ARI5B_BOVIN
ID ARI5B_BOVIN Reviewed; 1173 AA.
AC E1BLP6;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=AT-rich interactive domain-containing protein 5B;
DE Short=ARID domain-containing protein 5B;
GN Name=ARID5B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
CC -!- FUNCTION: Transcription coactivator that binds to the 5'-AATA[CT]-3'
CC core sequence and plays a key role in adipogenesis and liver
CC development. Acts by forming a complex with phosphorylated PHF2, which
CC mediates demethylation at Lys-340, leading to target the PHF2-ARID5B
CC complex to target promoters, where PHF2 mediates demethylation of
CC dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription
CC activation of target genes. The PHF2-ARID5B complex acts as a
CC coactivator of HNF4A in liver. Required for adipogenesis: regulates
CC triglyceride metabolism in adipocytes by regulating expression of
CC adipogenic genes. Overexpression leads to induction of smooth muscle
CC marker genes, suggesting that it may also act as a regulator of smooth
CC muscle cell differentiation and proliferation (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}.
CC -!- DOMAIN: The ARID domain mediates the interaction with DNA.
CC {ECO:0000250}.
CC -!- PTM: Methylation at Lys-340 prevents DNA-binding. Demethylation by PHF2
CC promotes recruitment of the PHF2-ARID5B complex to promoters (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ARID5B family. {ECO:0000305}.
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DR EMBL; AAFC03084653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03084656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03084657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03093203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03093204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03093205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03093206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03093207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03122947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BLP6; -.
DR BMRB; E1BLP6; -.
DR SMR; E1BLP6; -.
DR STRING; 9913.ENSBTAP00000008847; -.
DR iPTMnet; E1BLP6; -.
DR PaxDb; E1BLP6; -.
DR PRIDE; E1BLP6; -.
DR eggNOG; KOG2744; Eukaryota.
DR InParanoid; E1BLP6; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0060612; P:adipose tissue development; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR030408; ARID5B.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR PANTHER; PTHR13964:SF37; PTHR13964:SF37; 1.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1173
FT /note="AT-rich interactive domain-containing protein 5B"
FT /id="PRO_0000410899"
FT DOMAIN 322..414
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 249..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..801
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT MOD_RES 340
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT MOD_RES 1118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 499
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 763
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 769
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 878
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 901
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 905
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 920
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 973
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 985
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 998
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 1040
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 1055
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
SQ SEQUENCE 1173 AA; 130464 MW; C766AE6A2EDA23F9 CRC64;
MEPNSLQWVG SPCGLHGPYI FYKAFQFHLE GKPRILSLGD FFFVRCTPKD PICIAELQLL
WEERTSRQLL SSSKLYFLPE DTPQGRNSDH GEDEVIAVSE KVIVKLEDLV KWVHSDFSKW
RCGLQAGSVK TESLGRNGQK EALLKYRQST LNSGLNFKDV LKEKADLDCL GEDEEETNVI
VLSYPQYCRY RSMLKRIQDK PSSILTDQFA LALGGIAVVS KNPQILYCRD TFDHPTLIEN
ESICDEFAPN LKGRPRKKKP CPQRRDSFSG GKDPNNNSDG KSVAKVKCEA RSALNKPKNN
HNNCKKVSNE EKPKVAIGEE CRADEQAFLV ALYKYMKERK TPIERIPYLG FKQINLWTMF
QAAQKLGGYE TITARRQWKH IYDELGGNPG STSAATCTRR HYERLILPYE RFIKGEEDKP
LPPIKPRKQE NNSQENENKT KVSGAKRIKH EISKSKKEKE NAPKPQDASE VSSEQEKEQE
TVNQKSITEP LPIADTKKKL EGYQDFAARP LVSQADPEKD SETDQGANSE KVAEEAGEKG
PAPPLASAPL APTPGTGKQS LTSPSALVDS KEPKPCCFTE SPENELQEAS FPGFSTTQPP
LANQSEVEDD KLPAMADYIA NCTVKVDQLG SDDIHNALKQ TPKVLVVQSF DMFKDKDLTG
PMNENHGLNY TPLLYSRGNP GIMSPLAKKK LLSQVSGASL SSSYPYGSPP PLISKKKVIA
REDRCSSLSQ AHHGQSTDHM AVNRPSVIQH VQSFRSKPSE ERKISDIFKH DKLSRSEPRF
SFSKHHLSPS KKSRGRRTVE KRALPHSHMP SFLADFYSSP HLHSLYRHTE HHLHNEQTSK
YPCRDMYRET ENSSFPSHKH QEKLHVNYLA SLHLQDKKSA AVEAPTDDQP TDLSLPKNPH
KPTGKALGLA HSAPGPQESK GTSQFQVINS QSRDCHPKAC RVSPMTMSAP KKYPEALSRS
GKPHPVRLEN FRKMDSMVHP ILHRKMSPQN IGAARPIKRS LEDLDLVIAG KKARAVSPLD
PAKEVSGKEK ASEQESEGSK AAHSGHSGGT SEGHKLPLSS PIFPGLYSGS LCSSGLNSRL
PAGYSHSLQY LKNQAVLSPL MQPLAFHSLV MQRGIFTSPT NSQQLYRHLA AATPVGSSYG
DLLHNSIYPL AAINPQAAFP SSQLSSVHPS TKL
