HM20B_BOVIN
ID HM20B_BOVIN Reviewed; 317 AA.
AC Q32L68;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=HMG box-containing protein 20B;
GN Name=HMG20B; Synonyms=SMARCE1R;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
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}.
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DR EMBL; BC109740; AAI09741.1; -; mRNA.
DR RefSeq; NP_001033143.1; NM_001038054.1.
DR AlphaFoldDB; Q32L68; -.
DR SMR; Q32L68; -.
DR STRING; 9913.ENSBTAP00000011581; -.
DR PaxDb; Q32L68; -.
DR PRIDE; Q32L68; -.
DR Ensembl; ENSBTAT00000011581; ENSBTAP00000011581; ENSBTAG00000008789.
DR GeneID; 507723; -.
DR KEGG; bta:507723; -.
DR CTD; 10362; -.
DR VEuPathDB; HostDB:ENSBTAG00000008789; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000161213; -.
DR HOGENOM; CLU_060006_2_0_1; -.
DR InParanoid; Q32L68; -.
DR OMA; NIDRYMH; -.
DR OrthoDB; 1458939at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000008789; Expressed in digestive system secreted substance and 106 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell cycle; Chromatin regulator; Chromosome; Coiled coil; DNA-binding;
KW 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_0000281860"
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"
SQ SEQUENCE 317 AA; 35829 MW; E1A34C1F58D17008 CRC64;
MSHGPKQPGA ASAPASGKAP GQHGSFVVAV KQERGEGPRA GEKGSHEEEP VKKRGWPKGK
KRKKILPNGP KAPVTGYVRF LNERREQIRT RHPDLPFPEI TKMLGAEWSK LQPAEKQRYL
DEAEREKQQY MKELRAYQQS EAYKMCAEKI QEKKIKKEDS SSGLMNTLLN GHKGGDCDGF
STFDVPIFTE EFLDQNKARE AELRRLRKMN VAFEEQNAVL QRHTQSMSSA RERLEQELAL
EERRTLALQQ QLQAVRQALT ASFASLPVPG TGETPTLSTL DFYMARLHGA IERDPAQHEK
LIVRIKEILA QVASEHL