SUH_BOVIN
ID SUH_BOVIN Reviewed; 487 AA.
AC Q3SZ41;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Recombining binding protein suppressor of hairless;
DE AltName: Full=J kappa-recombination signal-binding protein;
DE AltName: Full=RBP-J kappa;
GN Name=RBPJ; Synonyms=RBPSUH;
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=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional regulator that plays a central role in Notch
CC signaling, a signaling pathway involved in cell-cell communication that
CC regulates a broad spectrum of cell-fate determinations. Acts as a
CC transcriptional repressor when it is not associated with Notch
CC proteins. When associated with some NICD product of Notch proteins
CC (Notch intracellular domain), it acts as a transcriptional activator
CC that activates transcription of Notch target genes. Probably represses
CC or activates transcription via the recruitment of chromatin remodeling
CC complexes containing histone deacetylase or histone acetylase proteins,
CC respectively. Specifically binds to the immunoglobulin kappa-type J
CC segment recombination signal sequence. Binds specifically to methylated
CC DNA. Binds to the oxygen responsive element of COX4I2 and activates its
CC transcription under hypoxia conditions (4% oxygen). Negatively
CC regulates the phagocyte oxidative burst in response to bacterial
CC infection by repressing transcription of NADPH oxidase subunits (By
CC similarity). {ECO:0000250|UniProtKB:P31266,
CC ECO:0000250|UniProtKB:Q06330}.
CC -!- SUBUNIT: Interacts with activated NOTCH1, NOTCH2 or NOTCH3. Interacts
CC with MINT/SHARP. This interaction may mediate the recruitment of large
CC corepressor complexes containing proteins such as HDAC1, HDAC2, NCOR2,
CC SAP30, FHL1/KYOT2 and CIR1. Interacts with EP300, MAML1 and PTF1A.
CC Interacts with RITA1, leading to nuclear export, prevent the
CC interaction between RBPJ and NICD product and subsequent down-
CC regulation of the Notch signaling pathway. Interacts with SNW1.
CC Interacts with CHCHD2 and CXXC5. Interacts with BEND6 (via BEN domain).
CC Interacts with NKAPL. Interacts with ZMIZ1. Interacts with RBM15.
CC {ECO:0000250|UniProtKB:P31266, ECO:0000250|UniProtKB:Q06330}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Mainly nuclear, upon interaction with RITA1, translocates to the
CC cytoplasm, down-regulating the Notch signaling pathway. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Su(H) family. {ECO:0000305}.
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DR EMBL; BC103164; AAI03165.1; -; mRNA.
DR RefSeq; NP_001070469.1; NM_001077001.2.
DR AlphaFoldDB; Q3SZ41; -.
DR SMR; Q3SZ41; -.
DR STRING; 9913.ENSBTAP00000004696; -.
DR PaxDb; Q3SZ41; -.
DR PRIDE; Q3SZ41; -.
DR Ensembl; ENSBTAT00000004696; ENSBTAP00000004696; ENSBTAG00000003602.
DR GeneID; 767928; -.
DR KEGG; bta:767928; -.
DR CTD; 3516; -.
DR VEuPathDB; HostDB:ENSBTAG00000003602; -.
DR VGNC; VGNC:53775; RBPJ.
DR eggNOG; KOG3743; Eukaryota.
DR GeneTree; ENSGT00390000005197; -.
DR HOGENOM; CLU_022207_2_1_1; -.
DR InParanoid; Q3SZ41; -.
DR OMA; ISEVQWN; -.
DR OrthoDB; 444988at2759; -.
DR TreeFam; TF314117; -.
DR Reactome; R-BTA-350054; Notch-HLH transcription pathway.
DR Reactome; R-BTA-8941856; RUNX3 regulates NOTCH signaling.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000003602; Expressed in milk and 109 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
DR GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; ISS:UniProtKB.
DR CDD; cd01176; IPT_RBP-Jkappa; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1450; -; 1.
DR InterPro; IPR015350; Beta-trefoil_DNA-bd_dom.
DR InterPro; IPR036358; BTD_sf.
DR InterPro; IPR040159; CLS_fam.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR015351; RBP-J/Cbf11/Cbf12_DNA-bd.
DR InterPro; IPR037095; RBP-J/Cbf11_DNA-bd_sf.
DR InterPro; IPR038007; RBP-Jkappa_IPT.
DR PANTHER; PTHR10665; PTHR10665; 2.
DR Pfam; PF09270; BTD; 1.
DR Pfam; PF09271; LAG1-DNAbind; 1.
DR Pfam; PF20144; TIG_SUH; 1.
DR SMART; SM01268; BTD; 1.
DR SMART; SM01267; LAG1_DNAbind; 1.
DR SUPFAM; SSF110217; SSF110217; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Cytoplasm; DNA-binding; Notch signaling pathway;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..487
FT /note="Recombining binding protein suppressor of hairless"
FT /id="PRO_0000260076"
FT DOMAIN 342..432
FT /note="IPT/TIG"
FT REGION 44..54
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q06330"
FT REGION 152..157
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q06330"
FT REGION 179..184
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q06330"
FT REGION 452..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31266"
SQ SEQUENCE 487 AA; 54341 MW; 0EA722EED8647942 CRC64;
MAPVVTGKFG ERPPPKRLTR EAMRNYLKER GDQTVLILHA KVAQKSYGNE KRFFCPPPCV
YLMGSGWKKK KEQMERDGCS EQESQPCAFI GIGNSDQEMQ QLNLEGKNYC TAKTLYISDS
DKRKHFMLSV KMFYGNSDDI GVFLSKRIKV ISKPSKKKQS LKNADLCIAS GTKVALFNRL
RSQTVSTRYL HVEGGNFHAS SQQWGAFYIH LLDDDESEGE EFTVRDGYIH YGQTVKLVCS
VTGMALPRLI IRKVDKQTAL LDADDPVSQL HKCAFYLKDT ERMYLCLSQE RIIQFQATPC
PKEPNKEMIN DGASWTIIST DKAEYTFYEG MGPVLAPVTP VPVVESLQLN GGGDVAMLEL
TGQNFTPNLR VWFGDVEAET MYRCGESMLC VVPDISAFRE GWRWVRQPVQ VPVTLVRNDG
IIYSTSLTFT YTPEPGPRPH CSAAGAILRA NSSQVPPNES NTNSEGSYTN VSTNSTSVTS
STATVVS
