ARI5B_HUMAN
ID ARI5B_HUMAN Reviewed; 1188 AA.
AC Q14865; B4DLB3; Q05DG6; Q32Q59; Q5VST4; Q6NZ42; Q7Z3M4; Q8N421; Q9H786;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=AT-rich interactive domain-containing protein 5B;
DE Short=ARID domain-containing protein 5B;
DE AltName: Full=MRF1-like protein;
DE AltName: Full=Modulator recognition factor 2;
DE Short=MRF-2;
GN Name=ARID5B; Synonyms=DESRT, MRF2;
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 [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-453 (ISOFORM 2).
RC TISSUE=Smooth muscle, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-450 AND 477-1188 (ISOFORM 1),
RP AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-453 (ISOFORM 2).
RC TISSUE=Placenta, and Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 302-547.
RC TISSUE=Foreskin;
RA Merrills B.W., Huang T.H., Oka T., LeBon T.R., Gertson P.N., Itakura K.;
RT "A new family of DNA binding factors contain a member responsive to
RT retinoic acid.";
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 587-1188.
RC TISSUE=Colon endothelium, and Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP DNA-BINDING.
RX PubMed=10329386; DOI=10.1006/bbrc.1999.0643;
RA Whitson R.H., Huang T., Itakura K.;
RT "The novel Mrf-2 DNA-binding domain recognizes a five-base core sequence
RT through major and minor-groove contacts.";
RL Biochem. Biophys. Res. Commun. 258:326-331(1999).
RN [7]
RP DNA-BINDING.
RX PubMed=15640446; DOI=10.1093/nar/gki145;
RA Patsialou A., Wilsker D., Moran E.;
RT "DNA-binding properties of ARID family proteins.";
RL Nucleic Acids Res. 33:66-80(2005).
RN [8]
RP POSSIBLE INVOLVEMENT IN CORONARY ATHEROSCLEROSIS.
RX PubMed=18612189; DOI=10.1536/ihj.49.313;
RA Wang G., Watanabe M., Imai Y., Hara K., Manabe I., Maemura K.,
RA Horikoshi M., Kohro T., Amiya E., Sugiyama T., Fujita T., Kadowaki T.,
RA Yamazaki T., Nagai R.;
RT "Genetic variations of Mrf-2/ARID5B confer risk of coronary atherosclerosis
RT in the Japanese population.";
RL Int. Heart J. 49:313-327(2008).
RN [9]
RP POSSIBLE INVOLVEMENT IN ALL.
RX PubMed=19684603; DOI=10.1038/ng.432;
RA Trevino L.R., Yang W., French D., Hunger S.P., Carroll W.L., Devidas M.,
RA Willman C., Neale G., Downing J., Raimondi S.C., Pui C.H., Evans W.E.,
RA Relling M.V.;
RT "Germline genomic variants associated with childhood acute lymphoblastic
RT leukemia.";
RL Nat. Genet. 41:1001-1005(2009).
RN [10]
RP POSSIBLE INVOLVEMENT IN ALL.
RX PubMed=19684604; DOI=10.1038/ng.430;
RA Papaemmanuil E., Hosking F.J., Vijayakrishnan J., Price A., Olver B.,
RA Sheridan E., Kinsey S.E., Lightfoot T., Roman E., Irving J.A., Allan J.M.,
RA Tomlinson I.P., Taylor M., Greaves M., Houlston R.S.;
RT "Loci on 7p12.2, 10q21.2 and 14q11.2 are associated with risk of childhood
RT acute lymphoblastic leukemia.";
RL Nat. Genet. 41:1006-1010(2009).
RN [11]
RP POSSIBLE INVOLVEMENT IN ALL.
RX PubMed=20042726; DOI=10.1182/blood-2009-09-241513;
RA Prasad R.B., Hosking F.J., Vijayakrishnan J., Papaemmanuil E., Koehler R.,
RA Greaves M., Sheridan E., Gast A., Kinsey S.E., Lightfoot T., Roman E.,
RA Taylor M., Pritchard-Jones K., Stanulla M., Schrappe M., Bartram C.R.,
RA Houlston R.S., Kumar R., Hemminki K.;
RT "Verification of the susceptibility loci on 7p12.2, 10q21.2, and 14q11.2 in
RT precursor B-cell acute lymphoblastic leukemia of childhood.";
RL Blood 115:1765-1767(2010).
RN [12]
RP POSSIBLE INVOLVEMENT IN ALL.
RX PubMed=20460642; DOI=10.3324/haematol.2010.022459;
RA Healy J., Richer C., Bourgey M., Kritikou E.A., Sinnett D.;
RT "Replication analysis confirms the association of ARID5B with childhood B-
RT cell acute lymphoblastic leukemia.";
RL Haematologica 95:1608-1611(2010).
RN [13]
RP POSSIBLE INVOLVEMENT IN ALL.
RX PubMed=20054350; DOI=10.1038/leu.2009.277;
RA Yang W., Trevino L.R., Yang J.J., Scheet P., Pui C.H., Evans W.E.,
RA Relling M.V.;
RT "ARID5B SNP rs10821936 is associated with risk of childhood acute
RT lymphoblastic leukemia in blacks and contributes to racial differences in
RT leukemia incidence.";
RL Leukemia 24:894-896(2010).
RN [14]
RP POSSIBLE INVOLVEMENT IN ALL.
RX PubMed=20189245; DOI=10.1016/j.leukres.2010.02.001;
RA Han S., Lee K.M., Park S.K., Lee J.E., Ahn H.S., Shin H.Y., Kang H.J.,
RA Koo H.H., Seo J.J., Choi J.E., Ahn Y.O., Kang D.;
RT "Genome-wide association study of childhood acute lymphoblastic leukemia in
RT Korea.";
RL Leuk. Res. 34:1271-1274(2010).
RN [15]
RP POSSIBLE INVOLVEMENT IN ALL.
RX PubMed=21098271; DOI=10.1073/pnas.1006981107;
RA Paulsson K., Forestier E., Lilljebjorn H., Heldrup J., Behrendtz M.,
RA Young B.D., Johansson B.;
RT "Genetic landscape of high hyperdiploid childhood acute lymphoblastic
RT leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21719-21724(2010).
RN [16]
RP FUNCTION, INTERACTION WITH PHF2, IDENTIFICATION BY MASS SPECTROMETRY,
RP TISSUE SPECIFICITY, DNA-BINDING, IDENTIFICATION IN THE PHF2-ARID5B COMPLEX,
RP METHYLATION AT LYS-336, AND MUTAGENESIS OF LYS-336.
RX PubMed=21532585; DOI=10.1038/ncb2228;
RA Baba A., Ohtake F., Okuno Y., Yokota K., Okada M., Imai Y., Ni M.,
RA Meyer C.A., Igarashi K., Kanno J., Brown M., Kato S.;
RT "PKA-dependent regulation of the histone lysine demethylase complex PHF2-
RT ARID5B.";
RL Nat. Cell Biol. 13:668-675(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-1032 AND SER-1133,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1032, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-803, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-803, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-774 AND LYS-803, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130; LYS-445; LYS-494; LYS-496;
RP LYS-767; LYS-774; LYS-803; LYS-810; LYS-893; LYS-916; LYS-920; LYS-935;
RP LYS-988; LYS-1000; LYS-1013; LYS-1055 AND LYS-1070, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP STRUCTURE BY NMR OF 318-417.
RX PubMed=9808040; DOI=10.1038/2934;
RA Yuan Y.-C., Whitson R.H., Liu Q., Itakura K., Chen Y.;
RT "A novel DNA-binding motif shares structural homology to DNA replication
RT and repair nucleases and polymerases.";
RL Nat. Struct. Biol. 5:959-964(1998).
RN [24]
RP STRUCTURE BY NMR OF 318-417 IN COMPLEX WITH DNA.
RX PubMed=11478881; DOI=10.1021/bi010476a;
RA Zhu L., Hu J., Lin D., Whitson R., Itakura K., Chen Y.;
RT "Dynamics of the Mrf-2 DNA-binding domain free and in complex with DNA.";
RL Biochemistry 40:9142-9150(2001).
RN [25]
RP STRUCTURE BY NMR OF 318-417 IN COMPLEX WITH DNA.
RX PubMed=17407261; DOI=10.1021/bi061738h;
RA Cai S., Zhu L., Zhang Z., Chen Y.;
RT "Determination of the three-dimensional structure of the Mrf2-DNA complex
RT using paramagnetic spin labeling.";
RL Biochemistry 46:4943-4950(2007).
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-336, 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. Represses the
CC cytomegalovirus enhancer. {ECO:0000269|PubMed:21532585}.
CC -!- INTERACTION:
CC Q14865; Q13547: HDAC1; NbExp=6; IntAct=EBI-1210388, EBI-301834;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14865-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14865-2; Sequence=VSP_009355, VSP_009356;
CC Name=3;
CC IsoId=Q14865-3; Sequence=VSP_041560, VSP_041561;
CC -!- TISSUE SPECIFICITY: Widely expressed, including in liver (at protein
CC level). {ECO:0000269|PubMed:21532585}.
CC -!- DOMAIN: The ARID domain mediates the interaction with DNA.
CC -!- PTM: Methylation at Lys-336 prevents DNA-binding. Demethylation by PHF2
CC promotes recruitment of the PHF2-ARID5B complex to promoters.
CC {ECO:0000269|PubMed:21532585}.
CC -!- DISEASE: Note=Defects in ARID5B may be a cause of susceptibility to
CC coronary atherosclerosis in the Japanese population.
CC -!- DISEASE: Leukemia, acute lymphoblastic (ALL) [MIM:613065]: A subtype of
CC acute leukemia, a cancer of the white blood cells. ALL is a malignant
CC disease of bone marrow and the most common malignancy diagnosed in
CC children. The malignant cells are lymphoid precursor cells
CC (lymphoblasts) that are arrested in an early stage of development. The
CC lymphoblasts replace the normal marrow elements, resulting in a marked
CC decrease in the production of normal blood cells. Consequently, anemia,
CC thrombocytopenia, and neutropenia occur to varying degrees. The
CC lymphoblasts also proliferate in organs other than the marrow,
CC particularly the liver, spleen, and lymphnodes.
CC {ECO:0000269|PubMed:19684603, ECO:0000269|PubMed:19684604,
CC ECO:0000269|PubMed:20042726, ECO:0000269|PubMed:20054350,
CC ECO:0000269|PubMed:20189245, ECO:0000269|PubMed:20460642,
CC ECO:0000269|PubMed:21098271}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ARID5B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15120.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH36831.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH66345.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI07801.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB15012.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AC067742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK024803; BAB15012.1; ALT_SEQ; mRNA.
DR EMBL; AK296921; BAG59475.1; -; mRNA.
DR EMBL; BC015120; AAH15120.1; ALT_SEQ; mRNA.
DR EMBL; BC036831; AAH36831.1; ALT_INIT; mRNA.
DR EMBL; BC066345; AAH66345.1; ALT_SEQ; mRNA.
DR EMBL; BC107800; AAI07801.1; ALT_SEQ; mRNA.
DR EMBL; M73837; AAA59870.1; -; mRNA.
DR EMBL; BX537690; CAD97814.1; -; mRNA.
DR EMBL; BX641020; CAE46013.1; -; mRNA.
DR CCDS; CCDS31208.1; -. [Q14865-1]
DR CCDS; CCDS58082.1; -. [Q14865-2]
DR PIR; S27963; S27963.
DR RefSeq; NP_001231567.1; NM_001244638.1. [Q14865-2]
DR RefSeq; NP_115575.1; NM_032199.2. [Q14865-1]
DR PDB; 1IG6; NMR; -; A=318-424.
DR PDB; 2OEH; NMR; -; A=318-424.
DR PDBsum; 1IG6; -.
DR PDBsum; 2OEH; -.
DR AlphaFoldDB; Q14865; -.
DR BMRB; Q14865; -.
DR SMR; Q14865; -.
DR BioGRID; 123918; 62.
DR IntAct; Q14865; 32.
DR MINT; Q14865; -.
DR STRING; 9606.ENSP00000279873; -.
DR iPTMnet; Q14865; -.
DR PhosphoSitePlus; Q14865; -.
DR BioMuta; ARID5B; -.
DR DMDM; 209572763; -.
DR EPD; Q14865; -.
DR jPOST; Q14865; -.
DR MassIVE; Q14865; -.
DR MaxQB; Q14865; -.
DR PaxDb; Q14865; -.
DR PeptideAtlas; Q14865; -.
DR PRIDE; Q14865; -.
DR ProteomicsDB; 60211; -. [Q14865-1]
DR ProteomicsDB; 60212; -. [Q14865-2]
DR ProteomicsDB; 60213; -. [Q14865-3]
DR Antibodypedia; 2974; 123 antibodies from 24 providers.
DR DNASU; 84159; -.
DR Ensembl; ENST00000279873.12; ENSP00000279873.7; ENSG00000150347.17. [Q14865-1]
DR Ensembl; ENST00000309334.5; ENSP00000308862.5; ENSG00000150347.17. [Q14865-2]
DR GeneID; 84159; -.
DR KEGG; hsa:84159; -.
DR MANE-Select; ENST00000279873.12; ENSP00000279873.7; NM_032199.3; NP_115575.1.
DR UCSC; uc001jlt.3; human. [Q14865-1]
DR CTD; 84159; -.
DR DisGeNET; 84159; -.
DR GeneCards; ARID5B; -.
DR HGNC; HGNC:17362; ARID5B.
DR HPA; ENSG00000150347; Tissue enhanced (skeletal).
DR MIM; 608538; gene.
DR MIM; 613065; phenotype.
DR neXtProt; NX_Q14865; -.
DR OpenTargets; ENSG00000150347; -.
DR PharmGKB; PA134943193; -.
DR VEuPathDB; HostDB:ENSG00000150347; -.
DR eggNOG; KOG2744; Eukaryota.
DR GeneTree; ENSGT00940000161078; -.
DR HOGENOM; CLU_007985_0_0_1; -.
DR InParanoid; Q14865; -.
DR OMA; YRQTEHH; -.
DR OrthoDB; 368297at2759; -.
DR PhylomeDB; Q14865; -.
DR TreeFam; TF324725; -.
DR PathwayCommons; Q14865; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR SignaLink; Q14865; -.
DR SIGNOR; Q14865; -.
DR BioGRID-ORCS; 84159; 38 hits in 1096 CRISPR screens.
DR ChiTaRS; ARID5B; human.
DR EvolutionaryTrace; Q14865; -.
DR GeneWiki; ARID5B; -.
DR GenomeRNAi; 84159; -.
DR Pharos; Q14865; Tbio.
DR PRO; PR:Q14865; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q14865; protein.
DR Bgee; ENSG00000150347; Expressed in type B pancreatic cell and 215 other tissues.
DR ExpressionAtlas; Q14865; baseline and differential.
DR Genevisible; Q14865; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:GDB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0060612; P:adipose tissue development; ISS:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
DR GO; GO:0048468; P:cell development; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0060613; P:fat pad development; IEA:Ensembl.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; TAS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0048644; P:muscle organ morphogenesis; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:GDB.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1188
FT /note="AT-rich interactive domain-containing protein 5B"
FT /id="PRO_0000200581"
FT DOMAIN 318..410
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 251..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 336
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000269|PubMed:21532585"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 445
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 494
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 496
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 767
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 803
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 810
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 893
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 916
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 920
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 935
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 988
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1000
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1013
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1055
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1070
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009355"
FT VAR_SEQ 244
FT /note="F -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009356"
FT VAR_SEQ 284..318
FT /note="KCEARSALTKPKNNHNCKKVSNEEKPKVAIGEECR -> RSFTPRYSFRCIF
FT LFLLFLFISLCLCLGGSFQFSI (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_041560"
FT VAR_SEQ 319..1188
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_041561"
FT MUTAGEN 336
FT /note="K->A,R: Abolishes methylation and FSK-dependent DNA-
FT binding of the PHF2-ARID5B complex to promoters."
FT /evidence="ECO:0000269|PubMed:21532585"
FT CONFLICT 401
FT /note="L -> S (in Ref. 3; AAH15120)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="S -> N (in Ref. 3; AAH15120)"
FT /evidence="ECO:0000305"
FT CONFLICT 827
FT /note="F -> L (in Ref. 5; CAE46013)"
FT /evidence="ECO:0000305"
FT HELIX 319..333
FT /evidence="ECO:0007829|PDB:1IG6"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:1IG6"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1IG6"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:1IG6"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:1IG6"
FT HELIX 364..371
FT /evidence="ECO:0007829|PDB:1IG6"
FT HELIX 374..381
FT /evidence="ECO:0007829|PDB:1IG6"
FT TURN 388..393
FT /evidence="ECO:0007829|PDB:1IG6"
FT HELIX 394..401
FT /evidence="ECO:0007829|PDB:1IG6"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:1IG6"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:1IG6"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:1IG6"
SQ SEQUENCE 1188 AA; 132375 MW; 23B7C525B0055330 CRC64;
MEPNSLQWVG SPCGLHGPYI FYKAFQFHLE GKPRILSLGD FFFVRCTPKD PICIAELQLL
WEERTSRQLL SSSKLYFLPE DTPQGRNSDH GEDEVIAVSE KVIVKLEDLV KWVHSDFSKW
RCGFHAGPVK TEALGRNGQK EALLKYRQST LNSGLNFKDV LKEKADLGED EEETNVIVLS
YPQYCRYRSM LKRIQDKPSS ILTDQFALAL GGIAVVSRNP QILYCRDTFD HPTLIENESI
CDEFAPNLKG RPRKKKPCPQ RRDSFSGVKD SNNNSDGKAV AKVKCEARSA LTKPKNNHNC
KKVSNEEKPK VAIGEECRAD EQAFLVALYK YMKERKTPIE RIPYLGFKQI NLWTMFQAAQ
KLGGYETITA RRQWKHIYDE LGGNPGSTSA ATCTRRHYER LILPYERFIK GEEDKPLPPI
KPRKQENSSQ ENENKTKVSG TKRIKHEIPK SKKEKENAPK PQDAAEVSSE QEKEQETLIS
QKSIPEPLPA ADMKKKIEGY QEFSAKPLAS RVDPEKDNET DQGSNSEKVA EEAGEKGPTP
PLPSAPLAPE KDSALVPGAS KQPLTSPSAL VDSKQESKLC CFTESPESEP QEASFPSFPT
TQPPLANQNE TEDDKLPAMA DYIANCTVKV DQLGSDDIHN ALKQTPKVLV VQSFDMFKDK
DLTGPMNENH GLNYTPLLYS RGNPGIMSPL AKKKLLSQVS GASLSSSYPY GSPPPLISKK
KLIARDDLCS SLSQTHHGQS TDHMAVSRPS VIQHVQSFRS KPSEERKTIN DIFKHEKLSR
SDPHRCSFSK HHLNPLADSY VLKQEIQEGK DKLLEKRALP HSHMPSFLAD FYSSPHLHSL
YRHTEHHLHN EQTSKYPSRD MYRESENSSF PSHRHQEKLH VNYLTSLHLQ DKKSAAAEAP
TDDQPTDLSL PKNPHKPTGK VLGLAHSTTG PQESKGISQF QVLGSQSRDC HPKACRVSPM
TMSGPKKYPE SLSRSGKPHH VRLENFRKME GMVHPILHRK MSPQNIGAAR PIKRSLEDLD
LVIAGKKARA VSPLDPSKEV SGKEKASEQE SEGSKAAHGG HSGGGSEGHK LPLSSPIFPG
LYSGSLCNSG LNSRLPAGYS HSLQYLKNQT VLSPLMQPLA FHSLVMQRGI FTSPTNSQQL
YRHLAAATPV GSSYGDLLHN SIYPLAAINP QAAFPSSQLS SVHPSTKL
