CLPX
entrez
10845
canonical
uniprot
O76031
canonical
ensembl
ENSG00000166855
resolver
ensp
ENSP00000300107
resolver
ensp
ENSP00000605167
resolver
enst
ENST00000300107
resolver
genesymbol
CLPX
resolver
hgnc
HGNC:2088
resolver
uniprot
A1L428
resolver
uniprot
A8K8F1
resolver
uniprot
B9EGI8
resolver
uniprot
Q9H4D9
resolver
uniprot_entry
CLPX_HUMAN
resolver
uniprot_sec
A1L428
resolver
uniprot_sec
A8K8F1
resolver
uniprot_sec
B9EGI8
resolver
uniprot_sec
Q9H4D9
resolver
amino_acid_sequence
MPSCGACTCGAAAVRLITSSLASAQRGISGGRIHMSVLGRLGTFETQILQRAPLRSFTETPAYFASKDGISKDGSGDGNKKSASEGSSKKSGSGNSGKGGNQLRCPKCGDLCTHVETFVSSTRFVKCEKCHHFFVVLSEADSKKSIIKEPESAAEAVKLAFQQKPPPPPKKIYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNIPANLRQQAEVEKQTSLTPRELEIRRREDEYRFTKLLQIAGISPHGNALGASMQQQVNQQIPQEKRGGEVLDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVEKAQQGIVFLDEVDKIGSVPGIHQLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRKLRGETVQVDTTNILFVASGAFNGLDRIISRRKNEKYLGFGTPSNLGKGRRAAAAADLANRSGESNTHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPNSDIVCVEVDKEVVEGKKEPGYIRAPTKESSEEEYDSGVEEEGWPRQADAANS
uniprot
proteins
disease_involvement
DISEASE: Protoporphyria, erythropoietic, 2 (EPP2) [MIM:618015]: An autosomal dominant form of porphyria with onset in infancy. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. Erythropoietic protoporphyria is marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals. {ECO:0000269|PubMed:28874591}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.4.10
uniprot
proteins
function
FUNCTION: ATP-dependent chaperone that functions as an unfoldase. As part of the ClpXP protease complex, it recognizes specific protein substrates, unfolds them using energy derived from ATP hydrolysis, and then translocates them to the proteolytic subunit (CLPP) of the ClpXP complex for degradation (PubMed:11923310, PubMed:22710082, PubMed:28874591). Thanks to its chaperone activity, it also functions in the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis (PubMed:28874591). This chaperone is also involved in the control of mtDNA nucleoid distribution, by regulating mitochondrial transcription factor A (TFAM) activity (PubMed:22841477). {ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:22710082, ECO:0000269|PubMed:22841477, ECO:0000269|PubMed:28874591}.
uniprot
proteins
mass_dalton
69224
uniprot
proteins
mutagenesis
MUTAGEN 359; /note="E->A: Abolishes ATP hydrolysis."; /evidence="ECO:0000269|PubMed:22710082
uniprot
proteins
protein_family
ClpX chaperone family
uniprot
proteins
pubmed
11003706
uniprot
proteins
pubmed
11923310
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15522782
uniprot
proteins
pubmed
16115876
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22710082
uniprot
proteins
pubmed
22841477
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
25957689
uniprot
proteins
pubmed
28874591
uniprot
proteins
sequence_length
633
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11003706}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:22841477}.
uniprot
proteins