ARI5B_CANLF
ID ARI5B_CANLF Reviewed; 1187 AA.
AC E2R9X2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=AT-rich interactive domain-containing protein 5B;
DE Short=ARID domain-containing protein 5B;
GN Name=ARID5B;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
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-337, 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-337 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 AlphaFoldDB; E2R9X2; -.
DR BMRB; E2R9X2; -.
DR SMR; E2R9X2; -.
DR STRING; 9615.ENSCAFP00000037005; -.
DR PaxDb; E2R9X2; -.
DR eggNOG; KOG2744; Eukaryota.
DR InParanoid; E2R9X2; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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..1187
FT /note="AT-rich interactive domain-containing protein 5B"
FT /id="PRO_0000410900"
FT DOMAIN 319..411
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 251..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT MOD_RES 337
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT MOD_RES 1132
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 446
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 494
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 496
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 767
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 803
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 810
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 893
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 916
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 935
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 988
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 1000
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
FT CROSSLNK 1013
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"
FT CROSSLNK 1069
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14865"
SQ SEQUENCE 1187 AA; 129976 MW; 38D0E94FD63C82A5 CRC64;
MEPNSLQWVG SPCGLHGPYI FYKAFQFHLE GKPRILSLGD FFFVRCTPKD PICIAELQLL
WEERTSRQLL SSSKLYFLPE DTPQGRNSDH GEDEVIAVSE KVIVKLEDLV KWVHSDFSKW
RCGLQAGAVK TTALGRNGQK EALLKYRQST LNSGLNFKDV LKEKADLGED EEETNVIVLS
YPQYCRYRSM LKRIQDKPPS ILTDQFALAL GGIAVVSKNP QILYCRDTFD HPTLIENESI
CDEFAPNLKG RPRKKKPCPQ RRDSFSGVKD SNNNSDGKAV AKVKCEARSA LSKPKNNHNN
CKKVSNEEKP KVAIGEECRA DEQAFLVALY KYMKERKTPI ERIPYLGFKQ INLWTMFQAA
QKLGGYETIT ARRQWKHIYD ELGGNPGSTS AATCTRRHYE RLILPYERFI KGEEDKPLPP
IKPRKQENSS QENENKTKVS GTKRIKHEIP KSKKEKENAP KPQESPEVSS EPEKEQETSN
QKSITEPLPA AEGKRKMEGY QDFAARPVGS RADPEKDSDA DRGAGGATAA EEAGEQGPVP
PLPSAPAAPD RGPALGPGAG KQPLTSPSAP ADSKQEPQPC CFAESPDSEP QEPPFPGFPA
AQPPLASQSE LEEDKLPAMA DYIANCTVKV DQLGSDDIHN ALKQTPKVLV VQSFDMFKDK
DLTGPMNENH GLNYTPLLYS RGNPGIMSPL AKKKLLSQVS GAGLSGSYPY GSPPPLISKK
KLIPRDELCS GLPQAHPGQG SDHAAVSRPS VIQHVQSFRS KASEERKGLG DLFKHDKLGR
SEPHRCSFSK HHLGPLADSY ALKPDAPEGK DKLLEKRALP HAHVPSFLAD FYSSPHLHSL
YRHAEHHLHA EQTSKYACRD AYRESENSSF PAHKHQEKLH VNYLASLHLQ DKKPAPAEAP
ADEQPTDLSL PKNLHKPTGK VLGLAHAAPG PQESKGAPQF PAGNGQSRDG HPKACRVSPM
TLSAPKKYPE PLSRASRPHH VRLESFRKLE GMVHPVLHRK AGPQAVGAAR PIKRGLEDLD
LVIAGKKARA VSPLDPPKEA CGKDKGAELE GEGGKAAAAH GGPAADGHKA ALSSPIFPGL
YSGSLCGSGL GSRLPAGYSH SLQYLKNQTV LSPLMQPLAF HSLVMQRGIF TSPTNSQQLY
RHLAAATPVG SSYGDLLHNS IYPLAAINPQ AAFPASQLSS VHPSTKL
