I2BP1_MOUSE
ID I2BP1_MOUSE Reviewed; 584 AA.
AC Q8R3Y8; Q8BJC9; Q8C0B1; Q8CI76;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Interferon regulatory factor 2-binding protein 1;
DE Short=IRF-2-binding protein 1;
DE Short=IRF-2BP1;
DE AltName: Full=Probable E3 ubiquitin-protein ligase IRF2BP1;
DE EC=2.3.2.27;
DE AltName: Full=Probable RING-type E3 ubiquitin transferase IRF2BP1 {ECO:0000305};
GN Name=Irf2bp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Eye, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384; SER-421; SER-436 AND
RP SER-453, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a transcriptional corepressor in a IRF2-dependent
CC manner; this repression is not mediated by histone deacetylase
CC activities. May act as an E3 ligase towards JDP2, enhancing its
CC polyubiquitination. Represses ATF2-dependent transcriptional
CC activation. {ECO:0000250|UniProtKB:Q8IU81}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- SUBUNIT: Interacts with IRF2. Part of a corepressor complex containing
CC IRF2 and IRF2BP2. Interacts with JDP2. {ECO:0000250|UniProtKB:Q8IU81}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IU81}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R3Y8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3Y8-2; Sequence=VSP_032768;
CC -!- SIMILARITY: Belongs to the IRF2BP family. {ECO:0000305}.
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DR EMBL; AK031834; BAC27572.1; -; mRNA.
DR EMBL; AK087457; BAC39883.1; -; mRNA.
DR EMBL; BC019164; AAH19164.2; -; mRNA.
DR EMBL; BC036162; AAH36162.1; -; mRNA.
DR CCDS; CCDS20885.1; -. [Q8R3Y8-1]
DR RefSeq; NP_848872.2; NM_178757.3. [Q8R3Y8-1]
DR AlphaFoldDB; Q8R3Y8; -.
DR SMR; Q8R3Y8; -.
DR BioGRID; 234867; 1.
DR IntAct; Q8R3Y8; 1.
DR STRING; 10090.ENSMUSP00000061234; -.
DR iPTMnet; Q8R3Y8; -.
DR PhosphoSitePlus; Q8R3Y8; -.
DR EPD; Q8R3Y8; -.
DR jPOST; Q8R3Y8; -.
DR MaxQB; Q8R3Y8; -.
DR PaxDb; Q8R3Y8; -.
DR PeptideAtlas; Q8R3Y8; -.
DR PRIDE; Q8R3Y8; -.
DR ProteomicsDB; 273082; -. [Q8R3Y8-1]
DR ProteomicsDB; 273083; -. [Q8R3Y8-2]
DR Antibodypedia; 31408; 235 antibodies from 31 providers.
DR DNASU; 272359; -.
DR Ensembl; ENSMUST00000053713; ENSMUSP00000061234; ENSMUSG00000044030. [Q8R3Y8-1]
DR GeneID; 272359; -.
DR KEGG; mmu:272359; -.
DR UCSC; uc009fkc.1; mouse. [Q8R3Y8-1]
DR CTD; 26145; -.
DR MGI; MGI:2442159; Irf2bp1.
DR VEuPathDB; HostDB:ENSMUSG00000044030; -.
DR eggNOG; KOG3579; Eukaryota.
DR GeneTree; ENSGT00940000162120; -.
DR HOGENOM; CLU_019307_2_0_1; -.
DR InParanoid; Q8R3Y8; -.
DR OMA; VEYPCGS; -.
DR OrthoDB; 1156771at2759; -.
DR PhylomeDB; Q8R3Y8; -.
DR TreeFam; TF317075; -.
DR BioGRID-ORCS; 272359; 6 hits in 72 CRISPR screens.
DR PRO; PR:Q8R3Y8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R3Y8; protein.
DR Bgee; ENSMUSG00000044030; Expressed in perirhinal cortex and 239 other tissues.
DR Genevisible; Q8R3Y8; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO: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 InterPro; IPR018957; Znf_C3HC4_RING-type.
DR Pfam; PF11261; IRF-2BP1_2; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Isopeptide bond; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..584
FT /note="Interferon regulatory factor 2-binding protein 1"
FT /id="PRO_0000328730"
FT ZN_FING 503..550
FT /note="RING-type; degenerate"
FT REGION 59..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..550
FT /note="Cys-rich"
FT COILED 197..217
FT /evidence="ECO:0000255"
FT COMPBIAS 78..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..373
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IU81"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IU81"
FT MOD_RES 177
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8IU81"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IU81"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IU81"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IU81"
FT CROSSLNK 227
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IU81"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IU81"
FT VAR_SEQ 1..20
FT /note="MASVQASRRQWCYLCDLPKM -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032768"
FT CONFLICT 54
FT /note="Q -> H (in Ref. 1; BAC39883)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="A -> P (in Ref. 1; BAC39883)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="S -> L (in Ref. 1; BAC39883)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="S -> T (in Ref. 1; BAC27572)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="R -> Q (in Ref. 1; BAC27572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 584 AA; 61751 MW; 0A0DF55E967B10BE CRC64;
MASVQASRRQ WCYLCDLPKM PWAMVWDFSE AVCRGCVNFE GADRIELLID AARQLKRSHV
LPEGRSPGPP ALKHPTSKDL ASTGSQGSQL PPPQAQAQPS GTGGSVSGPD RYDRATSSSR
LALPSPALEY TLGSRLANGL GREEAVAEGA RRALLGSIPS LMPPGLLAAA VSGLGGRALT
LAPGLSPARP LFGSDFEKEK QQRNADCLAE LNEAMRGRAE EWHGRPKAVR EQLLALSACA
PFNVRFKKDH GLVGRVFAFD ATARPPGYEF ELKLFTEYPC GSGNVYAGVL AVARQMFHDA
LREPGKALAS SGFKYLEYER RHGSGEWRQL GELLTDGVRS FREPAPAEAL PQQYPEPAPA
ALCGPPPRAP SRNLAPTPRR RKASPEPEGE TAGKMTTEEQ QQRHWVAPGG PYSSETPGVP
SPIAALKNVA EALGHSPKDP GGGGGSVRAG GASPAASSTT QPPAQHRLVA RNGEAEVSPT
AGAEAVSGGG SGTGATPGAP LCCTLCRERL EDTHFVQCPS VPGHKFCFPC SREFIKAQGP
AGEVYCPSGD KCPLVGSSVP WAFMQGEIAT ILAGDIKVKK ERDP
