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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.
11-DEC-2019, entry version 218.
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:
Reaction=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.;
EC=2.3.2.27;
-!- 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;
Q13588:GRAP; NbExp=5; IntAct=EBI-81290, EBI-2847510;
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=5; 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 {ECO:0000269|PubMed:18361920}. Note=Enters the
nucleus upon exposure to nitric oxide. Localizes to small dot- or rod-
like structures in the cytoplasm, called processing bodies (P-bodies)
that are located underneath the plasma membrane and also diffusely in
the cytoplasm. They are located along the microtubules and are highly
motile in cells. Colocalizes with DCP2 in P-bodies.
-!- 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;
-!- 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]
PDB; 2IWG; X-ray; 2.35 A; B/E=287-465.
PDB; 5JPX; NMR; -; A=86-130.
PDB; 5OLM; X-ray; 1.95 A; A/B=1-129.
PDB; 6FGA; X-ray; 2.82 A; A/B/C/D/E/F/G/H=1-98.
PDB; 6S53; X-ray; 2.80 A; A/B/G/H=1-85.
PDBsum; 2IWG; -.
PDBsum; 5JPX; -.
PDBsum; 5OLM; -.
PDBsum; 6FGA; -.
PDBsum; 6S53; -.
SMR; P19474; -.
BioGrid; 112615; 130.
IntAct; P19474; 61.
MINT; P19474; -.
STRING; 9606.ENSP00000254436; -.
iPTMnet; P19474; -.
PhosphoSitePlus; P19474; -.
BioMuta; TRIM21; -.
DMDM; 133250; -.
EPD; P19474; -.
jPOST; P19474; -.
MassIVE; P19474; -.
MaxQB; P19474; -.
PaxDb; P19474; -.
PeptideAtlas; P19474; -.
PRIDE; P19474; -.
ProteomicsDB; 53666; -. [P19474-1]
ProteomicsDB; 53667; -. [P19474-2]
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; ENSGT00940000161515; -.
HOGENOM; HOG000234133; -.
InParanoid; P19474; -.
KO; K10651; -.
OMA; EPMSIEC; -.
OrthoDB; 423686at2759; -.
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; -.
Pharos; P19474; Tbio.
PRO; PR:P19474; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; P19474; protein.
Bgee; ENSG00000132109; Expressed in 148 organ(s), highest expression level in leukocyte.
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:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:1990904; C:ribonucleoprotein complex; TAS:ProtInc.
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 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; 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
/note="E3 ubiquitin-protein ligase TRIM21"
/id="PRO_0000056115"
DOMAIN 268..465
/note="B30.2/SPRY"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
ZN_FING 16..55
/note="RING-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
ZN_FING 92..123
/note="B box-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
COILED 128..238
/evidence="ECO:0000255"
MOD_RES 266
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163"
VAR_SEQ 169..245
/note="Missing (in isoform 2)"
/evidence="ECO:0000305"
/id="VSP_039627"
VARIANT 52
/note="P -> A (in dbSNP:rs1042302)"
/evidence="ECO:0000269|PubMed:1985112"
/id="VAR_013749"
VARIANT 88
/note="Q -> K (in dbSNP:rs58403334)"
/id="VAR_061821"
VARIANT 96
/note="G -> R (in dbSNP:rs2975162)"
/evidence="ECO:0000269|PubMed:9933563"
/id="VAR_013750"
VARIANT 231
/note="E -> K (in dbSNP:rs2554934)"
/id="VAR_013751"
MUTAGEN 16
/note="C->A: Loss of E3 ubiquitin-protein ligase activity.
Does not inhibit NF-kappa-B-induced gene expression."
/evidence="ECO:0000269|PubMed:16297862,
ECO:0000269|PubMed:16472766, ECO:0000269|PubMed:19675099"
CONFLICT 10
/note="M -> T (in Ref. 6; AAU89982)"
/evidence="ECO:0000305"
CONFLICT 189
/note="L -> P (in Ref. 6; AAU89982)"
/evidence="ECO:0000305"
CONFLICT 216
/note="A -> T (in Ref. 6; AAU89982)"
/evidence="ECO:0000305"
CONFLICT 262
/note="L -> V (in Ref. 6; AAU89982)"
/evidence="ECO:0000305"
CONFLICT 313
/note="D -> V (in Ref. 6; AAU89982)"
/evidence="ECO:0000305"
HELIX 4..13
/evidence="ECO:0000244|PDB:5OLM"
TURN 17..19
/evidence="ECO:0000244|PDB:5OLM"
STRAND 20..22
/evidence="ECO:0000244|PDB:5OLM"
STRAND 24..28
/evidence="ECO:0000244|PDB:5OLM"
STRAND 34..36
/evidence="ECO:0000244|PDB:5OLM"
HELIX 37..44
/evidence="ECO:0000244|PDB:5OLM"
STRAND 48..50
/evidence="ECO:0000244|PDB:6S53"
TURN 52..54
/evidence="ECO:0000244|PDB:5OLM"
STRAND 57..59
/evidence="ECO:0000244|PDB:6S53"
HELIX 60..62
/evidence="ECO:0000244|PDB:5OLM"
HELIX 67..82
/evidence="ECO:0000244|PDB:5OLM"
TURN 93..95
/evidence="ECO:0000244|PDB:5OLM"
STRAND 101..103
/evidence="ECO:0000244|PDB:5OLM"
TURN 104..106
/evidence="ECO:0000244|PDB:5OLM"
HELIX 112..116
/evidence="ECO:0000244|PDB:5OLM"
TURN 118..122
/evidence="ECO:0000244|PDB:5OLM"
STRAND 125..127
/evidence="ECO:0000244|PDB:5OLM"
TURN 293..295
/evidence="ECO:0000244|PDB:2IWG"
STRAND 300..302
/evidence="ECO:0000244|PDB:2IWG"
STRAND 308..311
/evidence="ECO:0000244|PDB:2IWG"
STRAND 327..329
/evidence="ECO:0000244|PDB:2IWG"
STRAND 331..334
/evidence="ECO:0000244|PDB:2IWG"
STRAND 337..347
/evidence="ECO:0000244|PDB:2IWG"
STRAND 354..360
/evidence="ECO:0000244|PDB:2IWG"
TURN 373..376
/evidence="ECO:0000244|PDB:2IWG"
STRAND 377..383
/evidence="ECO:0000244|PDB:2IWG"
TURN 384..386
/evidence="ECO:0000244|PDB:2IWG"
STRAND 387..390
/evidence="ECO:0000244|PDB:2IWG"
STRAND 396..398
/evidence="ECO:0000244|PDB:2IWG"
STRAND 405..412
/evidence="ECO:0000244|PDB:2IWG"
TURN 413..416
/evidence="ECO:0000244|PDB:2IWG"
STRAND 417..422
/evidence="ECO:0000244|PDB:2IWG"
TURN 423..427
/evidence="ECO:0000244|PDB:2IWG"
STRAND 429..433
/evidence="ECO:0000244|PDB:2IWG"
STRAND 442..447
/evidence="ECO:0000244|PDB:2IWG"
STRAND 460..462
/evidence="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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