HM20B_MOUSE
ID HM20B_MOUSE Reviewed; 317 AA.
AC Q9Z104; Q9NSF7; Q9NSF8;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related;
DE Short=SMARCE1-related protein;
DE AltName: Full=BRCA2-associated factor 35;
DE AltName: Full=HMG box-containing protein 20B;
DE AltName: Full=Structural DNA-binding protein BRAF35;
GN Name=Hmg20b; Synonyms=Braf35, Hmgx2, Smarce1r;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10486208; DOI=10.1006/geno.1999.5913;
RA Wattler F., Wattler S., Kelly M., Skinner H.B., Nehls M.;
RT "Cloning, chromosomal location, and expression analysis of murine Smarce1-
RT related, a new member of the high-mobility 365 group gene family.";
RL Genomics 60:172-178(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10773667; DOI=10.1159/000015486;
RA Sumoy L., Carim-Todd L., Escarceller M., Nadal M., Gratacos M.,
RA Pujana M.A., Estivill X., Peral B.;
RT "HMG20A and HMG20B map to human chromosomes 15q24 and 19p13.3 and
RT constitute a distinct class of HMG-box genes with ubiquitous expression.";
RL Cytogenet. Cell Genet. 88:62-67(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH DTNB.
RX PubMed=20530487; DOI=10.1074/jbc.m109.090654;
RA Artegiani B., Labbaye C., Sferra A., Quaranta M.T., Torreri P., Macchia G.,
RA Ceccarini M., Petrucci T.C., Macioce P.;
RT "The interaction with HMG20a/b proteins suggests a potential role for beta-
RT dystrobrevin in neuronal differentiation.";
RL J. Biol. Chem. 285:24740-24750(2010).
RN [5]
RP STRUCTURE BY NMR OF 69-148.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the HMG domain of mouse HMG domain protein HMGX2.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Required for correct progression through G2 phase of the cell
CC cycle and entry into mitosis. Required for RCOR1/CoREST mediated
CC repression of neuronal specific gene promoters (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of a BHC histone deacetylase complex that contains
CC HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The
CC BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC Interacts with the BRCA2 tumor suppressor protein (By similarity).
CC Interacts with DTNB (PubMed:20530487). {ECO:0000250,
CC ECO:0000269|PubMed:20530487}.
CC -!- INTERACTION:
CC Q9Z104; P39428: Traf1; NbExp=3; IntAct=EBI-646920, EBI-520123;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC Chromosome {ECO:0000250}. Note=Localized to condensed chromosomes in
CC mitosis in conjunction with BRCA2. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues, particularly
CC kidney, skin, testis and uterus. Highly expressed in embryonic tissues
CC with high mitotic index, such as the proliferating ventricular zones of
CC the fore-, mid- and hindbrain.
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DR EMBL; AF067430; AAD15897.1; -; Genomic_DNA.
DR EMBL; AF146224; AAF66708.1; -; mRNA.
DR EMBL; AL355734; CAB90813.1; -; mRNA.
DR EMBL; AL355735; CAB90814.1; -; mRNA.
DR EMBL; BC011334; AAH11334.1; -; mRNA.
DR CCDS; CCDS24055.1; -.
DR RefSeq; NP_001156637.1; NM_001163165.1.
DR RefSeq; NP_001156638.1; NM_001163166.1.
DR RefSeq; NP_034570.1; NM_010440.3.
DR PDB; 2CRJ; NMR; -; A=70-148.
DR PDBsum; 2CRJ; -.
DR AlphaFoldDB; Q9Z104; -.
DR SMR; Q9Z104; -.
DR BioGRID; 200335; 6.
DR IntAct; Q9Z104; 1.
DR STRING; 10090.ENSMUSP00000020454; -.
DR iPTMnet; Q9Z104; -.
DR PhosphoSitePlus; Q9Z104; -.
DR EPD; Q9Z104; -.
DR MaxQB; Q9Z104; -.
DR PaxDb; Q9Z104; -.
DR PRIDE; Q9Z104; -.
DR ProteomicsDB; 273180; -.
DR Antibodypedia; 23254; 309 antibodies from 34 providers.
DR DNASU; 15353; -.
DR Ensembl; ENSMUST00000020454; ENSMUSP00000020454; ENSMUSG00000020232.
DR Ensembl; ENSMUST00000105323; ENSMUSP00000100960; ENSMUSG00000020232.
DR Ensembl; ENSMUST00000105324; ENSMUSP00000100961; ENSMUSG00000020232.
DR Ensembl; ENSMUST00000167481; ENSMUSP00000128807; ENSMUSG00000020232.
DR GeneID; 15353; -.
DR KEGG; mmu:15353; -.
DR UCSC; uc007ghj.2; mouse.
DR CTD; 10362; -.
DR MGI; MGI:1341190; Hmg20b.
DR VEuPathDB; HostDB:ENSMUSG00000020232; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000161213; -.
DR InParanoid; Q9Z104; -.
DR OMA; NIDRYMH; -.
DR OrthoDB; 1458939at2759; -.
DR PhylomeDB; Q9Z104; -.
DR TreeFam; TF106440; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 15353; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Hmg20b; mouse.
DR EvolutionaryTrace; Q9Z104; -.
DR PRO; PR:Q9Z104; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9Z104; protein.
DR Bgee; ENSMUSG00000020232; Expressed in interventricular septum and 196 other tissues.
DR ExpressionAtlas; Q9Z104; baseline and differential.
DR Genevisible; Q9Z104; MM.
DR GO; GO:0002111; C:BRCA2-BRAF35 complex; ISO:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; NAS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; TAS:ProtInc.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IGI:MGI.
DR GO; GO:0016925; P:protein sumoylation; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Chromatin regulator; Chromosome; Coiled coil;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..317
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily E member 1-related"
FT /id="PRO_0000048576"
FT DNA_BIND 70..138
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..257
FT /evidence="ECO:0000255"
FT COMPBIAS 35..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0W2"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P0W2"
FT HELIX 76..91
FT /evidence="ECO:0007829|PDB:2CRJ"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:2CRJ"
FT HELIX 115..138
FT /evidence="ECO:0007829|PDB:2CRJ"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:2CRJ"
SQ SEQUENCE 317 AA; 35870 MW; 6C4D45D2EB1D403B CRC64;
MSHGPRQPGA ATAPAGGKTP GQHGAFVVAV KQERSEGSRA GEKGPQEEEP VKKRGWPKGK
KRKKILPNGP KAPVTGYVRF LNERREQIRT RHPDLPFPEI TKMLGAEWSK LQPAEKQRYL
DEAEKEKQQY LKELWAYQQS EAYKVCTEKI QENKIKKEDS SSGLMNTLLN GHKGVDCDGF
STFDVPIFTE EFLDQNKARE AELRRLRKMN VAFEEQNAVL QRHTQSMSSA RERLEQELAL
EERRTLALQQ QLQAVRQALT ASFASLPVPG TGETPTLGTL DFYMARLHGA IERDPAQHER
LIARVKEILA RVASEHL
