ARI3B_MOUSE
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 03-AUG-2022, entry version 130.
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; Q9Z1N7; -.
DR PRIDE; Q9Z1N7; -.
DR Antibodypedia; 26965; 203 antibodies from 22 providers.
DR DNASU; 56380; -.
DR Ensembl; ENSMUST00000004780; ENSMUSP00000004780; ENSMUSG00000004661. [Q9Z1N7-1]
DR Ensembl; ENSMUST00000164035; ENSMUSP00000131677; ENSMUSG00000004661. [Q9Z1N7-3]
DR Ensembl; ENSMUST00000171444; ENSMUSP00000130173; ENSMUSG00000004661. [Q9Z1N7-1]
DR GeneID; 56380; -.
DR KEGG; mmu:56380; -.
DR UCSC; uc009pvt.2; mouse. [Q9Z1N7-1]
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; SMARQIP; -.
DR OrthoDB; 1347369at2759; -.
DR PhylomeDB; Q9Z1N7; -.
DR TreeFam; TF320364; -.
DR BioGRID-ORCS; 56380; 8 hits in 73 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 143 other tissues.
DR ExpressionAtlas; Q9Z1N7; baseline and differential.
DR Genevisible; Q9Z1N7; MM.
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 Gene3D; 1.10.150.60; -; 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; PTHR15348; 1.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51486; REKLES; 1.
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
