I2BP2_HUMAN
ID I2BP2_HUMAN Reviewed; 587 AA.
AC Q7Z5L9; B1AM35; B1AM36; Q6P083; Q7Z5L8; Q8N351; Q8WUH8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Interferon regulatory factor 2-binding protein 2;
DE Short=IRF-2-binding protein 2;
DE Short=IRF-2BP2;
GN Name=IRF2BP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP IRF2, AND SUBCELLULAR LOCATION.
RX PubMed=12799427; DOI=10.1093/nar/gkg431;
RA Childs K.S., Goodbourn S.;
RT "Identification of novel co-repressor molecules for interferon regulatory
RT factor-2.";
RL Nucleic Acids Res. 31:3016-3026(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 362-587 (ISOFORMS 1/2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175 AND SER-360, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-457 AND SER-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP FUNCTION, INTERACTION WITH VGLL4, AND SUBCELLULAR LOCATION.
RX PubMed=20702774; DOI=10.1096/fj.10-167049;
RA Teng A.C., Kuraitis D., Deeke S.A., Ahmadi A., Dugan S.G., Cheng B.L.,
RA Crowson M.G., Burgon P.G., Suuronen E.J., Chen H.H., Stewart A.F.;
RT "IRF2BP2 is a skeletal and cardiac muscle-enriched ischemia-inducible
RT activator of VEGFA expression.";
RL FASEB J. 24:4825-4834(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-360; SER-457 AND
RP SER-460, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION.
RX PubMed=21576369; DOI=10.1128/mcb.00974-10;
RA Carneiro F.R., Ramalho-Oliveira R., Mognol G.P., Viola J.P.;
RT "Interferon regulatory factor 2 binding protein 2 is a new NFAT1 partner
RT and represses its transcriptional activity.";
RL Mol. Cell. Biol. 31:2889-2901(2011).
RN [14]
RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND PHOSPHORYLATION AT
RP SER-360.
RX PubMed=21887377; DOI=10.1371/journal.pone.0024100;
RA Teng A.C., Al-Montashiri N.A., Cheng B.L., Lou P., Ozmizrak P., Chen H.H.,
RA Stewart A.F.;
RT "Identification of a phosphorylation-dependent nuclear localization motif
RT in interferon regulatory factor 2 binding protein 2.";
RL PLoS ONE 6:E24100-E24100(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457 AND SER-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-455; SER-457 AND
RP SER-460, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-175 AND SER-318, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-326 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-289; LYS-303; LYS-324; LYS-326
RP AND LYS-348, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP INVOLVEMENT IN CVID14, VARIANT CVID14 ASN-551, CHARACTERIZATION OF VARIANT
RP CVID14 ASN-551, AND FUNCTION.
RX PubMed=27016798; DOI=10.1016/j.jaci.2016.01.018;
RA Keller M.D., Pandey R., Li D., Glessner J., Tian L., Henrickson S.E.,
RA Chinn I.K., Monaco-Shawver L., Heimall J., Hou C., Otieno F.G.,
RA Jyonouchi S., Calabrese L., van Montfrans J., Orange J.S., Hakonarson H.;
RT "Mutation in IRF2BP2 is responsible for a familial form of common variable
RT immunodeficiency disorder.";
RL J. Allergy Clin. Immunol. 138:544-550(2016).
CC -!- FUNCTION: Acts as a transcriptional corepressor in a IRF2-dependent
CC manner; this repression is not mediated by histone deacetylase
CC activities (PubMed:12799427). Represses the NFAT1-dependent
CC transactivation of NFAT-responsive promoters (PubMed:21576369). Acts as
CC a coactivator of VEGFA expression in cardiac and skeletal muscles
CC (PubMed:20702774). Plays a role in immature B-cell differentiation
CC (PubMed:27016798). {ECO:0000269|PubMed:12799427,
CC ECO:0000269|PubMed:20702774, ECO:0000269|PubMed:21576369,
CC ECO:0000269|PubMed:27016798}.
CC -!- SUBUNIT: Interacts with IRF2. Part of a corepressor complex containing
CC IRF2 and IRF2BP1. Interacts with VGLL4. {ECO:0000269|PubMed:12799427,
CC ECO:0000269|PubMed:20702774}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=IRF-2BP2A;
CC IsoId=Q7Z5L9-1; Sequence=Displayed;
CC Name=2; Synonyms=IRF-2BP2B;
CC IsoId=Q7Z5L9-2; Sequence=VSP_032770;
CC Name=3;
CC IsoId=Q7Z5L9-3; Sequence=VSP_032769;
CC -!- DOMAIN: The C-terminal RING-type zinc finger domain is sufficient for
CC interaction with IRF2.
CC -!- PTM: Phosphorylation at Ser-360 is required for nuclear targeting.
CC {ECO:0000269|PubMed:21887377}.
CC -!- DISEASE: Immunodeficiency, common variable, 14 (CVID14) [MIM:617765]: A
CC primary immunodeficiency resulting in recurrent sinopulmonary
CC infections since early childhood, and characterized by
CC hypogammaglobulinemia with undetectable IgG and IgA, poor response to
CC vaccination, and decreased levels of switched memory B cells. CVID14
CC inheritance is autosomal dominant. {ECO:0000269|PubMed:27016798}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the IRF2BP family. {ECO:0000305}.
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DR EMBL; AY278023; AAP78944.1; -; mRNA.
DR EMBL; AY278024; AAP78945.1; -; mRNA.
DR EMBL; AL160408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020516; AAH20516.1; -; mRNA.
DR EMBL; BC065759; AAH65759.1; -; mRNA.
DR CCDS; CCDS1602.1; -. [Q7Z5L9-1]
DR CCDS; CCDS41475.1; -. [Q7Z5L9-2]
DR RefSeq; NP_001070865.1; NM_001077397.1. [Q7Z5L9-2]
DR RefSeq; NP_892017.2; NM_182972.2. [Q7Z5L9-1]
DR AlphaFoldDB; Q7Z5L9; -.
DR SMR; Q7Z5L9; -.
DR BioGRID; 131797; 93.
DR CORUM; Q7Z5L9; -.
DR IntAct; Q7Z5L9; 28.
DR MINT; Q7Z5L9; -.
DR STRING; 9606.ENSP00000355568; -.
DR GlyGen; Q7Z5L9; 12 sites, 2 O-linked glycans (12 sites).
DR iPTMnet; Q7Z5L9; -.
DR PhosphoSitePlus; Q7Z5L9; -.
DR BioMuta; IRF2BP2; -.
DR DMDM; 229462882; -.
DR EPD; Q7Z5L9; -.
DR jPOST; Q7Z5L9; -.
DR MassIVE; Q7Z5L9; -.
DR MaxQB; Q7Z5L9; -.
DR PaxDb; Q7Z5L9; -.
DR PeptideAtlas; Q7Z5L9; -.
DR PRIDE; Q7Z5L9; -.
DR ProteomicsDB; 69325; -. [Q7Z5L9-1]
DR ProteomicsDB; 69326; -. [Q7Z5L9-2]
DR ProteomicsDB; 69327; -. [Q7Z5L9-3]
DR TopDownProteomics; Q7Z5L9-2; -. [Q7Z5L9-2]
DR TopDownProteomics; Q7Z5L9-3; -. [Q7Z5L9-3]
DR Antibodypedia; 34693; 218 antibodies from 29 providers.
DR DNASU; 359948; -.
DR Ensembl; ENST00000366609.4; ENSP00000355568.3; ENSG00000168264.11. [Q7Z5L9-1]
DR Ensembl; ENST00000366610.7; ENSP00000355569.3; ENSG00000168264.11. [Q7Z5L9-2]
DR GeneID; 359948; -.
DR KEGG; hsa:359948; -.
DR MANE-Select; ENST00000366609.4; ENSP00000355568.3; NM_182972.3; NP_892017.2.
DR UCSC; uc001hwf.3; human. [Q7Z5L9-1]
DR CTD; 359948; -.
DR DisGeNET; 359948; -.
DR GeneCards; IRF2BP2; -.
DR HGNC; HGNC:21729; IRF2BP2.
DR HPA; ENSG00000168264; Low tissue specificity.
DR MalaCards; IRF2BP2; -.
DR MIM; 615332; gene.
DR MIM; 617765; phenotype.
DR neXtProt; NX_Q7Z5L9; -.
DR OpenTargets; ENSG00000168264; -.
DR Orphanet; 520; Acute promyelocytic leukemia.
DR Orphanet; 1572; Common variable immunodeficiency.
DR PharmGKB; PA134947294; -.
DR VEuPathDB; HostDB:ENSG00000168264; -.
DR eggNOG; KOG3579; Eukaryota.
DR GeneTree; ENSGT00940000160591; -.
DR HOGENOM; CLU_019307_2_0_1; -.
DR InParanoid; Q7Z5L9; -.
DR OMA; KAEHMSP; -.
DR OrthoDB; 1156771at2759; -.
DR PhylomeDB; Q7Z5L9; -.
DR TreeFam; TF317075; -.
DR PathwayCommons; Q7Z5L9; -.
DR SignaLink; Q7Z5L9; -.
DR SIGNOR; Q7Z5L9; -.
DR BioGRID-ORCS; 359948; 85 hits in 1081 CRISPR screens.
DR ChiTaRS; IRF2BP2; human.
DR GenomeRNAi; 359948; -.
DR Pharos; Q7Z5L9; Tbio.
DR PRO; PR:Q7Z5L9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z5L9; protein.
DR Bgee; ENSG00000168264; Expressed in epithelium of mammary gland and 194 other tissues.
DR Genevisible; Q7Z5L9; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0002327; P:immature B cell differentiation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.1580; -; 1.
DR InterPro; IPR044882; I2BP1/2_C3HC4-RING_sf.
DR InterPro; IPR022750; Interferon_reg_fac2-bd1_2_Znf.
DR Pfam; PF11261; IRF-2BP1_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cytoplasm; Disease variant;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..587
FT /note="Interferon regulatory factor 2-binding protein 2"
FT /id="PRO_0000328734"
FT ZN_FING 506..553
FT /note="RING-type; degenerate"
FT REGION 126..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..550
FT /note="Cys-rich"
FT MOTIF 354..361
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:21887377"
FT COMPBIAS 376..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..409
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q1P8"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21887377,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q1P8"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q1P8"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 289
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 348
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..424
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032769"
FT VAR_SEQ 333..348
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12799427"
FT /id="VSP_032770"
FT VARIANT 254
FT /note="A -> V (in dbSNP:rs11502)"
FT /id="VAR_042503"
FT VARIANT 551
FT /note="S -> N (in CVID14; increased protein abundance in
FT patient-derived B lymphocytes; impairs immature B cell
FT differentiation; dbSNP:rs1553319504)"
FT /evidence="ECO:0000269|PubMed:27016798"
FT /id="VAR_080578"
FT CONFLICT 177
FT /note="N -> K (in Ref. 1; AAP78944/AAP78945)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="A -> T (in Ref. 1; AAP78944/AAP78945)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="A -> T (in Ref. 1; AAP78944/AAP78945)"
FT /evidence="ECO:0000305"
FT CROSSLNK Q7Z5L9-2:326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297"
SQ SEQUENCE 587 AA; 61025 MW; 2B36B7EE2C3B96A6 CRC64;
MAAAVAVAAA SRRQSCYLCD LPRMPWAMIW DFTEPVCRGC VNYEGADRVE FVIETARQLK
RAHGCFPEGR SPPGAAASAA AKPPPLSAKD ILLQQQQQLG HGGPEAAPRA PQALERYPLA
AAAERPPRLG SDFGSSRPAA SLAQPPTPQP PPVNGILVPN GFSKLEEPPE LNRQSPNPRR
GHAVPPTLVP LMNGSATPLP TALGLGGRAA ASLAAVSGTA AASLGSAQPT DLGAHKRPAS
VSSSAAVEHE QREAAAKEKQ PPPPAHRGPA DSLSTAAGAA ELSAEGAGKS RGSGEQDWVN
RPKTVRDTLL ALHQHGHSGP FESKFKKEPA LTAGRLLGFE ANGANGSKAV ARTARKRKPS
PEPEGEVGPP KINGEAQPWL STSTEGLKIP MTPTSSFVSP PPPTASPHSN RTTPPEAAQN
GQSPMAALIL VADNAGGSHA SKDANQVHST TRRNSNSPPS PSSMNQRRLG PREVGGQGAG
NTGGLEPVHP ASLPDSSLAT SAPLCCTLCH ERLEDTHFVQ CPSVPSHKFC FPCSRQSIKQ
QGASGEVYCP SGEKCPLVGS NVPWAFMQGE IATILAGDVK VKKERDS
