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Q16740

- CLPP_HUMAN

UniProt

Q16740 - CLPP_HUMAN

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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

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 – 1781 By 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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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. 1 Publication

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 Publication
Add
BLAST
Chaini57 – 277221ATP-dependent Clp protease proteolytic subunit, mitochondrialUniRule annotation
PRO_0000005516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei200 – 2001N6-succinyllysine By 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

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.

Miscellaneous databases

EvolutionaryTraceiQ16740.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S14 family.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111N → S in BAG34912. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 130 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

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