Notch1 can trans-activate an APP target gene, Kai1, and vice versa.

CD82 molecule, KAI1, Metastasis suppressor Kangai-1
PDB Structure KAI1 was modeled based on crystal structure of the extracellular domain of tetraspanin protein member, CD81 1G8Q

KAI1 cell-surface glycoprotein and the molecular mechanisms underlying the TIP60 coactivator complexes for the metastasis suppressor gene NGF reverts by the expression of the, KAI1: for 'kang ai' (抗癌 Chinese for anticancer) locus: 11p11.2; [§§] is a members of the Transmembrane 4 superfamily (TM4SF), are likely to be a selective downregulation strategy for many genes it is an 'activation antigen' of T cells at the level of transcription or posttranscription is down-regulated in the progression of common solid epithelial tumors that leads to the down-regulation of the KAI1 gene. KAI1 is the human homolog of the mouse leukocyte surface antigen R2. DARC is essential for the function of CD82 antigen KAI1, CD82 specifically suppresses tumor metastasis of antigen R2, CD82 (KIA), is incorporated into the viral envelope, gp78 [AMFR-autocrine motility factor receptor] associates with KAI1 (also known as CD82) involved in ER-associated (endoplasmic reticulum) degradation (ERAD), calnexin (CANX) may play a role in this process. Notch1 can trans-activate an APP target gene, Kai1, and vice versa. Tetraspanin-enriched microdomains is important for KAI1/CD82's motility-inhibitory activity are glycoproteins of unknown function, and is directly associated with the EGF receptor (EGFR). KAI1 was modeled based on crystal structure of the extracellular domain of tetraspanin protein member, CD81 and two other tetraspans, CD9-(MRP-1) and CD19. DARC - Duffy blood group, chemokine receptor (Homo sapiens) is essential for the function of CD82, early B cell marker CD9 a molecular partner (CD9P-1) and CD151 (Raph blood group) was found to be coupled. CD151 and CO-029 (TSPAN8 tetraspanin 8) are supposed to promote metastasis formation. KISS1 triggers dormancy in solitary, metastatic tumor cells. COOH-terminal interacting tetraspanin (KITENIN)-vang-like 1 (van gogh, Drosophila) by interacting with KAI1 participates in the regulation of the tumor formation as well as increased invasiveness and cells. Adhesion forces laterally organize cellular membranes via the presence vs absence of, inversely associated univariate and multivariate, Laminin (LN)- or (FN) fibronectin, associations that usually occur in the context of "tetraspanin web"; its mechanism of action has not yet been fully elucidated.

Histone acetyltransferase KAT5 Down-regulation and up-stream binding protein LBP1 induces apoptosis via the amyloid beta (A4) precursor-like protein.

Histone acetyltransferase HTATIP, Histone acetyltransferase KAT5, HIV-1 Tat interactive protein, HTATIP
PDB Structure 2ou2

Histone acetyltransferase KAT5 also known as Tip60 belongs to the MYST protein family homologous to those of MOZ related to yeast Sas2 locus: 11q13: [§§]. TIP60 represses apoptosis, but also an interaction partner of the Mdm2 oncoprotein , p53 induces (exogenous and endogenous) either cell-cycle, TIP60 on chromatin is decreased following DNA damage after cell death PDCD5 (programmed cell death 5) functions as a Tip60 coactivator and accumulate after exposure to ionizing radiation (IR). A catalytic subunit of the NuA4 histone acetyltransferase complex and a conserved mechanism GCN5 interacts with HTATTIP/TIP60 is a component of the NuA4. Tip60 and HDAC7, interact with each other and repress transcription. A complex formed by Tip60, EPC1, and ING3 is sufficient to reconstitute a trimeric HDAC1 complex as transcriptional repressors in robust nucleosomal HAT (nuclear histone acetyltransferase) activity in vitro the amyloid beta (A4) precursor-like protein 2 (APLP2) induces apoptosis via Tip60 in H4 cells, the general transcription factor TFIID, PCAF complex contains proteins that have histone-like domains. NPAT recruits the TRRAP-Tip60 complex to histone gene promoters. Down-regulation of the tetraspanin KAI1 transcription factor by which phorbol 12-myristate 13-acetate (PMA) up-regulates KAI1, induces recruitment of TIP49 (RuvB-like 1 (E. coli))/Pontin activator complexes to the same motif.