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Q8IYM9

- TRI22_HUMAN

UniProt

Q8IYM9 - TRI22_HUMAN

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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

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
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

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. cytoplasm Source: UniProtKB
  2. 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.

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.
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.
GeneTreeiENSGT00760000118893.
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.
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. 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

        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.

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.
GeneTreei ENSGT00760000118893.
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

Bgeei Q8IYM9.
CleanExi HS_TRIM22.
ExpressionAtlasi Q8IYM9. baseline and differential.
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.
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 ]
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

« 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. "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 29, 2014
This is version 121 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