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Protein

E3 ubiquitin-protein ligase TRIM22

Gene

TRIM22

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri15 – 6046RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri92 – 13342B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • sequence-specific DNA binding transcription factor activity Source: ProtInc
  • transcription corepressor activity Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cytokine-mediated signaling pathway Source: Reactome
  • defense response to virus Source: UniProtKB-KW
  • immune response Source: ProtInc
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • negative regulation of nucleic acid-templated transcription Source: GOC
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • protein trimerization Source: UniProtKB
  • protein ubiquitination Source: UniProtKB-UniPathway
  • regulation of transcription, DNA-templated Source: ProtInc
  • response to virus Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Antiviral defense, Host-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.3.2.B10. 2681.
6.3.2.19. 2681.
ReactomeiREACT_25078. Interferon gamma signaling.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM22 (EC:6.3.2.-)
Alternative name(s):
50 kDa-stimulated trans-acting factor
RING finger protein 94
Staf-50
Tripartite motif-containing protein 22
Gene namesi
Name:TRIM22
Synonyms:RNF94, STAF50
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:16379. TRIM22.

Subcellular locationi

GO - Cellular componenti

  • Cajal body Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151C → 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. 3 Publications
Mutagenesisi18 – 181C → A: Loss of antiviral activity and not affect nuclear bodies formation; when associated with A-15. 2 Publications
Mutagenesisi493 – 4942VC → AA: Reduces formation of regular nuclear bodies. 1 Publication

Organism-specific databases

PharmGKBiPA38129.

Polymorphism and mutation databases

BioMutaiTRIM22.
DMDMi47606181.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498E3 ubiquitin-protein ligase TRIM22PRO_0000056232Add
BLAST

Post-translational modificationi

Auto-ubiquitinated.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ8IYM9.
PaxDbiQ8IYM9.
PRIDEiQ8IYM9.

PTM databases

PhosphoSiteiQ8IYM9.

Expressioni

Tissue specificityi

Strongly expressed in peripheral blood leukocytes, spleen, thymus, and ovary. Expressed at basal levels in other tissues.1 Publication

Inductioni

By interferons alpha and beta. Up-regulated by p53/TP53. Dramatically induced by progesterone in MDA-MB-231-derived ABC28 cells and T47D cells.4 Publications

Gene expression databases

BgeeiQ8IYM9.
CleanExiHS_TRIM22.
ExpressionAtlasiQ8IYM9. baseline and differential.
GenevisibleiQ8IYM9. HS.

Organism-specific databases

HPAiHPA003307.
HPA003575.

Interactioni

Subunit structurei

Homotrimer (PubMed:17156811). Interacts with HIV-1 Gag polyprotein; this interaction seems to reduce gag production or virus budding (PubMed:18389079). Interacts with EMCV protease 3C; this interaction leads to viral protease ubiquitination (PubMed:19218198).3 Publications

Protein-protein interaction databases

BioGridi115628. 10 interactions.
IntActiQ8IYM9. 9 interactions.
MINTiMINT-2868217.
STRINGi9606.ENSP00000369299.

Structurei

3D structure databases

ProteinModelPortaliQ8IYM9.
SMRiQ8IYM9. Positions 5-79, 90-496.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini283 – 498216B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili132 – 248117Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi257 – 27519Nuclear localization signalSequence AnalysisAdd
BLAST

Domaini

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.
The RING domain is essential for antiviral activity and for TRIM22 nuclear bodies (NB) formation but is not necessary for nuclear localization.

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri15 – 6046RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri92 – 13342B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG258942.
GeneTreeiENSGT00760000118893.
HOGENOMiHOG000234134.
HOVERGENiHBG001357.
InParanoidiQ8IYM9.
KOiK11999.
OMAiFNEMRVI.
OrthoDBiEOG7RJPR6.
PhylomeDBiQ8IYM9.
TreeFamiTF342569.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IYM9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDFSVKVDIE KEVTCPICLE LLTEPLSLDC GHSFCQACIT AKIKESVIIS
60 70 80 90 100
RGESSCPVCQ TRFQPGNLRP NRHLANIVER VKEVKMSPQE GQKRDVCEHH
110 120 130 140 150
GKKLQIFCKE DGKVICWVCE LSQEHQGHQT FRINEVVKEC QEKLQVALQR
160 170 180 190 200
LIKEDQEAEK LEDDIRQERT AWKNYIQIER QKILKGFNEM RVILDNEEQR
210 220 230 240 250
ELQKLEEGEV NVLDNLAAAT DQLVQQRQDA STLISDLQRR LRGSSVEMLQ
260 270 280 290 300
DVIDVMKRSE SWTLKKPKSV SKKLKSVFRV PDLSGMLQVL KELTDVQYYW
310 320 330 340 350
VDVMLNPGSA TSNVAISVDQ RQVKTVRTCT FKNSNPCDFS AFGVFGCQYF
360 370 380 390 400
SSGKYYWEVD VSGKIAWILG VHSKISSLNK RKSSGFAFDP SVNYSKVYSR
410 420 430 440 450
YRPQYGYWVI GLQNTCEYNA FEDSSSSDPK VLTLFMAVPP CRIGVFLDYE
460 470 480 490
AGIVSFFNVT NHGALIYKFS GCRFSRPAYP YFNPWNCLVP MTVCPPSS
Note: No experimental confirmation available.
Length:498
Mass (Da):56,947
Last modified:March 1, 2003 - v1
Checksum:iAFADB968DE76F7DD
GO
Isoform 2 (identifier: Q8IYM9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     174-177: Missing.

Note: No experimental confirmation available.
Show »
Length:494
Mass (Da):56,429
Checksum:i22A7DA4B4B697621
GO

Sequence cautioni

The sequence CAA57684.1 differs from that shown. Reason: Frameshift at position 439. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti464 – 4641A → R in CAA57684 (PubMed:7797467).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551D → N.1 Publication
Corresponds to variant rs7935564 [ dbSNP | Ensembl ].
VAR_052134
Natural varianti232 – 2321T → A.
Corresponds to variant rs2291843 [ dbSNP | Ensembl ].
VAR_052135
Natural varianti242 – 2421R → T.1 Publication
Corresponds to variant rs1063303 [ dbSNP | Ensembl ].
VAR_052136
Natural varianti321 – 3211R → K.
Corresponds to variant rs12364019 [ dbSNP | Ensembl ].
VAR_052137

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei174 – 1774Missing in isoform 2. 1 PublicationVSP_012060

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82200 mRNA. Translation: CAA57684.1. Frameshift.
BC022281 mRNA. Translation: AAH22281.1.
BC035582 mRNA. Translation: AAH35582.1.
CCDSiCCDS41612.1. [Q8IYM9-1]
PIRiA57041.
RefSeqiNP_001186502.1. NM_001199573.1. [Q8IYM9-2]
NP_006065.2. NM_006074.4. [Q8IYM9-1]
UniGeneiHs.501778.
Hs.684559.
Hs.733231.

Genome annotation databases

EnsembliENST00000379965; ENSP00000369299; ENSG00000132274.
GeneIDi10346.
KEGGihsa:10346.
UCSCiuc001mbr.3. human. [Q8IYM9-1]
uc009yes.3. human. [Q8IYM9-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82200 mRNA. Translation: CAA57684.1. Frameshift.
BC022281 mRNA. Translation: AAH22281.1.
BC035582 mRNA. Translation: AAH35582.1.
CCDSiCCDS41612.1. [Q8IYM9-1]
PIRiA57041.
RefSeqiNP_001186502.1. NM_001199573.1. [Q8IYM9-2]
NP_006065.2. NM_006074.4. [Q8IYM9-1]
UniGeneiHs.501778.
Hs.684559.
Hs.733231.

3D structure databases

ProteinModelPortaliQ8IYM9.
SMRiQ8IYM9. Positions 5-79, 90-496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115628. 10 interactions.
IntActiQ8IYM9. 9 interactions.
MINTiMINT-2868217.
STRINGi9606.ENSP00000369299.

PTM databases

PhosphoSiteiQ8IYM9.

Polymorphism and mutation databases

BioMutaiTRIM22.
DMDMi47606181.

Proteomic databases

MaxQBiQ8IYM9.
PaxDbiQ8IYM9.
PRIDEiQ8IYM9.

Protocols and materials databases

DNASUi10346.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379965; ENSP00000369299; ENSG00000132274.
GeneIDi10346.
KEGGihsa:10346.
UCSCiuc001mbr.3. human. [Q8IYM9-1]
uc009yes.3. human. [Q8IYM9-2]

Organism-specific databases

CTDi10346.
GeneCardsiGC11P005667.
HGNCiHGNC:16379. TRIM22.
HPAiHPA003307.
HPA003575.
MIMi606559. gene.
neXtProtiNX_Q8IYM9.
PharmGKBiPA38129.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG258942.
GeneTreeiENSGT00760000118893.
HOGENOMiHOG000234134.
HOVERGENiHBG001357.
InParanoidiQ8IYM9.
KOiK11999.
OMAiFNEMRVI.
OrthoDBiEOG7RJPR6.
PhylomeDBiQ8IYM9.
TreeFamiTF342569.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B10. 2681.
6.3.2.19. 2681.
ReactomeiREACT_25078. Interferon gamma signaling.

Miscellaneous databases

GeneWikiiTRIM22.
GenomeRNAii10346.
NextBioi39235.
PROiQ8IYM9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IYM9.
CleanExiHS_TRIM22.
ExpressionAtlasiQ8IYM9. baseline and differential.
GenevisibleiQ8IYM9. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression."
    Tissot C., Mechti N.
    J. Biol. Chem. 270:14891-14898(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, TISSUE SPECIFICITY, VARIANT THR-242.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-155.
    Tissue: Lung and Testis.
  3. Cited for: SUBCELLULAR LOCATION.
  4. "Staf50 is a novel p53 target gene conferring reduced clonogenic growth of leukemic U-937 cells."
    Obad S., Brunnstrom H., Vallon-Christersson J., Borg A., Drott K., Gullberg U.
    Oncogene 23:4050-4059(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  6. "Identification of TRIM22 as a RING finger E3 ubiquitin ligase."
    Duan Z., Gao B., Xu W., Xiong S.
    Biochem. Biophys. Res. Commun. 374:502-506(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION, MUTAGENESIS OF CYS-15.
  7. "The interferon response inhibits HIV particle production by induction of TRIM22."
    Barr S.D., Smiley J.R., Bushman F.D.
    PLoS Pathog. 4:E1000007-E1000007(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, INTERACTION WITH HIV-1 GAG POLYPROTEIN, MUTAGENESIS OF CYS-15 AND CYS-18.
  8. "Dynamic localization of tripartite motif-containing 22 in nuclear and nucleolar bodies."
    Sivaramakrishnan G., Sun Y., Tan S.K., Lin V.C.
    Exp. Cell Res. 315:1521-1532(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION.
  9. "B30.2/SPRY domain in tripartite motif-containing 22 is essential for the formation of distinct nuclear bodies."
    Sivaramakrishnan G., Sun Y., Rajmohan R., Lin V.C.
    FEBS Lett. 583:2093-2099(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-15; CYS-18 AND 493-VAL-CYS-494.
  10. "Tripartite motif-containing 22 inhibits the activity of hepatitis B virus core promoter, which is dependent on nuclear-located RING domain."
    Gao B., Duan Z., Xu W., Xiong S.
    Hepatology 50:424-433(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral activity against encephalomyocarditis virus."
    Eldin P., Papon L., Oteiza A., Brocchi E., Lawson T.G., Mechti N.
    J. Gen. Virol. 90:536-545(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EMCV PROTEASE 3C.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRI22_HUMAN
AccessioniPrimary (citable) accession number: Q8IYM9
Secondary accession number(s): Q05CQ0, Q15521
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 1, 2003
Last modified: July 22, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.