@prefix this: . @prefix sub: . @prefix beldoc: . @prefix rdfs: . @prefix rdf: . @prefix xsd: . @prefix dct: . @prefix dce: . @prefix pav: . @prefix np: . @prefix belv: . @prefix prov: . @prefix go: . @prefix scomp: . @prefix ProteinComplex: . @prefix hasAgent: . @prefix species: . @prefix occursIn: . @prefix pubmed: . @prefix orcid: . sub:Head { this: np:hasAssertion sub:assertion; np:hasProvenance sub:provenance; np:hasPublicationInfo sub:pubinfo; a np:Nanopublication . } sub:assertion { scomp:p85%2Fp110%20PI3Kinase%20Complex a ProteinComplex: . sub:_1 hasAgent: scomp:p85%2Fp110%20PI3Kinase%20Complex; a go:0016301 . sub:_2 occursIn: species:9606; rdf:object go:0016477; rdf:predicate belv:increases; rdf:subject sub:_1; a rdf:Statement . sub:assertion rdfs:label "kin(complex(SCOMP:\"p85/p110 PI3Kinase Complex\")) -> bp(GOBP:\"cell migration\")" . } sub:provenance { beldoc: dce:description "Approximately 61,000 statements."; dce:rights "Copyright (c) 2011-2012, Selventa. All rights reserved."; dce:title "BEL Framework Large Corpus Document"; pav:authoredBy sub:_4; pav:version "20131211" . sub:_3 prov:value "NF-?B transcriptional activity can be also regulated independently of I? B degradation by the direct phosphorylation of NF-?B subunits. The phosphorylation of NF-?B was demonstrated with I?B kinases [47, 48], protein kinase CK2 (formerly casein kinase II) [49, 50], protein kinase A (PKA) [51], phosphatidylinositol 3-kinase (PI3K) [52, 53] and protein kinase C? (PKC?) [53, 54]. In addition, mitogen-activated protein (MAP) kinase regulated the activity of NF-? B independently of the NF-? B phosphorylation [55]. Summary: NFKB1 (MIM 164011 ) or NFKB2 (MIM 164012 ) is bound to REL (MIM 164910 ), RELA (MIM 164014 ), or RELB (MIM 604758 ) to form the NFKB complex. The NFKB complex is inhibited by I-kappa-B proteins (NFKBIA, MIM 164008 , or NFKBIB, MIM 604495 ), which inactivate NF-kappa-B by trapping it in the cytoplasm. Phosphorylation of serine residues on the I-kappa-B proteins by kinases (IKBKA, MIM 600664 , or IKBKB) marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF-kappa-B complex. Activated NFKB complex translocates into the nucleus and binds DNA at kappa-B-binding motifs such as 5-prime GGGRNNYYCC 3-prime or 5-prime HGGARNYYCC 3-prime (where H is A, C, or T; R is an A or G purine; and Y is a C or T pyrimidine).[supplied by OMIM] The induction of cell motility has been linked to the activation of PI 3-kinase [57], and a significant increase of PI-3 kinase activity was detected in highly invasive MDA-MB-231 cells over that observed in MCF-7 cells [58]. However, the motility of breast cancer cells MDA-MB-231 was suppressed by the overexpression of dominant negative regulatory (p85?) subunit, as well as by the inhibition of catalytic (p110) subunit by specific inhibitors of p110, wortmannin and LY294002 [58]."; prov:wasQuotedFrom pubmed:15180498 . sub:_4 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:15180498; prov:wasDerivedFrom beldoc:, sub:_3 . } sub:pubinfo { this: dct:created "2014-07-03T14:32:22.143+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }