ADRM1
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Official Full Name
adhesion regulating molecule 1
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Overview
Currently, there are five ubiquitin receptors associated with the proteasome: two proteasome subunits, Rpn10/S5a/PSMD4 and Rpn13/ADRM1 (Adhesion-regulating molecule 1), and three families of shuttling factors, Rad23, Dsk2, and Ddi1. ADRM1 is a ubiquitin r -
Synonyms
ADRM1; adhesion regulating molecule 1; proteasomal ubiquitin receptor ADRM1; ARM1; GP110; Rpn13; ARM-1; hRpn13; rpn13 homolog; M(r) 110,000 surface antigen; adhesion-regulating molecule 1; regulatory particle non-ATPase 13; 110 kDa cell membrane glycoprot;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Chicken
- Human
- Mouse
- Rat
- Rhesus Macaque
- Zebrafish
- E.coli
- HEK293
- HEK293T
- In Vitro Cell Free System
- Mammalian Cell
- Wheat Germ
- GST
- His
- His (Fc)
- Avi
- SUMO
- Myc
- DDK
- N/A
- N
- Involved Pathway
- Protein Function
- Interacting Protein
ADRM1 involved in several pathways and played different roles in them. We selected most pathways ADRM1 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with ADRM1 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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ADRM1 has several biochemical functions, for example, endopeptidase activator activity, protease binding, proteasome binding. Some of the functions are cooperated with other proteins, some of the functions could acted by ADRM1 itself. We selected most functions ADRM1 had, and list some proteins which have the same functions with ADRM1. You can find most of the proteins on our site.
Function | Related Protein |
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endopeptidase activator activity | PSME2;SFRP2;ADRM1;PSME1;PSME3;PSMD14 |
protease binding | CCBE1;SELL;POLG;RYR1;NFRKB;INS2;RNF139;BCL10;C10orf2 |
proteasome binding | ID1;PSMG1;ADRM1;DNAJB2;PSMD14;BAG6;USP13;UCHL5;UBD |
protein binding | DCBLD2;ADAR;LRRC3;VTA1;GGA2;PALM;LCOR;NOTCH3;RPL30 |
ADRM1 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 ADRM1 here. Most of them are supplied by our site. Hope this information will be useful for your research of ADRM1.
UCHL5
- Q&As
- Reviews
Q&As (10)
Ask a questionThe expression level of ADRM1 protein is regulated at the transcriptional and post-transcriptional levels by various cellular factors.
Post-translational modifications, including phosphorylation and ubiquitination, have been identified on ADRM1 protein, which can modulate its stability and function.
ADRM1 protein is primarily involved in the regulation of protein degradation through the ubiquitin-proteasome system.
ADRM1 protein interacts with ubiquitinated proteins, serving as a receptor to deliver them to the proteasome for degradation.
Some pharmacological agents, such as proteasome inhibitors, can affect the activity of ADRM1 protein indirectly by modulating the overall proteasome function. However, specific small molecules targeting ADRM1 directly are currently under investigation.
Dysregulation of ADRM1 protein has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.
Genetic and epigenetic factors can influence the expression and activity of ADRM1 protein, although specific regulatory mechanisms are still being elucidated.
Various experimental techniques, such as protein-protein interaction assays, immunoprecipitation, and mass spectrometry, have been used to study the function of ADRM1 protein.
ADRM1 protein is mainly localized to the cytoplasm and is associated with the 26S proteasome.
Yes, ADRM1 protein can interact with other proteins and participate in protein complexes involved in protein degradation processes.
Customer Reviews (3)
Write a reviewExploring protein-protein interactions involved in viral infections.
Detecting protein-protein interactions in multiprotein complexes.
Understanding protein-protein interaction networks in chromatin remodeling.
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