UniProt ID | GRPE2_HUMAN | |
---|---|---|
UniProt AC | Q8TAA5 | |
Protein Name | GrpE protein homolog 2, mitochondrial | |
Gene Name | GRPEL2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 225 | |
Subcellular Localization | Mitochondrion matrix. | |
Protein Description | 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. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70 (By similarity).. | |
Protein Sequence | MAVRSLWAGRLRVQRLLAWSAAWESKGWPLPFSTATQRTAGEDCRSEDPPDELGPPLAERALRVKAVKLEKEVQDLTVRYQRAIADCENIRRRTQRCVEDAKIFGIQSFCKDLVEVADILEKTTECISEESEPEDQKLTLEKVFRGLLLLEAKLKSVFAKHGLEKLTPIGDKYDPHEHELICHVPAGVGVQPGTVALVRQDGYKLHGRTIRLARVEVAVESQRRL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
71 | Ubiquitination | VKAVKLEKEVQDLTV HHEEEHHHHHHHHHH | 73.88 | 29967540 | |
131 | Phosphorylation | TECISEESEPEDQKL HHHCCCCCCCHHHHC | 55.17 | 28985074 | |
137 | Ubiquitination | ESEPEDQKLTLEKVF CCCCHHHHCHHHHHH | 56.62 | 29967540 | |
142 | Acetylation | DQKLTLEKVFRGLLL HHHCHHHHHHHHHHH | 50.19 | 19608861 | |
155 | 2-Hydroxyisobutyrylation | LLLEAKLKSVFAKHG HHHHHHHHHHHHHCC | 43.81 | - | |
160 | Ubiquitination | KLKSVFAKHGLEKLT HHHHHHHHCCHHHCC | 27.09 | 29967540 | |
172 | Ubiquitination | KLTPIGDKYDPHEHE HCCCCCCCCCCCCCE | 46.47 | 29967540 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of GRPE2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GRPE2_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of GRPE2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MUTA_HUMAN | MUT | physical | 26186194 | |
ODB2_HUMAN | DBT | physical | 26186194 | |
NDUF5_HUMAN | NDUFAF5 | physical | 26186194 | |
YES_HUMAN | YES1 | physical | 26186194 | |
FMC1_HUMAN | C7orf55 | physical | 26186194 | |
LYRM7_HUMAN | LYRM7 | physical | 26186194 | |
ODB2_HUMAN | DBT | physical | 28514442 | |
FMC1_HUMAN | C7orf55 | physical | 28514442 | |
MUTA_HUMAN | MUT | physical | 28514442 | |
NDUF5_HUMAN | NDUFAF5 | physical | 28514442 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND MASS SPECTROMETRY. |