ARI5A_HUMAN
ID ARI5A_HUMAN Reviewed; 594 AA.
AC Q03989; C9J1Q0; Q6NX37;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=AT-rich interactive domain-containing protein 5A;
DE Short=ARID domain-containing protein 5A;
DE AltName: Full=Modulator recognition factor 1;
DE Short=MRF-1;
GN Name=ARID5A; Synonyms=MRF1;
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 1), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Foreskin fibroblast;
RX PubMed=8649988; DOI=10.1093/nar/24.9.1695;
RA Huang T.H., Oka T., Asai T., Okada T., Merrills B.W., Gertson P.N.,
RA Whitson R.H., Itakura K.;
RT "Repression by a differentiation-specific factor of the human
RT cytomegalovirus enhancer.";
RL Nucleic Acids Res. 24:1695-1701(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 INTERACTION WITH ESR1.
RX PubMed=15941852; DOI=10.1210/me.2004-0311;
RA Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.;
RT "Modulator recognition factor 1, an AT-rich interaction domain family
RT member, is a novel corepressor for estrogen receptor alpha.";
RL Mol. Endocrinol. 19:2491-2501(2005).
CC -!- FUNCTION: Binds to AT-rich stretches in the modulator region upstream
CC of the human cytomegalovirus major intermediate early gene enhancer.
CC May act as repressor and down-regulate enhancer-dependent gene
CC expressison (PubMed:8649988). May positively regulate chondrocyte-
CC specific transcription such as of COL2A1 in collaboration with SOX9 and
CC positively regulate histone H3 acetylation at chondrocyte-specific
CC genes. May stimulate early-stage chondrocyte differentiation and
CC inhibit later stage differention (By similarity). Can repress ESR1-
CC mediated transcriptional activation; proposed to act as corepressor for
CC selective nuclear hormone receptors (PubMed:15941852). As RNA-binding
CC protein involved in the regulation of inflammatory response by
CC stabilizing selective inflammation-related mRNAs, such as IL6, STAT3
CC and TBX21. Binds to stem loop structures located in the 3'UTRs of IL6,
CC STAT3 and TBX21 mRNAs; at least for STAT3 prevents binding of ZC3H12A
CC to the mRNA stem loop structure thus inhibiting its degradation
CC activity. Contributes to elevated IL6 levels possibly implicated in
CC autoimmunity processes. IL6-dependent stabilization of STAT3 mRNA may
CC promote differentiation of naive CD4+ T-cells into T-helper Th17 cells.
CC In CD4+ T-cells may also inhibit RORC-induced Th17 cell differentiation
CC independently of IL6 signaling. Stabilization of TBX21 mRNA contributes
CC to elevated interferon-gamma secretion in Th1 cells possibly implicated
CC in the establishment of septic shock (By similarity). Stabilizes
CC TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in
CC its 3'UTR; thereby competing with the mRNA-destabilizing functions of
CC RC3H1 and endoribonuclease ZC3H12A (By similarity).
CC {ECO:0000250|UniProtKB:Q3U108, ECO:0000269|PubMed:15941852,
CC ECO:0000269|PubMed:8649988}.
CC -!- SUBUNIT: Interacts with SOX9 (By similarity). Interacts with ESR1
CC (PubMed:15941852). Interacts with RORC (By similarity).
CC {ECO:0000250|UniProtKB:Q3U108, ECO:0000269|PubMed:15941852}.
CC -!- INTERACTION:
CC Q03989; X5D778: ANKRD11; NbExp=3; IntAct=EBI-948603, EBI-17183751;
CC Q03989; Q03989: ARID5A; NbExp=3; IntAct=EBI-948603, EBI-948603;
CC Q03989; Q8N8Y2: ATP6V0D2; NbExp=3; IntAct=EBI-948603, EBI-3923949;
CC Q03989; P54253: ATXN1; NbExp=9; IntAct=EBI-948603, EBI-930964;
CC Q03989; P0C7T5: ATXN1L; NbExp=3; IntAct=EBI-948603, EBI-8624731;
CC Q03989; O95429: BAG4; NbExp=3; IntAct=EBI-948603, EBI-2949658;
CC Q03989; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-948603, EBI-742750;
CC Q03989; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-948603, EBI-11524452;
CC Q03989; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-948603, EBI-11983447;
CC Q03989; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-948603, EBI-725606;
CC Q03989; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-948603, EBI-11976299;
CC Q03989; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-948603, EBI-1383687;
CC Q03989; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-948603, EBI-744545;
CC Q03989; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-948603, EBI-744556;
CC Q03989; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-948603, EBI-10961624;
CC Q03989; P61024: CKS1B; NbExp=5; IntAct=EBI-948603, EBI-456371;
CC Q03989; P10606: COX5B; NbExp=3; IntAct=EBI-948603, EBI-1053725;
CC Q03989; P05813: CRYBA1; NbExp=3; IntAct=EBI-948603, EBI-7043337;
CC Q03989; P53672: CRYBA2; NbExp=3; IntAct=EBI-948603, EBI-750444;
CC Q03989; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-948603, EBI-3867333;
CC Q03989; Q15038: DAZAP2; NbExp=8; IntAct=EBI-948603, EBI-724310;
CC Q03989; Q6PKX4: DOK6; NbExp=3; IntAct=EBI-948603, EBI-2880244;
CC Q03989; Q86UW9: DTX2; NbExp=3; IntAct=EBI-948603, EBI-740376;
CC Q03989; P03372: ESR1; NbExp=9; IntAct=EBI-948603, EBI-78473;
CC Q03989; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-948603, EBI-10213520;
CC Q03989; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-948603, EBI-12193763;
CC Q03989; Q13643: FHL3; NbExp=3; IntAct=EBI-948603, EBI-741101;
CC Q03989; O60548: FOXD2; NbExp=3; IntAct=EBI-948603, EBI-17282008;
CC Q03989; O75593: FOXH1; NbExp=4; IntAct=EBI-948603, EBI-1759806;
CC Q03989; Q9BWX5: GATA5; NbExp=3; IntAct=EBI-948603, EBI-12132270;
CC Q03989; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-948603, EBI-7251368;
CC Q03989; P62993: GRB2; NbExp=3; IntAct=EBI-948603, EBI-401755;
CC Q03989; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-948603, EBI-12094670;
CC Q03989; P49639: HOXA1; NbExp=3; IntAct=EBI-948603, EBI-740785;
CC Q03989; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-948603, EBI-3918847;
CC Q03989; Q9NRY2: INIP; NbExp=3; IntAct=EBI-948603, EBI-2881520;
CC Q03989; P78412: IRX6; NbExp=3; IntAct=EBI-948603, EBI-12100506;
CC Q03989; Q674X7-2: KAZN; NbExp=3; IntAct=EBI-948603, EBI-12024294;
CC Q03989; Q7L273: KCTD9; NbExp=3; IntAct=EBI-948603, EBI-4397613;
CC Q03989; Q8NAX2: KDF1; NbExp=3; IntAct=EBI-948603, EBI-11997992;
CC Q03989; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-948603, EBI-10171774;
CC Q03989; P59991: KRTAP12-2; NbExp=5; IntAct=EBI-948603, EBI-10176379;
CC Q03989; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-948603, EBI-11992140;
CC Q03989; Q7Z4W3: KRTAP19-3; NbExp=3; IntAct=EBI-948603, EBI-12020132;
CC Q03989; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-948603, EBI-1048945;
CC Q03989; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-948603, EBI-10241353;
CC Q03989; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-948603, EBI-3957672;
CC Q03989; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-948603, EBI-3957694;
CC Q03989; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-948603, EBI-12111050;
CC Q03989; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-948603, EBI-11962084;
CC Q03989; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-948603, EBI-18394498;
CC Q03989; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-948603, EBI-10261141;
CC Q03989; Q14847-2: LASP1; NbExp=3; IntAct=EBI-948603, EBI-9088686;
CC Q03989; Q96PV6: LENG8; NbExp=3; IntAct=EBI-948603, EBI-739546;
CC Q03989; P0CW20: LIMS4; NbExp=3; IntAct=EBI-948603, EBI-10196832;
CC Q03989; Q99732: LITAF; NbExp=3; IntAct=EBI-948603, EBI-725647;
CC Q03989; P25791-3: LMO2; NbExp=3; IntAct=EBI-948603, EBI-11959475;
CC Q03989; Q9Y586: MAB21L2; NbExp=3; IntAct=EBI-948603, EBI-6659161;
CC Q03989; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-948603, EBI-716006;
CC Q03989; Q99750: MDFI; NbExp=5; IntAct=EBI-948603, EBI-724076;
CC Q03989; Q9BRT3: MIEN1; NbExp=3; IntAct=EBI-948603, EBI-6137472;
CC Q03989; Q13064: MKRN3; NbExp=3; IntAct=EBI-948603, EBI-2340269;
CC Q03989; Q6PF18: MORN3; NbExp=3; IntAct=EBI-948603, EBI-9675802;
CC Q03989; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-948603, EBI-6952711;
CC Q03989; Q9BRQ3: NUDT22; NbExp=3; IntAct=EBI-948603, EBI-10297093;
CC Q03989; A1E959: ODAM; NbExp=3; IntAct=EBI-948603, EBI-5774125;
CC Q03989; Q7RTU3: OLIG3; NbExp=4; IntAct=EBI-948603, EBI-10225049;
CC Q03989; P32242: OTX1; NbExp=3; IntAct=EBI-948603, EBI-740446;
CC Q03989; O43189: PHF1; NbExp=3; IntAct=EBI-948603, EBI-530034;
CC Q03989; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-948603, EBI-14066006;
CC Q03989; Q13526: PIN1; NbExp=3; IntAct=EBI-948603, EBI-714158;
CC Q03989; P78337: PITX1; NbExp=3; IntAct=EBI-948603, EBI-748265;
CC Q03989; O15496: PLA2G10; NbExp=3; IntAct=EBI-948603, EBI-726466;
CC Q03989; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-948603, EBI-2876622;
CC Q03989; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-948603, EBI-12014286;
CC Q03989; D3DTS7: PMP22; NbExp=3; IntAct=EBI-948603, EBI-25882629;
CC Q03989; Q8ND90: PNMA1; NbExp=5; IntAct=EBI-948603, EBI-302345;
CC Q03989; P28069: POU1F1; NbExp=3; IntAct=EBI-948603, EBI-8673859;
CC Q03989; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-948603, EBI-11320284;
CC Q03989; O43741: PRKAB2; NbExp=3; IntAct=EBI-948603, EBI-1053424;
CC Q03989; P86480: PRR20D; NbExp=3; IntAct=EBI-948603, EBI-12754095;
CC Q03989; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-948603, EBI-2798044;
CC Q03989; Q9NWB1-5: RBFOX1; NbExp=3; IntAct=EBI-948603, EBI-12123390;
CC Q03989; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-948603, EBI-740343;
CC Q03989; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-948603, EBI-11987469;
CC Q03989; P40937: RFC5; NbExp=3; IntAct=EBI-948603, EBI-712376;
CC Q03989; Q7L0R7: RNF44; NbExp=3; IntAct=EBI-948603, EBI-2845060;
CC Q03989; Q01974: ROR2; NbExp=3; IntAct=EBI-948603, EBI-6422642;
CC Q03989; O95486-2: SEC24A; NbExp=3; IntAct=EBI-948603, EBI-12320085;
CC Q03989; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-948603, EBI-8463848;
CC Q03989; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-948603, EBI-12288855;
CC Q03989; Q9BXF9: TEKT3; NbExp=3; IntAct=EBI-948603, EBI-8644516;
CC Q03989; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-948603, EBI-750487;
CC Q03989; Q8NEK8: TENT5D; NbExp=3; IntAct=EBI-948603, EBI-744726;
CC Q03989; Q96PF1: TGM7; NbExp=3; IntAct=EBI-948603, EBI-12029034;
CC Q03989; Q63HR2: TNS2; NbExp=3; IntAct=EBI-948603, EBI-949753;
CC Q03989; Q13077: TRAF1; NbExp=3; IntAct=EBI-948603, EBI-359224;
CC Q03989; P14373: TRIM27; NbExp=3; IntAct=EBI-948603, EBI-719493;
CC Q03989; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-948603, EBI-10259086;
CC Q03989; Q86WV8: TSC1; NbExp=3; IntAct=EBI-948603, EBI-12806590;
CC Q03989; Q8WW01: TSEN15; NbExp=3; IntAct=EBI-948603, EBI-372432;
CC Q03989; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-948603, EBI-3918381;
CC Q03989; Q8WUN7: UBTD2; NbExp=3; IntAct=EBI-948603, EBI-12867288;
CC Q03989; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-948603, EBI-14096082;
CC Q03989; Q08AM6: VAC14; NbExp=3; IntAct=EBI-948603, EBI-2107455;
CC Q03989; O95231: VENTX; NbExp=5; IntAct=EBI-948603, EBI-10191303;
CC Q03989; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-948603, EBI-742550;
CC Q03989; Q15915: ZIC1; NbExp=3; IntAct=EBI-948603, EBI-11963196;
CC Q03989; Q96F45: ZNF503; NbExp=3; IntAct=EBI-948603, EBI-8832437;
CC Q03989; Q7L2R6-2: ZNF765; NbExp=3; IntAct=EBI-948603, EBI-12834294;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000269|PubMed:8649988}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q03989-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03989-5; Sequence=VSP_058969;
CC -!- PTM: Phosphorylated by MAPK14 on serine residues involving a TLR4
CC signaling pathway upon lipopolysaccharide (LPS) stimulation leading to
CC its ubiquitination and proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q3U108}.
CC -!- PTM: Ubiquitinated leading to proteasomal degradation; involving WWP1
CC linked to MAPK14-mediated phosphorylation upon LPS stimulation.
CC {ECO:0000250|UniProtKB:Q3U108}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36325.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M62324; AAA36325.1; ALT_INIT; mRNA.
DR EMBL; AC013270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471207; EAW71359.1; -; Genomic_DNA.
DR EMBL; BC047390; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS33251.1; -. [Q03989-1]
DR CCDS; CCDS82484.1; -. [Q03989-5]
DR PIR; S27962; S27962.
DR RefSeq; NP_001306021.1; NM_001319092.1. [Q03989-5]
DR RefSeq; NP_997646.1; NM_212481.2. [Q03989-1]
DR AlphaFoldDB; Q03989; -.
DR SMR; Q03989; -.
DR BioGRID; 116074; 132.
DR IntAct; Q03989; 125.
DR MINT; Q03989; -.
DR STRING; 9606.ENSP00000350078; -.
DR iPTMnet; Q03989; -.
DR PhosphoSitePlus; Q03989; -.
DR BioMuta; ARID5A; -.
DR DMDM; 148840818; -.
DR jPOST; Q03989; -.
DR MassIVE; Q03989; -.
DR MaxQB; Q03989; -.
DR PaxDb; Q03989; -.
DR PeptideAtlas; Q03989; -.
DR PRIDE; Q03989; -.
DR ProteomicsDB; 58234; -.
DR ProteomicsDB; 8111; -.
DR Antibodypedia; 1050; 219 antibodies from 18 providers.
DR DNASU; 10865; -.
DR Ensembl; ENST00000357485.8; ENSP00000350078.3; ENSG00000196843.17. [Q03989-1]
DR Ensembl; ENST00000454558.2; ENSP00000400785.1; ENSG00000196843.17. [Q03989-5]
DR GeneID; 10865; -.
DR KEGG; hsa:10865; -.
DR MANE-Select; ENST00000357485.8; ENSP00000350078.3; NM_212481.3; NP_997646.1.
DR UCSC; uc002swe.4; human. [Q03989-1]
DR UCSC; uc031ron.2; human.
DR CTD; 10865; -.
DR DisGeNET; 10865; -.
DR GeneCards; ARID5A; -.
DR HGNC; HGNC:17361; ARID5A.
DR HPA; ENSG00000196843; Low tissue specificity.
DR MIM; 611583; gene.
DR neXtProt; NX_Q03989; -.
DR OpenTargets; ENSG00000196843; -.
DR PharmGKB; PA134937822; -.
DR VEuPathDB; HostDB:ENSG00000196843; -.
DR eggNOG; KOG2744; Eukaryota.
DR GeneTree; ENSGT00940000161253; -.
DR InParanoid; Q03989; -.
DR OMA; ECGAKSM; -.
DR OrthoDB; 368297at2759; -.
DR PhylomeDB; Q03989; -.
DR TreeFam; TF324725; -.
DR PathwayCommons; Q03989; -.
DR SignaLink; Q03989; -.
DR BioGRID-ORCS; 10865; 30 hits in 1104 CRISPR screens.
DR ChiTaRS; ARID5A; human.
DR GenomeRNAi; 10865; -.
DR Pharos; Q03989; Tbio.
DR PRO; PR:Q03989; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q03989; protein.
DR Bgee; ENSG00000196843; Expressed in mucosa of stomach and 180 other tissues.
DR ExpressionAtlas; Q03989; baseline and differential.
DR Genevisible; Q03989; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; TAS:GDB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IDA:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IDA:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0035613; F:RNA stem-loop binding; IEA:Ensembl.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:GDB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IEA:Ensembl.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; 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; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
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 Activator; Alternative splicing; DNA-binding; Immunity; Innate immunity;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..594
FT /note="AT-rich interactive domain-containing protein 5A"
FT /id="PRO_0000288930"
FT DOMAIN 55..147
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 1..300
FT /note="Interaction with SOX9"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT CROSSLNK 85
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT CROSSLNK 94
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 2)"
FT /id="VSP_058969"
FT CONFLICT 392
FT /note="D -> G (in Ref. 4; BC047390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 64074 MW; 89A494C4560416FF CRC64;
MAAPVKGNRK QSTEGDALDP PASPKPAGKQ NGIQNPISLE DSPEAGGERE EEQEREEEQA
FLVSLYKFMK ERHTPIERVP HLGFKQINLW KIYKAVEKLG AYELVTGRRL WKNVYDELGG
SPGSTSAATC TRRHYERLVL PYVRHLKGED DKPLPTSKPR KQYKMAKENR GDDGATERPK
KAKEERRMDQ MMPGKTKADA ADPAPLPSQE PPRNSTEQQG LASGSSVSFV GASGCPEAYK
RLLSSFYCKG THGIMSPLAK KKLLAQVSKV EALQCQEEGC RHGAEPQASP AVHLPESPQS
PKGLTENSRH RLTPQEGLQA PGGSLREEAQ AGPCPAAPIF KGCFYTHPTE VLKPVSQHPR
DFFSRLKDGV LLGPPGKEGL SVKEPQLVWG GDANRPSAFH KGGSRKGILY PKPKACWVSP
MAKVPAESPT LPPTFPSSPG LGSKRSLEEE GAAHSGKRLR AVSPFLKEAD AKKCGAKPAG
SGLVSCLLGP ALGPVPPEAY RGTMLHCPLN FTGTPGPLKG QAALPFSPLV IPAFPAHFLA
TAGPSPMAAG LMHFPPTSFD SALRHRLCPA SSAWHAPPVT TYAAPHFFHL NTKL
