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Q16740

- CLPP_HUMAN

UniProt

Q16740 - CLPP_HUMAN

Protein

ATP-dependent Clp protease proteolytic subunit, mitochondrial

Gene

CLPP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates.2 Publications

    Catalytic activityi

    Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei153 – 1531Nucleophile1 Publication
    Active sitei178 – 1781By similarity

    GO - Molecular functioni

    1. peptidase activity Source: ProtInc
    2. protein binding Source: UniProtKB
    3. serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. protein homooligomerization Source: Ensembl
    2. proteolysis involved in cellular protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    BRENDAi3.4.21.92. 2681.

    Protein family/group databases

    MEROPSiS14.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent Clp protease proteolytic subunit, mitochondrial (EC:3.4.21.92)
    Alternative name(s):
    Endopeptidase Clp
    Gene namesi
    Name:CLPP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:2084. CLPP.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. endopeptidase Clp complex Source: UniProtKB
    2. mitochondrial matrix Source: UniProtKB
    3. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Perrault syndrome 3 (PRLTS3) [MIM:614129]: A sex-influenced disorder characterized by sensorineural deafness in both males and females, and ovarian dysgenesis in females. Affected females have primary amenorrhea, streak gonads, and infertility, whereas affected males show normal pubertal development and are fertile. A spectrum of additional clinical features, including cerebellar ataxia, learning disability, and peripheral neuropathy, have been described in some PRLTS3 affected individuals.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti145 – 1451T → P in PRLTS3. 1 Publication
    VAR_070092
    Natural varianti147 – 1471C → S in PRLTS3. 1 Publication
    VAR_070093

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi58 – 614Missing: Abolishes protease activity. 1 Publication
    Mutagenesisi153 – 1531S → A or C: Abolishes protease activity. 2 Publications

    Keywords - Diseasei

    Deafness, Disease mutation

    Organism-specific databases

    MIMi614129. phenotype.
    Orphaneti2855. Perrault syndrome.
    PharmGKBiPA26610.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5656Mitochondrion1 PublicationAdd
    BLAST
    Chaini57 – 277221ATP-dependent Clp protease proteolytic subunit, mitochondrialPRO_0000005516Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei200 – 2001N6-succinyllysineBy similarity
    Modified residuei211 – 2111N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ16740.
    PaxDbiQ16740.
    PeptideAtlasiQ16740.
    PRIDEiQ16740.

    PTM databases

    PhosphoSiteiQ16740.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level). Predominantly expressed in skeletal muscle. Intermediate levels in heart, liver and pancreas. Low in brain, placenta, lung and kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ16740.
    BgeeiQ16740.
    CleanExiHS_CLPP.
    GenevestigatoriQ16740.

    Organism-specific databases

    HPAiHPA010649.

    Interactioni

    Subunit structurei

    Fourteen CLPP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity. 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.4 Publications

    Protein-protein interaction databases

    BioGridi113835. 3 interactions.
    DIPiDIP-50384N.
    IntActiQ16740. 1 interaction.
    STRINGi9606.ENSP00000245816.

    Structurei

    Secondary structure

    1
    277
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi75 – 806
    Turni81 – 833
    Beta strandi84 – 918
    Helixi93 – 10917
    Beta strandi111 – 1133
    Beta strandi115 – 1217
    Helixi126 – 13813
    Beta strandi143 – 15210
    Helixi154 – 1607
    Beta strandi167 – 1693
    Beta strandi174 – 1774
    Helixi188 – 21326
    Helixi217 – 2248
    Beta strandi228 – 2303
    Helixi232 – 2387
    Beta strandi242 – 2443

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TG6X-ray2.10A/B/C/D/E/F/G1-277[»]
    ProteinModelPortaliQ16740.
    SMRiQ16740. Positions 57-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16740.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S14 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0740.
    HOGENOMiHOG000285833.
    HOVERGENiHBG001689.
    InParanoidiQ16740.
    KOiK01358.
    OMAiKGERSFD.
    OrthoDBiEOG77WWD5.
    PhylomeDBiQ16740.
    TreeFamiTF105002.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_00444. ClpP.
    InterProiIPR001907. ClpP.
    IPR029045. ClpP/crotonase-like_dom.
    IPR023562. ClpP/TepA.
    IPR018215. ClpP_AS.
    [Graphical view]
    PANTHERiPTHR10381. PTHR10381. 1 hit.
    PfamiPF00574. CLP_protease. 1 hit.
    [Graphical view]
    PRINTSiPR00127. CLPPROTEASEP.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
    PS00381. CLP_PROTEASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q16740-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWPGILVGGA RVASCRYPAL GPRLAAHFPA QRPPQRTLQN GLALQRCLHA    50
    TATRALPLIP IVVEQTGRGE RAYDIYSRLL RERIVCVMGP IDDSVASLVI 100
    AQLLFLQSES NKKPIHMYIN SPGGVVTAGL AIYDTMQYIL NPICTWCVGQ 150
    AASMGSLLLA AGTPGMRHSL PNSRIMIHQP SGGARGQATD IAIQAEEIMK 200
    LKKQLYNIYA KHTKQSLQVI ESAMERDRYM SPMEAQEFGI LDKVLVHPPQ 250
    DGEDEPTLVQ KEPVEAAPAA EPVPAST 277
    Length:277
    Mass (Da):30,180
    Last modified:November 1, 1996 - v1
    Checksum:iB03AAC5D50F7880E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111N → S in BAG34912. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti145 – 1451T → P in PRLTS3. 1 Publication
    VAR_070092
    Natural varianti147 – 1471C → S in PRLTS3. 1 Publication
    VAR_070093

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50853 mRNA. Translation: CAA90705.1.
    AK311973 mRNA. Translation: BAG34912.1.
    BC002956 mRNA. Translation: AAH02956.1.
    CCDSiCCDS12162.1.
    PIRiS68421.
    RefSeqiNP_006003.1. NM_006012.2.
    UniGeneiHs.515092.

    Genome annotation databases

    EnsembliENST00000245816; ENSP00000245816; ENSG00000125656.
    GeneIDi8192.
    KEGGihsa:8192.
    UCSCiuc002mem.1. human.

    Polymorphism databases

    DMDMi3023512.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50853 mRNA. Translation: CAA90705.1 .
    AK311973 mRNA. Translation: BAG34912.1 .
    BC002956 mRNA. Translation: AAH02956.1 .
    CCDSi CCDS12162.1.
    PIRi S68421.
    RefSeqi NP_006003.1. NM_006012.2.
    UniGenei Hs.515092.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TG6 X-ray 2.10 A/B/C/D/E/F/G 1-277 [» ]
    ProteinModelPortali Q16740.
    SMRi Q16740. Positions 57-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113835. 3 interactions.
    DIPi DIP-50384N.
    IntActi Q16740. 1 interaction.
    STRINGi 9606.ENSP00000245816.

    Protein family/group databases

    MEROPSi S14.003.

    PTM databases

    PhosphoSitei Q16740.

    Polymorphism databases

    DMDMi 3023512.

    Proteomic databases

    MaxQBi Q16740.
    PaxDbi Q16740.
    PeptideAtlasi Q16740.
    PRIDEi Q16740.

    Protocols and materials databases

    DNASUi 8192.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000245816 ; ENSP00000245816 ; ENSG00000125656 .
    GeneIDi 8192.
    KEGGi hsa:8192.
    UCSCi uc002mem.1. human.

    Organism-specific databases

    CTDi 8192.
    GeneCardsi GC19P006315.
    HGNCi HGNC:2084. CLPP.
    HPAi HPA010649.
    MIMi 601119. gene.
    614129. phenotype.
    neXtProti NX_Q16740.
    Orphaneti 2855. Perrault syndrome.
    PharmGKBi PA26610.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0740.
    HOGENOMi HOG000285833.
    HOVERGENi HBG001689.
    InParanoidi Q16740.
    KOi K01358.
    OMAi KGERSFD.
    OrthoDBi EOG77WWD5.
    PhylomeDBi Q16740.
    TreeFami TF105002.

    Enzyme and pathway databases

    BRENDAi 3.4.21.92. 2681.

    Miscellaneous databases

    EvolutionaryTracei Q16740.
    GeneWikii CLPP.
    GenomeRNAii 8192.
    NextBioi 30886.
    PROi Q16740.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16740.
    Bgeei Q16740.
    CleanExi HS_CLPP.
    Genevestigatori Q16740.

    Family and domain databases

    Gene3Di 3.90.226.10. 1 hit.
    HAMAPi MF_00444. ClpP.
    InterProi IPR001907. ClpP.
    IPR029045. ClpP/crotonase-like_dom.
    IPR023562. ClpP/TepA.
    IPR018215. ClpP_AS.
    [Graphical view ]
    PANTHERi PTHR10381. PTHR10381. 1 hit.
    Pfami PF00574. CLP_protease. 1 hit.
    [Graphical view ]
    PRINTSi PR00127. CLPPROTEASEP.
    SUPFAMi SSF52096. SSF52096. 1 hit.
    PROSITEi PS00382. CLP_PROTEASE_HIS. 1 hit.
    PS00381. CLP_PROTEASE_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human ClpP protease: cDNA sequence, tissue-specific expression and chromosomal assignment of the gene."
      Bross P., Andresen B.S., Knudsen I., Kruse T.A., Gregersen N.
      FEBS Lett. 377:249-252(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Placenta.
    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: Skeletal muscle.
    3. "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: Lymph.
    4. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
      Xu G., Shin S.B., Jaffrey S.R.
      Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 57-69.
      Tissue: Leukemic T-cell.
    5. "Mitochondrial localization and oligomeric structure of HClpP, the human homologue of E. coli ClpP."
      de Sagarra M.R., Mayo I., Marco S., Rodriguez-Vilarino S., Oliva J., Carrascosa J.L., Castano J.G.
      J. Mol. Biol. 292:819-825(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "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, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF SER-153, ACTIVE SITE, ELECTRON MICROSCOPY.
    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 CLPX.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH CLPX, MUTAGENESIS OF 58-LEU--ILE-61.
    12. Cited for: VARIANTS PRLTS3 PRO-145 AND SER-147.

    Entry informationi

    Entry nameiCLPP_HUMAN
    AccessioniPrimary (citable) accession number: Q16740
    Secondary accession number(s): B2R4W5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3