenomeRNAi; 6737; -.
PRO; PR:P19474; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000132109; -.
CleanEx; HS_TRIM21; -.
ExpressionAtlas; P19474; baseline and differential.
Genevisible; P19474; HS.
GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0090086; P:negative regulation of protein deubiquitination; IMP:UniProtKB.
GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB.
GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0046598; P:positive regulation of viral entry into host cell; IEA:Ensembl.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0070206; P:protein trimerization; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0032479; P:regulation of type I interferon production; TAS:Reactome.
GO; GO:0034341; P:response to interferon-gamma; IDA:UniProtKB.
CDD; cd00021; BBOX; 1.
CDD; cd12900; SPRY_PRY_TRIM21; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR006574; PRY.
InterPro; IPR035831; PRY/SPRY_TRIM21.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR003613; Ubox_domain.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR020457; Znf_B-box_chordata.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF13765; PRY; 1.
Pfam; PF00622; SPRY; 1.
Pfam; PF00643; zf-B_box; 1.
PRINTS; PR01406; BBOXZNFINGER.
PRINTS; PR01407; BUTYPHLNCDUF.
SMART; SM00336; BBOX; 1.
SMART; SM00589; PRY; 1.
SMART; SM00184; RING; 1.
SMART; SM00449; SPRY; 1.
SMART; SM00504; Ubox; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; DNA-binding;
Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ribonucleoprotein; RNA-binding; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 475 E3 ubiquitin-protein ligase TRIM21.
/FTId=PRO_0000056115.
DOMAIN 268 465 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 16 55 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 92 123 B box-type. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 128 238 {ECO:0000255}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 169 245 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_039627.
VARIANT 52 52 P -> A (in dbSNP:rs1042302).
{ECO:0000269|PubMed:1985112}.
/FTId=VAR_013749.
VARIANT 88 88 Q -> K (in dbSNP:rs58403334).
/FTId=VAR_061821.
VARIANT 96 96 G -> R (in dbSNP:rs2975162).
{ECO:0000269|PubMed:9933563}.
/FTId=VAR_013750.
VARIANT 231 231 E -> K (in dbSNP:rs2554934).
/FTId=VAR_013751.
MUTAGEN 16 16 C->A: Loss of E3 ubiquitin-protein ligase
activity. Does not inhibit NF-kappa-B-
induced gene expression.
{ECO:0000269|PubMed:16297862,
ECO:0000269|PubMed:16472766,
ECO:0000269|PubMed:19675099}.
CONFLICT 10 10 M -> T (in Ref. 6; AAU89982).
{ECO:0000305}.
CONFLICT 189 189 L -> P (in Ref. 6; AAU89982).
{ECO:0000305}.
CONFLICT 216 216 A -> T (in Ref. 6; AAU89982).
{ECO:0000305}.
CONFLICT 262 262 L -> V (in Ref. 6; AAU89982).
{ECO:0000305}.
CONFLICT 313 313 D -> V (in Ref. 6; AAU89982).
{ECO:0000305}.
TURN 93 96 {ECO:0000244|PDB:5JPX}.
TURN 104 107 {ECO:0000244|PDB:5JPX}.
HELIX 112 115 {ECO:0000244|PDB:5JPX}.
STRAND 118 120 {ECO:0000244|PDB:5JPX}.
STRAND 123 126 {ECO:0000244|PDB:5JPX}.
TURN 293 295 {ECO:0000244|PDB:2IWG}.
STRAND 300 302 {ECO:0000244|PDB:2IWG}.
STRAND 308 311 {ECO:0000244|PDB:2IWG}.
STRAND 327 329 {ECO:0000244|PDB:2IWG}.
STRAND 331 334 {ECO:0000244|PDB:2IWG}.
STRAND 337 347 {ECO:0000244|PDB:2IWG}.
STRAND 354 360 {ECO:0000244|PDB:2IWG}.
TURN 373 376 {ECO:0000244|PDB:2IWG}.
STRAND 377 383 {ECO:0000244|PDB:2IWG}.
TURN 384 386 {ECO:0000244|PDB:2IWG}.
STRAND 387 390 {ECO:0000244|PDB:2IWG}.
STRAND 396 398 {ECO:0000244|PDB:2IWG}.
STRAND 405 412 {ECO:0000244|PDB:2IWG}.
TURN 413 416 {ECO:0000244|PDB:2IWG}.
STRAND 417 422 {ECO:0000244|PDB:2IWG}.
TURN 423 427 {ECO:0000244|PDB:2IWG}.
STRAND 429 433 {ECO:0000244|PDB:2IWG}.
STRAND 442 447 {ECO:0000244|PDB:2IWG}.
STRAND 460 462 {ECO:0000244|PDB:2IWG}.
SEQUENCE 475 AA; 54170 MW; DDFF2944AFC629FB CRC64;
MASAARLTMM WEEVTCPICL DPFVEPVSIE CGHSFCQECI SQVGKGGGSV CPVCRQRFLL
KNLRPNRQLA NMVNNLKEIS QEAREGTQGE RCAVHGERLH LFCEKDGKAL CWVCAQSRKH
RDHAMVPLEE AAQEYQEKLQ VALGELRRKQ ELAEKLEVEI AIKRADWKKT VETQKSRIHA
EFVQQKNFLV EEEQRQLQEL EKDEREQLRI LGEKEAKLAQ QSQALQELIS ELDRRCHSSA
LELLQEVIIV LERSESWNLK DLDITSPELR SVCHVPGLKK MLRTCAVHIT LDPDTANPWL
ILSEDRRQVR LGDTQQSIPG NEERFDSYPM VLGAQHFHSG KHYWEVDVTG KEAWDLGVCR
DSVRRKGHFL LSSKSGFWTI WLWNKQKYEA GTYPQTPLHL QVPPCQVGIF LDYEAGMVSF
YNITDHGSLI YSFSECAFTG PLRPFFSPGF NDGGKNTAPL TLCPLNIGSQ GSTDY


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