UniProtKB - O76031 (CLPX_HUMAN)
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Protein
ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial
Gene
CLPX
Organism
Homo sapiens (Human)
Status
Functioni
ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex (PubMed:11923310, PubMed:22710082). Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure (PubMed:22841477). ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Important for efficient erythropoiesis through upregulation of heme biosynthesis (PubMed:25957689).4 Publications
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 105 – 130 | C4-typeAdd BLAST | 26 | |
Nucleotide bindingi | 294 – 301 | ATPBy similarity | 8 |
GO - Molecular functioni
- ATPase activity Source: UniProtKB
- ATP binding Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- peptidase activator activity Source: UniProtKB
- unfolded protein binding Source: InterPro
GO - Biological processi
- ATP metabolic process Source: UniProtKB
- protein folding Source: InterPro
- proteolysis involved in cellular protein catabolic process Source: UniProtKB
Keywordsi
Molecular function | Chaperone |
Ligand | ATP-binding, Metal-binding, Nucleotide-binding, Zinc |
Names & Taxonomyi
Protein namesi | Recommended name: ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial |
Gene namesi | Name:CLPX |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000166855.9. |
HGNCi | HGNC:2088. CLPX. |
MIMi | 615611. gene. |
neXtProti | NX_O76031. |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 359 | E → A: Abolishes ATP hydrolysis. 1 Publication | 1 |
Organism-specific databases
OpenTargetsi | ENSG00000166855. |
PharmGKBi | PA26614. |
Chemistry databases
ChEMBLi | CHEMBL3797014. |
Polymorphism and mutation databases
BioMutai | CLPX. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 56 | MitochondrionSequence analysisAdd BLAST | 56 | |
ChainiPRO_0000005518 | 57 – 633 | ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrialAdd BLAST | 577 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 437 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 617 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | O76031. |
MaxQBi | O76031. |
PaxDbi | O76031. |
PeptideAtlasi | O76031. |
PRIDEi | O76031. |
PTM databases
iPTMneti | O76031. |
PhosphoSitePlusi | O76031. |
Expressioni
Tissue specificityi
Higher expression in skeletal muscle and heart and to a lesser extent in liver, brain, placenta, lung, kidney and pancreas.1 Publication
Gene expression databases
Bgeei | ENSG00000166855. |
CleanExi | HS_CLPX. |
ExpressionAtlasi | O76031. baseline and differential. |
Genevisiblei | O76031. HS. |
Organism-specific databases
HPAi | HPA040262. HPA048199. |
Interactioni
Subunit structurei
Homohexamer that forms a ring structure; this hexamerization requires ATP binding. Component of the Clp complex formed by the assembly of two CLPP heptameric rings with two CLPX hexameric rings, giving rise to a symmetrical structure with two central CLPP rings flanked by a CLPX ring at either end of the complex. Interacts with TFAM.5 Publications
GO - Molecular functioni
- unfolded protein binding Source: InterPro
Protein-protein interaction databases
BioGridi | 116056. 58 interactors. |
CORUMi | O76031. |
DIPi | DIP-50293N. |
IntActi | O76031. 23 interactors. |
MINTi | O76031. |
STRINGi | 9606.ENSP00000300107. |
Family & Domainsi
Sequence similaritiesi
Belongs to the ClpX chaperone family.Curated
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 105 – 130 | C4-typeAdd BLAST | 26 |
Keywords - Domaini
Transit peptide, Zinc-fingerPhylogenomic databases
eggNOGi | KOG0745. Eukaryota. COG1219. LUCA. |
GeneTreei | ENSGT00390000017625. |
HOGENOMi | HOG000010093. |
HOVERGENi | HBG004940. |
InParanoidi | O76031. |
KOi | K03544. |
OMAi | FSETPAY. |
OrthoDBi | EOG091G07XR. |
PhylomeDBi | O76031. |
TreeFami | TF312884. |
Family and domain databases
InterProi | View protein in InterPro IPR003593. AAA+_ATPase. IPR003959. ATPase_AAA_core. IPR019489. Clp_ATPase_C. IPR004487. Clp_protease_ATP-bd_su_ClpX. IPR027417. P-loop_NTPase. |
PANTHERi | PTHR11262. PTHR11262. 1 hit. |
Pfami | View protein in Pfam PF07724. AAA_2. 1 hit. PF10431. ClpB_D2-small. 1 hit. |
SMARTi | View protein in SMART SM00382. AAA. 1 hit. SM01086. ClpB_D2-small. 1 hit. |
SUPFAMi | SSF52540. SSF52540. 2 hits. |
TIGRFAMsi | TIGR00382. clpX. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
O76031-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPSCGACTCG AAAVRLITSS LASAQRGISG GRIHMSVLGR LGTFETQILQ
60 70 80 90 100
RAPLRSFTET PAYFASKDGI SKDGSGDGNK KSASEGSSKK SGSGNSGKGG
110 120 130 140 150
NQLRCPKCGD LCTHVETFVS STRFVKCEKC HHFFVVLSEA DSKKSIIKEP
160 170 180 190 200
ESAAEAVKLA FQQKPPPPPK KIYNYLDKYV VGQSFAKKVL SVAVYNHYKR
210 220 230 240 250
IYNNIPANLR QQAEVEKQTS LTPRELEIRR REDEYRFTKL LQIAGISPHG
260 270 280 290 300
NALGASMQQQ VNQQIPQEKR GGEVLDSSHD DIKLEKSNIL LLGPTGSGKT
310 320 330 340 350
LLAQTLAKCL DVPFAICDCT TLTQAGYVGE DIESVIAKLL QDANYNVEKA
360 370 380 390 400
QQGIVFLDEV DKIGSVPGIH QLRDVGGEGV QQGLLKLLEG TIVNVPEKNS
410 420 430 440 450
RKLRGETVQV DTTNILFVAS GAFNGLDRII SRRKNEKYLG FGTPSNLGKG
460 470 480 490 500
RRAAAAADLA NRSGESNTHQ DIEEKDRLLR HVEARDLIEF GMIPEFVGRL
510 520 530 540 550
PVVVPLHSLD EKTLVQILTE PRNAVIPQYQ ALFSMDKCEL NVTEDALKAI
560 570 580 590 600
ARLALERKTG ARGLRSIMEK LLLEPMFEVP NSDIVCVEVD KEVVEGKKEP
610 620 630
GYIRAPTKES SEEEYDSGVE EEGWPRQADA ANS
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 21 | L → P in BAF85005 (PubMed:14702039).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_048826 | 488 | I → T. Corresponds to variant dbSNP:rs35754835Ensembl. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ006267 mRNA. Translation: CAA06933.2. AJ276980 AJ276977 Genomic DNA. Translation: CAC01291.1. AK292316 mRNA. Translation: BAF85005.1. CH471082 Genomic DNA. Translation: EAW77715.1. BC130373 mRNA. Translation: AAI30374.1. BC136487 mRNA. Translation: AAI36488.1. |
CCDSi | CCDS10202.1. |
RefSeqi | NP_006651.2. NM_006660.4. |
UniGenei | Hs.113823. |
Genome annotation databases
Ensembli | ENST00000300107; ENSP00000300107; ENSG00000166855. |
GeneIDi | 10845. |
KEGGi | hsa:10845. |
UCSCi | uc002aom.4. human. |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Entry informationi
Entry namei | CLPX_HUMAN | |
Accessioni | O76031Primary (citable) accession number: O76031 Secondary accession number(s): A1L428 Q9H4D9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | July 11, 2001 | |
Last modified: | March 28, 2018 | |
This is version 158 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |