ClpB
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Official Full Name
ClpB caseinolytic peptidase B homolog (E. coli) -
Synonyms
CLPB;ClpB caseinolytic peptidase B homolog (E. coli);caseinolytic peptidase B protein homolog;FLJ13152;HSP78;SKD3;suppressor of potassium transport defect 3
Recombinant Proteins
- Human
- Rat
- E.coli
- Rhesus macaque
- E.coli
- Mammalian Cells
- Wheat Germ
- HEK293
- In Vitro Cell Free System
- His
- GST
- Non
- His&Fc&Avi
Involved Pathway
ClpB involved in several pathways and played different roles in them. We selected most pathways ClpB participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with ClpB 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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Protein Function
ClpB has several biochemical functions, for example, ATP binding,ATPase activity,molecular_function. Some of the functions are cooperated with other proteins, some of the functions could acted by ClpB itself. We selected most functions ClpB had, and list some proteins which have the same functions with ClpB. You can find most of the proteins on our site.
Function | Related Protein |
---|---|
ATP binding | NTRK1,DHX58,SYN3,ITPKB,ADRBK1,AARSD1,MASTL,SIK2,UBE2G1A,UBE2U |
molecular_function | CRESTIN,FAM188B,TNNI1AL,OSGIN2,SPEF1,UBALD1B,PTCHD3,CRYGM5,CCDC73,MFSD7A |
protein binding | CDK5R2,ADAM1B,PEAK1,PTGDR,CYB5R2,GLS2,RPL12,TFF2,FAS,PASK |
ATPase activity | HAND2,KIFC2,MYH8,CARNS1,ABCE1,KIF2C,MACF1,Abca2,NSFB,PSMC2 |
Interacting Protein
ClpB 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 ClpB here. Most of them are supplied by our site. Hope this information will be useful for your research of ClpB.
CEP70;MDFI;UCHL3;SQSTM1;USP30;TRMT10C;COPS6;OSBPL10;SMAD9;q81ye8_bacan;TTF2;ATG2A;pi3p;ssrna_ag;IRS4;1C
Resources
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References
- Kanabus, M; Shahni, R; et al. Bi-allelic CLPB mutations cause cataract, renal cysts, nephrocalcinosis and 3-methylglutaconic aciduria, a novel disorder of mitochondrial protein disaggregation. JOURNAL OF INHERITED METABOLIC DISEASE 38:211-219(2015).
- Erives, AJ; Fassler, JS; et al. Metabolic and Chaperone Gene Loss Marks the Origin of Animals: Evidence for Hsp104 and Hsp78 Chaperones Sharing Mitochondrial Enzymes as Clients. PLOS ONE 10:-(2015).