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AT-rich interactive domain-containing protein 5B (ARID domain-containing protein 5B) (MRF1-like protein) (Modulator recognition factor 2) (MRF-2)

 ARI5B_HUMAN             Reviewed;        1188 AA.
Q14865; B4DLB3; Q05DG6; Q32Q59; Q5VST4; Q6NZ42; Q7Z3M4; Q8N421;
Q9H786;
02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
14-OCT-2008, sequence version 3.
10-OCT-2018, entry version 170.
RecName: Full=AT-rich interactive domain-containing protein 5B;
Short=ARID domain-containing protein 5B;
AltName: Full=MRF1-like protein;
AltName: Full=Modulator recognition factor 2;
Short=MRF-2;
Name=ARID5B; Synonyms=DESRT, MRF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-453 (ISOFORM 2).
TISSUE=Smooth muscle, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-450 AND 477-1188 (ISOFORM
1), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-453 (ISOFORM 2).
TISSUE=Placenta, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 302-547.
TISSUE=Foreskin;
Merrills B.W., Huang T.H., Oka T., LeBon T.R., Gertson P.N.,
Itakura K.;
"A new family of DNA binding factors contain a member responsive to
retinoic acid.";
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 587-1188.
TISSUE=Colon endothelium, and Fetal kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
DNA-BINDING.
PubMed=10329386; DOI=10.1006/bbrc.1999.0643;
Whitson R.H., Huang T., Itakura K.;
"The novel Mrf-2 DNA-binding domain recognizes a five-base core
sequence through major and minor-groove contacts.";
Biochem. Biophys. Res. Commun. 258:326-331(1999).
[7]
DNA-BINDING.
PubMed=15640446; DOI=10.1093/nar/gki145;
Patsialou A., Wilsker D., Moran E.;
"DNA-binding properties of ARID family proteins.";
Nucleic Acids Res. 33:66-80(2005).
[8]
POSSIBLE INVOLVEMENT IN CORONARY ATHEROSCLEROSIS.
PubMed=18612189; DOI=10.1536/ihj.49.313;
Wang G., Watanabe M., Imai Y., Hara K., Manabe I., Maemura K.,
Horikoshi M., Kohro T., Amiya E., Sugiyama T., Fujita T., Kadowaki T.,
Yamazaki T., Nagai R.;
"Genetic variations of Mrf-2/ARID5B confer risk of coronary
atherosclerosis in the Japanese population.";
Int. Heart J. 49:313-327(2008).
[9]
POSSIBLE INVOLVEMENT IN ALL.
PubMed=19684603; DOI=10.1038/ng.432;
Trevino L.R., Yang W., French D., Hunger S.P., Carroll W.L.,
Devidas M., Willman C., Neale G., Downing J., Raimondi S.C., Pui C.H.,
Evans W.E., Relling M.V.;
"Germline genomic variants associated with childhood acute
lymphoblastic leukemia.";
Nat. Genet. 41:1001-1005(2009).
[10]
POSSIBLE INVOLVEMENT IN ALL.
PubMed=19684604; DOI=10.1038/ng.430;
Papaemmanuil E., Hosking F.J., Vijayakrishnan J., Price A., Olver B.,
Sheridan E., Kinsey S.E., Lightfoot T., Roman E., Irving J.A.,
Allan J.M., Tomlinson I.P., Taylor M., Greaves M., Houlston R.S.;
"Loci on 7p12.2, 10q21.2 and 14q11.2 are associated with risk of
childhood acute lymphoblastic leukemia.";
Nat. Genet. 41:1006-1010(2009).
[11]
POSSIBLE INVOLVEMENT IN ALL.
PubMed=20042726; DOI=10.1182/blood-2009-09-241513;
Prasad R.B., Hosking F.J., Vijayakrishnan J., Papaemmanuil E.,
Koehler R., Greaves M., Sheridan E., Gast A., Kinsey S.E.,
Lightfoot T., Roman E., Taylor M., Pritchard-Jones K., Stanulla M.,
Schrappe M., Bartram C.R., Houlston R.S., Kumar R., Hemminki K.;
"Verification of the susceptibility loci on 7p12.2, 10q21.2, and
14q11.2 in precursor B-cell acute lymphoblastic leukemia of
childhood.";
Blood 115:1765-1767(2010).
[12]
POSSIBLE INVOLVEMENT IN ALL.
PubMed=20460642; DOI=10.3324/haematol.2010.022459;
Healy J., Richer C., Bourgey M., Kritikou E.A., Sinnett D.;
"Replication analysis confirms the association of ARID5B with
childhood B-cell acute lymphoblastic leukemia.";
Haematologica 95:1608-1611(2010).
[13]
POSSIBLE INVOLVEMENT IN ALL.
PubMed=20054350; DOI=10.1038/leu.2009.277;
Yang W., Trevino L.R., Yang J.J., Scheet P., Pui C.H., Evans W.E.,
Relling M.V.;
"ARID5B SNP rs10821936 is associated with risk of childhood acute
lymphoblastic leukemia in blacks and contributes to racial differences
in leukemia incidence.";
Leukemia 24:894-896(2010).
[14]
POSSIBLE INVOLVEMENT IN ALL.
PubMed=20189245; DOI=10.1016/j.leukres.2010.02.001;
Han S., Lee K.M., Park S.K., Lee J.E., Ahn H.S., Shin H.Y., Kang H.J.,
Koo H.H., Seo J.J., Choi J.E., Ahn Y.O., Kang D.;
"Genome-wide association study of childhood acute lymphoblastic
leukemia in Korea.";
Leuk. Res. 34:1271-1274(2010).
[15]
POSSIBLE INVOLVEMENT IN ALL.
PubMed=21098271; DOI=10.1073/pnas.1006981107;
Paulsson K., Forestier E., Lilljebjorn H., Heldrup J., Behrendtz M.,
Young B.D., Johansson B.;
"Genetic landscape of high hyperdiploid childhood acute lymphoblastic
leukemia.";
Proc. Natl. Acad. Sci. U.S.A. 107:21719-21724(2010).
[16]
FUNCTION, INTERACTION WITH PHF2, IDENTIFICATION BY MASS SPECTROMETRY,
TISSUE SPECIFICITY, DNA-BINDING, IDENTIFICATION IN THE PHF2-ARID5B
COMPLEX, METHYLATION AT LYS-336, AND MUTAGENESIS OF LYS-336.
PubMed=21532585; DOI=10.1038/ncb2228;
Baba A., Ohtake F., Okuno Y., Yokota K., Okada M., Imai Y., Ni M.,
Meyer C.A., Igarashi K., Kanno J., Brown M., Kato S.;
"PKA-dependent regulation of the histone lysine demethylase complex
PHF2-ARID5B.";
Nat. Cell Biol. 13:668-675(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-1032 AND
SER-1133, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1032, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-803, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-803, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-774 AND LYS-803, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130; LYS-445; LYS-494;
LYS-496; LYS-767; LYS-774; LYS-803; LYS-810; LYS-893; LYS-916;
LYS-920; LYS-935; LYS-988; LYS-1000; LYS-1013; LYS-1055 AND LYS-1070,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[23]
STRUCTURE BY NMR OF 318-417.
PubMed=9808040; DOI=10.1038/2934;
Yuan Y.-C., Whitson R.H., Liu Q., Itakura K., Chen Y.;
"A novel DNA-binding motif shares structural homology to DNA
replication and repair nucleases and polymerases.";
Nat. Struct. Biol. 5:959-964(1998).
[24]
STRUCTURE BY NMR OF 318-417 IN COMPLEX WITH DNA.
PubMed=11478881; DOI=10.1021/bi010476a;
Zhu L., Hu J., Lin D., Whitson R., Itakura K., Chen Y.;
"Dynamics of the Mrf-2 DNA-binding domain free and in complex with
DNA.";
Biochemistry 40:9142-9150(2001).
[25]
STRUCTURE BY NMR OF 318-417 IN COMPLEX WITH DNA.
PubMed=17407261; DOI=10.1021/bi061738h;
Cai S., Zhu L., Zhang Z., Chen Y.;
"Determination of the three-dimensional structure of the Mrf2-DNA
complex using paramagnetic spin labeling.";
Biochemistry 46:4943-4950(2007).
-!- FUNCTION: Transcription coactivator that binds to the 5'-AATA[CT]-
3' core sequence and plays a key role in adipogenesis and liver
development. Acts by forming a complex with phosphorylated PHF2,
which mediates demethylation at Lys-336, leading to target the
PHF2-ARID5B complex to target promoters, where PHF2 mediates
demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2),
followed by transcription activation of target genes. The PHF2-
ARID5B complex acts as a coactivator of HNF4A in liver. Required
for adipogenesis: regulates triglyceride metabolism in adipocytes
by regulating expression of adipogenic genes. Overexpression leads
to induction of smooth muscle marker genes, suggesting that it may
also act as a regulator of smooth muscle cell differentiation and
proliferation. Represses the cytomegalovirus enhancer.
{ECO:0000269|PubMed:21532585}.
-!- INTERACTION:
Q13547:HDAC1; NbExp=5; IntAct=EBI-1210388, EBI-301834;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00355}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q14865-1; Sequence=Displayed;
Name=2;
IsoId=Q14865-2; Sequence=VSP_009355, VSP_009356;
Name=3;
IsoId=Q14865-3; Sequence=VSP_041560, VSP_041561;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, including in liver (at
protein level). {ECO:0000269|PubMed:21532585}.
-!- DOMAIN: The ARID domain mediates the interaction with DNA.
-!- PTM: Methylation at Lys-336 prevents DNA-binding. Demethylation by
PHF2 promotes recruitment of the PHF2-ARID5B complex to promoters.
{ECO:0000269|PubMed:21532585}.
-!- DISEASE: Note=Defects in ARID5B may be a cause of susceptibility
to coronary atherosclerosis in the Japanese population.
-!- DISEASE: Leukemia, acute lymphoblastic (ALL) [MIM:613065]: A
subtype of acute leukemia, a cancer of the white blood cells. ALL
is a malignant disease of bone marrow and the most common
malignancy diagnosed in children. The malignant cells are lymphoid
precursor cells (lymphoblasts) that are arrested in an early stage
of development. The lymphoblasts replace the normal marrow
elements, resulting in a marked decrease in the production of
normal blood cells. Consequently, anemia, thrombocytopenia, and
neutropenia occur to varying degrees. The lymphoblasts also
proliferate in organs other than the marrow, particularly the
liver, spleen, and lymphnodes. {ECO:0000269|PubMed:19684603,
ECO:0000269|PubMed:19684604, ECO:0000269|PubMed:20042726,
ECO:0000269|PubMed:20054350, ECO:0000269|PubMed:20189245,
ECO:0000269|PubMed:20460642, ECO:0000269|PubMed:21098271}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ARID5B family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH15120.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH36831.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH66345.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAI07801.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAB15012.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AC067742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL671972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK024803; BAB15012.1; ALT_SEQ; mRNA.
EMBL; AK296921; BAG59475.1; -; mRNA.
EMBL; BC015120; AAH15120.1; ALT_SEQ; mRNA.
EMBL; BC036831; AAH36831.1; ALT_INIT; mRNA.
EMBL; BC066345; AAH66345.1; ALT_SEQ; mRNA.
EMBL; BC107800; AAI07801.1; ALT_SEQ; mRNA.
EMBL; M73837; AAA59870.1; -; mRNA.
EMBL; BX537690; CAD97814.1; -; mRNA.
EMBL; BX641020; CAE46013.1; -; mRNA.
CCDS; CCDS31208.1; -. [Q14865-1]
CCDS; CCDS58082.1; -. [Q14865-2]
PIR; S27963; S27963.
RefSeq; NP_001231567.1; NM_001244638.1. [Q14865-2]
RefSeq; NP_115575.1; NM_032199.2. [Q14865-1]
UniGene; Hs.535297; -.
PDB; 1IG6; NMR; -; A=318-424.
PDB; 2OEH; NMR; -; A=318-424.
PDBsum; 1IG6; -.
PDBsum; 2OEH; -.
ProteinModelPortal; Q14865; -.
SMR; Q14865; -.
BioGrid; 123918; 21.
IntAct; Q14865; 16.
STRING; 9606.ENSP00000279873; -.
iPTMnet; Q14865; -.
PhosphoSitePlus; Q14865; -.
BioMuta; ARID5B; -.
DMDM; 209572763; -.
EPD; Q14865; -.
MaxQB; Q14865; -.
PaxDb; Q14865; -.
PeptideAtlas; Q14865; -.
PRIDE; Q14865; -.
ProteomicsDB; 60211; -.
ProteomicsDB; 60212; -. [Q14865-2]
ProteomicsDB; 60213; -. [Q14865-3]
DNASU; 84159; -.
Ensembl; ENST00000279873; ENSP00000279873; ENSG00000150347. [Q14865-1]
Ensembl; ENST00000309334; ENSP00000308862; ENSG00000150347. [Q14865-2]
GeneID; 84159; -.
KEGG; hsa:84159; -.
UCSC; uc001jlt.3; human. [Q14865-1]
CTD; 84159; -.
DisGeNET; 84159; -.
EuPathDB; HostDB:ENSG00000150347.14; -.
GeneCards; ARID5B; -.
H-InvDB; HIX0008854; -.
HGNC; HGNC:17362; ARID5B.
HPA; HPA015037; -.
MIM; 608538; gene.
MIM; 613065; phenotype.
neXtProt; NX_Q14865; -.
OpenTargets; ENSG00000150347; -.
PharmGKB; PA134943193; -.
eggNOG; ENOG410IQ7B; Eukaryota.
eggNOG; ENOG4110NWK; LUCA.
GeneTree; ENSGT00900000140901; -.
HOVERGEN; HBG084756; -.
InParanoid; Q14865; -.
OMA; PKACRVS; -.
OrthoDB; EOG091G0E6N; -.
PhylomeDB; Q14865; -.
TreeFam; TF324725; -.
Reactome; R-HSA-3214842; HDMs demethylate histones.
SignaLink; Q14865; -.
ChiTaRS; ARID5B; human.
EvolutionaryTrace; Q14865; -.
GeneWiki; ARID5B; -.
GenomeRNAi; 84159; -.
PRO; PR:Q14865; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000150347; Expressed in 247 organ(s), highest expression level in uterine cervix.
CleanEx; HS_ARID5B; -.
Genevisible; Q14865; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IDA:GDB.
GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0060612; P:adipose tissue development; ISS:UniProtKB.
GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
GO; GO:0048468; P:cell development; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
GO; GO:0060613; P:fat pad development; IEA:Ensembl.
GO; GO:0008585; P:female gonad development; IEA:Ensembl.
GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0001889; P:liver development; TAS:UniProtKB.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0048644; P:muscle organ morphogenesis; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:GDB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.150.60; -; 1.
InterPro; IPR030408; ARID5B.
InterPro; IPR001606; ARID_dom.
InterPro; IPR036431; ARID_dom_sf.
PANTHER; PTHR13964:SF37; PTHR13964:SF37; 1.
Pfam; PF01388; ARID; 1.
SMART; SM00501; BRIGHT; 1.
SUPFAM; SSF46774; SSF46774; 1.
PROSITE; PS51011; ARID; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 1188 AT-rich interactive domain-containing
protein 5B.
/FTId=PRO_0000200581.
DOMAIN 318 410 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 336 336 N6,N6-dimethyllysine.
{ECO:0000269|PubMed:21532585}.
MOD_RES 1032 1032 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1133 1133 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 494 494 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 496 496 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 767 767 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 774 774 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 803 803 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 810 810 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 893 893 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 916 916 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 920 920 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 935 935 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 988 988 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1000 1000 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1013 1013 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1055 1055 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1070 1070 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 243 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_009355.
VAR_SEQ 244 244 F -> M (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_009356.
VAR_SEQ 284 318 KCEARSALTKPKNNHNCKKVSNEEKPKVAIGEECR -> RS
FTPRYSFRCIFLFLLFLFISLCLCLGGSFQFSI (in
isoform 3). {ECO:0000305}.
/FTId=VSP_041560.
VAR_SEQ 319 1188 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_041561.
MUTAGEN 336 336 K->A,R: Abolishes methylation and FSK-
dependent DNA-binding of the PHF2-ARID5B
complex to promoters.
{ECO:0000269|PubMed:21532585}.
CONFLICT 401 401 L -> S (in Ref. 3; AAH15120).
{ECO:0000305}.
CONFLICT 451 451 S -> N (in Ref. 3; AAH15120).
{ECO:0000305}.
CONFLICT 827 827 F -> L (in Ref. 5; CAE46013).
{ECO:0000305}.
HELIX 319 333 {ECO:0000244|PDB:1IG6}.
TURN 334 336 {ECO:0000244|PDB:1IG6}.
HELIX 339 341 {ECO:0000244|PDB:1IG6}.
STRAND 345 349 {ECO:0000244|PDB:1IG6}.
HELIX 352 361 {ECO:0000244|PDB:1IG6}.
HELIX 364 371 {ECO:0000244|PDB:1IG6}.
HELIX 374 381 {ECO:0000244|PDB:1IG6}.
TURN 388 393 {ECO:0000244|PDB:1IG6}.
HELIX 394 401 {ECO:0000244|PDB:1IG6}.
TURN 402 405 {ECO:0000244|PDB:1IG6}.
HELIX 406 412 {ECO:0000244|PDB:1IG6}.
STRAND 414 417 {ECO:0000244|PDB:1IG6}.
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


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