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Q9R002 (IFI2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon-activable protein 202

Short name=Ifi-202
Alternative name(s):
Interferon-inducible protein p202
Lupus susceptibility protein p202
Gene names
Name:Ifi202
Synonyms:Ifi202a, Ifi202b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits the transcriptional activity of several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin. Has anti-apoptotic effects due to inhibition of the transcriptional activity of p53. Binds dsDNA in the cytosol. Is involved in innate immune response and has anti-inflammatory activity. Inhibits caspase activation in response to cytosolic DNA and inhibits the activation of the AIM2 inflammasome, probably by sequestering cytoplasmic DNA and preventing its being bound by AIM2. Ref.9 Ref.10 Ref.11

Subunit structure

Binds to several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin. Also binds p53, the hypophosphorylated, growth-inhibitory form of the retinoblastoma protein and the p53-binding protein 1 (53BP1). Ref.9

Subcellular location

Cytoplasm. Nucleus. Note: Accumulates first in the cytoplasm, and is translocated to the nucleus after a delay, where it is primarily chromatin-associated. Ref.10

Induction

By beta interferon. By IL6 in splenocytes (at protein level). Ref.8

Domain

The HIN-20 domains mediate dsDNA binding via electrostatic interactions. Ref.11

Post-translational modification

Phosphorylated.

Polymorphism

NZB mice express 10 to 100 fold more Ifi202 in spleen than B6 or NZW mice. This could account for the high susceptibility of NZB mice to systemic lupus.

Sequence similarities

Belongs to the HIN-200 family.

Contains 2 HIN-200 domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RB1P064005EBI-3043899,EBI-491274From a different organism.
Rb1P134057EBI-3043899,EBI-971782

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Interferon-activable protein 202
PRO_0000153719

Regions

Domain46 – 243198HIN-200 1
Domain244 – 441198HIN-200 2

Sites

Site841Mediates interaction with 53BP1
Site2831Mediates interaction with 53BP1

Experimental info

Mutagenesis481K → A: Strongly reduces affinity for DNA; when associated with A-53 and W-54. Ref.11
Mutagenesis531K → A: Strongly reduces affinity for DNA; when associated with A-48 and W-54. Ref.11
Mutagenesis541G → W: Strongly reduces affinity for DNA; when associated with A-48 and A-53. Ref.11
Mutagenesis761K → A: Strongly reduces affinity for DNA; when associated with A-79 and A-236. Ref.11
Mutagenesis791K → A: Strongly reduces affinity for DNA; when associated with A-76 and A-236. Ref.11
Mutagenesis841H → F: Loss of interaction with 53BP1; when associated with F-283. Ref.6
Mutagenesis1661S → A: Strongly reduces affinity for DNA; when associated with. Ref.11
Mutagenesis182 – 1854NDKS → ADAA: Strongly reduces affinity for DNA. Ref.11
Mutagenesis1871T → A: Strongly reduces affinity for DNA; when associated with A-189 and A-198. Ref.11
Mutagenesis1891K → A: Strongly reduces affinity for DNA; when associated with A-187 and A-198. Ref.11
Mutagenesis1981K → A: Strongly reduces affinity for DNA; when associated with A-187 and A-189. Ref.11
Mutagenesis222 – 2243HLR → ALA: Strongly reduces affinity for DNA. Ref.11
Mutagenesis2261G → W: Strongly reduces affinity for DNA; when associated with A-166; A-227 and A-229. Ref.11
Mutagenesis2271N → A: Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-229. Ref.11
Mutagenesis2291K → A: Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-227. Ref.11
Mutagenesis2361N → A: Strongly reduces affinity for DNA; when associated with A-76 and A-79. Ref.11
Mutagenesis2831H → F: Loss of interaction with 53BP1; when associated with F-84. Ref.6
Sequence conflict13 – 153EFS → DLA in AAF04260. Ref.2
Sequence conflict13 – 153EFS → DLA in AAH55888. Ref.5
Sequence conflict791K → N in ABB00055. Ref.3
Sequence conflict921Q → K in AAF04260. Ref.2
Sequence conflict921Q → K in AAH18233. Ref.5
Sequence conflict1091E → G in ABB00055. Ref.3
Sequence conflict1111K → Q in AAH18233. Ref.5
Sequence conflict1271I → F in ABB00055. Ref.3
Sequence conflict141 – 1422II → MF in AAA39312. Ref.1
Sequence conflict141 – 1422II → MF in AAF04260. Ref.2
Sequence conflict141 – 1422II → MF in ABB00055. Ref.3
Sequence conflict141 – 1422II → MF in AAH18233. Ref.5
Sequence conflict141 – 1422II → MF in AAH55888. Ref.5
Sequence conflict1871T → I in ABB00055. Ref.3
Sequence conflict1901I → V in ABB00055. Ref.3
Sequence conflict2041K → E in AAA39312. Ref.1
Sequence conflict2041K → E in AAF04260. Ref.2
Sequence conflict2041K → E in ABB00055. Ref.3
Sequence conflict2041K → E in AAH18233. Ref.5
Sequence conflict2041K → E in AAH55888. Ref.5
Sequence conflict2401I → V in AAF04260. Ref.2
Sequence conflict3501L → P in AAA39312. Ref.1
Sequence conflict3501L → P in AAF04260. Ref.2
Sequence conflict3501L → P in ABB00055. Ref.3
Sequence conflict3501L → P in AAH18233. Ref.5
Sequence conflict3501L → P in AAH55888. Ref.5
Sequence conflict3641K → E in AAA39312. Ref.1
Sequence conflict3641K → E in AAF04260. Ref.2
Sequence conflict3641K → E in ABB00055. Ref.3
Sequence conflict3641K → E in AAH18233. Ref.5
Sequence conflict3641K → E in AAH55888. Ref.5
Sequence conflict3681V → F in AAA39312. Ref.1
Sequence conflict3791T → S in AAA39312. Ref.1
Sequence conflict3791T → S in AAF04260. Ref.2
Sequence conflict3791T → S in ABB00055. Ref.3
Sequence conflict3791T → S in AAH18233. Ref.5
Sequence conflict3791T → S in AAH55888. Ref.5
Sequence conflict4321S → A in AAA39312. Ref.1
Sequence conflict4321S → A in AAF04260. Ref.2
Sequence conflict4321S → A in ABB00055. Ref.3
Sequence conflict4321S → A in AAH18233. Ref.5
Sequence conflict4321S → A in AAH55888. Ref.5

Secondary structure

.............................................................................. 445
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9R002 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 5EA0E93E143C58EA

FASTA44550,466
        10         20         30         40         50         60 
MSNRNLRSST NSEFSEGQHQ TPSSDSSGHG EDQPQASPGP NKKSHTPKKN ISKGAVLHEK 

        70         80         90        100        110        120 
PMTVMVLTAT EPFNYKEGKE NMFHATVATE SQYYRVKVFN MDLKEKFTEN KFITISKYFN 

       130        140        150        160        170        180 
SSGILEINET ATVSEAAPNQ IIEVPKNIIR SAKETLKISK IKELDSGTLI YGVFAVEKKK 

       190        200        210        220        230        240 
VNDKSITFKI KDNEDNIKVV WDKKQHNINY EKGDKLQLFS FHLRKGNGKP ILHSGNHSFI 

       250        260        270        280        290        300 
KGEKLLKESF EGDGYHKGPK QVVALKATKL FTYDSIKSKK MFHATVATDT EFFRVMVFEE 

       310        320        330        340        350        360 
NLEKKFIPGN TIALSDYFGM YGSLAIHEYS SVSEVKSQNK EDSSSSDERL IEHLKICDLH 

       370        380        390        400        410        420 
LQTKERLVDG EFKVYRKSTG NNCICYGIWD DTGAMKVVVS GQLTSVNCEI GNTIRLVCFE 

       430        440 
LTSNADEWFL RSTRYSYMEV IMPEK 

« Hide

References

« Hide 'large scale' references
[1]"Interferons as gene activators. Indications for repeated gene duplication during the evolution of a cluster of interferon-activatable genes on murine chromosome 1."
Choubey D., Snoddy J., Chaturvedi V., Toniato E., Opdenakker G., Thakur A., Samanta H., Engel D.A., Lengyel P.
J. Biol. Chem. 264:17182-17189(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: AKR.
[2]"Characteristics of three homologous 202 genes (Ifi202a, ifi202b, and ifi202c) from the murine interferon-activatable gene 200 cluster."
Wang H., Chatterjee G., Meyer J.J., Liu C.J., Manjunath N.A., Bray-Ward P., Lengyel P.
Genomics 60:281-294(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/Sv.
[3]"Coding cDNA sequence for p202 in New Zealand Black mice."
Chen J., Choubey D.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: NZB.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"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].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
[6]"p202, an interferon-inducible modulator of transcription, inhibits transcriptional activation by the p53 tumor suppressor protein, and a segment from the p53-binding protein 1 that binds to p202 overcomes this inhibition."
Datta B., Li B., Choubey D., Nallur G., Lengyel P.
J. Biol. Chem. 271:27544-27555(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-84 AND HIS-283.
[7]"Evidence for an interferon-inducible gene, Ifi202, in the susceptibility to systemic lupus."
Rozzo S.J., Allard J.D., Choubey D., Vyse T.J., Izui S., Peltz G., Kotzin B.L.
Immunity 15:435-443(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM.
[8]"Interleukin-6 induces expression of Ifi202, an interferon-inducible candidate gene for lupus susceptibility."
Pramanik R., Jorgensen T.N., Xin H., Kotzin B.L., Choubey D.
J. Biol. Chem. 279:16121-16127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY IL6.
[9]"Increased expression of Ifi202, an IFN-activatable gene, in B6.Nba2 lupus susceptible mice inhibits p53-mediated apoptosis."
Xin H., D'Souza S., Jorgensen T.N., Vaughan A.T., Lengyel P., Kotzin B.L., Choubey D.
J. Immunol. 176:5863-5870(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TP53.
[10]"HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA."
Roberts T.L., Idris A., Dunn J.A., Kelly G.M., Burnton C.M., Hodgson S., Hardy L.L., Garceau V., Sweet M.J., Ross I.L., Hume D.A., Stacey K.J.
Science 323:1057-1060(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"Structural basis for termination of AIM2-mediated signaling by p202."
Ru H., Ni X., Zhao L., Crowley C., Ding W., Hung L.W., Shaw N., Cheng G., Liu Z.J.
Cell Res. 23:855-858(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 46-242 IN COMPLEX WITH DNA, FUNCTION, DOMAIN, MUTAGENESIS OF LYS-48; LYS-53; GLY-54; LYS-76; LYS-79; SER-166; 182-ASN--SER-185; THR-187; LYS-189; LYS-198; 222-HIS--ARG-224; GLY-226; ASN-227; LYS-229 AND ASN-236, DNA BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31418 mRNA. Translation: AAA39312.1.
AF140672 mRNA. Translation: AAF04260.1.
DQ222946 mRNA. Translation: ABB00055.1.
AC170584 Genomic DNA. No translation available.
BC018233 mRNA. Translation: AAH18233.1.
BC055888 mRNA. Translation: AAH55888.1.
PIRA34457.
RefSeqNP_032353.2. NM_008327.2.
NP_036070.2. NM_011940.2.
XP_001473923.2. XM_001473873.3.
XP_006536966.1. XM_006536903.1.
UniGeneMm.218770.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4JBJX-ray2.69A/B46-242[»]
4JBKX-ray2.96A/B/C/D46-242[»]
4L5QX-ray2.23A46-243[»]
4L5RX-ray1.87C46-243[»]
4L5SX-ray2.94A/B46-243[»]
4L5TX-ray3.40A/B/C/D244-445[»]
4LNQX-ray2.00A/B53-245[»]
ProteinModelPortalQ9R002.
SMRQ9R002. Positions 46-242, 244-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204945. 1 interaction.
IntActQ9R002. 4 interactions.
MINTMINT-4098521.

PTM databases

PhosphoSiteQ9R002.

Proteomic databases

PaxDbQ9R002.
PRIDEQ9R002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000266; ENSMUSP00000000266; ENSMUSG00000026535.
GeneID100044068.
26388.
KEGGmmu:100044068.
mmu:26388.
UCSCuc007dsk.2. mouse.

Organism-specific databases

CTD26388.
MGIMGI:1347080. Ifi202a.
MGI:1347083. Ifi202b.

Phylogenomic databases

eggNOGNOG81691.
GeneTreeENSGT00390000013296.
InParanoidQ9R002.
KOK12971.
OrthoDBEOG7ZD1V8.
TreeFamTF337385.

Gene expression databases

BgeeQ9R002.
CleanExMM_IFI202B.
GenevestigatorQ9R002.

Family and domain databases

Gene3D2.40.50.140. 4 hits.
InterProIPR004021. HIN200/IF120x.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamPF02760. HIN. 2 hits.
[Graphical view]
PROSITEPS50834. HIN_200. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIfi202b. mouse.
NextBio304323.
PROQ9R002.
SOURCESearch...

Entry information

Entry nameIFI2_MOUSE
AccessionPrimary (citable) accession number: Q9R002
Secondary accession number(s): E9QLD9 expand/collapse secondary AC list , P15091, Q38JF1, Q7TMN6, Q8VEL7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot