ID   ARI3B_MOUSE             Reviewed;         568 AA.
AC   Q9Z1N7; Q3UTG1; Q810L9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 137.
DE   RecName: Full=AT-rich interactive domain-containing protein 3B;
DE            Short=ARID domain-containing protein 3B;
DE   AltName: Full=Bright and dead ringer protein;
DE   AltName: Full=Bright-like protein;
GN   Name=Arid3b; Synonyms=Bdp, Dril2;
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] (ISOFORM 1).
RX   PubMed=10446990;
RA   Numata S., Claudio P.P., Dean C., Giordano A., Croce C.M.;
RT   "Bdp, a new member of a family of DNA-binding proteins, associates with the
RT   retinoblastoma gene product.";
RL   Cancer Res. 59:3741-3747(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
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] (ISOFORM 2).
RC   TISSUE=Embryo;
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   DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP   FUNCTION.
RX   PubMed=16530748; DOI=10.1016/j.ydbio.2005.12.016;
RA   Takebe A., Era T., Okada M., Martin Jakt L., Kuroda Y., Nishikawa S.;
RT   "Microarray analysis of PDGFR alpha+ populations in ES cell differentiation
RT   culture identifies genes involved in differentiation of mesoderm and
RT   mesenchyme including ARID3b that is essential for development of embryonic
RT   mesenchymal cells.";
RL   Dev. Biol. 293:25-37(2006).
RN   [5]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-370, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Transcription factor involved in the production of cranial
CC       mesenchymal tissues. Favors nuclear targeting of ARID3A.
CC       {ECO:0000269|PubMed:16530748}.
CC   -!- SUBUNIT: Heterodimer with ARID3A. Interacts with unphosphorylated RB1
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Z1N7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z1N7-2; Sequence=VSP_026776, VSP_026777;
CC       Name=3;
CC         IsoId=Q9Z1N7-3; Sequence=VSP_026775, VSP_026778;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in testis. Also expressed
CC       in prostate, thyroid and thymus. {ECO:0000269|PubMed:16530748}.
CC   -!- DEVELOPMENTAL STAGE: First detected at 7 dpc. Strongly expressed in
CC       cranial mesenchyme and caudal mesoderm. Expression in cranial
CC       mesenchyme decreases starting from 10.5 dpc.
CC       {ECO:0000269|PubMed:16530748}.
CC   -!- DISRUPTION PHENOTYPE: Embryos die before 11.5 dpc and display various
CC       abnormalities, including wavy neural tube, small branchial arches and
CC       defects of cardiovascular system. {ECO:0000269|PubMed:16530748}.
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DR   EMBL; AF116847; AAD09134.1; -; mRNA.
DR   EMBL; AK139455; BAE24019.1; -; mRNA.
DR   EMBL; BC049776; AAH49776.1; -; mRNA.
DR   CCDS; CCDS23233.1; -. [Q9Z1N7-1]
DR   RefSeq; NP_062663.1; NM_019689.2. [Q9Z1N7-1]
DR   RefSeq; XP_006511354.1; XM_006511291.3.
DR   AlphaFoldDB; Q9Z1N7; -.
DR   SMR; Q9Z1N7; -.
DR   BioGRID; 207941; 3.
DR   IntAct; Q9Z1N7; 1.
DR   STRING; 10090.ENSMUSP00000130173; -.
DR   iPTMnet; Q9Z1N7; -.
DR   PhosphoSitePlus; Q9Z1N7; -.
DR   EPD; Q9Z1N7; -.
DR   MaxQB; Q9Z1N7; -.
DR   PaxDb; 10090-ENSMUSP00000130173; -.
DR   ProteomicsDB; 277286; -. [Q9Z1N7-1]
DR   ProteomicsDB; 277287; -. [Q9Z1N7-2]
DR   ProteomicsDB; 277288; -. [Q9Z1N7-3]
DR   Antibodypedia; 26965; 228 antibodies from 23 providers.
DR   DNASU; 56380; -.
DR   Ensembl; ENSMUST00000004780.16; ENSMUSP00000004780.10; ENSMUSG00000004661.16. [Q9Z1N7-1]
DR   Ensembl; ENSMUST00000164035.8; ENSMUSP00000131677.2; ENSMUSG00000004661.16. [Q9Z1N7-3]
DR   Ensembl; ENSMUST00000171444.8; ENSMUSP00000130173.2; ENSMUSG00000004661.16. [Q9Z1N7-1]
DR   GeneID; 56380; -.
DR   KEGG; mmu:56380; -.
DR   UCSC; uc009pvt.2; mouse. [Q9Z1N7-1]
DR   AGR; MGI:1930768; -.
DR   CTD; 10620; -.
DR   MGI; MGI:1930768; Arid3b.
DR   VEuPathDB; HostDB:ENSMUSG00000004661; -.
DR   eggNOG; KOG2744; Eukaryota.
DR   GeneTree; ENSGT00940000156052; -.
DR   HOGENOM; CLU_026952_2_0_1; -.
DR   InParanoid; Q9Z1N7; -.
DR   OMA; PMKVKIN; -.
DR   OrthoDB; 445024at2759; -.
DR   PhylomeDB; Q9Z1N7; -.
DR   TreeFam; TF320364; -.
DR   BioGRID-ORCS; 56380; 8 hits in 79 CRISPR screens.
DR   ChiTaRS; Arid3b; mouse.
DR   PRO; PR:Q9Z1N7; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9Z1N7; Protein.
DR   Bgee; ENSMUSG00000004661; Expressed in embryonic post-anal tail and 146 other cell types or tissues.
DR   ExpressionAtlas; Q9Z1N7; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd16879; ARID_ARID3B; 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:SF3; AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 3B; 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.
DR   Genevisible; Q9Z1N7; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Developmental protein; DNA-binding;
KW   Methylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..568
FT                   /note="AT-rich interactive domain-containing protein 3B"
FT                   /id="PRO_0000295163"
FT   DOMAIN          213..305
FT                   /note="ARID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT   DOMAIN          425..522
FT                   /note="REKLES"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00819"
FT   REGION          1..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..374
FT                   /note="Interaction with RB1"
FT                   /evidence="ECO:0000250"
FT   REGION          378..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..518
FT                   /note="Interaction with ARID3A"
FT                   /evidence="ECO:0000250"
FT   REGION          529..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..107
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IVW6"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IVW6"
FT   MOD_RES         309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IVW6"
FT   MOD_RES         370
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   VAR_SEQ         232..287
FT                   /note="TPINRIPIMAKQILDLYMLYKLVTEKGGLVEIINKKIWREITKGLNLPTSIT
FT                   SAAF -> DPAAAAECTAFLLPSLIVIKYPGTTQLSTIMQKGVWHPNQPDSHHGQADPG
FT                   PVHAV (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026775"
FT   VAR_SEQ         234..282
FT                   /note="INRIPIMAKQILDLYMLYKLVTEKGGLVEIINKKIWREITKGLNLPTSI ->
FT                   SGASPAGIVLKATWPCGWPGQPPPLLCLVCILTRKKKKNVIAHGSLGRD (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026776"
FT   VAR_SEQ         283..568
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026777"
FT   VAR_SEQ         288..568
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026778"
FT   CONFLICT        99
FT                   /note="E -> G (in Ref. 2; BAE24019)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   568 AA;  61015 MW;  70250959E6EAF526 CRC64;
     MEPLQQQQQQ QQQKQPQQPL LQMDAREKQG PQTRESQFLY ASKLGTQPAL LSITPGRPSG
     SSVLGPLARV PPATPVARMS EQSNVNSEPE EEEGGLEDED GDDDVAEVAE KEAQAASKYF
     HMQKVTRQEP RATPMSSLLP VPGLSPQGQQ TKEDHTKDAS KAPPSVPTAG QPSWSLDEQL
     KQNGALAWSD DADGGRGREI SRDFAKLYEL DGDPERKEFL DDLFIFMQKR GTPINRIPIM
     AKQILDLYML YKLVTEKGGL VEIINKKIWR EITKGLNLPT SITSAAFTLR TQYMKYLYAY
     ECEKKALSSP AELQAAIDGN RREGRRPSYS SSLFGYSPAA AAAAAAAAAA AAASAASAGT
     PALLSSPKIR FSILGLGSSS GTSASSPRIP PASTLRKGDG VPVPVPNRLA VSGTLAGQQA
     GNRPGPLEHL RERLESGEPP EKKASRLSEE EQRLVQQAFQ RNLFSMARQL PMKIRINGRE
     DRAEPSAPAL NLTTSNIGSI NMSVDIDGTT YTGVLFAQKP VVHLIAGSTP QSIGSSASSS
     NSSSSHCSPS PTSSRGTPSA EPSTSWSL
//