SNF5_BOVIN
ID SNF5_BOVIN Reviewed; 385 AA.
AC Q5BIN2; A2VE50;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;
DE AltName: Full=BRG1-associated factor 47;
DE Short=BAF47;
GN Name=SMARCB1; Synonyms=BAF47;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal medulla;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Core component of the BAF (SWI/SNF) complex. This ATP-
CC dependent chromatin-remodeling complex plays important roles in cell
CC proliferation and differentiation, in cellular antiviral activities and
CC inhibition of tumor formation. The BAF complex is able to create a
CC stable, altered form of chromatin that constrains fewer negative
CC supercoils than normal. This change in supercoiling would be due to the
CC conversion of up to one-half of the nucleosomes on polynucleosomal
CC arrays into asymmetric structures, termed altosomes, each composed of 2
CC histones octamers. Stimulates in vitro the remodeling activity of
CC SMARCA4/BRG1/BAF190A. Plays a key role in cell-cycle control and causes
CC cell cycle arrest in G0/G1. Belongs to the neural progenitors-specific
CC chromatin remodeling complex (npBAF complex) and the neuron-specific
CC chromatin remodeling complex (nBAF complex). During neural development
CC a switch from a stem/progenitor to a postmitotic chromatin remodeling
CC mechanism occurs as neurons exit the cell cycle and become committed to
CC their adult state. The transition from proliferating neural
CC stem/progenitor cells to postmitotic neurons requires a switch in
CC subunit composition of the npBAF and nBAF complexes. As neural
CC progenitors exit mitosis and differentiate into neurons, npBAF
CC complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged
CC for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C
CC subunits in neuron-specific complexes (nBAF). The npBAF complex is
CC 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 (By similarity). {ECO:0000250|UniProtKB:Q12824}.
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 combinations developmentally and tissue
CC specific (By similarity). Component of the BAF complex, which includes
CC at least 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 (By similarity). Component of neural
CC progenitors-specific chromatin remodeling complex (npBAF complex)
CC composed of at 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 (By similarity). Component of the
CC SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of
CC SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B,
CC SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C,
CC SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin.
CC Binds to double-stranded DNA. Interacts with CEBPB (when not
CC methylated). Interacts with PIH1D1. Interacts with MYK and MAEL.
CC Interacts with PPP1R15A (By similarity). Interacts with DPF2 (By
CC similarity). Interacts with YWHAZ (By similarity). Interacts with ERCC6
CC (By similarity). Interacts with FOS, FOSB, FOSL1 and FOSL2 (By
CC similarity). {ECO:0000250|UniProtKB:Q12824,
CC ECO:0000250|UniProtKB:Q9Z0H3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The N-terminal DNA-binding region is structurally similar to
CC winged helix domains. {ECO:0000250|UniProtKB:Q12824}.
CC -!- SIMILARITY: Belongs to the SNF5 family. {ECO:0000305}.
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DR EMBL; BT021192; AAX31374.1; -; mRNA.
DR EMBL; BC133572; AAI33573.1; -; mRNA.
DR RefSeq; NP_001035647.1; NM_001040557.2.
DR AlphaFoldDB; Q5BIN2; -.
DR BMRB; Q5BIN2; -.
DR SMR; Q5BIN2; -.
DR STRING; 9913.ENSBTAP00000013170; -.
DR PaxDb; Q5BIN2; -.
DR PRIDE; Q5BIN2; -.
DR Ensembl; ENSBTAT00000013170; ENSBTAP00000013170; ENSBTAG00000009988.
DR GeneID; 537412; -.
DR KEGG; bta:537412; -.
DR CTD; 6598; -.
DR VEuPathDB; HostDB:ENSBTAG00000009988; -.
DR VGNC; VGNC:34991; SMARCB1.
DR eggNOG; KOG1649; Eukaryota.
DR GeneTree; ENSGT00440000038585; -.
DR HOGENOM; CLU_035084_0_0_1; -.
DR InParanoid; Q5BIN2; -.
DR OMA; QLWKRMA; -.
DR OrthoDB; 790205at2759; -.
DR TreeFam; TF105993; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000009988; Expressed in retina and 108 other tissues.
DR ExpressionAtlas; Q5BIN2; baseline and differential.
DR GO; GO:0035060; C:brahma complex; IBA:GO_Central.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016514; C:SWI/SNF complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR017393; Sfh1/SNF5.
DR InterPro; IPR006939; SNF5.
DR Pfam; PF04855; SNF5; 1.
DR PIRSF; PIRSF038126; SWI_SNF; 1.
PE 2: Evidence at transcript level;
KW Activator; Cell cycle; Chromatin regulator; DNA-binding; Isopeptide bond;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..385
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily B member 1"
FT /id="PRO_0000205947"
FT REPEAT 186..245
FT /note="1"
FT REPEAT 259..319
FT /note="2"
FT REGION 1..113
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q12824"
FT REGION 186..319
FT /note="2 X approximate tandem repeats"
FT REGION 186..245
FT /note="MYC-binding"
FT /evidence="ECO:0000250|UniProtKB:Q12824"
FT REGION 304..318
FT /note="Interaction with PPP1R15A"
FT /evidence="ECO:0000250|UniProtKB:Q12824"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12824"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12824"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12824"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12824"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12824"
SQ SEQUENCE 385 AA; 44111 MW; B2B1DA187CC2384D CRC64;
MMMMALSKTF GQKPVKFQLE DDGEFYMIGS EVGNYLRMFR GSLYKRYPSL WRRLATVEER
KKIVASSHGK KTKPNAKDHG YTTLATSVTL LKASEVEEIL DGNDEKYKAV SISTEPPTYL
REQKAKRNSQ WVPTLPNSSH HLDAVPCSTT INRNRMGRDK KRTFPLCFDD HDPAVIHENA
SQPEVLVPIR LDMEIDGQKL RDAFTWNMNE KLMTPEMFSE ILCDDLDLNP LTFVPAIASA
IRQQIESYPT DSILEDQSDQ RVIIKLNIHV GNISLVDQFE WDMSEKENSP EKFALKLCSE
LGLGGEFVTT IAYSIRGQLS WHQKTYAFSE NPLPTVEIAI RNTGDADQWC PLLETLTDAE
MEKKIRDQDR NTRRMRRLAN TAPAW
