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Protein

Interferon-activable protein 202

Gene

Ifi202

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 AIM2.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei84Mediates interaction with 53BP11
Sitei283Mediates interaction with 53BP11

GO - Molecular functioni

  • double-stranded DNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to interferon-beta Source: MGI
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • negative regulation of innate immune response Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon-activable protein 202
Short name:
Ifi-202
Alternative name(s):
Interferon-inducible protein p202
Lupus susceptibility protein p202
Gene namesi
Name:Ifi202
Synonyms:Ifi202a, Ifi202b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1347080. Ifi202a.
MGI:1347083. Ifi202b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi48K → A: Strongly reduces affinity for DNA; when associated with A-53 and W-54. 1 Publication1
Mutagenesisi53K → A: Strongly reduces affinity for DNA; when associated with A-48 and W-54. 1 Publication1
Mutagenesisi54G → W: Strongly reduces affinity for DNA; when associated with A-48 and A-53. 1 Publication1
Mutagenesisi76K → A: Strongly reduces affinity for DNA; when associated with A-79 and A-236. 1 Publication1
Mutagenesisi79K → A: Strongly reduces affinity for DNA; when associated with A-76 and A-236. 1 Publication1
Mutagenesisi84H → F: Loss of interaction with 53BP1; when associated with F-283. 1 Publication1
Mutagenesisi166S → A: Strongly reduces affinity for DNA; when associated with. 1 Publication1
Mutagenesisi182 – 185NDKS → ADAA: Strongly reduces affinity for DNA. 1 Publication4
Mutagenesisi187T → A: Strongly reduces affinity for DNA; when associated with A-189 and A-198. 1 Publication1
Mutagenesisi189K → A: Strongly reduces affinity for DNA; when associated with A-187 and A-198. 1 Publication1
Mutagenesisi198K → A: Strongly reduces affinity for DNA; when associated with A-187 and A-189. 1 Publication1
Mutagenesisi222 – 224HLR → ALA: Strongly reduces affinity for DNA. 1 Publication3
Mutagenesisi226G → W: Strongly reduces affinity for DNA; when associated with A-166; A-227 and A-229. 1 Publication1
Mutagenesisi227N → A: Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-229. 1 Publication1
Mutagenesisi229K → A: Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-227. 1 Publication1
Mutagenesisi236N → A: Strongly reduces affinity for DNA; when associated with A-76 and A-79. 1 Publication1
Mutagenesisi283H → F: Loss of interaction with 53BP1; when associated with F-84. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001537191 – 445Interferon-activable protein 202Add BLAST445

Post-translational modificationi

Phosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9R002.
PRIDEiQ9R002.

PTM databases

iPTMnetiQ9R002.
PhosphoSitePlusiQ9R002.

Expressioni

Inductioni

By beta interferon. By IL6 in splenocytes (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000026535.
CleanExiMM_IFI202B.
GenevisibleiQ9R002. MM.

Interactioni

Subunit structurei

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).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RB1P064005EBI-3043899,EBI-491274From a different organism.
Rb1P134057EBI-3043899,EBI-971782

Protein-protein interaction databases

BioGridi204945. 1 interactor.
IntActiQ9R002. 4 interactors.
MINTiMINT-4098521.
STRINGi10090.ENSMUSP00000000266.

Structurei

Secondary structure

1445
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni47 – 50Combined sources4
Beta strandi56 – 58Combined sources3
Beta strandi62 – 69Combined sources8
Beta strandi73 – 75Combined sources3
Turni76 – 79Combined sources4
Beta strandi80 – 88Combined sources9
Beta strandi93 – 98Combined sources6
Helixi101 – 106Combined sources6
Beta strandi112 – 121Combined sources10
Beta strandi124 – 127Combined sources4
Beta strandi132 – 135Combined sources4
Helixi138 – 140Combined sources3
Helixi146 – 153Combined sources8
Helixi158 – 161Combined sources4
Beta strandi169 – 181Combined sources13
Beta strandi186 – 191Combined sources6
Beta strandi196 – 201Combined sources6
Turni211 – 213Combined sources3
Beta strandi216 – 224Combined sources9
Beta strandi226 – 228Combined sources3
Beta strandi231 – 233Combined sources3
Beta strandi239 – 242Combined sources4
Beta strandi253 – 256Combined sources4
Beta strandi260 – 267Combined sources8
Beta strandi271 – 274Combined sources4
Turni275 – 278Combined sources4
Beta strandi279 – 287Combined sources9
Beta strandi289 – 297Combined sources9
Helixi300 – 306Combined sources7
Beta strandi311 – 314Combined sources4
Beta strandi316 – 320Combined sources5
Beta strandi323 – 326Combined sources4
Helixi329 – 331Combined sources3
Beta strandi332 – 334Combined sources3
Helixi356 – 361Combined sources6
Beta strandi368 – 379Combined sources12
Beta strandi381 – 389Combined sources9
Beta strandi395 – 399Combined sources5
Helixi401 – 405Combined sources5
Beta strandi413 – 422Combined sources10
Beta strandi429 – 441Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9R002.
SMRiQ9R002.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 243HIN-200 1PROSITE-ProRule annotationAdd BLAST198
Domaini244 – 441HIN-200 2PROSITE-ProRule annotationAdd BLAST198

Domaini

The HIN-20 domains mediate dsDNA binding via electrostatic interactions.1 Publication

Sequence similaritiesi

Belongs to the HIN-200 family.Curated
Contains 2 HIN-200 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000013296.
InParanoidiQ9R002.
KOiK12971.
OrthoDBiEOG091G02W0.
TreeFamiTF337385.

Family and domain databases

InterProiIPR004021. HIN200/IF120x.
[Graphical view]
PfamiPF02760. HIN. 2 hits.
[Graphical view]
PROSITEiPS50834. HIN_200. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R002-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNRNLRSST NSEFSEGQHQ TPSSDSSGHG EDQPQASPGP NKKSHTPKKN
60 70 80 90 100
ISKGAVLHEK PMTVMVLTAT EPFNYKEGKE NMFHATVATE SQYYRVKVFN
110 120 130 140 150
MDLKEKFTEN KFITISKYFN SSGILEINET ATVSEAAPNQ IIEVPKNIIR
160 170 180 190 200
SAKETLKISK IKELDSGTLI YGVFAVEKKK VNDKSITFKI KDNEDNIKVV
210 220 230 240 250
WDKKQHNINY EKGDKLQLFS FHLRKGNGKP ILHSGNHSFI KGEKLLKESF
260 270 280 290 300
EGDGYHKGPK QVVALKATKL FTYDSIKSKK MFHATVATDT EFFRVMVFEE
310 320 330 340 350
NLEKKFIPGN TIALSDYFGM YGSLAIHEYS SVSEVKSQNK EDSSSSDERL
360 370 380 390 400
IEHLKICDLH LQTKERLVDG EFKVYRKSTG NNCICYGIWD DTGAMKVVVS
410 420 430 440
GQLTSVNCEI GNTIRLVCFE LTSNADEWFL RSTRYSYMEV IMPEK
Length:445
Mass (Da):50,466
Last modified:July 27, 2011 - v3
Checksum:i5EA0E93E143C58EA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13 – 15EFS → DLA in AAF04260 (PubMed:10493828).Curated3
Sequence conflicti13 – 15EFS → DLA in AAH55888 (PubMed:15489334).Curated3
Sequence conflicti79K → N in ABB00055 (Ref. 3) Curated1
Sequence conflicti92Q → K in AAF04260 (PubMed:10493828).Curated1
Sequence conflicti92Q → K in AAH18233 (PubMed:15489334).Curated1
Sequence conflicti109E → G in ABB00055 (Ref. 3) Curated1
Sequence conflicti111K → Q in AAH18233 (PubMed:15489334).Curated1
Sequence conflicti127I → F in ABB00055 (Ref. 3) Curated1
Sequence conflicti141 – 142II → MF in AAA39312 (PubMed:2477366).Curated2
Sequence conflicti141 – 142II → MF in AAF04260 (PubMed:10493828).Curated2
Sequence conflicti141 – 142II → MF in ABB00055 (Ref. 3) Curated2
Sequence conflicti141 – 142II → MF in AAH18233 (PubMed:15489334).Curated2
Sequence conflicti141 – 142II → MF in AAH55888 (PubMed:15489334).Curated2
Sequence conflicti187T → I in ABB00055 (Ref. 3) Curated1
Sequence conflicti190I → V in ABB00055 (Ref. 3) Curated1
Sequence conflicti204K → E in AAA39312 (PubMed:2477366).Curated1
Sequence conflicti204K → E in AAF04260 (PubMed:10493828).Curated1
Sequence conflicti204K → E in ABB00055 (Ref. 3) Curated1
Sequence conflicti204K → E in AAH18233 (PubMed:15489334).Curated1
Sequence conflicti204K → E in AAH55888 (PubMed:15489334).Curated1
Sequence conflicti240I → V in AAF04260 (PubMed:10493828).Curated1
Sequence conflicti350L → P in AAA39312 (PubMed:2477366).Curated1
Sequence conflicti350L → P in AAF04260 (PubMed:10493828).Curated1
Sequence conflicti350L → P in ABB00055 (Ref. 3) Curated1
Sequence conflicti350L → P in AAH18233 (PubMed:15489334).Curated1
Sequence conflicti350L → P in AAH55888 (PubMed:15489334).Curated1
Sequence conflicti364K → E in AAA39312 (PubMed:2477366).Curated1
Sequence conflicti364K → E in AAF04260 (PubMed:10493828).Curated1
Sequence conflicti364K → E in ABB00055 (Ref. 3) Curated1
Sequence conflicti364K → E in AAH18233 (PubMed:15489334).Curated1
Sequence conflicti364K → E in AAH55888 (PubMed:15489334).Curated1
Sequence conflicti368V → F in AAA39312 (PubMed:2477366).Curated1
Sequence conflicti379T → S in AAA39312 (PubMed:2477366).Curated1
Sequence conflicti379T → S in AAF04260 (PubMed:10493828).Curated1
Sequence conflicti379T → S in ABB00055 (Ref. 3) Curated1
Sequence conflicti379T → S in AAH18233 (PubMed:15489334).Curated1
Sequence conflicti379T → S in AAH55888 (PubMed:15489334).Curated1
Sequence conflicti432S → A in AAA39312 (PubMed:2477366).Curated1
Sequence conflicti432S → A in AAF04260 (PubMed:10493828).Curated1
Sequence conflicti432S → A in ABB00055 (Ref. 3) Curated1
Sequence conflicti432S → A in AAH18233 (PubMed:15489334).Curated1
Sequence conflicti432S → A in AAH55888 (PubMed:15489334).Curated1

Polymorphismi

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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35794.1.
PIRiA34457.
RefSeqiNP_032353.2. NM_008327.2.
NP_036070.2. NM_011940.2.
XP_006536966.1. XM_006536903.2.
UniGeneiMm.218770.

Genome annotation databases

EnsembliENSMUST00000000266; ENSMUSP00000000266; ENSMUSG00000026535.
GeneIDi100044068.
26388.
KEGGimmu:100044068.
mmu:26388.
UCSCiuc007dsk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35794.1.
PIRiA34457.
RefSeqiNP_032353.2. NM_008327.2.
NP_036070.2. NM_011940.2.
XP_006536966.1. XM_006536903.2.
UniGeneiMm.218770.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9R002.
SMRiQ9R002.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204945. 1 interactor.
IntActiQ9R002. 4 interactors.
MINTiMINT-4098521.
STRINGi10090.ENSMUSP00000000266.

PTM databases

iPTMnetiQ9R002.
PhosphoSitePlusiQ9R002.

Proteomic databases

PaxDbiQ9R002.
PRIDEiQ9R002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000266; ENSMUSP00000000266; ENSMUSG00000026535.
GeneIDi100044068.
26388.
KEGGimmu:100044068.
mmu:26388.
UCSCiuc007dsk.2. mouse.

Organism-specific databases

CTDi26388.
MGIiMGI:1347080. Ifi202a.
MGI:1347083. Ifi202b.

Phylogenomic databases

GeneTreeiENSGT00390000013296.
InParanoidiQ9R002.
KOiK12971.
OrthoDBiEOG091G02W0.
TreeFamiTF337385.

Miscellaneous databases

ChiTaRSiIfi202b. mouse.
PROiQ9R002.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026535.
CleanExiMM_IFI202B.
GenevisibleiQ9R002. MM.

Family and domain databases

InterProiIPR004021. HIN200/IF120x.
[Graphical view]
PfamiPF02760. HIN. 2 hits.
[Graphical view]
PROSITEiPS50834. HIN_200. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIFI2_MOUSE
AccessioniPrimary (citable) accession number: Q9R002
Secondary accession number(s): E9QLD9
, P15091, Q38JF1, Q7TMN6, Q8VEL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.