Akap17b
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Official Full Name
A kinase (PRKA) anchor protein 17B
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Synonyms
Akap17b; Talia; PRKA17B; Sfrs17b; Srsf17b; AA407619; AKAP-17B; B230333C21Rik; C230056F04Rik; A-kinase anchor protein 17B; protein Talia; protein kinase A-anchoring protein 17B; serine/arginine-rich splicing factor 17B; splicing factor, arginine/serine-rich 17b;
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
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Mouse | Akap17b-3024M | Recombinant Mouse Akap17b, His-tagged | E.Coli or Yeast | His | 959 | |
Mouse | AKAP17B-1475M | Recombinant Mouse AKAP17B Protein | Mammalian Cell | His | ||
Mouse | AKAP17B-427M | Recombinant Mouse AKAP17B Protein, His (Fc)-Avi-tagged | HEK293 | His (Fc)-Avi | ||
Mouse | AKAP17B-427M-B | Recombinant Mouse AKAP17B Protein Pre-coupled Magnetic Beads | HEK293 |
- Involved Pathway
- Protein Function
- Interacting Protein
Akap17b involved in several pathways and played different roles in them. We selected most pathways Akap17b participated on our site, such as mRNA processing, which may be useful for your reference. Also, other proteins which involved in the same pathway with Akap17b 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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mRNA processing | SF3B4;RAVER1;PRPF8;RBM12B2;PRPF4BB;DHX15;DDX20;RBM39;CLK1 |
Akap17b has several biochemical functions, for example, RNA binding, molecular_function, nucleic acid binding. Some of the functions are cooperated with other proteins, some of the functions could acted by Akap17b itself. We selected most functions Akap17b had, and list some proteins which have the same functions with Akap17b. You can find most of the proteins on our site.
Function | Related Protein |
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RNA binding | SARNP;PSMA1;MIF4GDB;FXR2;ADARB1A;EIF4G2B;RBMX;EMG1;BARD1 |
molecular_function | TMEFF1B;GM14430;MUP12;LYPD8;GM749;TMEM144;GM4312;MRPS10;LENG1 |
nucleic acid binding | RNASE4;CIZ1B;SP8A;HNRNPA0A;TREX2;ZFP516;HNRNPA0B;FAM200A;REXO2 |
nucleotide binding | MAP2K2B;ATAD5B;PDPK1A;RBM4;GNAT1;SNRNP35;U2SURP;RHOUB;RBM44 |
Akap17b 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 Akap17b here. Most of them are supplied by our site. Hope this information will be useful for your research of Akap17b.
- Q&As
- Reviews
Q&As (16)
Ask a questionThe tissue and cell type-specific expression pattern of AKAP17B has not been extensively characterized. However, data from publicly available gene expression databases suggest that AKAP17B is expressed in various tissues, including the brain, heart, and testis. Further studies, such as RNA expression profiling, would provide more detailed information about the specific tissues and cell types in which AKAP17B is expressed.
As of now, there is limited information on genetic alterations or mutations in AKAP17B. However, genetic variations, such as single nucleotide polymorphisms (SNPs), can occur within AKAP genes and potentially impact their function. It is possible that similar genetic alterations or mutations can occur in AKAP17B, but further research is needed to determine the prevalence and functional consequences of these alterations.
There is currently no evidence suggesting a direct involvement of AKAP17B in cancer progression. However, the dysregulation of PKA signaling pathways, which AKAP17B may be involved in, has been linked to various types of cancer. It is worth exploring whether AKAP17B or related signaling pathways have any impact on cancer biology, but more research is necessary to establish any direct associations.
The structural features of AKAP17B have not been extensively characterized. AKAPs typically contain multiple protein-protein interaction domains, such as an amphipathic helix (AH) domain and one or more PKA-binding domains (PKA-BDs). These domains allow AKAPs to interact with PKA and other signaling molecules. Further research, such as structural studies or domain mapping experiments, would be necessary to elucidate the structural features and domain organization of AKAP17B.
Currently, there is limited information available regarding the specific interacting partners of AKAP17B. Further experimental studies, such as protein-protein interaction assays, are needed to identify potential binding partners and elucidate the molecular networks in which AKAP17B may be involved.
The specific role of AKAP17B in cellular signaling pathways is not yet well understood. However, AKAPs in general are known to play crucial roles in organizing and directing signaling events by scaffolding various signaling molecules.
Currently, there is limited information available regarding genetic variants or mutations in AKAP17B. It would be important to investigate the presence of any sequence variations in the AKAP17B gene across individuals or disease cohorts to determine if such variants may be associated with specific phenotypes or diseases.
Currently, there is limited information available regarding the phosphorylation sites on AKAP17B. Phosphorylation of a protein is a common post-translational modification that can regulate protein function and interactions. Further experimental studies, such as phosphoproteomic analyses or site-directed mutagenesis, would be required to identify and characterize potential phosphorylation sites on AKAP17B.
The post-translational modifications of AKAP17B have not been extensively studied. However, like many proteins, AKAP17B could potentially undergo various modifications, including phosphorylation, acetylation, or ubiquitination, which might regulate its function and activity. Future research is needed to ascertain the specific post-translational modifications that AKAP17B may undergo and their functional consequences.
The involvement of AKAP17B in neuronal signaling has not been extensively studied. However, as an AKAP protein, it is possible that AKAP17B may have a role in regulating PKA-mediated signaling pathways in neurons. Further research is necessary to investigate its specific involvement in neuronal signaling processes.
The interaction of AKAP17B with other AKAPs or its ability to form protein complexes has not been well documented. However, AKAPs in general are known to participate in dynamic protein-protein interactions and the formation of multi-protein complexes. Therefore, it is possible that AKAP17B may interact with other AKAPs or proteins to regulate signaling pathways, but further experimental studies are needed to confirm this.
As of now, there is no specific evidence for post-translational modifications of AKAP17B. However, AKAPs in general can be subject to various post-translational modifications, including phosphorylation, acetylation, ubiquitination, and sumoylation. These modifications can regulate the function, localization, or stability of AKAP proteins. Further research is needed to determine if AKAP17B undergoes post-translational modifications and the functional consequences of those modifications.
The specific cellular localization of AKAP17B has not been extensively characterized. However, studies have reported that AKAP17B is targeted to the centrioles during mitosis and is involved in regulating the formation and function of the mitotic spindle. Additional research is needed to determine the precise subcellular localization of AKAP17B and its potential roles in other cellular compartments.
Currently, there is limited information available on the isoforms or splice variants of AKAP17B. Further research is needed to explore the existence and potential functional differences of any isoforms or splice variants of this protein.
AKAP17B is predicted to contain an AKAP domain, which is responsible for interacting with PKA and anchoring it to specific subcellular locations. The presence of this domain suggests that AKAP17B may function as a scaffolding protein in PKA-mediated signaling pathways.
The specific involvement of AKAP17B in diseases or disorders is not well understood. However, dysregulation of PKA signaling pathways, in which AKAP17B may be involved, has been implicated in various diseases, including cardiovascular diseases, neurological disorders, and cancer. It would be interesting to determine if AKAP17B has any direct associations with specific diseases or disorders through its role in these signaling pathways, but further investigation is needed.
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