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Protein

ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial

Gene

CLPX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. 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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri105 – 13026C4-typeAdd
BLAST
Nucleotide bindingi294 – 3018ATPBy similarity

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • peptidase activator activity Source: UniProtKB

GO - Biological processi

  • positive regulation of peptidase activity Source: GOC
  • protein folding Source: InterPro
  • proteolysis involved in cellular protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:2088. CLPX.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • endopeptidase Clp complex Source: UniProtKB
  • mitochondrial endopeptidase Clp complex Source: UniProtKB
  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial matrix Source: UniProtKB
  • mitochondrial nucleoid Source: BHF-UCL
  • mitochondrion Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Mitochondrion nucleoid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi359 – 3591E → A: Abolishes ATP hydrolysis. 1 Publication

Organism-specific databases

PharmGKBiPA26614.

Polymorphism and mutation databases

BioMutaiCLPX.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5656MitochondrionSequence AnalysisAdd
BLAST
Chaini57 – 633577ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrialPRO_0000005518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei437 – 4371N6-acetyllysine1 Publication
Modified residuei617 – 6171Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO76031.
PaxDbiO76031.
PeptideAtlasiO76031.
PRIDEiO76031.

PTM databases

PhosphoSiteiO76031.

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

BgeeiO76031.
CleanExiHS_CLPX.
ExpressionAtlasiO76031. baseline and differential.
GenevisibleiO76031. HS.

Organism-specific databases

HPAiHPA040262.
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

Protein-protein interaction databases

BioGridi116056. 26 interactions.
IntActiO76031. 12 interactions.
MINTiMINT-3002168.
STRINGi9606.ENSP00000300107.

Structurei

3D structure databases

ProteinModelPortaliO76031.
SMRiO76031. Positions 167-600.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ClpX chaperone family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri105 – 13026C4-typeAdd
BLAST

Keywords - Domaini

Transit peptide, Zinc-finger

Phylogenomic databases

eggNOGiCOG1219.
GeneTreeiENSGT00390000017625.
HOGENOMiHOG000010093.
HOVERGENiHBG004940.
InParanoidiO76031.
KOiK03544.
OMAiFSETPAY.
OrthoDBiEOG7J17ZF.
PhylomeDBiO76031.
TreeFamiTF312884.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004487. Clp_protease_ATP-bd_su_ClpX.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11262:SF4. PTHR11262:SF4. 1 hit.
PfamiPF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00382. clpX. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O76031-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:633
Mass (Da):69,224
Last modified:July 11, 2001 - v2
Checksum:iCF46A6DC0DDBF022
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211L → P in BAF85005 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti488 – 4881I → T.
Corresponds to variant rs35754835 [ dbSNP | Ensembl ].
VAR_048826

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006267 mRNA. Translation: CAA06933.2.
AJ276980
, AJ276981, AJ276966, AJ276967, AJ276968, AJ276969, AJ276970, AJ276971, AJ276972, AJ276973, AJ276974, AJ276975, AJ276976, 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.
CCDSiCCDS10202.1.
RefSeqiNP_006651.2. NM_006660.3.
UniGeneiHs.113823.

Genome annotation databases

EnsembliENST00000300107; ENSP00000300107; ENSG00000166855.
GeneIDi10845.
KEGGihsa:10845.
UCSCiuc002aom.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006267 mRNA. Translation: CAA06933.2.
AJ276980
, AJ276981, AJ276966, AJ276967, AJ276968, AJ276969, AJ276970, AJ276971, AJ276972, AJ276973, AJ276974, AJ276975, AJ276976, 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.
CCDSiCCDS10202.1.
RefSeqiNP_006651.2. NM_006660.3.
UniGeneiHs.113823.

3D structure databases

ProteinModelPortaliO76031.
SMRiO76031. Positions 167-600.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116056. 26 interactions.
IntActiO76031. 12 interactions.
MINTiMINT-3002168.
STRINGi9606.ENSP00000300107.

PTM databases

PhosphoSiteiO76031.

Polymorphism and mutation databases

BioMutaiCLPX.

Proteomic databases

MaxQBiO76031.
PaxDbiO76031.
PeptideAtlasiO76031.
PRIDEiO76031.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300107; ENSP00000300107; ENSG00000166855.
GeneIDi10845.
KEGGihsa:10845.
UCSCiuc002aom.3. human.

Organism-specific databases

CTDi10845.
GeneCardsiGC15M065440.
HGNCiHGNC:2088. CLPX.
HPAiHPA040262.
HPA048199.
MIMi615611. gene.
neXtProtiNX_O76031.
PharmGKBiPA26614.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1219.
GeneTreeiENSGT00390000017625.
HOGENOMiHOG000010093.
HOVERGENiHBG004940.
InParanoidiO76031.
KOiK03544.
OMAiFSETPAY.
OrthoDBiEOG7J17ZF.
PhylomeDBiO76031.
TreeFamiTF312884.

Miscellaneous databases

ChiTaRSiCLPX. human.
GenomeRNAii10845.
NextBioi41174.
PROiO76031.
SOURCEiSearch...

Gene expression databases

BgeeiO76031.
CleanExiHS_CLPX.
ExpressionAtlasiO76031. baseline and differential.
GenevisibleiO76031. HS.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004487. Clp_protease_ATP-bd_su_ClpX.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11262:SF4. PTHR11262:SF4. 1 hit.
PfamiPF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00382. clpX. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Skeletal muscle.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Testis.
  5. "Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP."
    Kang S.G., Ortega J., Singh S.K., Wang N., Huang N.N., Steven A.C., Maurizi M.R.
    J. Biol. Chem. 277:21095-21102(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  6. "Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP."
    Kang S.G., Maurizi M.R., Thompson M., Mueser T., Ahvazi B.
    J. Struct. Biol. 148:338-352(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH CLPP.
  7. "Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX."
    Kang S.G., Dimitrova M.N., Ortega J., Ginsburg A., Maurizi M.R.
    J. Biol. Chem. 280:35424-35432(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION IN A COMPLEX WITH CLPP.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Maintenance of mitochondrial genome distribution by mitochondrial AAA+ protein ClpX."
    Kasashima K., Sumitani M., Endo H.
    Exp. Cell Res. 318:2335-2343(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TFAM.
  13. "Substrate recognition and processing by a Walker B mutant of the human mitochondrial AAA+ protein CLPX."
    Lowth B.R., Kirstein-Miles J., Saiyed T., Broetz-Oesterhelt H., Morimoto R.I., Truscott K.N., Dougan D.A.
    J. Struct. Biol. 179:193-201(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-359, SUBUNIT, INTERACTION WITH CLPP.
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCLPX_HUMAN
AccessioniPrimary (citable) accession number: O76031
Secondary accession number(s): A1L428
, A8K8F1, B9EGI8, Q9H4D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 11, 2001
Last modified: June 24, 2015
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.