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O76031

- CLPX_HUMAN

UniProt

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
Reviewed - 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-type
Add
BLAST
Nucleotide bindingi294 – 3018ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. ATPase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. peptidase activator activity Source: UniProtKB
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: UniProtKB
  2. positive regulation of peptidase activity Source: GOC
  3. protein folding Source: InterPro
  4. 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: Chromosome 15

Organism-specific databases

HGNCiHGNC:2088. CLPX.

Subcellular locationi

Mitochondrion. Mitochondrion matrixmitochondrion nucleoid 2 Publications

GO - Cellular componenti

  1. endopeptidase Clp complex Source: UniProtKB
  2. mitochondrial endopeptidase Clp complex Source: UniProtKB
  3. mitochondrial inner membrane Source: UniProtKB
  4. mitochondrial matrix Source: UniProtKB
  5. mitochondrial nucleoid Source: BHF-UCL
  6. mitochondrion Source: UniProtKB
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5656Mitochondrion Reviewed prediction
Add
BLAST
Chaini57 – 633577ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial
PRO_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

ArrayExpressiO76031.
BgeeiO76031.
CleanExiHS_CLPX.
GenevestigatoriO76031.

Organism-specific databases

HPAiHPA040262.

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. 16 interactions.
IntActiO76031. 12 interactions.
MINTiMINT-3002168.
STRINGi9606.ENSP00000300107.

Structurei

3D structure databases

ProteinModelPortaliO76031.
SMRiO76031. Positions 167-600.

Family & Domainsi

Sequence similaritiesi

Belongs to the ClpX chaperone family.

Keywords - Domaini

Transit peptide, Zinc-finger

Phylogenomic databases

eggNOGiCOG1219.
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

MPSCGACTCG AAAVRLITSS LASAQRGISG GRIHMSVLGR LGTFETQILQ    50
RAPLRSFTET PAYFASKDGI SKDGSGDGNK KSASEGSSKK SGSGNSGKGG 100
NQLRCPKCGD LCTHVETFVS STRFVKCEKC HHFFVVLSEA DSKKSIIKEP 150
ESAAEAVKLA FQQKPPPPPK KIYNYLDKYV VGQSFAKKVL SVAVYNHYKR 200
IYNNIPANLR QQAEVEKQTS LTPRELEIRR REDEYRFTKL LQIAGISPHG 250
NALGASMQQQ VNQQIPQEKR GGEVLDSSHD DIKLEKSNIL LLGPTGSGKT 300
LLAQTLAKCL DVPFAICDCT TLTQAGYVGE DIESVIAKLL QDANYNVEKA 350
QQGIVFLDEV DKIGSVPGIH QLRDVGGEGV QQGLLKLLEG TIVNVPEKNS 400
RKLRGETVQV DTTNILFVAS GAFNGLDRII SRRKNEKYLG FGTPSNLGKG 450
RRAAAAADLA NRSGESNTHQ DIEEKDRLLR HVEARDLIEF GMIPEFVGRL 500
PVVVPLHSLD EKTLVQILTE PRNAVIPQYQ ALFSMDKCEL NVTEDALKAI 550
ARLALERKTG ARGLRSIMEK LLLEPMFEVP NSDIVCVEVD KEVVEGKKEP 600
GYIRAPTKES SEEEYDSGVE EEGWPRQADA ANS 633
Length:633
Mass (Da):69,224
Last modified:July 11, 2001 - v2
Checksum:iCF46A6DC0DDBF022
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211L → P in BAF85005. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10202.1.
RefSeqi NP_006651.2. NM_006660.3.
UniGenei Hs.113823.

3D structure databases

ProteinModelPortali O76031.
SMRi O76031. Positions 167-600.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116056. 16 interactions.
IntActi O76031. 12 interactions.
MINTi MINT-3002168.
STRINGi 9606.ENSP00000300107.

PTM databases

PhosphoSitei O76031.

Proteomic databases

MaxQBi O76031.
PaxDbi O76031.
PeptideAtlasi O76031.
PRIDEi O76031.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300107 ; ENSP00000300107 ; ENSG00000166855 .
GeneIDi 10845.
KEGGi hsa:10845.
UCSCi uc002aom.3. human.

Organism-specific databases

CTDi 10845.
GeneCardsi GC15M065440.
HGNCi HGNC:2088. CLPX.
HPAi HPA040262.
MIMi 615611. gene.
neXtProti NX_O76031.
PharmGKBi PA26614.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1219.
HOGENOMi HOG000010093.
HOVERGENi HBG004940.
InParanoidi O76031.
KOi K03544.
OMAi FSETPAY.
OrthoDBi EOG7J17ZF.
PhylomeDBi O76031.
TreeFami TF312884.

Miscellaneous databases

GenomeRNAii 10845.
NextBioi 41174.
PROi O76031.
SOURCEi Search...

Gene expression databases

ArrayExpressi O76031.
Bgeei O76031.
CleanExi HS_CLPX.
Genevestigatori O76031.

Family and domain databases

Gene3Di 3.40.50.300. 3 hits.
InterProi IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004487. Clp_protease_ATP-bd_su_ClpX.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR11262:SF4. PTHR11262:SF4. 1 hit.
Pfami PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
TIGRFAMsi TIGR00382. clpX. 1 hit.
ProtoNeti Search...

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.

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: September 3, 2014
This is version 124 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

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