grpel1
Share
  • Official Full Name
  • GrpE-like 1, mitochondrial (E. coli)
  • Background
  • Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.
  • Synonyms
  • GRPEL1; GrpE-like 1, mitochondrial (E. coli); grpE protein homolog 1, mitochondrial; FLJ25609; HMGE; GREPEL 1; GREPEL1; GrpE like 1; GrpE like 1 mitochondrial; GrpE like protein cochaperone; GrpE protein homolog 1 mitochondrial; GRPE1_HUMAN; GRPEL 1; Mt GrpE#1; Mt-GrpE#1; GrpE-like protein cochaperone
Cat.#:GRPEL1-5380HTag:GST
Source (Host):Wheat GermSpecies:Human
Product nameRecombinant Human GRPEL1 Protein, GST-tagged
+Inquiry
Cat.#:GRPEL1-27415THTag:His
Source (Host):E. coliSpecies:Human
Product nameRecombinant Human GRPEL1, His-tagged
+Inquiry
Cat.#:GRPEL1-7293MTag:His
Source (Host):Mammalian CellsSpecies:Mouse
Product nameRecombinant Mouse GRPEL1 Protein
+Inquiry
Cat.#:GRPEL1-2722RTag:His
Source (Host):Mammalian CellsSpecies:Rat
Product nameRecombinant Rat GRPEL1 Protein
+Inquiry
Cat.#:GRPEL1-568CTag:His
Source (Host):Mammalian CellsSpecies:Cynomolgus Monkey
Product nameRecombinant Cynomolgus GRPEL1 Protein, His-tagged
+Inquiry
Cat.#:GRPEL1-1979RTag:His
Source (Host):Mammalian CellsSpecies:Rhesus Macaque
Product nameRecombinant Rhesus monkey GRPEL1 Protein, His-tagged
+Inquiry
Cat.#:GRPEL1-1597CTag:His
Source (Host):Mammalian CellsSpecies:Chicken
Product nameRecombinant Chicken GRPEL1
+Inquiry
Cat.#:GRPEL1-3509ZTag:His
Source (Host):Mammalian CellsSpecies:Zebrafish
Product nameRecombinant Zebrafish GRPEL1
+Inquiry
Cat.#:GRPEL1-2840HTag:His
Source (Host):E. coliSpecies:Human
Product nameRecombinant Human GrpE-like 1, Mitochondrial (E. coli), His-tagged
+Inquiry
Cat.#:GRPEL1-754HCLTag:
Source (Host):Species:Human
Product nameRecombinant Human GRPEL1 cell lysate
+Inquiry

Involved Pathway

GRPEL1 involved in several pathways and played different roles in them. We selected most pathways GRPEL1 participated on our site, such as Metabolism of proteins, Mitochondrial protein import, which may be useful for your reference. Also, other proteins which involved in the same pathway with GRPEL1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name
Pathway Related Protein
Metabolism of proteins
ADAMTS4; TRAPPC6B; PFDN6; SMC6; SEC61B; MPDU1B; DPH5; TRAPPC2; EXOC1; TIMM50
Mitochondrial protein import
TOMM20; MTX2; TIMM22; TIMM17A; TIMM44; PMPCB; FXC1; TIMM13; TIMM21; TIMM23

Protein Function

GRPEL1 has several biochemical functions, for example, adenyl-nucleotide exchange factor activity, chaperone binding, protein homodimerization activity. Some of the functions are cooperated with other proteins, some of the functions could acted by GRPEL1 itself. We selected most functions GRPEL1 had, and list some proteins which have the same functions with GRPEL1. You can find most of the proteins on our site.
Function
Related Protein
Function adenyl-nucleotide exchange factor activity
Related Protein PFN1; PFN2; HSPBP1; SIL1; GRPEL2; GRPEL1
Function chaperone binding
Related Protein DLST; DNAJC3; HSCB; BAK1; GRPEL1; DNAJB8; CDKN1B; DNAJC10; BAG4; TFRC
Function protein homodimerization activity
Related Protein TREX2; PYGB; AIMP1; PCYT1A; UNC13A; ATPIF1A; NLRC4; VIL1; TRIM8; CHRNA7
Function unfolded protein binding
Related Protein RP2; DNAJB1A; CALR; CRYABB; PFDN6; CALRL2; AHSP; CLPX; AIP; MKKS

Interacting Protein

GRPEL1 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 GRPEL1 here. Most of them are supplied by our site. Hope this information will be useful for your research of GRPEL1.
HLA-B; VHL; EIF6; PRKAB1; tsr; NS1; US11; IFIT1; ATF2; Nedd1; PPP2R2B; ICT1; EBNA-LP; Bag2

GRPEL1 Related Articles

Amick, J; Schlanger, SE; et al. Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone. PROTEIN SCIENCE 23:833-842(2014).
Yan, J; Takahashi, T; et al. Combined linkage analysis and exome sequencing identifies novel genes for familial goiter. JOURNAL OF HUMAN GENETICS 58:366-377(2013).