ARI3B_HUMAN
ID ARI3B_HUMAN Reviewed; 561 AA.
AC Q8IVW6; O95443; Q59HC9; Q6P9C9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, DNA-BINDING, INTERACTION WITH RB1, AND MUTAGENESIS OF PRO-240 AND
RP TRP-271.
RC TISSUE=Testis;
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 TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16951138; DOI=10.1158/0008-5472.can-06-0756;
RA Kobayashi K., Era T., Takebe A., Jakt L.M., Nishikawa S.;
RT "ARID3B induces malignant transformation of mouse embryonic fibroblasts and
RT is strongly associated with malignant neuroblastoma.";
RL Cancer Res. 66:8331-8336(2006).
RN [6]
RP INTERACTION WITH ARID3A, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17400556; DOI=10.1074/jbc.m700397200;
RA Kim D., Probst L., Das C., Tucker P.W.;
RT "REKLES is an ARID3-restricted multifunctional domain.";
RL J. Biol. Chem. 282:15768-15777(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-165 AND SER-311, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Transcription factor which may be involved in neuroblastoma
CC growth and malignant transformation. Favors nuclear targeting of
CC ARID3A. {ECO:0000269|PubMed:16951138, ECO:0000269|PubMed:17400556}.
CC -!- SUBUNIT: Heterodimer with ARID3A. Interacts with unphosphorylated RB1.
CC {ECO:0000269|PubMed:10446990, ECO:0000269|PubMed:17400556}.
CC -!- INTERACTION:
CC Q8IVW6; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-5458329, EBI-717399;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000269|PubMed:10446990, ECO:0000269|PubMed:17400556}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IVW6-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q8IVW6-3; Sequence=VSP_026773, VSP_026774;
CC Name=4;
CC IsoId=Q8IVW6-4; Sequence=VSP_039860;
CC -!- TISSUE SPECIFICITY: Expressed in placenta, testis and leukocytes.
CC Expressed in neuroblastoma. Present in K-562 erythrocytic leukemia cell
CC line (at protein level). {ECO:0000269|PubMed:10446990,
CC ECO:0000269|PubMed:16951138}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92067.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF116846; AAD09133.1; -; mRNA.
DR EMBL; AB208830; BAD92067.1; ALT_INIT; mRNA.
DR EMBL; AC100835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041792; AAH41792.1; -; mRNA.
DR CCDS; CCDS10264.1; -. [Q8IVW6-4]
DR CCDS; CCDS76777.1; -. [Q8IVW6-1]
DR RefSeq; NP_001294868.1; NM_001307939.1. [Q8IVW6-1]
DR RefSeq; NP_006456.1; NM_006465.3. [Q8IVW6-4]
DR AlphaFoldDB; Q8IVW6; -.
DR SMR; Q8IVW6; -.
DR BioGRID; 115865; 90.
DR IntAct; Q8IVW6; 47.
DR MINT; Q8IVW6; -.
DR STRING; 9606.ENSP00000343126; -.
DR GlyGen; Q8IVW6; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q8IVW6; -.
DR PhosphoSitePlus; Q8IVW6; -.
DR BioMuta; ARID3B; -.
DR DMDM; 152013359; -.
DR EPD; Q8IVW6; -.
DR jPOST; Q8IVW6; -.
DR MassIVE; Q8IVW6; -.
DR MaxQB; Q8IVW6; -.
DR PaxDb; Q8IVW6; -.
DR PeptideAtlas; Q8IVW6; -.
DR PRIDE; Q8IVW6; -.
DR ProteomicsDB; 70785; -. [Q8IVW6-1]
DR ProteomicsDB; 70786; -. [Q8IVW6-3]
DR ProteomicsDB; 70787; -. [Q8IVW6-4]
DR Antibodypedia; 26965; 203 antibodies from 22 providers.
DR DNASU; 10620; -.
DR Ensembl; ENST00000346246.10; ENSP00000343126.5; ENSG00000179361.18. [Q8IVW6-4]
DR Ensembl; ENST00000622429.1; ENSP00000477878.1; ENSG00000179361.18. [Q8IVW6-1]
DR GeneID; 10620; -.
DR KEGG; hsa:10620; -.
DR MANE-Select; ENST00000346246.10; ENSP00000343126.5; NM_006465.4; NP_006456.1. [Q8IVW6-4]
DR UCSC; uc002ayd.4; human. [Q8IVW6-1]
DR CTD; 10620; -.
DR DisGeNET; 10620; -.
DR GeneCards; ARID3B; -.
DR HGNC; HGNC:14350; ARID3B.
DR HPA; ENSG00000179361; Tissue enhanced (bone).
DR MIM; 612457; gene.
DR neXtProt; NX_Q8IVW6; -.
DR OpenTargets; ENSG00000179361; -.
DR PharmGKB; PA134896829; -.
DR VEuPathDB; HostDB:ENSG00000179361; -.
DR eggNOG; KOG2744; Eukaryota.
DR GeneTree; ENSGT00940000156052; -.
DR HOGENOM; CLU_026952_2_0_1; -.
DR InParanoid; Q8IVW6; -.
DR OMA; SMARQIP; -.
DR OrthoDB; 1347369at2759; -.
DR PhylomeDB; Q8IVW6; -.
DR TreeFam; TF320364; -.
DR PathwayCommons; Q8IVW6; -.
DR SignaLink; Q8IVW6; -.
DR BioGRID-ORCS; 10620; 23 hits in 1064 CRISPR screens.
DR GeneWiki; ARID3B; -.
DR GenomeRNAi; 10620; -.
DR Pharos; Q8IVW6; Tbio.
DR PRO; PR:Q8IVW6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8IVW6; protein.
DR Bgee; ENSG00000179361; Expressed in oocyte and 161 other tissues.
DR ExpressionAtlas; Q8IVW6; baseline and differential.
DR Genevisible; Q8IVW6; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IEA:Ensembl.
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; DNA-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor.
FT CHAIN 1..561
FT /note="AT-rich interactive domain-containing protein 3B"
FT /id="PRO_0000295162"
FT DOMAIN 215..307
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 419..517
FT /note="REKLES"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00819"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..365
FT /note="Interaction with RB1"
FT /evidence="ECO:0000269|PubMed:10446990"
FT REGION 370..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..513
FT /note="Interaction with ARID3A"
FT /evidence="ECO:0000269|PubMed:17400556"
FT REGION 523..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N7"
FT VAR_SEQ 390..471
FT /note="DGAPVTTVPVPNRLAVPVTLASQQAGTRTAALEQLRERLESGEPAEKKASRL
FT SEEEQRLVQQAFQRNFFSMARQLPMKIRIN -> QQGSWGRRKKGRKGCQFPVFKTGVL
FT GQEGQLWIGPAPVPLQVMEPQ (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026773"
FT VAR_SEQ 472..561
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026774"
FT VAR_SEQ 474
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10446990"
FT /id="VSP_039860"
FT MUTAGEN 240
FT /note="P->H: Impairs binding to RB1."
FT /evidence="ECO:0000269|PubMed:10446990"
FT MUTAGEN 271
FT /note="W->S: Impairs binding to RB1."
FT /evidence="ECO:0000269|PubMed:10446990"
FT CONFLICT 7
FT /note="Q -> QQ (in Ref. 4; AAH41792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 60637 MW; 5F0CFF83BAFC12D2 CRC64;
MEPLQQQQQQ QQQQQKQPHL APLQMDAREK QGQQMREAQF LYAQKLVTQP TLLSATAGRP
SGSTPLGPLA RVPPTAAVAQ VFERGNMNSE PEEEDGGLED EDGDDEVAEV AEKETQAASK
YFHVQKVARQ DPRVAPMSNL LPAPGLPPHG QQAKEDHTKD ASKASPSVST AGQPNWNLDE
QLKQNGGLAW SDDADGGRGR EISRDFAKLY ELDGDPERKE FLDDLFVFMQ KRGTPINRIP
IMAKQILDLY MLYKLVTEKG GLVEIINKKI WREITKGLNL PTSITSAAFT LRTQYMKYLY
AYECEKKALS SPAELQAAID GNRREGRRPS YSSSLFGYSP AAATAAAAAG APALLSPPKI
RFPILGLGSS SGTNTSSPRI SPATTLRKGD GAPVTTVPVP NRLAVPVTLA SQQAGTRTAA
LEQLRERLES GEPAEKKASR LSEEEQRLVQ QAFQRNFFSM ARQLPMKIRI NGRAEDRAEA
SAAALNLTTS SIGSINMSVD IDGTTYAGVL FAQKPVVHLI TGSAPQSLGS SASSSSSSHC
SPSPTSSRGT PSAEPSTSWS L
