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E3 ubiquitin-protein ligase TRIM22 (EC 2.3.2.27) (50 kDa-stimulated trans-acting factor) (RING finger protein 94) (RING-type E3 ubiquitin transferase TRIM22) (Staf-50) (Tripartite motif-containing protein 22)

 TRI22_HUMAN             Reviewed;         498 AA.
Q8IYM9; Q05CQ0; Q15521;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
18-JUL-2018, entry version 155.
RecName: Full=E3 ubiquitin-protein ligase TRIM22;
EC=2.3.2.27;
AltName: Full=50 kDa-stimulated trans-acting factor;
AltName: Full=RING finger protein 94;
AltName: Full=RING-type E3 ubiquitin transferase TRIM22 {ECO:0000305};
AltName: Full=Staf-50;
AltName: Full=Tripartite motif-containing protein 22;
Name=TRIM22; Synonyms=RNF94, STAF50;
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 2), INDUCTION, TISSUE SPECIFICITY,
AND VARIANT THR-242.
PubMed=7797467; DOI=10.1074/jbc.270.25.14891;
Tissot C., Mechti N.;
"Molecular cloning of a new interferon-induced factor that represses
human immunodeficiency virus type 1 long terminal repeat expression.";
J. Biol. Chem. 270:14891-14898(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASN-155.
TISSUE=Lung, and Testis;
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).
[3]
SUBCELLULAR LOCATION.
PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
Minucci S., Pelicci P.G., Ballabio A.;
"The tripartite motif family identifies cell compartments.";
EMBO J. 20:2140-2151(2001).
[4]
INDUCTION.
PubMed=15064739; DOI=10.1038/sj.onc.1207524;
Obad S., Brunnstrom H., Vallon-Christersson J., Borg A., Drott K.,
Gullberg U.;
"Staf50 is a novel p53 target gene conferring reduced clonogenic
growth of leukemic U-937 cells.";
Oncogene 23:4050-4059(2004).
[5]
SUBUNIT, 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).
[6]
FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION, AND MUTAGENESIS OF
CYS-15.
PubMed=18656448; DOI=10.1016/j.bbrc.2008.07.070;
Duan Z., Gao B., Xu W., Xiong S.;
"Identification of TRIM22 as a RING finger E3 ubiquitin ligase.";
Biochem. Biophys. Res. Commun. 374:502-506(2008).
[7]
FUNCTION, INDUCTION, INTERACTION WITH HIV-1 GAG POLYPROTEIN (MICROBIAL
INFECTION), AND MUTAGENESIS OF CYS-15 AND CYS-18.
PubMed=18389079; DOI=10.1371/journal.ppat.1000007;
Barr S.D., Smiley J.R., Bushman F.D.;
"The interferon response inhibits HIV particle production by induction
of TRIM22.";
PLoS Pathog. 4:E1000007-E1000007(2008).
[8]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=19331816; DOI=10.1016/j.yexcr.2009.01.028;
Sivaramakrishnan G., Sun Y., Tan S.K., Lin V.C.;
"Dynamic localization of tripartite motif-containing 22 in nuclear and
nucleolar bodies.";
Exp. Cell Res. 315:1521-1532(2009).
[9]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-15; CYS-18 AND
493-VAL-CYS-494.
PubMed=19481078; DOI=10.1016/j.febslet.2009.05.036;
Sivaramakrishnan G., Sun Y., Rajmohan R., Lin V.C.;
"B30.2/SPRY domain in tripartite motif-containing 22 is essential for
the formation of distinct nuclear bodies.";
FEBS Lett. 583:2093-2099(2009).
[10]
FUNCTION.
PubMed=19585648; DOI=10.1002/hep.23011;
Gao B., Duan Z., Xu W., Xiong S.;
"Tripartite motif-containing 22 inhibits the activity of hepatitis B
virus core promoter, which is dependent on nuclear-located RING
domain.";
Hepatology 50:424-433(2009).
[11]
FUNCTION, AND INTERACTION WITH EMCV PROTEASE 3C (MICROBIAL INFECTION).
PubMed=19218198; DOI=10.1099/vir.0.006288-0;
Eldin P., Papon L., Oteiza A., Brocchi E., Lawson T.G., Mechti N.;
"TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral
activity against encephalomyocarditis virus.";
J. Gen. Virol. 90:536-545(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Interferon-induced antiviral protein involved in cell
innate immunity. The antiviral activity could in part be mediated
by TRIM22-dependent ubiquitination of viral proteins. Plays a role
in restricting the replication of HIV-1, encephalomyocarditis
virus (EMCV) and hepatitis B virus (HBV). Acts as a
transcriptional repressor of HBV core promoter. May have E3
ubiquitin-protein ligase activity. {ECO:0000269|PubMed:18389079,
ECO:0000269|PubMed:18656448, ECO:0000269|PubMed:19218198,
ECO:0000269|PubMed:19585648}.
-!- 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).
{ECO:0000269|PubMed:17156811}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Gag
polyprotein; this interaction seems to reduce gag production or
virus budding. {ECO:0000269|PubMed:18389079}.
-!- SUBUNIT: (Microbial infection) Interacts with EMCV protease 3C;
this interaction leads to viral protease ubiquitination.
{ECO:0000269|PubMed:19218198}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17156811}.
Nucleus {ECO:0000269|PubMed:17156811}. Nucleus speckle. Nucleus,
Cajal body. Note=Localizes predominantly to the nucleus, found in
cytoplasm to some extent. Forms distinct nuclear bodies that
undergo dynamic changes during cell cycle progression. Nuclear
bodies start to form in the early G0/G1 phase but become speckle-
like in the S-phase and completely dispersed in mitosis. 35% of
TRIM22 nuclear bodies overlap or are found adjacent to Cajal
bodies.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8IYM9-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q8IYM9-2; Sequence=VSP_012060;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Strongly expressed in peripheral blood
leukocytes, spleen, thymus, and ovary. Expressed at basal levels
in other tissues. {ECO:0000269|PubMed:7797467}.
-!- INDUCTION: By interferons alpha and beta. Up-regulated by
p53/TP53. Dramatically induced by progesterone in MDA-MB-231-
derived ABC28 cells and T47D cells. {ECO:0000269|PubMed:15064739,
ECO:0000269|PubMed:18389079, ECO:0000269|PubMed:19331816,
ECO:0000269|PubMed:7797467}.
-!- DOMAIN: The C-terminal SPRY domain is required for the
transcriptional suppressor activity, probably by mediating correct
nuclear localization. Residues 491-494 are essential for nuclear
localization and nuclear bodies formation.
-!- DOMAIN: The RING domain is essential for antiviral activity and
for TRIM22 nuclear bodies (NB) formation but is not necessary for
nuclear localization.
-!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:18656448}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA57684.1; Type=Frameshift; Positions=439; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X82200; CAA57684.1; ALT_FRAME; mRNA.
EMBL; BC022281; AAH22281.1; -; mRNA.
EMBL; BC035582; AAH35582.1; -; mRNA.
CCDS; CCDS41612.1; -. [Q8IYM9-1]
PIR; A57041; A57041.
RefSeq; NP_001186502.1; NM_001199573.1. [Q8IYM9-2]
RefSeq; NP_006065.2; NM_006074.4. [Q8IYM9-1]
UniGene; Hs.501778; -.
UniGene; Hs.684559; -.
UniGene; Hs.733231; -.
ProteinModelPortal; Q8IYM9; -.
SMR; Q8IYM9; -.
BioGrid; 115628; 16.
IntAct; Q8IYM9; 10.
STRING; 9606.ENSP00000369299; -.
iPTMnet; Q8IYM9; -.
PhosphoSitePlus; Q8IYM9; -.
BioMuta; TRIM22; -.
DMDM; 47606181; -.
EPD; Q8IYM9; -.
MaxQB; Q8IYM9; -.
PaxDb; Q8IYM9; -.
PeptideAtlas; Q8IYM9; -.
PRIDE; Q8IYM9; -.
ProteomicsDB; 71205; -.
ProteomicsDB; 71206; -. [Q8IYM9-2]
DNASU; 10346; -.
Ensembl; ENST00000379965; ENSP00000369299; ENSG00000132274. [Q8IYM9-1]
GeneID; 10346; -.
KEGG; hsa:10346; -.
UCSC; uc001mbr.4; human. [Q8IYM9-1]
CTD; 10346; -.
DisGeNET; 10346; -.
EuPathDB; HostDB:ENSG00000132274.15; -.
GeneCards; TRIM22; -.
HGNC; HGNC:16379; TRIM22.
HPA; HPA003307; -.
HPA; HPA003575; -.
MIM; 606559; gene.
neXtProt; NX_Q8IYM9; -.
OpenTargets; ENSG00000132274; -.
PharmGKB; PA38129; -.
eggNOG; ENOG410ITG7; Eukaryota.
eggNOG; ENOG410XWDC; LUCA.
GeneTree; ENSGT00760000118893; -.
HOGENOM; HOG000234134; -.
HOVERGEN; HBG001357; -.
InParanoid; Q8IYM9; -.
KO; K11999; -.
OMA; SGKIAWI; -.
OrthoDB; EOG091G04O8; -.
PhylomeDB; Q8IYM9; -.
TreeFam; TF342569; -.
BRENDA; 2.3.2.B10; 2681.
BRENDA; 6.3.2.19; 2681.
Reactome; R-HSA-877300; Interferon gamma signaling.
UniPathway; UPA00143; -.
GeneWiki; TRIM22; -.
GenomeRNAi; 10346; -.
PRO; PR:Q8IYM9; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000132274; -.
CleanEx; HS_TRIM22; -.
ExpressionAtlas; Q8IYM9; baseline and differential.
Genevisible; Q8IYM9; HS.
GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0030674; F:protein binding, bridging; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0070206; P:protein trimerization; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
GO; GO:0009615; P:response to virus; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00021; BBOX; 1.
CDD; cd15824; SPRY_PRY_TRIM22; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR035827; PRY/SPRY_TRIM22.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR027370; Znf-RING_LisH.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00622; SPRY; 1.
Pfam; PF00643; zf-B_box; 1.
Pfam; PF13445; zf-RING_UBOX; 1.
PRINTS; PR01407; BUTYPHLNCDUF.
SMART; SM00336; BBOX; 1.
SMART; SM00184; RING; 1.
SMART; SM00449; SPRY; 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;
Alternative splicing; Antiviral defense; Coiled coil;
Complete proteome; Cytoplasm; Host-virus interaction; Metal-binding;
Nucleus; Polymorphism; Reference proteome; Repressor; Transcription;
Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 498 E3 ubiquitin-protein ligase TRIM22.
/FTId=PRO_0000056232.
DOMAIN 283 498 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 15 60 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 92 133 B box-type. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 132 248 {ECO:0000255}.
MOTIF 257 275 Nuclear localization signal.
{ECO:0000255}.
VAR_SEQ 174 177 Missing (in isoform 2).
{ECO:0000303|PubMed:7797467}.
/FTId=VSP_012060.
VARIANT 155 155 D -> N (in dbSNP:rs7935564).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_052134.
VARIANT 232 232 T -> A (in dbSNP:rs2291843).
/FTId=VAR_052135.
VARIANT 242 242 R -> T (in dbSNP:rs1063303).
{ECO:0000269|PubMed:7797467}.
/FTId=VAR_052136.
VARIANT 321 321 R -> K (in dbSNP:rs12364019).
/FTId=VAR_052137.
MUTAGEN 15 15 C->A: Loss of E3 ubiquitin-protein ligase
activity, reduces auto-ubiquitination and
not affect nuclear bodies formation. Loss
of antiviral activity; when associated
with A-18. {ECO:0000269|PubMed:18389079,
ECO:0000269|PubMed:18656448,
ECO:0000269|PubMed:19481078}.
MUTAGEN 18 18 C->A: Loss of antiviral activity and not
affect nuclear bodies formation; when
associated with A-15.
{ECO:0000269|PubMed:18389079,
ECO:0000269|PubMed:19481078}.
MUTAGEN 493 494 VC->AA: Reduces formation of regular
nuclear bodies.
{ECO:0000269|PubMed:19481078}.
CONFLICT 464 464 A -> R (in Ref. 1; CAA57684).
{ECO:0000305}.
SEQUENCE 498 AA; 56947 MW; AFADB968DE76F7DD CRC64;
MDFSVKVDIE KEVTCPICLE LLTEPLSLDC GHSFCQACIT AKIKESVIIS RGESSCPVCQ
TRFQPGNLRP NRHLANIVER VKEVKMSPQE GQKRDVCEHH GKKLQIFCKE DGKVICWVCE
LSQEHQGHQT FRINEVVKEC QEKLQVALQR LIKEDQEAEK LEDDIRQERT AWKNYIQIER
QKILKGFNEM RVILDNEEQR ELQKLEEGEV NVLDNLAAAT DQLVQQRQDA STLISDLQRR
LRGSSVEMLQ DVIDVMKRSE SWTLKKPKSV SKKLKSVFRV PDLSGMLQVL KELTDVQYYW
VDVMLNPGSA TSNVAISVDQ RQVKTVRTCT FKNSNPCDFS AFGVFGCQYF SSGKYYWEVD
VSGKIAWILG VHSKISSLNK RKSSGFAFDP SVNYSKVYSR YRPQYGYWVI GLQNTCEYNA
FEDSSSSDPK VLTLFMAVPP CRIGVFLDYE AGIVSFFNVT NHGALIYKFS GCRFSRPAYP
YFNPWNCLVP MTVCPPSS


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