SMCA4_RAT
ID SMCA4_RAT Reviewed; 1613 AA.
AC Q8K1P7;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Transcription activator BRG1;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase SMARCA4;
DE AltName: Full=BRG1-associated factor 190A;
DE Short=BAF190A;
DE AltName: Full=Protein brahma homolog 1;
DE AltName: Full=SNF2-beta;
DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4;
GN Name=Smarca4; Synonyms=Baf190a, Brg1, Snf2b, Snf2l4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Hippocampus;
RA Hirsch O., Almeida O.F.X.;
RT "Isolation and characterization of the rat brahma related gene-1 (BRG-1).";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND INTERACTION WITH SS18L1; HDAC1; RB1 AND SP1.
RX PubMed=19081374; DOI=10.1016/j.neuron.2008.09.040;
RA Qiu Z., Ghosh A.;
RT "A calcium-dependent switch in a CREST-BRG1 complex regulates activity-
RT dependent gene expression.";
RL Neuron 60:775-787(2008).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-695; SER-699;
RP SER-1419; SER-1536; SER-1541; SER-1552; SER-1593 AND SER-1597, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in transcriptional activation and repression of
CC select genes by chromatin remodeling (alteration of DNA-nucleosome
CC topology). Component of SWI/SNF chromatin remodeling complexes that
CC carry out key enzymatic activities, changing chromatin structure by
CC altering DNA-histone contacts within a nucleosome in an ATP-dependent
CC manner. Component of the CREST-BRG1 complex, a multiprotein complex
CC that regulates promoter activation by orchestrating the calcium-
CC dependent release of a repressor complex and the recruitment of an
CC activator complex. In resting neurons, transcription of the c-FOS
CC promoter is inhibited by SMARCA4-dependent recruitment of a phospho-
CC RB1-HDAC repressor complex. Upon calcium influx, RB1 is
CC dephosphorylated by calcineurin, which leads to release of the
CC repressor complex. At the same time, there is increased recruitment of
CC CREBBP to the promoter by a CREST-dependent mechanism, which leads to
CC transcriptional activation. The CREST-BRG1 complex also binds to the
CC NR2B promoter, and activity-dependent induction of NR2B expression
CC involves the release of HDAC1 and recruitment of CREBBP. Belongs to the
CC neural progenitors-specific chromatin remodeling complex (npBAF
CC complex) and the neuron-specific chromatin remodeling complex (nBAF
CC complex). During neural development, a switch from a stem/progenitor to
CC a postmitotic chromatin remodeling mechanism occurs as neurons exit the
CC cell cycle and become committed to their adult state. The transition
CC from proliferating neural stem/progenitor cells to postmitotic neurons
CC requires a switch in subunit composition of the npBAF and nBAF
CC complexes. As neural progenitors exit mitosis and differentiate into
CC neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A,
CC are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
CC or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF
CC complex is essential for the self-renewal/proliferative capacity of the
CC multipotent neural stem cells. The nBAF complex along with CREST plays
CC a role regulating the activity of genes essential for dendrite growth.
CC SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation
CC by enhancing Notch-dependent proliferative signals, while concurrently
CC making the neural stem cell insensitive to SHH-dependent
CC differentiating cues. Acts as a corepressor of ZEB1 to regulate E-
CC cadherin transcription and is required for induction of epithelial-
CC mesenchymal transition (EMT) by ZEB1 (By similarity). Binds via DLX1 to
CC enhancers located in the intergenic region between DLX5 and DLX6 and
CC this binding is stabilized by the long non-coding RNA (lncRNA) Evf2 (By
CC similarity). Binds to RNA in a promiscuous manner (By similarity).
CC Binding to RNAs including lncRNA Evf2 leads to inhibition of SMARCA4
CC ATPase and chromatin remodeling activities (By similarity).
CC {ECO:0000250|UniProtKB:P51532, ECO:0000250|UniProtKB:Q3TKT4,
CC ECO:0000269|PubMed:19081374}.
CC -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes
CC SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The
CC canonical complex contains a catalytic subunit (either
CC SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1,
CC ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47.
CC Other subunits specific to each of the complexes may also be present
CC permitting several possible developmental- and tissue-specific
CC combinations. Component of the BAF complex, which includes at least
CC actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the
CC BAF complex also contains DPF3. Component of neural progenitors-
CC specific chromatin remodeling complex (npBAF complex) composed of at
CC least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific
CC chromatin remodeling complex (nBAF complex) composed of at least,
CC ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC DPF3/BAF45C, ACTL6B/BAF53B and actin. Component of the SWI/SNF-B (PBAF)
CC chromatin remodeling complex, at least composed of SMARCA4/BRG1,
CC SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57,
CC SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155,
CC SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin. Component of
CC SWI/SNF (GBAF) subcomplex, which includes at least BICRA or BICRAL
CC (mutually exclusive), BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A,
CC ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A. Component of the
CC BAF53 complex, at least composed of BAF53A, RUVBL1,
CC SMARCA4/BRG1/BAF190A, and TRRAP, which preferentially acetylates
CC histone H4 (and H2A) within nucleosomes (By similarity). Component of
CC the CREST-BRG1 complex, at least composed of SMARCA4/BRG1/BAF190A,
CC SS18L1/CREST, HDAC1, RB1 and SP1 (By similarity). Interacts with
CC PHF10/BAF45A (By similarity). Interacts with MYOG (By similarity).
CC Interacts directly with IKFZ1; the interaction associates IKFZ1 with
CC the BAF complex. Interacts with ZEB1 (via N-terminus). Interacts with
CC NR3C1, PGR, SMARD1, TOPBP1 and ZMIM2/ZIMP7. Interacts with (via the
CC bromodomain) with TERT; the interaction regulates Wnt-mediated
CC signaling (By similarity). Interacts with TBX21 in a KDM6B-dependent
CC manner (By similarity). Interacts with KDM6A and KDM6B (By similarity).
CC Interacts with HNRNPU; this interaction occurs in embryonic stem cells
CC and stimulates global Pol II-mediated transcription (By similarity).
CC Interacts with ACTL6A (By similarity). Interacts with DLX1 (By
CC similarity). Interacts with DPF2 (By similarity).
CC {ECO:0000250|UniProtKB:P51532, ECO:0000250|UniProtKB:Q3TKT4}.
CC -!- INTERACTION:
CC Q8K1P7; G3V612: Olig2; NbExp=2; IntAct=EBI-689301, EBI-6676662;
CC Q8K1P7; Q4KLI0: Smarcb1; NbExp=2; IntAct=EBI-689301, EBI-689316;
CC Q8K1P7; Q12824: SMARCB1; Xeno; NbExp=2; IntAct=EBI-689301, EBI-358419;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3TKT4}.
CC Note=Colocalizes with long non-coding RNA Evf2 in nuclear RNA clouds.
CC {ECO:0000250|UniProtKB:Q3TKT4}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AJ504723; CAD43278.1; -; mRNA.
DR AlphaFoldDB; Q8K1P7; -.
DR SMR; Q8K1P7; -.
DR IntAct; Q8K1P7; 4.
DR STRING; 10116.ENSRNOP00000013166; -.
DR iPTMnet; Q8K1P7; -.
DR PhosphoSitePlus; Q8K1P7; -.
DR jPOST; Q8K1P7; -.
DR PaxDb; Q8K1P7; -.
DR PRIDE; Q8K1P7; -.
DR UCSC; RGD:621728; rat.
DR RGD; 621728; Smarca4.
DR eggNOG; KOG0386; Eukaryota.
DR InParanoid; Q8K1P7; -.
DR PhylomeDB; Q8K1P7; -.
DR Reactome; R-RNO-1266695; Interleukin-7 signaling.
DR Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-RNO-3214858; RMTs methylate histone arginines.
DR Reactome; R-RNO-3247509; Chromatin modifying enzymes.
DR Reactome; R-RNO-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR PRO; PR:Q8K1P7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0000792; C:heterochromatin; ISO:RGD.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005726; C:perichromatin fibrils; ISO:RGD.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:RGD.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:RGD.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0106222; F:lncRNA binding; ISO:RGD.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISO:RGD.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:RGD.
DR GO; GO:0002039; F:p53 binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0030957; F:Tat protein binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0035904; P:aorta development; ISO:RGD.
DR GO; GO:0035887; P:aortic smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0001832; P:blastocyst growth; ISO:RGD.
DR GO; GO:0001835; P:blastocyst hatching; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:RGD.
DR GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR GO; GO:0060318; P:definitive erythrocyte differentiation; ISO:RGD.
DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; ISO:RGD.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; ISO:RGD.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; ISO:RGD.
DR GO; GO:0048562; P:embryonic organ morphogenesis; ISO:RGD.
DR GO; GO:0048730; P:epidermis morphogenesis; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0007403; P:glial cell fate determination; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0060347; P:heart trabecula formation; ISO:RGD.
DR GO; GO:0030902; P:hindbrain development; ISO:RGD.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0070307; P:lens fiber cell development; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:RGD.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0003407; P:neural retina development; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:RGD.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:RGD.
DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; ISO:RGD.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:RGD.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:RGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; ISO:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IEA:GOC.
DR GO; GO:0007286; P:spermatid development; IEP:RGD.
DR GO; GO:0019827; P:stem cell population maintenance; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR GO; GO:0003281; P:ventricular septum development; ISO:RGD.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030100; BRG1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF76; PTHR10799:SF76; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; SSF160481; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; ATP-binding; Bromodomain; Chromatin regulator;
KW Helicase; Hydrolase; Isopeptide bond; Neurogenesis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1613
FT /note="Transcription activator BRG1"
FT /id="PRO_0000391344"
FT DOMAIN 171..206
FT /note="QLQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001"
FT DOMAIN 460..532
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 766..931
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1084..1246
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1443..1513
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..282
FT /note="Necessary for interaction with SS18L1/CREST"
FT /evidence="ECO:0000269|PubMed:19081374"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..728
FT /note="RNA-binding region which is sufficient for binding
FT to lncRNA Evf2"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT REGION 577..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..916
FT /note="Sufficient for interaction with DLX1"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT REGION 1247..1413
FT /note="Sufficient for interaction with DLX1"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT REGION 1366..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 881..884
FT /note="DEGH box"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..674
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1552
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1613
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 779..786
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 1505..1506
FT /note="Required for binding to 'Lys-15'-acetylated histone
FT 3"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 188
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 353
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 626
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6DIC0"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1390
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT MOD_RES 1419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 1332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51532"
SQ SEQUENCE 1613 AA; 181427 MW; 7E5F1B04D4C26C87 CRC64;
MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPMPTQG
PGGYPQDNMH QMHKPMESMH EKGMPDDPRY NQMKGMGMRS GAHTGMGPPP SPMDQHSQGY
PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGSDPQ ALGQQNRGPT PFNQNQLHQL
RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP
GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ
KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PLVPLHQKQS RITPIQKPRG
LDPVEILQER EYRLQARIVH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV
VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL
QHAKDFREYH RSVTGKLQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK
LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG
PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES
GSEEEEEEEE EEQPQPAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA KQDVDDEYGV
SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE
MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA
RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH
YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT GEKVDLNEEE
TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH MQAKGVLLTD
GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV QGLDLYRASG
KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK
TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR
VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI LEHEEQDEEE
DEVPDDETVN QMIARHEEEF DLFMRMDLDR RREEARNPKR KPRLMEEDEL PSWIIKDDAE
VERLTCEEEE EKMFGRGSRH RKEVDYSDSL TEKQWLKAIE EGTLEEIEEE VRQKKSSRKR
KRDSEAGSST PTTSTRSRDK DEESKKQKKR GRPPAEKLSP NPPNLTKKMK KIVDAVIKYK
DSSGRQLSEV FIQLPSRKEL PEYYELIRKP VDFKKIKERI RNHKYRSLND LEKDVMLLCQ
NAQTFNLEGS LIYEDSIVLQ SVFTSVRQKI EKEDDSEGEE SEEEEEGEEE GSESESRSVK
VKIKLGRKEK AQDRLKGGRR RPSRGSRAKP VVSDDDSDEE QEEDRSGSGS EED
