Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O76031

- CLPX_HUMAN

UniProt

O76031 - CLPX_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (11 Jul 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. ATPase activity Source: UniProtKB
    2. ATP binding 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

    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

    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

    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 – 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

    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. 17 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.
    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

    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:
    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. 17 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

    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: October 1, 2014
    This is version 125 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