ID ARI3A_MOUSE Reviewed; 601 AA. AC Q62431; Q3U338; Q80YP8; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 22-FEB-2023, entry version 162. DE RecName: Full=AT-rich interactive domain-containing protein 3A; DE Short=ARID domain-containing protein 3A; DE AltName: Full=B-cell regulator of IgH transcription; DE Short=Bright; DE AltName: Full=Dead ringer-like protein 1; GN Name=Arid3a; Synonyms=Dri1, Dril1; 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], AND FUNCTION. RX PubMed=8543152; DOI=10.1101/gad.9.24.3067; RA Herrscher R.F., Kaplan M.H., Lelsz D.L., Das C., Scheuermann R., RA Tucker P.W.; RT "The immunoglobulin heavy-chain matrix-associating regions are bound by RT Bright: a B cell-specific trans-activator that describes a new DNA-binding RT protein family."; RL Genes Dev. 9:3067-3082(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; 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 [3] 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 [4] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=9590220; RA Webb C.F., Smith E.A., Medina K.L., Buchanan K.L., Smithson G., Dou S.; RT "Expression of bright at two distinct stages of B lymphocyte development."; RL J. Immunol. 160:4747-4754(1998). RN [5] RP INTERACTION WITH BTK. RX PubMed=11120822; DOI=10.4049/jimmunol.165.12.6956; RA Webb C.F., Yamashita Y., Ayers N., Evetts S., Paulin Y., Conley M.E., RA Smith E.A.; RT "The transcription factor Bright associates with Bruton's tyrosine kinase, RT the defective protein in immunodeficiency disease."; RL J. Immunol. 165:6956-6965(2000). RN [6] RP FUNCTION. RX PubMed=11294836; DOI=10.1074/jbc.m100836200; RA Kaplan M.H., Zong R.-T., Herrscher R.F., Scheuermann R.H., Tucker P.W.; RT "Transcriptional activation by a matrix associating region-binding protein. RT contextual requirements for the function of bright."; RL J. Biol. Chem. 276:21325-21330(2001). RN [7] RP DNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-268; RP TRP-299; PHE-317 AND TYR-330. RX PubMed=15456761; DOI=10.1074/jbc.m403028200; RA Nixon J.C., Rajaiya J., Webb C.F.; RT "Mutations in the DNA-binding domain of the transcription factor Bright act RT as dominant negative proteins and interfere with immunoglobulin RT transactivation."; RL J. Biol. Chem. 279:52465-52472(2004). RN [8] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-457; PRO-463; LYS-466; RP LYS-467; GLY-532; TYR-535; GLY-537 AND LEU-539. RX PubMed=16507996; DOI=10.1128/mcb.26.6.2187-2201.2006; RA Kim D., Tucker P.W.; RT "A regulated nucleocytoplasmic shuttle contributes to Bright's function as RT a transcriptional activator of immunoglobulin genes."; RL Mol. Cell. Biol. 26:2187-2201(2006). RN [9] RP INTERACTION WITH GTF2I AND BTK. RX PubMed=16738337; DOI=10.1128/mcb.02009-05; RA Rajaiya J., Nixon J.C., Ayers N., Desgranges Z.P., Roy A.L., Webb C.F.; RT "Induction of immunoglobulin heavy-chain transcription through the RT transcription factor Bright requires TFII-I."; RL Mol. Cell. Biol. 26:4758-4768(2006). RN [10] RP FUNCTION. RX PubMed=17312145; DOI=10.4049/jimmunol.178.5.2996; RA Shankar M., Nixon J.C., Maier S., Workman J., Farris A.D., Webb C.F.; RT "Anti-nuclear antibody production and autoimmunity in transgenic mice that RT overexpress the transcription factor Bright."; RL J. Immunol. 178:2996-3006(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-89; SER-127 AND RP SER-358, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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: Transcription factor involved in B-cell differentiation. CC Binds a VH promoter proximal site necessary for induced mu-heavy-chain CC transcription. Binds the minor groove of a restricted ATC sequence that CC is sufficient for nuclear matrix association. This sequence motif is CC present in matrix-associating regions (MARS) proximal to the promoter CC and flanking E mu. Activates E mu-driven transcription by binding these CC sites. May be involved in the control of cell cycle progression by the CC RB1/E2F1 pathway. {ECO:0000269|PubMed:11294836, CC ECO:0000269|PubMed:17312145, ECO:0000269|PubMed:8543152}. CC -!- SUBUNIT: Homodimer. Heterodimer with ARID3B. Interacts with E2F1 (By CC similarity). Interacts with GTF2I and BTK. {ECO:0000250, CC ECO:0000269|PubMed:11120822, ECO:0000269|PubMed:15456761, CC ECO:0000269|PubMed:16738337}. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between nucleus CC and cytoplasm. CC -!- TISSUE SPECIFICITY: B-cell specific in the adult. Expressed in B-cell CC progenitors, down-regulated in the immature B-cell stage, and is up- CC regulated again at later stages of B-lymphocyte differentiation. CC {ECO:0000269|PubMed:9590220}. CC -!- DEVELOPMENTAL STAGE: Expressed in lymphocytes from fetal liver. CC Expressed in fetal thymus and brain. {ECO:0000269|PubMed:9590220}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U60335; AAB03416.1; -; mRNA. DR EMBL; AK141283; BAE24635.1; -; mRNA. DR EMBL; AK154956; BAE32951.1; -; mRNA. DR EMBL; BC050925; AAH50925.1; -; mRNA. DR CCDS; CCDS23999.1; -. DR RefSeq; NP_001275554.1; NM_001288625.1. DR RefSeq; NP_001275555.1; NM_001288626.1. DR RefSeq; NP_031906.1; NM_007880.4. DR RefSeq; XP_006513264.1; XM_006513201.3. DR RefSeq; XP_006513265.1; XM_006513202.3. DR AlphaFoldDB; Q62431; -. DR SMR; Q62431; -. DR BioGRID; 199312; 3. DR STRING; 10090.ENSMUSP00000019708; -. DR iPTMnet; Q62431; -. DR PhosphoSitePlus; Q62431; -. DR EPD; Q62431; -. DR MaxQB; Q62431; -. DR PaxDb; Q62431; -. DR PeptideAtlas; Q62431; -. DR ProteomicsDB; 282018; -. DR Antibodypedia; 1435; 288 antibodies from 33 providers. DR DNASU; 13496; -. DR Ensembl; ENSMUST00000019708.12; ENSMUSP00000019708.6; ENSMUSG00000019564.13. DR Ensembl; ENSMUST00000105376.2; ENSMUSP00000101015.2; ENSMUSG00000019564.13. DR GeneID; 13496; -. DR KEGG; mmu:13496; -. DR UCSC; uc007gap.2; mouse. DR AGR; MGI:1328360; -. DR CTD; 1820; -. DR MGI; MGI:1328360; Arid3a. DR VEuPathDB; HostDB:ENSMUSG00000019564; -. DR eggNOG; KOG2744; Eukaryota. DR GeneTree; ENSGT00940000160899; -. DR HOGENOM; CLU_026952_3_0_1; -. DR InParanoid; Q62431; -. DR OMA; MKPKWEE; -. DR OrthoDB; 445024at2759; -. DR PhylomeDB; Q62431; -. DR TreeFam; TF320364; -. DR BioGRID-ORCS; 13496; 3 hits in 79 CRISPR screens. DR ChiTaRS; Arid3a; mouse. DR PRO; PR:Q62431; -. DR Proteomes; UP000000589; Chromosome 10. DR RNAct; Q62431; protein. DR Bgee; ENSMUSG00000019564; Expressed in granulocyte and 153 other tissues. DR ExpressionAtlas; Q62431; baseline and differential. DR Genevisible; Q62431; MM. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0045121; C:membrane raft; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:MGI. DR GO; GO:0003712; F:transcription coregulator activity; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd16878; ARID_ARID3A; 1. DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1. DR InterPro; IPR045147; ARI3A/B/C. DR InterPro; IPR001606; ARID_dom. DR InterPro; IPR036431; ARID_dom_sf. DR InterPro; IPR023334; REKLES_domain. DR PANTHER; PTHR15348:SF1; AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 3A; 1. DR PANTHER; PTHR15348; AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN ARID DOMAIN- CONTAINING PROTEIN DEAD RINGER PROTEIN B-CELL REGULATOR OF IGH TRANSCRIPTION BRIGHT; 1. DR Pfam; PF01388; ARID; 1. DR SMART; SM01014; ARID; 1. DR SMART; SM00501; BRIGHT; 1. DR SUPFAM; SSF46774; ARID-like; 1. DR PROSITE; PS51011; ARID; 1. DR PROSITE; PS51486; REKLES; 1. PE 1: Evidence at protein level; KW Activator; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..601 FT /note="AT-rich interactive domain-containing protein 3A" FT /id="PRO_0000200579" FT DOMAIN 243..335 FT /note="ARID" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355" FT DOMAIN 449..546 FT /note="REKLES" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00819" FT REGION 1..224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 128..165 FT /note="Acidic" FT REGION 450..493 FT /note="Important for nuclear localization" FT REGION 495..518 FT /note="Homodimerization" FT /evidence="ECO:0000250" FT REGION 542..562 FT /note="Important for cytoplasmic localization" FT REGION 545..601 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 40..55 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 113..140 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 141..168 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 556..601 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 78 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99856" FT MOD_RES 82 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 89 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 99 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q99856" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99856" FT MOD_RES 127 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 358 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 367 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99856" FT CROSSLNK 403 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q99856" FT CROSSLNK 404 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q99856" FT CROSSLNK 457 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q99856" FT CROSSLNK 467 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q99856" FT MUTAGEN 268 FT /note="P->A: Impairs DNA-binding." FT /evidence="ECO:0000269|PubMed:15456761" FT MUTAGEN 299 FT /note="W->A: Impairs DNA-binding." FT /evidence="ECO:0000269|PubMed:15456761" FT MUTAGEN 317 FT /note="F->A: Impairs DNA-binding." FT /evidence="ECO:0000269|PubMed:15456761" FT MUTAGEN 330 FT /note="Y->A: Impairs DNA-binding." FT /evidence="ECO:0000269|PubMed:15456761" FT MUTAGEN 457 FT /note="K->A: No effect on cellular location." FT /evidence="ECO:0000269|PubMed:16507996" FT MUTAGEN 463 FT /note="P->A: Abolishes nuclear localization." FT /evidence="ECO:0000269|PubMed:16507996" FT MUTAGEN 466 FT /note="K->A: Abolishes nuclear localization." FT /evidence="ECO:0000269|PubMed:16507996" FT MUTAGEN 467 FT /note="K->A: Abolishes nuclear localization." FT /evidence="ECO:0000269|PubMed:16507996" FT MUTAGEN 532 FT /note="G->A: Abolishes cytosolic localization." FT /evidence="ECO:0000269|PubMed:16507996" FT MUTAGEN 535 FT /note="Y->A: Abolishes cytosolic localization." FT /evidence="ECO:0000269|PubMed:16507996" FT MUTAGEN 535 FT /note="Y->F: No effect on cellular location." FT /evidence="ECO:0000269|PubMed:16507996" FT MUTAGEN 537 FT /note="G->A: Abolishes cytosolic localization." FT /evidence="ECO:0000269|PubMed:16507996" FT MUTAGEN 539 FT /note="L->A: Abolishes cytosolic localization." FT /evidence="ECO:0000269|PubMed:16507996" FT CONFLICT 405..406 FT /note="Missing (in Ref. 3; AAH50925)" FT /evidence="ECO:0000305" SQ SEQUENCE 601 AA; 64173 MW; 66994C01E1FB68CD CRC64; MKLQAVMETL IQRQQRARQE LEARQAPPPP PPEPTGVRAR TTMTDEDREP ENARMHRTQM AALAAMRAAA AGLGHPSSPG GSEDGPPISG DEDTAREGTL SSPALHGSVL EGAGHAEGDR HLMDVGSDDD DTKSKWEEQE LEELGEEEEE EEEEDDFEEE EEEEEGLGPP ESASLGTAGL FTRKAPPAQA FRGDGGPRML SGPERLGPGP AHPSHMASQM PPPDHGDWTF EEQFKQLYEL DADPKRKEFL DDLFSFMQKR GTPVNRIPIM AKQVLDLFML YVLVTEKGGL VEVINKKLWR EITKGLNLPT SITSAAFTLR TQYMKYLYPY ECERRGLSSP NELQAAIDSN RREGRRQSFG GSLFAYSPSG AHSMLPSPKL PVTPLGLAAS TNGSSITPAP KIKKEEDSAI PITVPGRLPV SLAGHPVVAA QAAAVQAAAA QAAVAAQAAA LEQLREKLES TEPPEKKMAL VADEQQRLMQ RAVQQSFLAM TAQLPMNIRI NSQASESRQD SAVSLTSANG SNSISMSVEM NGIVYTGVLF AQPPPPTAPS APGKGGVSSI GTNTTTGSRT GASGSTVSGG QVGLPGVSTP TMSSTSNNSL P //