ANAPC11
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Official Full Name
anaphase promoting complex subunit 11
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Overview
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex. -
Synonyms
ANAPC11; anaphase promoting complex subunit 11; APC11; Apc11p; MGC882; HSPC214; Anaphase-promoting complex subunit 11; Cyclosome subunit 11; Hepatocellular carcinoma-associated RING finger protein; APC11 anaphase promoting complex subunit 11 homolog; anaphase promoting complex subunit 11 (yeast APC11 homolog);
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Human
- Mouse
- Rhesus Macaque
- Zebrafish
- E.coli
- HEK293
- HEK293T
- In Vitro Cell Free System
- Mammalian Cell
- Wheat Germ
- GST
- His
- His (Fc)
- Avi
- Myc
- DDK
- N/A
- Involved Pathway
- Protein Function
- Interacting Protein
ANAPC11 involved in several pathways and played different roles in them. We selected most pathways ANAPC11 participated on our site, such as Cell cycle, Oocyte meiosis, Ubiquitin mediated proteolysis, which may be useful for your reference. Also, other proteins which involved in the same pathway with ANAPC11 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Cell cycle | CENPQ;HIST3H2BB;RUVBL2;MAPRE1A;TFDP2;SDCCAG8;WEE2;WEE1;PTTG2 |
Oocyte meiosis | YWHAE2;CALM3B;FBXW11B;MOS;INS2;CAMK2D;PPP1CC;IGF1RA;INS1 |
Ubiquitin mediated proteolysis | UBE2E2;KLHL13;PPIL2;UBE2KB;PIAS4B;NEDD4L;XIAP;NHLRC1;UBE2NB |
Progesterone-mediated oocyte maturation | CPEB3;MAD2L1;HSP90AA1.2;INS;PIK3R3A;MAPK8A;RAF1B;IGF1;CPEB1A |
HTLV-I infection | WNT11;HLA-DQA1;NFATC1;HLA-DRA;FZD5;ZFP36;NFKB2;WNT3;RRAS |
ANAPC11 has several biochemical functions, for example, cullin family protein binding, ubiquitin protein ligase activity, contributes_to ubiquitin-protein transferase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by ANAPC11 itself. We selected most functions ANAPC11 had, and list some proteins which have the same functions with ANAPC11. You can find most of the proteins on our site.
Function | Related Protein |
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cullin family protein binding | KCTD17;TCHP;DCUN1D5;RNF7;PARK2;DCUN1D2B;DCUN1D2;RBX1;DCUN1D1 |
ubiquitin protein ligase activity | BRAP;MYLIP;HERC4;RNF144A;UBE2U;UBE3A;HECW1B;UBE2G2;HACE1 |
contributes_to ubiquitin-protein transferase activity | BARD1;RNF2;KLHL30;TCEB3B;KBTBD13;RNF40;UBE2S;IPP;KLHL28 |
ubiquitin-ubiquitin ligase activity | UBOX5;PPIL2;UBE2K;STUB1;PRPF19;UBE4B;AMFR;ANAPC11;RBX1 |
zinc ion binding | Car4;RNF185;CAPNS2;ZKSCAN5;IGHMBP2;RABGGTA;NR2F1A;SHANK3;NR4A1 |
ANAPC11 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ANAPC11 here. Most of them are supplied by our site. Hope this information will be useful for your research of ANAPC11.
CDC20; Cdc23; Cdc16; MAK; ZAP70; UBE2U; TRIM65; RNF111; MLKL; NKD2; CAPN11; CDC16
- Q&As
- Reviews
Q&As (17)
Ask a questionWhile ANAPC11 is best known for its role in cell cycle regulation as a component of the APC/C complex, emerging research suggests that it may have additional functions. For instance, ANAPC11 has been implicated in DNA damage response and repair mechanisms, and it may play a role in chromatin remodeling and gene expression regulation. Further investigations are needed to fully understand these potential non-canonical roles of ANAPC11.
ANAPC11 is primarily localized to the nucleus, specifically in the nucleoplasm, where it associates with other subunits of the APC/C complex. However, in some cases, ANAPC11 can also be detected in the cytoplasm.
The expression of ANAPC11 can be regulated by various factors. For example, studies have shown that the transcription factor E2F1 can directly bind to the ANAPC11 promoter and enhance its expression, thus promoting cell cycle progression. Additionally, microRNAs (miRNAs), such as miR-27a and miR-148a, have been identified as negative regulators of ANAPC11 expression. These miRNAs can directly bind to the ANAPC11 mRNA and inhibit its translation.
Ongoing and future research on ANAPC11 aims to deepen our understanding of its cellular functions and regulatory mechanisms. This includes investigating its roles outside of cell cycle regulation, exploring its interactions with other signaling pathways, and identifying potential therapeutic interventions for diseases associated with ANAPC11 dysregulation. Additionally, further studies may elucidate the precise molecular mechanisms by which ANAPC11 contributes to normal cell cycle progression and cellular homeostasis.
To study ANAPC11, researchers commonly use techniques such as gene expression analysis, protein-protein interaction assays, and functional assays using cell lines or animal models. These methods can help elucidate its role in cell cycle regulation, identify interacting partners, and investigate the effects of ANAPC11 dysregulation. Additionally, gene editing techniques like CRISPR/Cas9 can be employed to manipulate ANAPC11 expression and study its effects on cellular processes.
ANAPC11 has shown potential as a diagnostic and prognostic marker in various types of cancer. Alterations in ANAPC11 expression have been correlated with tumor stage, grade, and patient survival in cancers such as colorectal cancer, breast cancer, and hepatocellular carcinoma.
While ANAPC11's primary role is in the cell cycle as part of the APC/C complex, it also participates in other cellular processes. ANAPC11 is involved in the degradation of proteins associated with DNA replication, centrosome duplication, checkpoint control, and cellular differentiation, indicating its broader role in regulating various cellular events.
ANAPC11 dysregulation has been implicated in various diseases and disorders. For example, alterations in the expression or function of ANAPC11 have been observed in several types of cancer, including colorectal cancer, breast cancer, and hepatocellular carcinoma. Additionally, mutations in ANAPC11 have been linked to developmental disorders such as Cornelia de Lange syndrome and Roberts syndrome.
Targeting the components of the APC/C complex, including ANAPC11, has been explored as a potential strategy for cancer treatment. The APC/C complex dysfunction often leads to defective cell cycle regulation in cancer cells, making it an attractive target for therapy. However, further research is needed to develop specific inhibitors or modulators of ANAPC11 for clinical applications.
Mutations in genes encoding APC/C subunits, including ANAPC11, have been observed in certain cancers. Altered expression or mutations in ANAPC11 have been correlated with tumor progression and poor prognosis in gastric cancer, colorectal cancer, and hepatocellular carcinoma. However, more research is required to establish a direct causative role and understand the underlying mechanisms.
Researchers use various techniques to study the function and regulation of ANAPC11. Common methods include Western blotting, immunoprecipitation, site-directed mutagenesis, siRNA-mediated knockdown, and CRISPR/Cas9 gene editing. Additionally, techniques such as cell cycle analysis, fluorescence microscopy, and biochemical assays are employed to investigate ANAPC11's role in the cell cycle and protein degradation processes.
Studies have shown that depletion of ANAPC11 leads to defects in cell cycle progression, improper chromosome segregation, and accumulation of DNA damage, indicating that ANAPC11 is essential for normal cell viability and division. However, the extent of its indispensability may vary among different cell types and tissues.
ANAPC11 can interact with various proteins and participate in several signaling pathways. For example, it interacts with the spindle assembly checkpoint protein BUB3, regulating the recruitment of BUBR1 to kinetochores during mitosis. ANAPC11 also interacts with the tumor suppressor protein p53, influencing its stability and activity. These interactions suggest a role for ANAPC11 outside of the APC/C complex.
Yes, ANAPC11 is highly conserved across different species. Homologs of ANAPC11 have been identified in various organisms, ranging from yeast to humans. This conservation suggests that ANAPC11 plays a fundamental role in essential cellular processes and highlights its evolutionary significance.
Post-translational modifications (PTMs) of ANAPC11 have not been extensively studied. However, emerging evidence suggests that ANAPC11 may undergo modifications such as phosphorylation and sumoylation. These PTMs can potentially influence the stability, activity, or interaction partners of ANAPC11, thereby modulating its function within the APC/C complex. Future research is needed to fully characterize the PTMs of ANAPC11 and their functional significance.
ANAPC11 protein levels are regulated throughout the cell cycle. Its expression is tightly controlled, with increased levels during the G2/M phase when the APC/C complex is most active. Multiple mechanisms, including transcriptional regulation, protein stabilization, and post-translational modifications such as phosphorylation, are involved in the regulation of ANAPC11.
As of now, there are no specific drugs that target ANAPC11 directly. However, due to the critical role of the APC/C complex in cell cycle regulation and its involvement in various diseases, including cancer, targeting other components of the APC/C complex is an active area of research for developing therapeutic interventions. These efforts may indirectly impact ANAPC11 function.
Customer Reviews (4)
Write a reviewThe technical support provided by the manufacturer is invaluable in overcoming experimental hurdles and optimizing the utilization of ANAPC11 protein.
The ANAPC11 protein offered by the manufacturer is of exceptional quality, making it an ideal choice to fulfill my experimental needs.
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Its purity, integrity, and functionality are ensured through stringent quality control measures, which instills confidence in the reliability and accuracy of my research results.
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