Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Interferon regulatory factor 2

Gene

IRF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) and represses those genes. Also acts as an activator for several genes including H4 and IL7. Constitutively binds to the ISRE promoter to activate IL7. Involved in cell cycle regulation through binding the site II (HiNF-M) promoter region of H4 and activating transcription during cell growth. Antagonizes IRF1 transcriptional activation.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi5 – 113109IRF tryptophan pentad repeatPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  3. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  4. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cell proliferation Source: ProtInc
  3. cytokine-mediated signaling pathway Source: Reactome
  4. interferon-gamma-mediated signaling pathway Source: Reactome
  5. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
  6. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  7. regulation of transcription, DNA-templated Source: UniProtKB
  8. type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_24938. TRAF6 mediated IRF7 activation.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.
SignaLinkiP14316.

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon regulatory factor 2
Short name:
IRF-2
Gene namesi
Name:IRF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:6117. IRF2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. focal adhesion Source: HPA
  4. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi75 – 751K → R: Diminished acetylation by both CREBBP/p300 and PCAF. Greatly reduced enhancement of H4 promoter activity. 1 Publication
Mutagenesisi78 – 781K → R: Greatly diminished acetylation by PCAF. Lesser loss of acetylation by CREBBP/p300. Loss of DNA binding and no enhancement of H4 promoter activity. 1 Publication
Mutagenesisi137 – 1371K → R: Some loss of sumoylation. Increases IRF2-mediation activation of ISRE and H4 promoters. Increased inhibition of IRF1-mediated transcription. Additional small loss of sumoylation; when associated with R-166. Great loss of sumoylation; when associated with R-296. Abolishes sumoylation. Greatly increased activation of ISRE and H4 promoters and further increased ability to inhibit IRF1-mediated transcription; when associated with R-166 and R-293. 1 Publication
Mutagenesisi166 – 1661K → R: Little loss of sumoylation. Increases IRF2-mediation activation of ISRE and H4 promoters. Increased inhibition of IRF1-mediated transcription. Greater loss of sumoylation; when associated with R-137. Further loss of sumoylation; when associated with R-293. Abolishes sumoylation. Greatly increased activation of ISRE and H4 promoters and further increased ability to inhibit IRF1-mediated transcription; when associated with R-137 and R-293. 1 Publication
Mutagenesisi293 – 2931K → R: Some loss of sumoylation. Increases IRF2-mediation activation of ISRE and H4 promoters. Increased inhibition of IRF1-mediated transcription. Further small loss of sumoylation; when associated with R-166. Great loss of sumoylation; when associated with R-137. Abolishes sumoylation. Greatly increased activation of ISRE and H4 promoters and further increased ability to inhibit IRF1-mediated transcription; when associated with R-166 and R-293. 1 Publication

Organism-specific databases

PharmGKBiPA29916.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Interferon regulatory factor 2PRO_0000154549Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751N6-acetyllysine1 Publication
Modified residuei78 – 781N6-acetyllysine1 Publication
Cross-linki137 – 137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki166 – 166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei225 – 2251Phosphoserine1 Publication
Cross-linki293 – 293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Acetylated by CBP/ p300 during cell-growth. Acetylation on Lys-75 is required for stimulation of H4 promoter activity.1 Publication
The major sites of sumoylation are Lys-137 and Lys-293. Sumoylation with SUMO1 increases its transcriptional repressor activity on IRF1 and diminishes its ability to activate ISRE and H4 promoter.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP14316.
PaxDbiP14316.
PRIDEiP14316.

PTM databases

PhosphoSiteiP14316.

Expressioni

Tissue specificityi

Expressed throughout the epithelium of the colon. Also expressed in lamina propria.1 Publication

Inductioni

By viruses and IFN.

Gene expression databases

BgeeiP14316.
CleanExiHS_IRF2.
ExpressionAtlasiP14316. baseline and differential.
GenevestigatoriP14316.

Organism-specific databases

HPAiCAB032306.
HPA030813.
HPA057327.

Interactioni

Subunit structurei

Interacts with BRD7, IRF2BP1 and IRF2BP2. Interacts with CREBBP in growing cells; the interaction acetylates IRF2 and regulates IRF2-dependent H4 promoter activity.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATG7O953522EBI-2866589,EBI-987834
FOXK1P850372EBI-2866589,EBI-2509974
FOXK2Q011672EBI-2866589,EBI-2509991
PPP3CBP162982EBI-2866589,EBI-1759540

Protein-protein interaction databases

BioGridi109868. 30 interactions.
IntActiP14316. 14 interactions.
STRINGi9606.ENSP00000377218.

Structurei

3D structure databases

ProteinModelPortaliP14316.
SMRiP14316. Positions 5-113.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IRF family.PROSITE-ProRule annotation
Contains 1 IRF tryptophan pentad repeat DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG41436.
GeneTreeiENSGT00760000119093.
HOGENOMiHOG000037937.
HOVERGENiHBG003455.
InParanoidiP14316.
KOiK10153.
OMAiSWPPFPD.
OrthoDBiEOG72ZCFD.
PhylomeDBiP14316.
TreeFamiTF328512.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR017431. Interferon_reg_fac-1/2.
IPR019817. Interferon_reg_fac_CS.
IPR001346. Interferon_reg_fact_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00605. IRF. 1 hit.
[Graphical view]
PIRSFiPIRSF038196. IFN_RF1/2. 1 hit.
PRINTSiPR00267. INTFRNREGFCT.
SMARTiSM00348. IRF. 1 hit.
[Graphical view]
PROSITEiPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P14316-1) [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
MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMH AARHGWDVEK
60 70 80 90 100
DAPLFRNWAI HTGKHQPGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIK
110 120 130 140 150
KGNNAFRVYR MLPLSERPSK KGKKPKTEKE DKVKHIKQEP VESSLGLSNG
160 170 180 190 200
VSDLSPEYAV LTSTIKNEVD STVNIIVVGQ SHLDSNIENQ EIVTNPPDIC
210 220 230 240 250
QVVEVTTESD EQPVSMSELY PLQISPVSSY AESETTDSVP SDEESAEGRP
260 270 280 290 300
HWRKRNIEGK QYLSNMGTRG SYLLPGMASF VTSNKPDLQV TIKEESNPVP
310 320 330 340
YNSSWPPFQD LPLSSSMTPA SSSSRPDRET RASVIKKTSD ITQARVKSC
Length:349
Mass (Da):39,354
Last modified:February 11, 2002 - v2
Checksum:i6298341652466560
GO
Isoform 2 (identifier: P14316-2) [UniParc]FASTAAdd to basket

Also known as: IRF-2s, IRF-2[S]

The sequence of this isoform differs from the canonical sequence as follows:
     177-178: Missing.

Note: Unable to bind to IRF2BP1 and IRF2BP2 corepressors and cannot mediate repression.

Show »
Length:347
Mass (Da):39,156
Checksum:iEE67F41029BFD6BD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581W → R in CAA34073 (PubMed:2813069).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei177 – 1782Missing in isoform 2. CuratedVSP_043965

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15949 mRNA. Translation: CAA34073.1.
BT007264 mRNA. Translation: AAP35928.1.
AK312953 mRNA. Translation: BAG35793.1.
CR457077 mRNA. Translation: CAG33358.1.
AC099343 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04677.1.
CH471056 Genomic DNA. Translation: EAX04678.1.
CH471056 Genomic DNA. Translation: EAX04680.1.
BC015803 mRNA. Translation: AAH15803.1.
CCDSiCCDS3835.1. [P14316-1]
PIRiA53340.
RefSeqiNP_002190.2. NM_002199.3. [P14316-1]
XP_005263041.1. XM_005262984.1. [P14316-2]
UniGeneiHs.654566.

Genome annotation databases

EnsembliENST00000393593; ENSP00000377218; ENSG00000168310. [P14316-1]
GeneIDi3660.
KEGGihsa:3660.
UCSCiuc003iwf.4. human. [P14316-1]

Polymorphism databases

DMDMi20141499.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15949 mRNA. Translation: CAA34073.1.
BT007264 mRNA. Translation: AAP35928.1.
AK312953 mRNA. Translation: BAG35793.1.
CR457077 mRNA. Translation: CAG33358.1.
AC099343 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04677.1.
CH471056 Genomic DNA. Translation: EAX04678.1.
CH471056 Genomic DNA. Translation: EAX04680.1.
BC015803 mRNA. Translation: AAH15803.1.
CCDSiCCDS3835.1. [P14316-1]
PIRiA53340.
RefSeqiNP_002190.2. NM_002199.3. [P14316-1]
XP_005263041.1. XM_005262984.1. [P14316-2]
UniGeneiHs.654566.

3D structure databases

ProteinModelPortaliP14316.
SMRiP14316. Positions 5-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109868. 30 interactions.
IntActiP14316. 14 interactions.
STRINGi9606.ENSP00000377218.

PTM databases

PhosphoSiteiP14316.

Polymorphism databases

DMDMi20141499.

Proteomic databases

MaxQBiP14316.
PaxDbiP14316.
PRIDEiP14316.

Protocols and materials databases

DNASUi3660.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393593; ENSP00000377218; ENSG00000168310. [P14316-1]
GeneIDi3660.
KEGGihsa:3660.
UCSCiuc003iwf.4. human. [P14316-1]

Organism-specific databases

CTDi3660.
GeneCardsiGC04M185308.
H-InvDBHIX0004671.
HGNCiHGNC:6117. IRF2.
HPAiCAB032306.
HPA030813.
HPA057327.
MIMi147576. gene.
neXtProtiNX_P14316.
PharmGKBiPA29916.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41436.
GeneTreeiENSGT00760000119093.
HOGENOMiHOG000037937.
HOVERGENiHBG003455.
InParanoidiP14316.
KOiK10153.
OMAiSWPPFPD.
OrthoDBiEOG72ZCFD.
PhylomeDBiP14316.
TreeFamiTF328512.

Enzyme and pathway databases

ReactomeiREACT_24938. TRAF6 mediated IRF7 activation.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.
SignaLinkiP14316.

Miscellaneous databases

ChiTaRSiIRF2. human.
GeneWikiiIRF2.
GenomeRNAii3660.
NextBioi14315.
PROiP14316.
SOURCEiSearch...

Gene expression databases

BgeeiP14316.
CleanExiHS_IRF2.
ExpressionAtlasiP14316. baseline and differential.
GenevestigatoriP14316.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR017431. Interferon_reg_fac-1/2.
IPR019817. Interferon_reg_fac_CS.
IPR001346. Interferon_reg_fact_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00605. IRF. 1 hit.
[Graphical view]
PIRSFiPIRSF038196. IFN_RF1/2. 1 hit.
PRINTSiPR00267. INTFRNREGFCT.
SMARTiSM00348. IRF. 1 hit.
[Graphical view]
PROSITEiPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: T-cell.
  2. "Human interferon regulatory factor 2 gene. Intron-exon organization and functional analysis of 5'-flanking region."
    Cha Y., Deisseroth A.B.
    J. Biol. Chem. 269:5279-5287(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Trachea.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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).
    Tissue: Skin.
  9. "The integrated activities of IRF-2 (HiNF-M), CDP/cut (HiNF-D) and H4TF-2 (HiNF-P) regulate transcription of a cell cycle controlled human histone H4 gene: mechanistic differences between distinct H4 genes."
    Aziz F., van Wijnen A.J., Vaughan P.S., Wu S., Shakoori A.R., Lian J.B., Soprano K.J., Stein J.L., Stein G.S.
    Mol. Biol. Rep. 25:1-12(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, FUNCTION AS AN ACTIVATOR.
  10. "Molecular characterization of celtix-1, a bromodomain protein interacting with the transcription factor interferon regulatory factor 2."
    Staal A., Enserink J.M., Stein J.L., Stein G.S., van Wijnen A.J.
    J. Cell. Physiol. 185:269-279(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRD7.
  11. "Cloning of an interferon regulatory factor 2 isoform with different regulatory ability."
    Koenig Merediz S.A., Schmidt M., Hoppe G.J., Alfken J., Meraro D., Levi B.Z., Neubauer A., Wittig B.
    Nucleic Acids Res. 28:4219-4224(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  12. "Interferon regulatory factor-2 regulates cell growth through its acetylation."
    Masumi A., Yamakawa Y., Fukazawa H., Ozato K., Komuro K.
    J. Biol. Chem. 278:25401-25407(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-75 AND LYS-78, INTERACTION WITH CREBBP, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-75 AND LYS-78.
  13. "Identification of novel co-repressor molecules for interferon regulatory factor-2."
    Childs K.S., Goodbourn S.
    Nucleic Acids Res. 31:3016-3026(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, INTERACTION WITH IRF2BP1 AND IRF2BP2.
  14. "Interferon regulatory factor 1 (IRF-1) and IRF-2 distinctively up-regulate gene expression and production of interleukin-7 in human intestinal epithelial cells."
    Oshima S., Nakamura T., Namiki S., Okada E., Tsuchiya K., Okamoto R., Yamazaki M., Yokota T., Aida M., Yamaguchi Y., Kanai T., Handa H., Watanabe M.
    Mol. Cell. Biol. 24:6298-6310(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  15. "Regulation of IRF2 transcriptional activity by its sumoylation."
    Han K.-J., Jiang L., Shu H.-B.
    Biochem. Biophys. Res. Commun. 372:772-778(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-137; LYS-166 AND LYS-293, FUNCTION, MUTAGENESIS OF LYS-137; LYS-166 AND LYS-293.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiIRF2_HUMAN
AccessioniPrimary (citable) accession number: P14316
Secondary accession number(s): D6RCK5
, H0Y8S3, Q6IAS7, Q96B99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 11, 2002
Last modified: March 4, 2015
This is version 146 of the entry and version 2 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.