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Q8IYM9 (TRI22_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TRIM22
Synonyms:RNF94, STAF50
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.5 Ref.6 Ref.9 Ref.10

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with HIV-1 Gag polyprotein; this interaction seems to reduce gag production or virus budding. Interacts with EMCV protease 3C; this interaction leads to viral protease ubiquitination. Ref.6 Ref.10

Subcellular location

Cytoplasm. Nucleus. Nucleus speckle. NucleusCajal body. Note: Localizes predominanltly into 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. Ref.3 Ref.5 Ref.7 Ref.8

Tissue specificity

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

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. Ref.1 Ref.4 Ref.6 Ref.7

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.

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

Post-translational modification

Auto-ubiquitinated.

Sequence similarities

Belongs to the TRIM/RBCC family.

Contains 1 B box-type zinc finger.

Contains 1 B30.2/SPRY domain.

Contains 1 RING-type zinc finger.

Sequence caution

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

Ontologies

Keywords
   Biological processAntiviral defense
Host-virus interaction
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
Repressor
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

immune response

Traceable author statement Ref.1. Source: ProtInc

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 23077300. Source: UniProt

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 23077300. Source: UniProt

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 23077300. Source: UniProt

protein trimerization

Inferred from direct assay PubMed 17156811. Source: UniProtKB

protein ubiquitination

Inferred from electronic annotation. Source: UniProtKB-UniPathway

regulation of transcription, DNA-templated

Traceable author statement Ref.1. Source: ProtInc

response to virus

Traceable author statement Ref.1. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCajal body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 17156811. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 17156811. Source: UniProtKB

   Molecular_functionligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

transcription corepressor activity

Traceable author statement Ref.1. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IYM9-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q8IYM9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     174-177: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498E3 ubiquitin-protein ligase TRIM22
PRO_0000056232

Regions

Domain283 – 498216B30.2/SPRY
Zinc finger15 – 6046RING-type
Zinc finger92 – 13342B box-type
Coiled coil132 – 248117 Potential
Motif257 – 27519Nuclear localization signal Potential

Natural variations

Alternative sequence174 – 1774Missing in isoform 2.
VSP_012060
Natural variant1551D → N. Ref.2
Corresponds to variant rs7935564 [ dbSNP | Ensembl ].
VAR_052134
Natural variant2321T → A.
Corresponds to variant rs2291843 [ dbSNP | Ensembl ].
VAR_052135
Natural variant2421R → T. Ref.1
Corresponds to variant rs1063303 [ dbSNP | Ensembl ].
VAR_052136
Natural variant3211R → K.
Corresponds to variant rs12364019 [ dbSNP | Ensembl ].
VAR_052137

Experimental info

Mutagenesis151C → 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. Ref.5 Ref.6 Ref.8
Mutagenesis181C → A: Loss of antiviral activity and not affect nuclear bodies formation; when associated with A-15. Ref.6 Ref.8
Mutagenesis493 – 4942VC → AA: Reduces formation of regular nuclear bodies.
Sequence conflict4641A → R in CAA57684. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: AFADB968DE76F7DD

FASTA49856,947
        10         20         30         40         50         60 
MDFSVKVDIE KEVTCPICLE LLTEPLSLDC GHSFCQACIT AKIKESVIIS RGESSCPVCQ 

        70         80         90        100        110        120 
TRFQPGNLRP NRHLANIVER VKEVKMSPQE GQKRDVCEHH GKKLQIFCKE DGKVICWVCE 

       130        140        150        160        170        180 
LSQEHQGHQT FRINEVVKEC QEKLQVALQR LIKEDQEAEK LEDDIRQERT AWKNYIQIER 

       190        200        210        220        230        240 
QKILKGFNEM RVILDNEEQR ELQKLEEGEV NVLDNLAAAT DQLVQQRQDA STLISDLQRR 

       250        260        270        280        290        300 
LRGSSVEMLQ DVIDVMKRSE SWTLKKPKSV SKKLKSVFRV PDLSGMLQVL KELTDVQYYW 

       310        320        330        340        350        360 
VDVMLNPGSA TSNVAISVDQ RQVKTVRTCT FKNSNPCDFS AFGVFGCQYF SSGKYYWEVD 

       370        380        390        400        410        420 
VSGKIAWILG VHSKISSLNK RKSSGFAFDP SVNYSKVYSR YRPQYGYWVI GLQNTCEYNA 

       430        440        450        460        470        480 
FEDSSSSDPK VLTLFMAVPP CRIGVFLDYE AGIVSFFNVT NHGALIYKFS GCRFSRPAYP 

       490 
YFNPWNCLVP MTVCPPSS 

« Hide

Isoform 2 [UniParc].

Checksum: 22A7DA4B4B697621
Show »

FASTA49456,429

References

« Hide 'large scale' references
[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]"The tripartite motif family identifies cell compartments."
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.
EMBO J. 20:2140-2151(2001) [PubMed] [Europe PMC] [Abstract]
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]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82200 mRNA. Translation: CAA57684.1. Frameshift.
BC022281 mRNA. Translation: AAH22281.1.
BC035582 mRNA. Translation: AAH35582.1.
PIRA57041.
RefSeqNP_001186502.1. NM_001199573.1.
NP_006065.2. NM_006074.4.
UniGeneHs.501778.
Hs.684559.
Hs.733231.

3D structure databases

ProteinModelPortalQ8IYM9.
SMRQ8IYM9. Positions 5-79, 90-131, 275-496.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115628. 10 interactions.
IntActQ8IYM9. 9 interactions.
MINTMINT-2868217.
STRING9606.ENSP00000369299.

PTM databases

PhosphoSiteQ8IYM9.

Polymorphism databases

DMDM47606181.

Proteomic databases

PaxDbQ8IYM9.
PRIDEQ8IYM9.

Protocols and materials databases

DNASU10346.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379965; ENSP00000369299; ENSG00000132274. [Q8IYM9-1]
GeneID10346.
KEGGhsa:10346.
UCSCuc001mbr.3. human. [Q8IYM9-1]
uc009yes.3. human. [Q8IYM9-2]

Organism-specific databases

CTD10346.
GeneCardsGC11P005667.
HGNCHGNC:16379. TRIM22.
HPAHPA003307.
HPA003575.
MIM606559. gene.
neXtProtNX_Q8IYM9.
PharmGKBPA38129.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258942.
HOGENOMHOG000234134.
HOVERGENHBG001357.
InParanoidQ8IYM9.
KOK11999.
OMAICWVCEL.
OrthoDBEOG7RJPR6.
PhylomeDBQ8IYM9.
TreeFamTF342569.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ8IYM9.
BgeeQ8IYM9.
CleanExHS_TRIM22.
GenevestigatorQ8IYM9.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR008985. ConA-like_lec_gl_sf.
IPR003877. SPRY_rcpt.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSPR01407. BUTYPHLNCDUF.
SMARTSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRIM22. human.
GeneWikiTRIM22.
GenomeRNAi10346.
NextBio39235.
PROQ8IYM9.
SOURCESearch...

Entry information

Entry nameTRI22_HUMAN
AccessionPrimary (citable) accession number: Q8IYM9
Secondary accession number(s): Q05CQ0, Q15521
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM