I2BPL_MOUSE
ID I2BPL_MOUSE Reviewed; 775 AA.
AC Q8K3X4; Q3TBU9; Q3U483; Q3USE5; Q69Z84; Q8BUS1; Q8C011;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable E3 ubiquitin-protein ligase IRF2BPL {ECO:0000250|UniProtKB:Q9H1B7};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9H1B7};
DE AltName: Full=Enhanced at puberty protein 1;
DE AltName: Full=Interferon regulatory factor 2-binding protein-like;
GN Name=Irf2bpl; Synonyms=Eap1, Kiaa1865;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Heart;
RA Chen X.G., Li Y.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Eye, Medulla oblongata, and Olfactory bulb;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636; SER-638 AND SER-641, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-526; SER-636;
RP SER-638 AND SER-641, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Probable E3 ubiquitin protein ligase involved in the
CC proteasome-mediated ubiquitin-dependent degradation of target proteins.
CC Through the degradation of CTNNB1, functions downstream of FOXF2 to
CC negatively regulate the Wnt signaling pathway. Probably plays a role in
CC the development of the central nervous system and in neuronal
CC maintenance (By similarity). Also acts as a transcriptional regulator
CC of genes controlling female reproductive function. May play a role in
CC gene transcription by transactivating GNRH1 promoter and repressing
CC PENK promoter (By similarity). {ECO:0000250|UniProtKB:Q5EIC4,
CC ECO:0000250|UniProtKB:Q9H1B7}.
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; Evidence={ECO:0000250|UniProtKB:Q9H1B7};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9H1B7}.
CC -!- SUBUNIT: Interacts with CTNNB1. {ECO:0000250|UniProtKB:Q9H1B7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q2MJS2,
CC ECO:0000250|UniProtKB:Q5EIC4}.
CC -!- SIMILARITY: Belongs to the IRF2BP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32560.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF525300; AAM82165.1; -; mRNA.
DR EMBL; AK173282; BAD32560.1; ALT_INIT; mRNA.
DR EMBL; AK032366; BAC27837.1; -; mRNA.
DR EMBL; AK032622; BAC27955.1; -; mRNA.
DR EMBL; AK082791; BAC38621.1; -; mRNA.
DR EMBL; AK140441; BAE24388.1; -; mRNA.
DR EMBL; AK154383; BAE32550.1; -; mRNA.
DR EMBL; AK155373; BAE33226.1; -; mRNA.
DR EMBL; AK171043; BAE42208.1; -; mRNA.
DR EMBL; BC057128; AAH57128.1; -; mRNA.
DR EMBL; BC063253; AAH63253.1; -; mRNA.
DR CCDS; CCDS26068.1; -.
DR RefSeq; NP_665835.1; NM_145836.2.
DR AlphaFoldDB; Q8K3X4; -.
DR SMR; Q8K3X4; -.
DR BioGRID; 231970; 8.
DR STRING; 10090.ENSMUSP00000041070; -.
DR iPTMnet; Q8K3X4; -.
DR PhosphoSitePlus; Q8K3X4; -.
DR EPD; Q8K3X4; -.
DR jPOST; Q8K3X4; -.
DR MaxQB; Q8K3X4; -.
DR PaxDb; Q8K3X4; -.
DR PeptideAtlas; Q8K3X4; -.
DR PRIDE; Q8K3X4; -.
DR ProteomicsDB; 267034; -.
DR Antibodypedia; 54435; 16 antibodies from 8 providers.
DR DNASU; 238330; -.
DR Ensembl; ENSMUST00000038422; ENSMUSP00000041070; ENSMUSG00000034168.
DR GeneID; 238330; -.
DR KEGG; mmu:238330; -.
DR UCSC; uc007oia.2; mouse.
DR CTD; 64207; -.
DR MGI; MGI:2442463; Irf2bpl.
DR VEuPathDB; HostDB:ENSMUSG00000034168; -.
DR eggNOG; KOG3579; Eukaryota.
DR GeneTree; ENSGT00940000162596; -.
DR HOGENOM; CLU_019307_1_0_1; -.
DR InParanoid; Q8K3X4; -.
DR OMA; WASKPKM; -.
DR OrthoDB; 1156771at2759; -.
DR PhylomeDB; Q8K3X4; -.
DR TreeFam; TF317075; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 238330; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Irf2bpl; mouse.
DR PRO; PR:Q8K3X4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8K3X4; protein.
DR Bgee; ENSMUSG00000034168; Expressed in dorsal pancreas and 221 other tissues.
DR Genevisible; Q8K3X4; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:ParkinsonsUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0046543; P:development of secondary female sexual characteristics; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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 Pfam; PF11261; IRF-2BP1_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..775
FT /note="Probable E3 ubiquitin-protein ligase IRF2BPL"
FT /id="PRO_0000056412"
FT ZN_FING 694..741
FT /note="RING-type; degenerate"
FT REGION 93..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 83..113
FT /evidence="ECO:0000255"
FT COILED 314..350
FT /evidence="ECO:0000255"
FT COMPBIAS 191..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..276
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..587
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT CONFLICT 226
FT /note="G -> E (in Ref. 3; BAC38621)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="G -> E (in Ref. 3; BAE32550)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="A -> P (in Ref. 3; BAC27955)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="E -> G (in Ref. 3; BAC27955)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="P -> S (in Ref. 3; BAE33226/BAE42208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 80565 MW; ECB11652F2F7C2AB CRC64;
MSAAQVSSSR RQSCYLCDLP RMPWAMIWDF SEPVCRGCVN YEGADRIEFV IETARQLKRA
HGCFQDGRSP GPPPPVGVKT VALSAKEAAA AAAAAQQQQQ QQQQQQQQLN HVDGSTKPAV
LAAPSGLERY GLSAAAAAAA AAAAVEQRSR FEYPPPPVSL GSSSHAARLP NGLGGPNGFP
KPAPEEGPPE LNRQSPNSSS AATSVASRRG THSGLVTGLP NPGGGGGPQL TVPPNLLPQT
LLNGPASAAV LPPPHGLGGS RGPPTPAPPG APGGPACLGG PPGVSATVSS APSSTSSTVA
EVGVGAAGKR PGSVSSTDQE RELKEKQRNA EALAELSESL RNRAEEWANK PKMVRDTLLT
LAGCTPYEVR FKKDHSLLGR VFAFDAVSKP GMDYELKLFI EYPTGSGNVY SSASGVAKQM
YQDCMKDFGR GLSSGFKYLE YEKKHGSGDW RLLGDLLPEA VRFFKEGVPG ADMLPQPYLD
ASCPMLPTAL VSLSRAPSAP PGTGALPPAA PTGRGAASSL RKRKASPEPP DSAESALKLG
EEQQRQQWMA NQSEALKLTM SAGGFAAPGH SAGGPPPPPP PLGPHSNRTT PPESAPQNGP
SPMAALMSVA DTLGTAHSPK DGSSVHSTTA SARRNSSSPV SPASVPGQRR LASRNGDLNL
QVAPPPPSAH PGMDQVHPQN IPDSPMANSG PLCCTICHER LEDTHFVQCP SVPSHKFCFP
CSRESIKAQG ATGEVYCPSG EKCPLVGSNV PWAFMQGEIA TILAGDVKVK KERDP
