ARI4A_HUMAN
ID ARI4A_HUMAN Reviewed; 1257 AA.
AC P29374; Q15991; Q15992; Q15993;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=AT-rich interactive domain-containing protein 4A;
DE Short=ARID domain-containing protein 4A;
DE AltName: Full=Retinoblastoma-binding protein 1;
DE Short=RBBP-1;
GN Name=ARID4A; Synonyms=RBBP1, RBP1;
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 I), INTERACTION WITH RB1, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION, AND VARIANT ALA-779.
RX PubMed=8414517;
RA Fattaey A.R., Helin K., Dembski M.S., Dyson N., Harlow E., Vuocolo G.A.,
RA Hanobik M.G., Haskell K.M., Oliff A., Defeo-Jones D., Jones R.E.;
RT "Characterization of the retinoblastoma binding proteins RBP1 and RBP2.";
RL Oncogene 8:3149-3156(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 338-1257 (ISOFORMS I; II AND III),
RP INTERACTION WITH RB1, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=8455946;
RA Otterson G.A., Kratzke R.A., Lin A.Y., Johnston P.G., Kaye F.J.;
RT "Alternative splicing of the RBP1 gene clusters in an internal exon that
RT encodes potential phosphorylation sites.";
RL Oncogene 8:949-957(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 855-1203 (ISOFORM I).
RX PubMed=1857421; DOI=10.1038/352251a0;
RA Defeo-Jones D., Huang P.S., Jones R.E., Haskell K.M., Vuocolo G.A.,
RA Hanobik M.G., Huber H.E., Oliff A.;
RT "Cloning of cDNAs for cellular proteins that bind to the retinoblastoma
RT gene product.";
RL Nature 352:251-254(1991).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH SIN3A; SIN3B; HDAC1; HDAC2; SAP30; BRMS1;
RP RBBP4 AND RBBP7.
RX PubMed=14581478; DOI=10.1074/jbc.m307969200;
RA Meehan W.J., Samant R.S., Hopper J.E., Carrozza M.J., Shevde L.A.,
RA Workman J.L., Eckert K.A., Verderame M.F., Welch D.R.;
RT "Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with
RT retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase
RT complex and represses transcription.";
RL J. Biol. Chem. 279:1562-1569(2004).
RN [6]
RP INTERACTION WITH ARID4B.
RX PubMed=17043311; DOI=10.1101/gad.1452206;
RA Wu M.Y., Tsai T.F., Beaudet A.L.;
RT "Deficiency of Rbbp1/Arid4a and Rbbp1l1/Arid4b alters epigenetic
RT modifications and suppresses an imprinting defect in the PWS/AS domain.";
RL Genes Dev. 20:2859-2870(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676 AND SER-1109, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716; SER-864 AND SER-1145,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [13]
RP INTERACTION WITH AR.
RX PubMed=23487765; DOI=10.1073/pnas.1218318110;
RA Wu R.C., Jiang M., Beaudet A.L., Wu M.Y.;
RT "ARID4A and ARID4B regulate male fertility, a functional link to the AR and
RT RB pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:4616-4621(2013).
RN [14]
RP IDENTIFICATION BY 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481, 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481 AND LYS-718, 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-513; LYS-718; LYS-738 AND
RP LYS-759, AND IDENTIFICATION BY 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 [18]
RP STRUCTURE BY NMR OF 170-273.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RBB1NT domain of human RB(Retinoblastoma)-
RT binding protein 1.";
RL Submitted (APR-2008) to the PDB data bank.
RN [19] {ECO:0007744|PDB:2LCC}
RP STRUCTURE BY NMR OF 568-635, DOMAIN, AND MUTAGENESIS OF TYR-583; TYR-592;
RP TYR-612; TRP-615 AND TYR-619.
RX PubMed=22247551; DOI=10.1074/jbc.m111.299149;
RA Gong W., Zhou T., Mo J., Perrett S., Wang J., Feng Y.;
RT "Structural insight into recognition of methylated histone tails by
RT retinoblastoma-binding protein 1.";
RL J. Biol. Chem. 287:8531-8540(2012).
RN [20] {ECO:0007744|PDB:2MAM}
RP STRUCTURE BY NMR OF 4-121, AND DNA-BINDING.
RX PubMed=24379399; DOI=10.1074/jbc.m113.501940;
RA Gong W., Wang J., Perrett S., Feng Y.;
RT "Retinoblastoma-binding protein 1 has an interdigitated double Tudor domain
RT with DNA binding activity.";
RL J. Biol. Chem. 289:4882-4895(2014).
RN [21] {ECO:0007744|PDB:6BPH}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 568-635, AND DOMAIN.
RX PubMed=29408527; DOI=10.1016/j.bbrc.2018.02.016;
RA Lei M., Feng Y., Zhou M., Yang Y., Loppnau P., Li Y., Yang Y., Liu Y.;
RT "Crystal structure of chromo barrel domain of RBBP1.";
RL Biochem. Biophys. Res. Commun. 496:1344-1348(2018).
CC -!- FUNCTION: DNA-binding protein which modulates activity of several
CC transcription factors including RB1 (retinoblastoma-associated protein)
CC and AR (androgen receptor) (By similarity). May function as part of an
CC mSin3A repressor complex (PubMed:14581478). Has no intrinsic
CC transcriptional activity (By similarity). Plays a role in the
CC regulation of epigenetic modifications at the PWS/AS imprinting center
CC near the SNRPN promoter, where it might function as part of a complex
CC with RB1 and ARID4B (By similarity). Involved in spermatogenesis,
CC together with ARID4B, where it acts as a transcriptional coactivator
CC for AR and enhances expression of genes required for sperm maturation.
CC Regulates expression of the tight junction protein CLDN3 in the testis,
CC which is important for integrity of the blood-testis barrier (By
CC similarity). Plays a role in myeloid homeostasis where it regulates the
CC histone methylation state of bone marrow cells and expression of
CC various genes involved in hematopoiesis. May function as a leukemia
CC suppressor (By similarity). {ECO:0000250|UniProtKB:F8VPQ2,
CC ECO:0000269|PubMed:14581478}.
CC -!- SUBUNIT: Identified in mSin3A corepressor complexes together with
CC SIN3A, SIN3B, RBBP4, RBBP7, SAP30, BRMS1, HDAC1 and HDAC2
CC (PubMed:14581478). Interacts with BRMS1 (PubMed:14581478). Interacts
CC with RB1 (PubMed:8414517, PubMed:8455946). Interacts with ARID4B
CC (PubMed:17043311). Interacts with AR (PubMed:23487765).
CC {ECO:0000269|PubMed:14581478, ECO:0000269|PubMed:17043311,
CC ECO:0000269|PubMed:23487765, ECO:0000269|PubMed:8414517,
CC ECO:0000269|PubMed:8455946}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000269|PubMed:8414517, ECO:0000269|PubMed:8455946}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=I;
CC IsoId=P29374-1; Sequence=Displayed;
CC Name=II;
CC IsoId=P29374-2; Sequence=VSP_004373;
CC Name=III;
CC IsoId=P29374-3; Sequence=VSP_004371, VSP_004372;
CC -!- DOMAIN: The function of the Tudor-knot domain, also named chromodomain-
CC like, is uncertain (PubMed:22247551, PubMed:29408527). One study
CC suggests that it mediates binding to lysine-methylated histone tails,
CC with strongest affinity for H4K20me3 and H3K36me3 (PubMed:22247551).
CC However, another study failed to find any interaction between this
CC domain and histone H4K20me3 peptide (PubMed:29408527).
CC {ECO:0000269|PubMed:22247551, ECO:0000269|PubMed:29408527}.
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DR EMBL; S66427; AAB28543.1; -; mRNA.
DR EMBL; AL132989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S57153; AAB25833.1; -; mRNA.
DR EMBL; S57160; AAB25834.1; -; mRNA.
DR EMBL; S57162; AAB25835.2; -; mRNA.
DR CCDS; CCDS45114.1; -. [P29374-2]
DR CCDS; CCDS9732.1; -. [P29374-1]
DR CCDS; CCDS9733.1; -. [P29374-3]
DR PIR; I58383; I58383.
DR RefSeq; NP_002883.3; NM_002892.3. [P29374-1]
DR RefSeq; NP_075376.2; NM_023000.2. [P29374-2]
DR RefSeq; NP_075377.2; NM_023001.2. [P29374-3]
DR PDB; 2LCC; NMR; -; A=568-635.
DR PDB; 2MAM; NMR; -; A=4-121.
DR PDB; 2YRV; NMR; -; A=170-273.
DR PDB; 6BPH; X-ray; 1.85 A; A=568-635.
DR PDB; 6L87; NMR; -; A=171-414.
DR PDBsum; 2LCC; -.
DR PDBsum; 2MAM; -.
DR PDBsum; 2YRV; -.
DR PDBsum; 6BPH; -.
DR PDBsum; 6L87; -.
DR AlphaFoldDB; P29374; -.
DR BMRB; P29374; -.
DR SMR; P29374; -.
DR BioGRID; 111861; 55.
DR ComplexPortal; CPX-3321; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
DR CORUM; P29374; -.
DR DIP; DIP-463N; -.
DR IntAct; P29374; 20.
DR MINT; P29374; -.
DR STRING; 9606.ENSP00000347602; -.
DR ChEMBL; CHEMBL3709855; -.
DR iPTMnet; P29374; -.
DR PhosphoSitePlus; P29374; -.
DR BioMuta; ARID4A; -.
DR DMDM; 206729929; -.
DR EPD; P29374; -.
DR jPOST; P29374; -.
DR MassIVE; P29374; -.
DR MaxQB; P29374; -.
DR PaxDb; P29374; -.
DR PeptideAtlas; P29374; -.
DR PRIDE; P29374; -.
DR ProteomicsDB; 54556; -. [P29374-1]
DR ProteomicsDB; 54557; -. [P29374-2]
DR ProteomicsDB; 54558; -. [P29374-3]
DR Antibodypedia; 11317; 60 antibodies from 19 providers.
DR DNASU; 5926; -.
DR Ensembl; ENST00000348476.7; ENSP00000344556.3; ENSG00000032219.19. [P29374-3]
DR Ensembl; ENST00000355431.8; ENSP00000347602.3; ENSG00000032219.19. [P29374-1]
DR Ensembl; ENST00000395168.7; ENSP00000378597.3; ENSG00000032219.19. [P29374-2]
DR Ensembl; ENST00000431317.6; ENSP00000397368.2; ENSG00000032219.19. [P29374-3]
DR GeneID; 5926; -.
DR KEGG; hsa:5926; -.
DR MANE-Select; ENST00000355431.8; ENSP00000347602.3; NM_002892.4; NP_002883.3.
DR UCSC; uc001xdo.4; human. [P29374-1]
DR CTD; 5926; -.
DR DisGeNET; 5926; -.
DR GeneCards; ARID4A; -.
DR HGNC; HGNC:9885; ARID4A.
DR HPA; ENSG00000032219; Low tissue specificity.
DR MIM; 180201; gene.
DR neXtProt; NX_P29374; -.
DR OpenTargets; ENSG00000032219; -.
DR PharmGKB; PA34249; -.
DR VEuPathDB; HostDB:ENSG00000032219; -.
DR eggNOG; KOG2744; Eukaryota.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00940000156159; -.
DR HOGENOM; CLU_007419_1_0_1; -.
DR InParanoid; P29374; -.
DR OMA; MSPHIKD; -.
DR OrthoDB; 329541at2759; -.
DR PhylomeDB; P29374; -.
DR TreeFam; TF106427; -.
DR PathwayCommons; P29374; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; P29374; -.
DR SIGNOR; P29374; -.
DR BioGRID-ORCS; 5926; 35 hits in 1119 CRISPR screens.
DR ChiTaRS; ARID4A; human.
DR EvolutionaryTrace; P29374; -.
DR GeneWiki; ARID4A; -.
DR GenomeRNAi; 5926; -.
DR Pharos; P29374; Tbio.
DR PRO; PR:P29374; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P29374; protein.
DR Bgee; ENSG00000032219; Expressed in calcaneal tendon and 196 other tissues.
DR ExpressionAtlas; P29374; baseline and differential.
DR Genevisible; P29374; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:GDB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0017053; C:transcription repressor complex; IDA:GDB.
DR GO; GO:0003677; F:DNA binding; IDA:GDB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; IEA:Ensembl.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IEA:Ensembl.
DR GO; GO:0036124; P:histone H3-K9 trimethylation; IEA:Ensembl.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:GDB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR012603; RBB1NT.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR025995; Tudor-knot.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF08169; RBB1NT; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51011; ARID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Differentiation;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1257
FT /note="AT-rich interactive domain-containing protein 4A"
FT /id="PRO_0000200580"
FT DOMAIN 309..401
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 576..628
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT REGION 4..121
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:24379399"
FT REGION 141..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..964
FT /note="Retinoblastoma protein binding"
FT /evidence="ECO:0000255"
FT REGION 1063..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364"
FT CROSSLNK 513
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 718
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 738
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 759
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1106..1174
FT /note="Missing (in isoform III)"
FT /evidence="ECO:0000303|PubMed:8455946"
FT /id="VSP_004371"
FT VAR_SEQ 1121..1174
FT /note="Missing (in isoform II)"
FT /evidence="ECO:0000303|PubMed:8455946"
FT /id="VSP_004373"
FT VAR_SEQ 1175
FT /note="N -> D (in isoform III)"
FT /evidence="ECO:0000303|PubMed:8455946"
FT /id="VSP_004372"
FT VARIANT 412
FT /note="H -> P (in dbSNP:rs34982206)"
FT /id="VAR_031566"
FT VARIANT 724
FT /note="N -> S (in dbSNP:rs2230098)"
FT /id="VAR_031567"
FT VARIANT 779
FT /note="T -> A (in dbSNP:rs1051858)"
FT /evidence="ECO:0000269|PubMed:8414517"
FT /id="VAR_031568"
FT MUTAGEN 583
FT /note="Y->A: No effect on binding to trimethylated
FT lysines."
FT /evidence="ECO:0000269|PubMed:22247551"
FT MUTAGEN 592
FT /note="Y->A: Significantly reduces affinity for
FT trimethylated lysines."
FT /evidence="ECO:0000269|PubMed:22247551"
FT MUTAGEN 612
FT /note="Y->A: Abolishes binding to trimethylated lysines."
FT /evidence="ECO:0000269|PubMed:22247551"
FT MUTAGEN 615
FT /note="W->A: Abolishes binding to trimethylated lysines."
FT /evidence="ECO:0000269|PubMed:22247551"
FT MUTAGEN 619
FT /note="Y->A: Abolishes binding to trimethylated lysines."
FT /evidence="ECO:0000269|PubMed:22247551"
FT CONFLICT 385
FT /note="V -> L (in Ref. 1; AAB28543)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="R -> S (in Ref. 1; AAB28543)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="K -> V (in Ref. 3; AAB25833/AAB25834/AAB25835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1178
FT /note="D -> S (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1196..1201
FT /note="IRKYYM -> SENIICL (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2MAM"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:2MAM"
FT STRAND 23..42
FT /evidence="ECO:0007829|PDB:2MAM"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2MAM"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2MAM"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:2MAM"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2MAM"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:2MAM"
FT STRAND 75..93
FT /evidence="ECO:0007829|PDB:2MAM"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2MAM"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2MAM"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2MAM"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:6L87"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:2YRV"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:2YRV"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6L87"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:2YRV"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2YRV"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:2YRV"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6L87"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:2YRV"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:2YRV"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:2YRV"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:2YRV"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:6L87"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:6L87"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:6L87"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:6L87"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6L87"
FT HELIX 362..372
FT /evidence="ECO:0007829|PDB:6L87"
FT HELIX 379..392
FT /evidence="ECO:0007829|PDB:6L87"
FT HELIX 394..402
FT /evidence="ECO:0007829|PDB:6L87"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:6L87"
FT STRAND 578..584
FT /evidence="ECO:0007829|PDB:6BPH"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:6BPH"
FT STRAND 590..602
FT /evidence="ECO:0007829|PDB:6BPH"
FT STRAND 605..612
FT /evidence="ECO:0007829|PDB:6BPH"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:6BPH"
FT STRAND 621..624
FT /evidence="ECO:0007829|PDB:6BPH"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:6BPH"
SQ SEQUENCE 1257 AA; 142752 MW; 5B3F6A5AFB7588CF CRC64;
MKAADEPAYL TVGTDVSAKY RGAFCEAKIK TVKRLVKVKV LLKQDNTTQL VQDDQVKGPL
RVGAIVETRT SDGSFQEAII SKLTDASWYT VVFDDGDERT LRRTSLCLKG ERHFAESETL
DQLPLTNPEH FGTPVIAKKT NRGRRSSLPV TEDEKEEESS EEEDEDKRRL NDELLGKVVS
VVSATERTEW YPALVISPSC NDDITVKKDQ CLVRSFIDSK FYSIARKDIK EVDILNLPES
ELSTKPGLQK ASIFLKTRVV PDNWKMDISE ILESSSSDDE DGPAEENDEE KEKEAKKTEE
EVPEEELDPE ERDNFLQQLY KFMEDRGTPI NKPPVLGYKD LNLFKLFRLV YHQGGCDNID
SGAVWKQIYM DLGIPILNSA ASYNVKTAYR KYLYGFEEYC RSANIQFRTV HHHEPKVKEE
KKDLEESMEE ALKLDQEMPL TEVKSEPEEN IDSNSESERE EIELKSPRGR RRIARDVNSI
KKEIEEEKTE DKLKDNDTEN KDVDDDYETA EKKENELLLG RKNTPKQKEK KIKKQEDSDK
DSDEEEEKSQ EREETESKCD SEGEEDEEDM EPCLTGTKVK VKYGRGKTQK IYEASIKSTE
IDDGEVLYLV HYYGWNVRYD EWVKADRIIW PLDKGGPKKK QKKKAKNKED SEKDEKRDEE
RQKSKRGRPP LKSTLSSNMP YGLSKTANSE GKSDSCSSDS ETEDALEKNL INEELSLKDE
LEKNENLNDD KLDEENPKIS AHILKENDRT QMQPLETLKL EVGENEQIVQ IFGNKMEKTE
EVKKEAEKSP KGKGRRSKTK DLSLEIIKIS SFGQNEAGSE PHIEAHSLEL SSLDNKNFSS
ATEDEIDQCV KEKKLKRKIL GQSSPEKKIR IENGMEMTNT VSQERTSDCI GSEGMKNLNF
EQHFERENEG MPSLIAESNQ CIQQLTSERF DSPAEETVNI PLKEDEDAMP LIGPETLVCH
EVDLDDLDEK DKTSIEDVAV ESSESNSLVS IPPALPPVVQ HNFSVASPLT LSQDESRSVK
SESDITIEVD SIAEESQEGL CERESANGFE TNVASGTCSI IVQERESREK GQKRPSDGNS
GLMAKKQKRT PKRTSAAAKN EKNGTGQSSD SEDLPVLDNS SKCTPVKHLN VSKPQKLARS
PARISPHIKD GEKDKHREKH PNSSPRTYKW SFQLNELDNM NSTERISFLQ EKLQEIRKYY
MSLKSEVATI DRRRKRLKKK DREVSHAGAS MSSASSDTGM SPSSSSPPQN VLAVECR
