(data stored in ACNUC19916 zone)

HOGENOM: MOUSE7_PE575

ID   MOUSE7_PE575                         STANDARD;      PRT;   558 AA.
AC   MOUSE7_PE575; Q04863; Q8VE46;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Transcription factor RelB; (MOUSE7.PE575).
GN   Name=Relb;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE7.PE575.
CC       Mus musculus chromosome 7 NCBIM37  sequence 1..152524553 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:RELB_MOUSE
CC   -!- FUNCTION: NF-kappa-B is a pleiotropic transcription factor which
CC       is present in almost all cell types and is involved in many
CC       biological processed such as inflammation, immunity,
CC       differentiation, cell growth, tumorigenesis and apoptosis. NF-
CC       kappa-B is a homo- or heterodimeric complex formed by the Rel-like
CC       domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50,
CC       REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of
CC       their target genes and the individual dimers have distinct
CC       preferences for different kappa-B sites that they can bind with
CC       distinguishable affinity and specificity. Different dimer
CC       combinations act as transcriptional activators or repressors,
CC       respectively. NF-kappa-B is controlled by various mechanisms of
CC       post-translational modification and subcellular
CC       compartmentalization as well as by interactions with other
CC       cofactors or corepressors. NF-kappa-B complexes are held in the
CC       cytoplasm in an inactive state complexed with members of the NF-
CC       kappa-B inhibitor (I-kappa-B) family. In a conventional activation
CC       pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs)
CC       in response to different activators, subsequently degraded thus
CC       liberating the active NF-kappa-B complex which translocates to the
CC       nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes
CC       are transcriptional activators. RELB neither associates with DNA
CC       nor with RELA/p65 or REL. Stimulates promoter activity in the
CC       presence of NFKB2/p49 (By similarity).
CC   -!- SUBUNIT: Component of the NF-kappa-B RelB-p50 complex. Component
CC       of the NF-kappa-B RelB-p52 complex (By similarity). Self-
CC       associates; the interaction seems to be transient and may prevent
CC       degradation allowing for heterodimer formation p50 or p52.
CC       Interacts with NFKB1/p50, NFKB2/p52 and NFKB2/p100. Interacts with
CC       NFKBID.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, centrosome
CC       (By similarity). Note=Co-localizes with NEK6 in the centrosome (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in intestine, thymus and spleen.
CC       Undetectable in liver, bome marrow, kidney and testis.
CC   -!- DOMAIN: Both N- and C-terminal domains are required for
CC       transcriptional activation.
CC   -!- PTM: Phosphorylation at 'Thr-103' and 'Ser-573' is followed by
CC       proteasomal degradation.
CC   -!- SIMILARITY: Contains 1 RHD (Rel-like) domain.
CC   -!- GENE_FAMILY: HOG000148598 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000002983;ENSMUST00000094762;ENSMUSP00000092355.
DR   EMBL; AK146932; - ;
DR   EMBL; AK156767; - ;
DR   EMBL; BC019765; - ;
DR   EMBL; BC117793; - ;
DR   EMBL; DQ020178; - ;
DR   EMBL; M83380; - ;
DR   EMBL; S56076; - ;
DR   EMBL; S76754; - ;
DR   UniProtKB/Swiss-Prot; Q04863; Q8VE46; -.
DR   EMBL; M83380; AAA40041.1; -; mRNA.
DR   EMBL; AK146932; BAE27543.1; -; mRNA.
DR   EMBL; BC019765; AAH19765.1; -; mRNA.
DR   EMBL; BC117793; AAI17794.1; -; mRNA.
DR   EMBL; S56076; AAB25493.2; -; mRNA.
DR   EMBL; S76754; AAB33259.1; -; Genomic_DNA.
DR   IPI; IPI00331502; -.
DR   PIR; A42023; A42023.
DR   PIR; I58091; I58091.
DR   RefSeq; NP_033072.2; NM_009046.2.
DR   UniGene; Mm.1741; -.
DR   PDB; 1ZK9; X-ray; 2.18 A; A=277-378.
DR   PDB; 1ZKA; X-ray; 2.20 A; A=277-378.
DR   PDB; 2V2T; X-ray; 3.05 A; A=91-378.
DR   PDB; 3DO7; X-ray; 3.05 A; A=88-383.
DR   PDB; 3JSS; X-ray; 2.60 A; A=278-378.
DR   PDB; 3JUZ; X-ray; 2.51 A; A=278-378.
DR   PDB; 3JV0; X-ray; 2.65 A; A=278-378.
DR   PDB; 3JV4; X-ray; 3.15 A; A/C/E=278-378.
DR   PDB; 3JV6; X-ray; 2.78 A; A/C/E=278-378.
DR   PDBsum; 1ZK9; -.
DR   PDBsum; 1ZKA; -.
DR   PDBsum; 2V2T; -.
DR   PDBsum; 3DO7; -.
DR   PDBsum; 3JSS; -.
DR   PDBsum; 3JUZ; -.
DR   PDBsum; 3JV0; -.
DR   PDBsum; 3JV4; -.
DR   PDBsum; 3JV6; -.
DR   ProteinModelPortal; Q04863; -.
DR   DIP; DIP-39585N; -.
DR   IntAct; Q04863; 1.
DR   MINT; MINT-225343; -.
DR   STRING; Q04863; -.
DR   PhosphoSite; Q04863; -.
DR   PRIDE; Q04863; -.
DR   Ensembl; ENSMUST00000094762; ENSMUSP00000092355; ENSMUSG00000002983.
DR   GeneID; 19698; -.
DR   CTD; 5971; -.
DR   MGI; MGI:103289; Relb.
DR   eggNOG; roNOG13607; -.
DR   GeneTree; ENSGT00500000044765; -.
DR   InParanoid; Q04863; -.
DR   OrthoDB; EOG4GQQ4T; -.
DR   ArrayExpress; Q04863; -.
DR   Bgee; Q04863; -.
DR   Genevestigator; Q04863; -.
DR   GermOnline; ENSMUSG00000002983; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR000451; NF_Rel_dor.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR011539; RHD.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:2.60.40.340; RHD; 1.
DR   Pfam; PF00554; RHD; 1.
DR   PRINTS; PR00057; NFKBTNSCPFCT.
DR   SMART; SM00429; IPT; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
DR   SUPFAM; SSF49417; P53_like_DNA_bnd; 1.
DR   PROSITE; PS01204; REL_1; 1.
DR   PROSITE; PS50254; REL_2; 1.
DR   HOGENOMDNA; MOUSE7.PE575; -.
KW   ENSMUSG000000029835old_1320000031; ENSMUSP000000923551old_1320000031;
KW   Q3U0K7_MOUSE; Q4U112_MOUSE; Q8VE46_MOUSE; AK146932; AK156767; BC019765;
KW   DQ020178; M83380; S56076; S76754;
KW   3D-structure; Activator; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
SQ   SEQUENCE   558 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPSRRAARES APELGALGSS DLSSLSLTVS RTTDELEIID EYIKENGFGL DGTQLSEMPR
     LVPRGPASLS SVTLGPAAPP PPATPSWSCT LGRLVSPGPC PRPYLVITEQ PKQRGMRFRY
     ECEGRSAGSI LGESSTEASK TLPAIELRDC GGLREVEVTA CLVWKDWPHR VHPHSLVGKD
     CTDGVCRVRL RPHVSPRHSF NNLGIQCVRK KEIEAAIERK IQLGIDPYNA GSLKNHQEVD
     MNVVRICFQA SYRDQQGHLH RMDPILSEPV YDKKSTNTSE LRICRINKES GPCTGGEELY
     LLCDKVQKED ISVVFSTASW EGRADFSQAD VHRQIAIVFK TPPYEDLEIS EPVTVNVFLQ
     RLTDGVCSEP LPFTYLPRDH DSYGVDKKRK RGLPDVLGEL SSSDPHGIES KRRKKKPVFL
     DHFLPGHSSG LFLPPSALQP ADSDFFPASI SLPGLEPPGG PDLLDDGFAY DPSAPTLFTM
     LDLLPPAPPL ASAVVGSGGA GATVVESSGP EPLSLDSFAA PGPGDVGTAS LVGSNMFPNQ
     YREAAFGGGL LSPGPEAT
//

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