SUH_PONAB
ID SUH_PONAB Reviewed; 486 AA.
AC Q5RFK6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR857150; CAH89451.1; -; mRNA.
DR AlphaFoldDB; Q5RFK6; -.
DR SMR; Q5RFK6; -.
DR STRING; 9601.ENSPPYP00000016373; -.
DR Ensembl; ENSPPYT00000037130; ENSPPYP00000043620; ENSPPYG00000014652.
DR eggNOG; KOG3743; Eukaryota.
DR GeneTree; ENSGT00390000005197; -.
DR InParanoid; Q5RFK6; -.
DR Proteomes; UP000001595; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
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..486
FT /note="Recombining binding protein suppressor of hairless"
FT /id="PRO_0000260077"
FT DOMAIN 341..431
FT /note="IPT/TIG"
FT REGION 43..53
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q06330"
FT REGION 151..156
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q06330"
FT REGION 178..183
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q06330"
FT REGION 451..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 161
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31266"
SQ SEQUENCE 486 AA; 54399 MW; 99713B72FE31D6E6 CRC64;
MAWIKRKFGE RPPPKRLTKE AMRNYLKERG DQTVLILHAK VAQKSYGNEK RFFCPPPCVY
LMGSGWKKKK EQMERDGCSE QESQPCAFIG IGNSDQEMQQ LNLEGKNYCT AKTLYISDSD
KRKHFMLSVK MFYGNSDDIG VFLSKRIKVI SKPSKKKQSL KNADLCIASG TKVALFNRLR
SQTVSTRYLH VEGGNFHASS QQWGAFFIHL LDDDESEGEE FTVRDGYIHY GQTVKLVCSV
TGMALPRLII RKVDKQTALL DADDPVSQLH KCAFYLKDTE RMYLCLSQER IIQFQATPCP
KEPNKEMIND GASWTIISTD KAEYTFYEGM GPVLAPVTPV PVVESLQLNG GGDVAMLELT
GQNFTPNLRV WFGDVEAETM YRCGESMLCV VPDISAFREG WRWVRQPVQV PVTLVRNDGI
IYSTSLTFTY TPEPGPRPHC SAAGAILRAN SSQVPPNESN TNSEGSYTNA STNSTSVTSS
TATVVS
