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Protein

Interferon regulatory factor 2-binding protein 2

Gene

Irf2bp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a transcriptional corepressor in a IRF2-dependent manner, this repression is not mediated by histone deacetylase activities. Represses the NFAT1-dependent transactivation of NFAT-responsive promoters. Acts as a coactivator of VEGFA expression in cardiac and skeletal muscle (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri489 – 53648RING-type; degenerateAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon regulatory factor 2-binding protein 2
Short name:
IRF-2-binding protein 2
Short name:
IRF-2BP2
Gene namesi
Name:Irf2bp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2443921. Irf2bp2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 570569Interferon regulatory factor 2-binding protein 2PRO_0000418085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei71 – 711PhosphoserineBy similarity
Modified residuei169 – 1691PhosphoserineCombined sources
Modified residuei226 – 2261PhosphoserineCombined sources
Modified residuei250 – 2501PhosphoserineCombined sources
Modified residuei300 – 3001PhosphoserineBy similarity
Modified residuei343 – 3431PhosphoserineCombined sources
Modified residuei389 – 3891PhosphoserineCombined sources
Modified residuei406 – 4061PhosphoserineCombined sources
Modified residuei438 – 4381PhosphoserineCombined sources
Modified residuei440 – 4401PhosphoserineCombined sources
Modified residuei443 – 4431PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Ser-343 is required for nuclear targeting.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiE9Q1P8.
MaxQBiE9Q1P8.
PaxDbiE9Q1P8.
PeptideAtlasiE9Q1P8.
PRIDEiE9Q1P8.

PTM databases

iPTMnetiE9Q1P8.

Expressioni

Gene expression databases

BgeeiE9Q1P8.
GenevisibleiE9Q1P8. MM.

Interactioni

Subunit structurei

Interacts with IRF2. Part of a corepressor complex containing IRF2 and IRF2BP1. Interacts with VGLL4 (By similarity).By similarity

Protein-protein interaction databases

IntActiE9Q1P8. 1 interaction.
MINTiMINT-8178500.
STRINGi10090.ENSMUSP00000062753.

Structurei

3D structure databases

ProteinModelPortaliE9Q1P8.
SMRiE9Q1P8. Positions 481-560.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi342 – 39857Pro-richAdd
BLAST
Compositional biasi383 – 3864Poly-Pro

Domaini

The C-terminal RING-type zinc finger domain is sufficient for interaction with IRF2.By similarity

Sequence similaritiesi

Belongs to the IRF2BP family.Curated
Contains 1 RING-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri489 – 53648RING-type; degenerateAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IPPD. Eukaryota.
ENOG4110EVD. LUCA.
GeneTreeiENSGT00390000005089.
HOGENOMiHOG000049069.
InParanoidiE9Q1P8.
OMAiSESHKNR.
OrthoDBiEOG7673CH.
TreeFamiTF317075.

Family and domain databases

InterProiIPR022750. Interferon_reg_fac2-bd1_2_Znf.
[Graphical view]
PfamiPF11261. IRF-2BP1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

E9Q1P8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAVAVAAA SRRQSCYLCD LPRMPWAMIW DFTEPVCRGC VNYEGADRVE
60 70 80 90 100
FVIETARQLK RAHGCFPEGR SPTGAQPAAA KPPPLSAKDL LLQPPPQLGH
110 120 130 140 150
AGAEAARAQA MERYPLAPDR APRLASDFST RAGAGLPQSA AQQSAPANGI
160 170 180 190 200
LVPNGFSKLE EPPELNRQSP NPRRAHAVPP TLVPLVNGSA ALGLSGRAAA
210 220 230 240 250
TLAAVSGTPG LGAQPAELGT HKRPASVSSA AAEHEAREPS KEKAQPAHRS
260 270 280 290 300
PADSLSSAAG ASELSAEGAG KGRAPGEQDW ASRPKTVRDT LLALHQHGHS
310 320 330 340 350
GPFESKFKKE PALTAAGRLL GFEANGANGS KAVARTARKR KPSPEPEGEV
360 370 380 390 400
GPPKINGETQ PWLSTSTEGL KIPITPTSSF VSPPPPTASP HSNRTTPPEA
410 420 430 440 450
AQNGQSPMAA LILVADNAGG SHASKDATQV HSTTRRNSSS PPSPSSMNQR
460 470 480 490 500
RLGPREVGGQ ATGSTGGLEP VHPASLPDSS LAASAPLCCT LCHERLEDTH
510 520 530 540 550
FVQCPSVPSH KFCFPCSRQS IKQQGASGEV YCPSGEKCPL VGSNVPWAFM
560 570
QGEIATILAG DVKVKKERDS
Length:570
Mass (Da):59,292
Last modified:April 5, 2011 - v1
Checksum:i533BE0AC9CE6A527
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC118255 Genomic DNA. No translation available.
AK087491 mRNA. Translation: BAC39896.1.
CCDSiCCDS52711.1.
RefSeqiNP_001158070.1. NM_001164598.1.
UniGeneiMm.334918.
Mm.491125.

Genome annotation databases

EnsembliENSMUST00000054960; ENSMUSP00000062753; ENSMUSG00000051495.
GeneIDi270110.
KEGGimmu:270110.
UCSCiuc009nyw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC118255 Genomic DNA. No translation available.
AK087491 mRNA. Translation: BAC39896.1.
CCDSiCCDS52711.1.
RefSeqiNP_001158070.1. NM_001164598.1.
UniGeneiMm.334918.
Mm.491125.

3D structure databases

ProteinModelPortaliE9Q1P8.
SMRiE9Q1P8. Positions 481-560.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiE9Q1P8. 1 interaction.
MINTiMINT-8178500.
STRINGi10090.ENSMUSP00000062753.

PTM databases

iPTMnetiE9Q1P8.

Proteomic databases

EPDiE9Q1P8.
MaxQBiE9Q1P8.
PaxDbiE9Q1P8.
PeptideAtlasiE9Q1P8.
PRIDEiE9Q1P8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054960; ENSMUSP00000062753; ENSMUSG00000051495.
GeneIDi270110.
KEGGimmu:270110.
UCSCiuc009nyw.2. mouse.

Organism-specific databases

CTDi359948.
MGIiMGI:2443921. Irf2bp2.

Phylogenomic databases

eggNOGiENOG410IPPD. Eukaryota.
ENOG4110EVD. LUCA.
GeneTreeiENSGT00390000005089.
HOGENOMiHOG000049069.
InParanoidiE9Q1P8.
OMAiSESHKNR.
OrthoDBiEOG7673CH.
TreeFamiTF317075.

Miscellaneous databases

PROiE9Q1P8.
SOURCEiSearch...

Gene expression databases

BgeeiE9Q1P8.
GenevisibleiE9Q1P8. MM.

Family and domain databases

InterProiIPR022750. Interferon_reg_fac2-bd1_2_Znf.
[Graphical view]
PfamiPF11261. IRF-2BP1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 432-570.
    Strain: C57BL/6J.
    Tissue: Eye.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250; SER-438 AND SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-226 AND SER-343, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-250; SER-343; SER-389; SER-406 AND SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas and Spleen.

Entry informationi

Entry nameiI2BP2_MOUSE
AccessioniPrimary (citable) accession number: E9Q1P8
Secondary accession number(s): Q8BJC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: April 5, 2011
Last modified: July 6, 2016
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.