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Q8IYM9

- TRI22_HUMAN

UniProt

Q8IYM9 - TRI22_HUMAN

Protein

E3 ubiquitin-protein ligase TRIM22

Gene

TRIM22

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    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

    Pathwayi

    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

    1. ligase activity Source: UniProtKB-KW
    2. sequence-specific DNA binding transcription factor activity Source: ProtInc
    3. transcription corepressor activity Source: ProtInc
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. defense response to virus Source: UniProtKB-KW
    2. immune response Source: ProtInc
    3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProt
    4. positive regulation of NF-kappaB transcription factor activity Source: UniProt
    5. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProt
    6. protein trimerization Source: UniProtKB
    7. protein ubiquitination Source: UniProtKB-UniPathway
    8. regulation of transcription, DNA-templated Source: ProtInc
    9. response to virus Source: ProtInc
    10. transcription, DNA-templated Source: UniProtKB-KW
    11. viral process Source: UniProtKB-KW

    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

    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: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:16379. TRIM22.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. Cajal body Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB
    3. nuclear speck Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB

    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.

    Organism-specific databases

    PharmGKBiPA38129.

    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

    ArrayExpressiQ8IYM9.
    BgeeiQ8IYM9.
    CleanExiHS_TRIM22.
    GenevestigatoriQ8IYM9.

    Organism-specific databases

    HPAiHPA003307.
    HPA003575.

    Interactioni

    Subunit structurei

    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.2 Publications

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IYM9.
    SMRiQ8IYM9. Positions 5-79, 90-131, 292-496.
    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.
    HOGENOMiHOG000234134.
    HOVERGENiHBG001357.
    InParanoidiQ8IYM9.
    KOiK11999.
    OMAiICWVCEL.
    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.
    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]
    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. Align

    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

    MDFSVKVDIE KEVTCPICLE LLTEPLSLDC GHSFCQACIT AKIKESVIIS    50
    RGESSCPVCQ TRFQPGNLRP NRHLANIVER VKEVKMSPQE GQKRDVCEHH 100
    GKKLQIFCKE DGKVICWVCE LSQEHQGHQT FRINEVVKEC QEKLQVALQR 150
    LIKEDQEAEK LEDDIRQERT AWKNYIQIER QKILKGFNEM RVILDNEEQR 200
    ELQKLEEGEV NVLDNLAAAT DQLVQQRQDA STLISDLQRR LRGSSVEMLQ 250
    DVIDVMKRSE SWTLKKPKSV SKKLKSVFRV PDLSGMLQVL KELTDVQYYW 300
    VDVMLNPGSA TSNVAISVDQ RQVKTVRTCT FKNSNPCDFS AFGVFGCQYF 350
    SSGKYYWEVD VSGKIAWILG VHSKISSLNK RKSSGFAFDP SVNYSKVYSR 400
    YRPQYGYWVI GLQNTCEYNA FEDSSSSDPK VLTLFMAVPP CRIGVFLDYE 450
    AGIVSFFNVT NHGALIYKFS GCRFSRPAYP YFNPWNCLVP MTVCPPSS 498

    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.

    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:
    EMBL
    GenBank
    DDBJ
    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. [Q8IYM9-1]
    GeneIDi10346.
    KEGGihsa:10346.
    UCSCiuc001mbr.3. human. [Q8IYM9-1]
    uc009yes.3. human. [Q8IYM9-2]

    Polymorphism databases

    DMDMi47606181.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82200 mRNA. Translation: CAA57684.1 . Frameshift.
    BC022281 mRNA. Translation: AAH22281.1 .
    BC035582 mRNA. Translation: AAH35582.1 .
    CCDSi CCDS41612.1. [Q8IYM9-1 ]
    PIRi A57041.
    RefSeqi NP_001186502.1. NM_001199573.1. [Q8IYM9-2 ]
    NP_006065.2. NM_006074.4. [Q8IYM9-1 ]
    UniGenei Hs.501778.
    Hs.684559.
    Hs.733231.

    3D structure databases

    ProteinModelPortali Q8IYM9.
    SMRi Q8IYM9. Positions 5-79, 90-131, 292-496.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115628. 10 interactions.
    IntActi Q8IYM9. 9 interactions.
    MINTi MINT-2868217.
    STRINGi 9606.ENSP00000369299.

    PTM databases

    PhosphoSitei Q8IYM9.

    Polymorphism databases

    DMDMi 47606181.

    Proteomic databases

    MaxQBi Q8IYM9.
    PaxDbi Q8IYM9.
    PRIDEi Q8IYM9.

    Protocols and materials databases

    DNASUi 10346.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379965 ; ENSP00000369299 ; ENSG00000132274 . [Q8IYM9-1 ]
    GeneIDi 10346.
    KEGGi hsa:10346.
    UCSCi uc001mbr.3. human. [Q8IYM9-1 ]
    uc009yes.3. human. [Q8IYM9-2 ]

    Organism-specific databases

    CTDi 10346.
    GeneCardsi GC11P005667.
    HGNCi HGNC:16379. TRIM22.
    HPAi HPA003307.
    HPA003575.
    MIMi 606559. gene.
    neXtProti NX_Q8IYM9.
    PharmGKBi PA38129.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258942.
    HOGENOMi HOG000234134.
    HOVERGENi HBG001357.
    InParanoidi Q8IYM9.
    KOi K11999.
    OMAi ICWVCEL.
    OrthoDBi EOG7RJPR6.
    PhylomeDBi Q8IYM9.
    TreeFami TF342569.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi TRIM22. human.
    GeneWikii TRIM22.
    GenomeRNAii 10346.
    NextBioi 39235.
    PROi Q8IYM9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IYM9.
    Bgeei Q8IYM9.
    CleanExi HS_TRIM22.
    Genevestigatori Q8IYM9.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    4.10.45.10. 1 hit.
    InterProi IPR001870. 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 ]
    Pfami PF00622. SPRY. 1 hit.
    PF00643. zf-B_box. 1 hit.
    [Graphical view ]
    PRINTSi PR01407. BUTYPHLNCDUF.
    SMARTi SM00336. BBOX. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS50188. B302_SPRY. 1 hit.
    PS50119. ZF_BBOX. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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. 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: October 1, 2014
    This is version 120 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