HCF1 Polyclonal Antibody

domain:The HCF repeat is a highly specific proteolytic cleavage signal.,domain:The kelch repeats fold into a 6-bladed kelch beta-propeller called the beta-propeller domain which mediates interaction with HCFC1R1.,function:Involved in control of the cell cycle. Upon lytic infection of permissive cells, the HSV transactivator protein VP16 associates with HCFC1. Binding to HCFC1 activates VP16 for association with the octamer motif-binding protein POU2F1, to form a multiprotein-DNA complex responsible for activating transcription of the HSV immediate early genes. Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300. Coactivator for EGR2 and GABP2. Tethers the chromatin modifying Set1/Ash2 histone H3-K4 methyltransferase (HMT) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together.,PTM:O-glycosylated.,PTM:Proteolytically cleaved at one or several PPCE--THET sites within the HCF repeats. Further cleavage of the primary N- and C-terminal chains results in a 'trimming' and accumulation of the smaller chains.,similarity:Contains 5 Kelch repeats.,subcellular location:HCFC1R1 modulates its subcellular localization and overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm.,subunit:Composed predominantly of six polypeptides ranging from 110 to 150 kDa and a minor 300 kDa polypeptide. The majority of N-and C-terminal cleavage products remain tightly, albeit non-covalently, associated. Interacts with POU2F1, VP16, CREB3, ZBTB17, EGR2, E2F4, CREBZF, SP1, GABP2, Sin3 HDAC complex (SIN3A, HDAC1, HDAC2, SDS3), Set1/Ash2 HMT complex (SET1, ASH2, WDR5), SAP30, SIN3B, OGT1 and FHL2. Component of the MLL complex, at least composed of MLL, ASH2L, RBBP5, DPY30, WDR5, MEN1, HCFC1 and HCFC2. Interacts with HCFC1R1 and THAP11.,tissue specificity:Highly expressed in fetal tissues and the adult kidney. Present in all tissues tested.,