(data stored in ACNUC19916 zone)

HOGENOM: HS19_PE2341

ID   HS19_PE2341                          STANDARD;      PRT;   579 AA.
AC   HS19_PE2341; Q01201; Q6GTX7; Q9UEI7;
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;AltName: Full=I-Rel;
DE   (HS19.PE2341).
GN   Name=RELB;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS19.PE2341.
CC       Homo sapiens chromosome 19 GRCh37  sequence 1..59118983 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:RELB_HUMAN
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.
CC   -!- SUBUNIT: Component of the NF-kappa-B RelB-p50 complex. Component
CC       of the NF-kappa-B RelB-p52 complex. Self-associates; the
CC       interaction seems to be transient and may prevent degradation
CC       allowing for heterodimer formation with p50 or p52. Interacts with
CC       NFKB1/p50, NFKB2/p52 and NFKB2/p100. Interacts with NFKBID (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q8N668:COMMD1; NbExp=2; IntAct=EBI-357837, EBI-1550112;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton,
CC       centrosome. Note=Co-localizes with NEK6 in the centrosome.
CC   -!- INDUCTION: By mitogens.
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 (By similarity).
CC   -!- SIMILARITY: Contains 1 RHD (Rel-like) domain.
CC   -!- CAUTION: Was originally (PubMed:1577270) thought to inhibit the
CC       transcriptional activity of nuclear factor NF-kappa-B.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/RELBID324.html";
CC   -!- GENE_FAMILY: HOG000148598 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000104856;ENST00000221452;ENSP00000221452.
DR   EMBL; AF043454; - ;
DR   EMBL; AF043455; - ;
DR   EMBL; AF043456; - ;
DR   EMBL; AF043457; - ;
DR   EMBL; AF043458; - ;
DR   EMBL; AF043459; - ;
DR   EMBL; AF043460; - ;
DR   EMBL; AF043461; - ;
DR   EMBL; AF043462; - ;
DR   EMBL; AF043463; - ;
DR   EMBL; AK290594; - ;
DR   EMBL; BC028013; - ;
DR   EMBL; DQ314887; - ;
DR   EMBL; M83221; - ;
DR   UniProtKB/Swiss-Prot; Q01201; Q6GTX7; Q9UEI7; -.
DR   EMBL; M83221; AAA36127.1; -; mRNA.
DR   EMBL; AF043463; AAC82346.1; -; Genomic_DNA.
DR   EMBL; AF043454; AAC82346.1; JOINED; Genomic_DNA.
DR   EMBL; AF043455; AAC82346.1; JOINED; Genomic_DNA.
DR   EMBL; AF043456; AAC82346.1; JOINED; Genomic_DNA.
DR   EMBL; AF043457; AAC82346.1; JOINED; Genomic_DNA.
DR   EMBL; AF043458; AAC82346.1; JOINED; Genomic_DNA.
DR   EMBL; AF043459; AAC82346.1; JOINED; Genomic_DNA.
DR   EMBL; AF043460; AAC82346.1; JOINED; Genomic_DNA.
DR   EMBL; AF043461; AAC82346.1; JOINED; Genomic_DNA.
DR   EMBL; AF043462; AAC82346.1; JOINED; Genomic_DNA.
DR   EMBL; DQ314887; ABC40746.1; -; Genomic_DNA.
DR   EMBL; BC028013; AAH28013.1; -; mRNA.
DR   IPI; IPI00221034; -.
DR   PIR; A42617; A42617.
DR   RefSeq; NP_006500.2; NM_006509.3.
DR   UniGene; Hs.654402; -.
DR   ProteinModelPortal; Q01201; -.
DR   SMR; Q01201; 123-400.
DR   DIP; DIP-27531N; -.
DR   IntAct; Q01201; 8.
DR   MINT; MINT-1131428; -.
DR   STRING; Q01201; -.
DR   PhosphoSite; Q01201; -.
DR   PRIDE; Q01201; -.
DR   Ensembl; ENST00000221452; ENSP00000221452; ENSG00000104856.
DR   GeneID; 5971; -.
DR   KEGG; hsa:5971; -.
DR   UCSC; uc002paj.1; human.
DR   CTD; 5971; -.
DR   GeneCards; GC19P041935; -.
DR   H-InvDB; HIX0015220; -.
DR   HGNC; HGNC:9956; RELB.
DR   HPA; CAB007753; -.
DR   MIM; 604758; gene.
DR   neXtProt; NX_Q01201; -.
DR   PharmGKB; PA34322; -.
DR   eggNOG; prNOG19269; -.
DR   GeneTree; ENSGT00500000044765; -.
DR   InParanoid; Q01201; -.
DR   OMA; DLLDDGF; -.
DR   OrthoDB; EOG4GQQ4T; -.
DR   Pathway_Interaction_DB; nfkappabalternativepathway; Alternative NF-kappaB pathway.
DR   Pathway_Interaction_DB; il12_2pathway; IL12-mediated signaling events.
DR   NextBio; 23245; -.
DR   ArrayExpress; Q01201; -.
DR   Bgee; Q01201; -.
DR   CleanEx; HS_RELB; -.
DR   Genevestigator; Q01201; -.
DR   GermOnline; ENSG00000104856; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
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; HS19.PE2341; -.
KW   ENSG000001048561755old_1320000031; ENSP000002214527901old_1320000031;
KW   A8K3H9_HUMAN; AF043454; AF043455; AF043456; AF043457; AF043458; AF043459;
KW   AF043461; AF043462; AF043463; AK290594; BC028013; DQ314887; M83221;
KW   Activator; Complete proteome; Cytoplasm; Cytoskeleton; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Transcription;
KW   Transcription regulation.
SQ   SEQUENCE   579 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLRSGPASGP SVPTGRAMPS RRVARPPAAP ELGALGSPDL SSLSLAVSRS TDELEIIDEY
     IKENGFGLDG GQPGPGEGLP RLVSRGAASL STVTLGPVAP PATPPPWGCP LGRLVSPAPG
     PGPQPHLVIT EQPKQRGMRF RYECEGRSAG SILGESSTEA SKTLPAIELR DCGGLREVEV
     TACLVWKDWP HRVHPHSLVG KDCTDGICRV RLRPHVSPRH SFNNLGIQCV RKKEIEAAIE
     RKIQLGIDPY NAGSLKNHQE VDMNVVRICF QASYRDQQGQ MRRMDPVLSE PVYDKKSTNT
     SELRICRINK ESGPCTGGEE LYLLCDKVQK EDISVVFSRA SWEGRADFSQ ADVHRQIAIV
     FKTPPYEDLE IVEPVTVNVF LQRLTDGVCS EPLPFTYLPR DHDSYGVDKK RKRGMPDVLG
     ELNSSDPHGI ESKRRKKKPA ILDHFLPNHG SGPFLPPSAL LPDPDFFSGT VSLPGLEPPG
     GPDLLDDGFA YDPTAPTLFT MLDLLPPAPP HASAVVCSGG AGAVVGETPG PEPLTLDSYQ
     APGPGDGGTA SLVGSNMFPN HYREAAFGGG LLSPGPEAT
//

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